Patent Publication Number: US-2003232363-A1

Title: Fatty acid transport proteins

Description:
RELATED APPLICATIONS  
     [0001] This application is a divisional of U.S. application Ser. No. 09/611,197 filed Jul. 6, 2000 which is a continuation-in-part of U.S. patent application Ser. No. 09/506,252 filed Feb. 17, 2000 which is a continuation-in-part of U.S. patent application Ser. No. 09/465,280 filed Dec. 16, 1999, a continuation-in-part of U.S. patent application Ser. No. 09/405,504 filed Sep. 23, 1999, a continuation-in-part of U.S. patent application Ser. No. 09/405,505 filed Sep. 23, 1999, a continuation-in-part of U.S. patent application Ser. No. 09/232,197 filed Jan. 14, 1999, now U.S. Pat. No. 6,300,096, a continuation-in-part of U.S. patent application Ser. No. 09/232,200 filed Jan. 14, 1999, now U.S. Pat. No. 6,288,213, a continuation-in-part of U.S. patent application Ser. No. 09/232,201 filed Jan. 14, 1999, now U.S. Pat. No. 6,348,321, a continuation-in-part of U.S. patent application Ser. No. 09/232,195 filed Jan. 14, 1999, a continuation-in-part of U.S. patent application Ser. No. 09/232,191 filed Jan. 14, 1999, now U.S. Pat. No. 6,284,487, each of which claims the benefit of U.S. Provisional Application No. 60/110,941 filed Dec. 4, 1998; U.S. Provisional Application No. 60/093,491 filed Jul. 20, 1998; and U.S. Provisional Application No. 60/071,374 filed Jan. 15, 1998. The teachings of each of these referenced applications are incorporated herein by reference in their entirety.  
    
    
     GOVERNMENT SUPPORT  
     [0002] The invention was supported, in whole or in part, by a grant from the National Heart, Lung, and Blood Institute (HL41484), by National Institutes of Health Grant DK 47618 and National Institutes of Health Grant 5 T32 CA 09541. The United States Government has certain rights in the invention. 
    
    
     
       BACKGROUND OF THE INVENTION  
       [0003] Long chain fatty acids (LCFAs) are an important source of energy for most organisms. They also function as blood hormones, regulating key metabolic functions such as hepatic glucose production. Although LCFAs can diffuse through the hydrophobic core of the plasma membrane into cells, this nonspecific transport cannot account for the high affinity and specific transport of LCFAs exhibited by cells such as cardiac muscle, hepatocytes, enterocytes, and adipocytes. The molecular mechanisms of LCFA transport remains largely unknown. Identifying these mechanisms can lead to pharmaceuticals that modulate fatty acid uptake by the intestine and by other organs, thereby alleviating certain medical conditions (e.g. obesity).  
       SUMMARY OF THE INVENTION  
       [0004] Described herein is a diverse family of fatty acid transport proteins (FATPs) which are evolutionarily conserved; these FATPs are plasma membrane proteins which mediate transport of LCFAs across the membranes and into cells. Members of the FATP family described herein are present in a wide variety of organisms, from mycobacteria to humans, and exhibit very different expression patterns in tissues among the organisms. FATP family members are expressed in prokaryotic and eukaryotic organisms and comprise characteristic amino acid domains or sequences which are highly conserved across family members. In addition, the function of the FATP gene family is conserved throughout evolution, as shown by the fact that the  Caenorhabditis  ( C ).  elegans  and mycobacterial FATPs described herein facilitate LCFA uptake when they are overexpressed in COS cells or  Escherichia ( E. )  coli , respectively. FATPs are expressed in a wide variety of tissues, including all tissues which are important to fatty acid metabolism (uptake and processing).  
       [0005] In specific embodiments, FATPs of the present invention are from such diverse organisms as humans ( Homo  ( H. )  sapiens ), mice, ( Mus  ( M. )  musculus ),  F. rubripes, C. elegans, Drosophila  ( D. )  melanogaster, Saccharomyces  ( S. )  cerevisiae, Aspergillus nidulans, Cochliobolu heterostrophus, Magnaporthe grisea  and Mycobacterium (M.), such as  M. tuberculosis . As described herein, four novel mouse FATPs, referred to as mmFATP2, mmFATP3, mmFATP4 and mmFATP5, and six human FATPs, referred to as hsFATP1, hsFATP2, hsFATP3, hsFATP4, hsFATP5 and hsFATP6, have been identified. All four novel murine FATPs (mmFATP2-5) and a previously identified murine FATP (renamed herein FATP1) have orthologs in humans (hsFATP1-5); the sixth human FATP (hsFATP6) does not as yet have a mouse ortholog. The expression patterns of these FATPs vary, as described in detail below.  
       [0006] The present invention relates to FATP family members from prokaryotes and eukaryotes, nucleic acids (DNA, RNA) encoding FATPs, and nucleic acids which are useful as probes or primers (e.g., for use in hybridization methods, amplification methods) for example, in methods of detecting FATP-encoding genes, producing FATPs, and purifying or isolating FATP-encoding DNA or RNA. Also the subject of this invention are antibodies (polyclonal or monoclonal) which bind an FATP or FATPs; methods of identifying additional FATP family members (for example, orthologs of those FATPs described herein by amino acid sequence) and variant alleles of known FATP genes; methods of identifying compounds which bind to an FATP, or modulate or alter (enhance or inhibit) FATP function; compounds which modulate or alter FATP function; methods of modulating or altering (enhancing or inhibiting) FATP function and, thus, LCFA uptake into tissues of a mammal (e.g. human) by administering a compound or molecule (a drug or agent) which increases or reduces FATP activity; and methods of targeting compounds to tissues by administering a complex of the compound to be targeted to tissues and a component which is bound by an FATP present on cells of the tissues to which the compound is to be targeted. For example, a complex of a drug to be delivered to the liver and a component which is bound by an FATP present on liver cells (e.g., FATP5) can be administered.  
       [0007] In one embodiment, the present invention relates to modulating or altering (enhancing or inhibiting/reducing) LCFA uptake in the small intestine and, thus, increasing or reducing the number of calories in the form of fats available to an individual. In another embodiment, the present invention relates to inhibiting or reducing LCFA uptake in the small intestine in order to reduce circulating fatty acid levels; that is, LCFA uptake in the small intestine is reduced and, therefore, circulating (blood) levels are not as high as they otherwise would be. FATP4 has been shown to be expressed in epithelial cells of the small intestine and particularly in the brush border layer of the small intestine. FATP2 has also been shown to be expressed at low levels in epithelial cells of the small intestine, particularly in the duodenum. In contrast, FATP1, FATP3, FATP5 and FATP6 were not detected in any of the intestinal tissues. Thus, also described herein are FATPs which are present in the epithelial cell layer of the small intestine where they mediate LCFA uptake. These FATPs, particularly FATP4 and also FATP2, are targets for methods and drugs which block their function or activity and are useful in treating obesity, diabetes and heart disease. The ability of these FATPs to mediate fat uptake can be modulated or altered (enhanced or inhibited), thus modulating fat uptake in the small intestine. This can be done, for example, by administering to an individual, such as a human or other animal, a drug which blocks interaction of LCFAs with FATP4 and/or FATP2 in the small intestine, thus inhibiting LCFA passage into the cells of the small intestine. As a result, fat absorption is reduced and, although the individual has consumed a certain quantity of fat, the LCFAs are not absorbed to the same extent they would have been in the absence of the compound administered.  
       [0008] Thus, one embodiment of this invention is a method of reducing LCFA uptake (absorption) in the small intestine and, as a result, reducing caloric uptake in the form of fat. A further embodiment is a compound (drug) useful in inhibiting or reducing fat absorption in the small intestine. In another embodiment, the invention is a method of reducing circulating fatty acid levels by administering to an individual a compound which blocks interactions of LCFAs with FATP4 and/or FATP2 in the small intestine, thus inhibiting LCFA passage into cells of the small intestine. As a result, fatty acids pass into the circulatory system at a diminished level and/or rate, and circulating fatty acid levels are lower than they would be in the absence of the compound administered. This method is particularly useful for therapy in individuals who are at risk for or have hyperlipidemia. That is, it can be used to prevent the occurrence of elevated levels of lipids in the blood or to treat an individual in whom blood lipid levels are elevated. Also the subject of this invention is a method of identifying compounds which alter FATP function (and thus, in the case of FATP2 and/or FATP4, alter LCFA uptake in the small intestine).  
       [0009] In another embodiment, the present invention relates to a method of modulating or altering (enhancing or inhibiting) the function of FATP6, which is expressed at high levels in the heart. A method of inhibiting FATP6 function is useful, for example, in individuals with heart disease, such as ischemia, since reducing LCFA uptake into heart muscle in an individual who has ischemic heart disease, which may be manifested by, for example, angina or heart attack, can reduce symptoms or reduce the extent of damage caused by the ischemia. In this embodiment, a drug which inhibits FATP6 function is administered to an individual who has had or is having a heart attack, to reduce LCFA uptake by the individual&#39;s heart and, as a result, reduce the damage caused by ischemia. In a further embodiment, this invention is a method of targeting a compound, such as a therapeutic drug or an imaging reagent, to heart tissue by administering to an individual (e.g., a human) a complex of the compound and a component (e.g., a LCFA or LCFA-like compound) which is bound by an FATP (e.g., FATP6) present in cells of heart tissue.  
       [0010] In a further embodiment, LCFA uptake by the liver is modulated or altered (enhanced or reduced), in an individual. For example, a drug which inhibits the function of an FATP present in liver (e.g., FATP5) is administered to an individual who is diabetic, in order to reduce LCFA uptake by liver cells and, thus reduce insulin resistance.  
       [0011] The present invention, thus, provides methods which are useful to alter, particularly reduce, LCFA uptake in individuals and, as a result, to alter (particularly reduce), availability of the LCFAs for further metabolism. In a specific embodiment, the present invention provides methods useful to reduce LCFA uptake and, thus, fatty acid metabolism in individuals, with the result that caloric availability from fats is reduced, and circulating fatty acid levels are lower than they otherwise would be. These methods are useful, for example, as a means of weight control in individuals, (e.g., humans) and as a means of preventing elevated serum lipid levels or reducing serum lipid levels in humans. FATPs expressed in the small intestine, such as FATP4, are useful targets to be blocked in treating obesity (e.g., chronic obesity) or to be enhanced in treating conditions in which enhanced LCFA uptake is desired (e.g., malabsorption syndrome or other wasting conditions).  
       [0012] The identification of this evolutionarily conserved fatty acid transporter family will allow a better understanding of the mechanisms whereby LCFAs traverse the lipid bilayer as well as yield insight into the control of energy homeostasis and its dysregulation in diseases such as diabetes and obesity. 
     
    
    
     BRIEF DESCRIPTION OF THE DRAWINGS  
     [0013] The file of this patent contains at least one color photograph. Copies of this patent with color photographs will be provided by the Patent and Trademark Office upon request and payment of necessary fee.  
     [0014]FIG. 1 shows the amino acid sequence alignment of FATPs: mmFATP1 (SEQ ID NO:92), mmFATP2 (SEQ ID NO:93), mmFATP3 (SEQ ID NO:94), mmFATP4 (SEQ ID NO:95), mmFATP5 (SEQ ID NO:96), ceFATPa (SEQ ID NO:97), scFATP (SEQ ID NO:98) and mtFATP (SEQ ID NO:99). The underlining (amino acid residues 204-212 of mtFATP) indicates an AMP binding motif which is found in many classes of proteins; the underlining at amino acid residues 204-507 of the mtFATP sequence indicates the FATP 360 amino acid signature sequence.  
     [0015] FIGS.  2 A- 2 D show results of LCFA uptake assays. FIGS.  2 A- 2 D: COS cells were cotransfected using the DEAE-dextran method with the mammalian expression vectors pCDNA-CD2 either alone (control; FIG. 2A) or in combination with one of the FATP-containing expression vectors (pCDNA-mmFATP1, FIG. 2B; pCDNA-mmFATP2, FIG. 2C; or pCMV-SPORT2-mmFATP5, FIG. 2D) as described in Materials and Methods for Example 2. COS cells were gated on forward scatter (FSC) and side scatter (SS), and the results shown represent &gt;10,000 cells. Cells exhibiting &gt;300 CD2 fluorescence units (vertical line) representing 15% of all cells were deemed CD2 positive.  
     [0016]FIG. 3 is a graph of fluorescence of cells expressing a FATP gene. As in FIGS.  2 A- 2 D, COS cells were cotransfected with pCDNA-CD2 either alone (control) or in combination with one of the FATP-containing expression vectors (pCDNA-mmFATP1, pCDNA-mmFATP2, pCMV-SPORT2-mmFATP5, or pCDNA-ceFATPb). The mean BODIPY-FA fluorescence of the CD2-positive cells is plotted; results shown represent the average of three experiments, each consisting of greater than 50,000 COS cells. Note that a logarithmic scale is used on the ordinate.  
     [0017]FIG. 4 is a graph of the uptake of palmitate with time. The full-length coding region of mtFATP (squares) or a control protein (TFE3; circles) was subcloned into the inducible, prokaryotic expression vector pET (Novagen, Madison, Wis.). Expression from the resulting plasmid was induced (solid symbols) in transformed  E. coli  cells with 1 mM isopropyl-β-D-thiogalactoside (IPTG) for 1 hour, or cells were left uninduced (open symbols). Data points were done in triplicate and counts were normalized to the number of bacteria as determined by OD 600 .  
     [0018]FIG. 5 is a phylogenetic tree produced by aligning complete and partial sequences for FATP genes from human, rat, mouse, puffer fish,  D. melanogaster, C. elegans, S. cerevisiae , and  M. tuberculosis  using ClustalX and using these data to produce a phylogenetic tree using TreeViewPPC. The bar indicates the number of substitutions per residue, i.e., 0.1 corresponds to a distance of 10 substitutions per 100 residues.  
     [0019]FIG. 6 shows a comparison of the FATP signature sequences of mmFATP1 (SEQ ID NO:1), mmFATP5, (SEQ ID NO:2), ceFATPa (SEQ ID NO:3), scFATP (SEQ ID NO:4) and mtFATP (SEQ ID NO:5).  
     [0020]FIG. 7 shows the sequence identity among the FATP family members and VLACs, based on the 360 amino acid signature sequence of FATP from FIG. 1.  
     [0021]FIGS. 8A and 8B are the mmFATP3 DNA sequence (SEQ ID NO:6).  
     [0022]FIG. 9 is the mmFATP3 protein sequence (SEQ ID NO:7).  
     [0023]FIGS. 10A and 10B are the mmFATP4 DNA sequence (SEQ ID NO:8).  
     [0024]FIG. 11 is the mmFATP4 protein sequence (SEQ ID NO:9).  
     [0025]FIGS. 12A and 12B are the mmFATP5 DNA sequence (SEQ ID NO:10).  
     [0026]FIG. 13 is the mmFATP5 protein sequence (SEQ ID NO:11).  
     [0027]FIGS. 14A and 14B are the hsFATP2 DNA sequence (SEQ ID NO:12).  
     [0028]FIG. 15 is the hsFATP2 protein sequence (SEQ ID NO:13).  
     [0029]FIGS. 16A and 16B are the hsFATP3 DNA sequence (SEQ ID NO:14).  
     [0030]FIG. 17 is the hsFATP3 protein sequence (SEQ ID NO:15).  
     [0031]FIGS. 18A and 18B are the hsFATP4 DNA sequence (SEQ ID NO:16).  
     [0032]FIG. 19 is the hsFATP4 protein sequence (SEQ ID NO:17).  
     [0033]FIGS. 20A and 20B are the hsFATP5 DNA sequence (SEQ ID NO:18).  
     [0034]FIG. 21 is the hsFATP5 protein sequence (SEQ ID NO:19).  
     [0035]FIGS. 22A and 22B are the hsFATP6 DNA sequence (SEQ ID NO:20).  
     [0036]FIG. 23 is the hsFATP6 protein sequence (SEQ ID NO:21).  
     [0037]FIGS. 24A and 24B are the mtFATP DNA sequence (SEQ ID NO:22).  
     [0038]FIG. 25 is the mtFATP protein sequence (SEQ ID NO:23).  
     [0039]FIG. 26 shows the DNA sequence (SEQ ID NO:24) and predicted amino acid sequence (SEQ ID NO:25) of human FATP1.  
     [0040]FIG. 27 shows the DNA sequence (SEQ ID NO:26) and predicted amino acid sequence (SEQ ID NO:27) of human FATP4.  
     [0041]FIG. 28A is a hydrophobicity plot for hsFATP1, showing that it has multiple membrane-spanning domains.  
     [0042]FIG. 28B is the amino acid composition of hsFATP1.  
     [0043]FIG. 28C is a hydrophilicity plot for hsFATP 1, made using the Kyte-Doolittle method, averaging hydrophilicity values for 18 amino acid residues at a time.  
     [0044]FIG. 29A is a hydrophobicity plot for hsFATP4, showing that it has multiple membrane-spanning domains.  
     [0045]FIG. 29B is a listing of the amino acid composition of hsFATP4.  
     [0046]FIG. 29C is a hydrophilicity plot for hsFATP4, made using the Kyte-Doolittle method, averaging hydrophilicity values for 18 amino acid residues at a time.  
     [0047]FIGS. 30A and 30B show a comparison of the nucleotide sequence of human FATP1 (SEQ ID NO:28) and the nucleotide sequence of mouse FATP1 (SEQ ID NO:29).  
     [0048]FIGS. 31A and 31B show a comparison of the nucleotide sequence of human FATP4 (SEQ ID NO:30) and the nucleotide sequence of mouse FATP4 (SEQ ID NO:31).  
     [0049]FIG. 32 shows a comparison of the amino acid sequence of human FATP1 (SEQ ID NO:32) and the amino acid sequence of mouse FATP1 (SEQ ID NO:33). Shaded amino acid residues match the consensus sequence exactly.  
     [0050]FIG. 33 shows a comparison at the amino acid level of human FATP4 (SEQ ID NO:34) and mouse FATP4 (SEQ ID NO:35). Shaded amino acid residues match the consensus sequence exactly.  
     [0051]FIG. 34 shows the nucleotide sequence (SEQ ID NO:36) and predicted amino acid sequence (SEQ ID NO:37) of hsFATP6.  
     [0052]FIG. 35A is a hydrophobicity plot for hsFATP6, showing that it has multiple membrane-spanning domains.  
     [0053]FIG. 35B is a listing of the amino acid composition of hsFATP6.  
     [0054]FIG. 35C is a hydrophilicity plot for hsFATP6, made using the Kyte-Doolittle method, averaging hydrophilicity values for 18 amino acid residues at a time.  
     [0055]FIG. 36 shows an alignment of the amino acid sequences of hsFATP1 (SEQ ID NO:38), hsFATP4 (SEQ ID NO:39) and hsFATP6 (SEQ ID NO:40). Shaded amino acid residues match the consensus sequence exactly.  
     [0056]FIG. 37 shows results of assessment of fatty acid uptake by human FATP1 and human FATP4. The percent of CD2-positive cells exhibiting a BODIPY-fluorescence of more than 300 arbitrary units is plotted for the three different conditions tested.  
     [0057]FIG. 38 is a graph showing uptake of tritiated oleate, with time, by 293 cells transfected with either (diamonds) a plasmid for expression of human FATP4 or (squares) a control plasmid.  
     [0058]FIG. 39 is an illustration of the amino acid sequences of human FATP4 (SEQ ID NO:41) and mouse FATP4 (SEQ ID NO:42) compared to human FATP1 (SEQ ID NO:43). Shown by underlining are the FATP consensus sequence (236-556 of hsFATP1) and the AMP-binding motif (246-254 of hsFATP1). The human FATPs were cloned by screening libraries with sequences from ESTs (expressed sequence tags). Mouse FATP4 was cloned by PCR using degenerate primers.  
     [0059]FIG. 40 is a graph showing the uptake, with time, of tritiated oleate by mouse enterocytes in the presence of no oligonucleotide (squares), sense oligonucleotide (circles) or antisense oligonucleotide (diamonds).  
     [0060]FIG. 41 is a bar graph showing uptake of tritiated oleate, by mouse enterocytes in the presence of various concentrations of antisense (solid bars), mismatch (stippled bars) or sense (lined bars) oligonucleotides.  
     [0061]FIG. 42 is a bar graph showing uptake of tritiated oleate and uptake of  35 S-labeled methionine by mouse enterocytes to which were added no oligonucleotide, the antisense oligonucleotide, or the mismatch oligonucleotide.  
     [0062]FIG. 43A is the nucleotide sequence of the gene encoding mouse FATP4 (SEQ ID NO:44).  
     [0063]FIG. 43B is the amino acid sequence of mouse FATP4 protein (SEQ ID NO:45).  
     [0064]FIGS. 44A, 44B, and  44 C are the hsFATP1 DNA sequence (SEQ ID NO:46). Coding region: 175-2115 (1941 nt).  
     [0065]FIG. 45 is the hsFATP1 protein sequence (SEQ ID NO:47).  
     [0066]FIGS. 46A and 46B are the hsFATP2 DNA sequence (SEQ ID NO:48). Coding region: 223-2085 (1863 nt).  
     [0067]FIG. 47 is the hsFATP2 protein sequence (SEQ ID NO:49).  
     [0068]FIG. 48 is the partial DNA sequence of hsFATP3 (SEQ ID NO:50). Coding region: 1-993.  
     [0069]FIG. 49 is the partial protein sequence of hsFATP3 (SEQ ID NO:51).  
     [0070]FIGS. 50A, 50B, and  50 C are the hsFATP4 DNA sequence (SEQ ID NO:52). Coding region: 208-2139 (1932 nt).  
     [0071]FIG. 51 is the hsFATP4 protein sequence (SEQ ID NO:53).  
     [0072]FIG. 52 is the hsFATP5 partial DNA sequence (SEQ ID NO:54). Coding region: 1-1062.  
     [0073]FIG. 53 is the hsFATP5 partial protein sequence (SEQ ID NO:55).  
     [0074]FIGS. 54A, 54B, and  54 C are the hsFATP6 DNA sequence (SEQ ID NO:56). Coding region: 643-2502 (1860 nt).  
     [0075]FIG. 55 is the hsFATP6 protein sequence (SEQ ID NO:57).  
     [0076]FIGS. 56A, 56B, and  56 C are the rnFATP1 DNA sequence (rn= Rattus norvegicus ; (SEQ ID NO:58). Coding region: 75-2015 (1941 nt).  
     [0077]FIG. 57 is the rnFATP1 protein sequence (SEQ ID NO:59).  
     [0078]FIGS. 58A, 58B, and  58 C are the rnFATP2 DNA sequence (SEQ ID NO:60). Coding region: 795-2657 (1863 nt).  
     [0079]FIG. 59 is the rnFATP2 protein sequence (SEQ ID NO:61).  
     [0080]FIGS. 60A and 60B are the mFATP4 partial DNA sequence (SEQ ID NO:62). Coding region: 1-1218.  
     [0081]FIG. 61 is the rnFATP4 partial DNA sequence (SEQ ID NO:63).  
     [0082]FIGS. 62A, 62B, and  62 C are the mmFATP1 DNA sequence (SEQ ID NO:64). Coding region: 1-1944.  
     [0083]FIG. 63 is the mmFATP1 protein sequence (SEQ ID NO:65).  
     [0084]FIGS. 64A and 64B are the mmFATP2 DNA sequence (SEQ ID NO:66). Coding region: 121-1992 (1872 nt).  
     [0085]FIG. 65 is the mmFATP2 protein sequence (SEQ ID NO:67).  
     [0086]FIGS. 66A and 66B are the mmFATP3 partial DNA sequence (SEQ ID NO:68). Coding region: 1-1830.  
     [0087]FIG. 67 is the mmFATP3 partial protein sequence (SEQ ID NO:69).  
     [0088]FIGS. 68A, 68B, and  68 C are the mmFATP4 DNA sequence (SEQ ID NO:70). Coding region: 1-1932.  
     [0089]FIG. 69 is the mmFATP4 protein sequence (SEQ ID NO:71).  
     [0090]FIGS. 70A and 70B are the mmFATP5 DNA sequence (SEQ ID NO:72). Coding region: 60-2129.  
     [0091]FIG. 71 is the mmFATP5 protein sequence (SEQ ID NO:73).  
     [0092]FIGS. 72A and 72B are the dmFATP partial DNA sequence (dm= Drosophila melanogaster ; SEQ ID NO:74). Coding region: 1-1773.  
     [0093]FIG. 73 is the dmFATP partial protein sequence (SEQ ID NO:75).  
     [0094]FIG. 74 is the drFATP partial DNA sequence (dr= Danio rerio , zebrafish; SEQ ID NO:76) Coding region: 1-173.  
     [0095]FIG. 75 is the drFATP partial protein sequence (SEQ ID NO:77).  
     [0096]FIGS. 76A and 76B are the ceFATPa DNA sequence (SEQ ID NO:78). Coding region: 1-1953.  
     [0097]FIG. 77 is the ceFATPa protein sequence (SEQ ID NO:79).  
     [0098]FIGS. 78A and 78B are the ceFATPb DNA sequence (SEQ ID NO:80). Coding region: 1-1968.  
     [0099]FIG. 79 is the ceFATPb protein sequence (SEQ ID NO:81).  
     [0100]FIGS. 80A and 80B are the chFATP DNA sequence (SEQ ID NO:82; ch= Cochliobolu heterostrophus ). Coding region: 1-1932.  
     [0101]FIG. 81 is the chFATP protein sequence (SEQ ID NO:83).  
     [0102]FIG. 82 is the anFATP partial protein sequence (an= Aspergillus nidulans ; SEQ ID NO:84). Coding region: 1-597.  
     [0103]FIG. 83 is the anFATP partial protein sequence (SEQ ID NO:85).  
     [0104]FIG. 84 is the mgFATP partial DNA sequence (mg= Magnaporthe grisea , rice blast; SEQ ID NO:86). Coding region: 1-522.  
     [0105]FIG. 85 is the mgFATP partial protein sequence (SEQ ID NO:87).  
     [0106]FIGS. 86A and 86B are the scFATP DNA sequence (SEQ ID NO:88). Coding region: 1-1872.  
     [0107]FIG. 87 is the scFATP protein sequence (SEQ ID NO:89).  
     [0108]FIGS. 88A and 88B are the mtFATP DNA sequence (SEQ ID NO:90).  
     [0109]FIG. 89 is the mtFATP protein sequence (SEQ ID NO:91). Coding region: 1-1794.  
     [0110]FIG. 90 is a consensus sequence of the FATP signature sequence (SEQ ID NO:100), based on 23 independent sequences aligned in ClustalX. The height of the bar at each amino acid residue position indicates the degree of conservation at that position. Gaps have been inserted to maintain the strength of the alignment.  
     [0111]FIG. 91 is a hydrophilicity plot for hsFATP2, made using the Kyte-Doolittle method, averaging hydrophilicity values for 18 amino acid residues at a time.  
     [0112]FIG. 92 is a hydrophilicity plot for the hsFATP3 partial protein, made using the Kyte-Doolittle method, averaging hydrophilicity values for 18 amino acid residues at a time.  
     [0113]FIG. 93 is a hydrophilicity plot for the hsFATP5 partial protein, made using the Kyte-Doolittle method, averaging hydrophilicity values for 18 amino acid residues at a time.  
     [0114]FIGS. 94A and 94B are a representation of the DNA sequence (SEQ ID NO:101) of the hsFATP3 gene, and the amino acid sequence (SEQ ID NO:102) of the hsFATP3 protein.  
     [0115]FIG. 95 shows that mammalian expression constructs containing either hsFATP4 (squares and triangles) or empty control vector (circles) were stably transfected into 293 cells. Short-term uptake of Bodipy-FA in the presence of BSA was determined by FACS. The mean fluorescence of the viable cell population is expressed in arbitrary fluorescence units. FATP4 protein expression was determined by densitometry of anti-FATP4 Western blots, and is expressed in arbitrary units.  
     [0116]FIG. 96 is a bar graph illustrating short-term uptake of Bodipy-palmitate (1 μM), either by control cells (black bars) or FATP4-expressing cells (hatched bars), was measured in the presence of 0, 10, 100 μM unlabeled palmitate. FA uptake was quantified by FACS and expressed in arbitrary fluorescence units.  
     [0117]FIG. 97 shows the rate of [ 2 H]palmitate uptake by 293 cells, which were stably transfected with a construct for either human FATP4 (diamonds) or an empty vector (circles), compared to that of isolated enterocytes (squares).  
     [0118]FIG. 98 is a bar graph illustrating the results when isolated enterocytes were incubated for 48 h with increasing concentrations of the FATP4 antisense oligonucleotide or with 100 μM of a randomized control oligonucleotide with identical nucleotide composition to the FATP4 antisense oligonucleotide. The uptake of oleate by the enterocytes was then measured over a 5 min time interval (solid bars). In parallel, the levels of FATP4 protein and, as a loading control, β-catenin, were determined by Western blotting and quantitated using densitometry (hatched bars). FA uptake and FATP4 protein levels were normalized to that of untreated cells. The averages and standard deviations of 4 independent experiments are shown.  
     [0119]FIG. 99 is a bar graph illustrating the uptake rates of [ 3 H]oleate, [ 3 H]palmitate and [ 35 S]methionine by primary enterocytes were measured after 48 h incubation with either 100 μM FATP4 antisense (solid bars) or 100 μM randomized control oligonucleotide (hatched bars) and expressed as % of untreated cells.  
     [0120]FIG. 100 is a bar graph illustrating that 8 kb of FATP5 genomic sequence SEQ ID NO.: 106 is sufficient for liver specific transcription in vitro. A luciferase reporter construct containing 8 kb upstream of the FATP5 initiator methionine was transfected into various cell lines using calcium phosphate as described in Example 17. Forty-eight hours after transfection, luciferase activity was measured and normalized to β-galactosidase activity. For each cell line, fold induction was determined by dividing the relative luciferase activity of the 8 kb construct by that of the promoter-less luciferase reporter vector. The data shown represent the mean of three experiments done in triplicate. Error bars indicate the SEM.  
     [0121]FIG. 101 is a bar graph illustrating deletion analysis of the FATP5 promoter. Constructs containing deletions of the FATP5 promoter were transfected into HepG2 cells, assayed for luciferase activity, and normalized to β-galactosidase (RLU). The labels on the vertical axis correspond to the length of the promoter segment as measured from the initiator methionine. The data shown represents the mean of three experiments done in triplicate. Error bars indicate the SEM.  
     [0122]FIG. 102 is a bar graph illustrating that 271 base pairs upstream of the FATP5 initiator methionine are sufficient for liver specific luciferase activity. A luciferase reporter construct containing 271 base pairs upstream of the FATP5 initiator methionine was transfected into various cell lines using calcium phosphate as described in Methods Example 17. Forty eight hours after transfection, luciferase activity was measured and normalized to β-galactosidase activity. For each cell line, fold induction was determined by dividing the relative luciferase activity of the −271 base pair construct by that of the promoter-less luciferase reporter vector. The data shown represent the mean of three experiments done in triplicate. Error bars indicate the SEM.  
     [0123]FIGS. 103A and 103B illustrate mutations of the GC box which abolish transcriptional activity. A: Schematic of mutations in the GC box aligned with the normal sequence (SEQ ID NO.: 106, SEQ ID NO.: 107, SEQ ID NO.: 108). The GC box consensus sequence is underlined. B: Constructs containing 271 base pairs upstream of the FATP5 initiator methionine with the mutations in the GC box depicted in part A were transfected into HepG2 cells, assayed for luciferase activity, and normalized to -galactosidase (RLU). The data shown represent the mean of three experiments done in triplicate. Error bars indicate the SEM.  
     [0124]FIG. 104 shows a gel shift analysis of the GC box with HepG2 nuclear extracts. Schematic showing the sequence of the oligonucleotides used in gel shift studies. The numbering reflects the distance from the initiator methionine. The two pairs of oligonucleotides are indicated by the lines and labeled AF-1 (SEQ ID NO.: 111, SEQ ID NO.: 112) and AF-2 (SEQ ID NO.: 109, SEQ ID NO.: 110).  
     [0125]FIG. 105 is a bar graph illustrating that 30 bp internal deletions of the FATP5 promoter identify another region required for luciferase activity in HepG2 cells. Reporter constructs were transfected into HepG2 cells. Luciferase activity was measured and normalized to β-galactosidase activity (RLU). The labels on the horizontal axis correspond to the nucleotides that were deleted and the numbering on the vertical axis represents the distance from the initiator methionine. The data shown represent the mean of three experiments done in triplicate. Error bars indicate the SEM. Note that the five fold higher RLU activity in this figure relative to FIGS. 101 and 103 is the result of a manufacturer change in the β-galactosidase reagent.  
     [0126]FIG. 106 is a bar graph illustrating that a linker scan of the FATP5 promoter identifies two additional elements required for transcription in HepG2 cells. Reporter constructs were transfected into HepG2 cells. Luciferase activity was measured and normalized to β-galactosidase activity (RLU). The labels on the horizontal axis correspond to the constructs in part A. The data shown represent the mean of three experiments done in triplicate. Error bars indicate the SEM. Please note that the lower RLU activity in this figure relative to FIGS. 101 and 103 is also the result of a manufacturer change in the β-galactosidase reagent.  
     [0127]FIG. 107 is a schematic of the FATP5 promoter (SEQ ID NO.: 113). The GC box and two motifs identified in the linker scan are boxed and labeled. An arrow indicates the translational initiator of the FATP5 protein. The two halves of the palindrome contained in the novel motifs and referred to in the discussion are underlined.  
     [0128]FIG. 108 is a photograph showing FATP2 expression in the mouse gall bladder epithelium.  
     [0129]FIG. 109 is a photograph showing FATP2 expression in chimpanzee liver.  
     [0130]FIG. 110 is a photograph showing FATP5 expression in chimpanzee liver.  
     [0131]FIGS. 111A and 111B represent the DNA sequence (SEQ ID NO:116) of human FATP3.  
     [0132]FIG. 112 represents the amino acid sequence (SEQ ID NO:1 17) of human FATP3.  
     [0133]FIG. 113 is a bar graph showing the results of an experiment comparing fatty acid transport between cells transfected with SEQ ID NO:116 and untransfected cells.  
     [0134]FIGS. 114A, 114B,  114 C and  114 D represent portions of the amino acid sequence of mmFATP4 which were produced as fusion polypeptides in  E. coli  cells.  
     [0135]FIG. 115 is a schematic illustrating certain components of the fusion polypeptides depicted in FIGS.  114 A-D. The schematic shows the lipocalin domain as well as other identified motifs and notes the relative location of each in the mmFATP4 fusion polypeptide.  
     [0136]FIG. 116 is a bar graph illustrating the results of an experiment comparing the binding capabilities of the fusion polypeptides shown in FIGS.  114 A-D for an oleate fatty acid.  
     [0137]FIG. 117 is a bar graph showing the results of an experiment comparing binding of various fatty acids between two of the fusion polypeptides depicted in FIGS.  114 A-D.  
     [0138] FIGS.  118 A-G illustrates the consensus sequence of hsFATP1, hsFATP2, hsFATP3, hsFATP4, hsFATP5 and hsFATP6 with the lipocalin domain and AMP-binding domain of each noted. 
    
    
     [0139] The foregoing and other objects, features and advantages of the invention will be apparent from the following more particular description of preferred embodiments of the invention, as illustrated in the accompanying drawings in which like reference characters refer to the same parts throughout the different views. The drawings are not necessarily to scale, emphasis instead being placed upon illustrating the principles of the invention.  
     DETAILED DESCRIPTION OF THE INVENTION  
     [0140] As described herein, FATPs are a large evolutionarily conserved family of proteins that mediate the transport of LCFAs into cells. The family includes proteins which are conserved from mycobacteria to humans and exhibit very different expression patterns in tissues. Specific embodiments described include FATPs from mice, humans, nematodes, fungi and mycobacteria which have been shown to be functional LCFA transporters. The term “fatty acid transport proteins” (“FATPs”) as used herein, refers to the proteins described herein as FATP1, FATP2, FATP3, FATP4, FATP5 and FATP6, which have been described in one or more species of mammals, as well as mtFATP, ceFATP, scFATP, anFATP, mgFATP, and chFATP, and other proteins sharing at least about 50% amino acid sequence similarity, preferably at least about 60% sequence similarity, more preferably at least about 70% sequence similarity, and still more preferably, at least about 80% sequence similarity, and most preferably, at least about 90% sequence similarity in the approximately 360 amino acid signature sequence. The approximately 360 amino acid FATP signature sequence is shown in FIG. 1. The consensus sequence of the signature sequence is shown in FIG. 90. The nomenclature used herein to refer to FATPs includes a species-specific prefix (e.g., mm,  Mus musculus ; hs or h,  Homo sapiens  or human; mt  M. tuberculosis ; dm,  D. melanogaster ; ce,  C. elegans ; sc,  Saccharomyces cerevisiae ) and a number such that mammalian homologues in different species share the same number. For example, six human and five mouse FATP genes which are expressed in a variety of tissues are described herein and are referred to, respectively, as hsFATP1-hsFATP6 and mmFATP1-mmFATP5; for example, hsFATP4 and mmFATP4 are the human and mouse orthologs.  
     [0141] Expression patterns of human and mouse FATPs have been assessed and are described below. Briefly, results of these assessments show that FATP5 is a liver-specific gene. FATP2 is highly expressed in liver, kidney and gall bladder epithelium. Both of these proteins, as well as FATP4 and FATPs from nematodes and mycobacteria, have been shown to be functional LCFA transporters. Results have also shown that FATP4 mRNA is present at high levels in epithelial cells of two regions of the small intestine (the jejunum and ileum) and at lower, but significant, levels in a third region (the duodenum). They further showed that FATP2 mRNA is present in epithelial cells of the duodenum at a level similar to that of FATP4 mRNA levels, but is present at lower levels in the jejunum and ileum. FATP4 mRNA was absent from other cell types of the small intestine and no FATP4 mRNA could be detected in any cells of the colon. No signals above background could be detected for FATP 1, FATP3 and FATP5 in any of the intestinal tissues. Thus, FATP4 is the major FATP in the mouse small intestine, which supports a major role for FATP4 (along with FATP2 to a lesser extent) in absorption of free fatty acids. hsFATP4 was clearly expressed in the jejunum and ileum; expression was absent in the stomach. This, too, is consistent with a major role for FATP4 in absorption of fatty acids in the human gut. Analysis of FATP expression in human tissues, also described in detail below, showed that hsFATP6, which has no mouse ortholog as yet, is expressed at high levels in the heart and at low levels in the placenta, but is undetectable in the other tissues assessed (Example 9). This is consistent with a major role for FATP6 in absorption of fatty acids in the heart.  
     [0142] Analysis of FATP3 expression in murine tissues, also described in detail below, showed that expression occurs at detectable levels in liver, spleen, heart, kidney, testis, white adipose tissue, exocrine and endocrine pancreatic cells, and also in lung tissues. FATP3 is expressed at high levels in type-II pneumocytes, a cell type noted for secretion a surfactant, a phospholipid-rich film critical for lung function (Example 19).  
     [0143] Long chain fatty acids (LCFAs) are an important energy source for pro- and eukaryotes and are involved in diverse cellular processes, such as membrane synthesis, intracellular signaling, protein modification, and transcriptional regulation. In developed Western countries, human dietary lipids are mainly di- and triglycerides and account for approximately 40% of caloric intake (Weisburger, J. H. (1997)  J. Am. Diet. Assoc.  97:S16-S23). These lipids are broken down into fatty acids and glycerol by pancreatic lipases in the small intestine (Chapus, C., Rovery, M., Sarda, L &amp; Verger, R. (1988)  Biochimie  70:1223-34); LCFAs are then transported into brush border cells, where the majority is re-esterified and secreted into the lymphatic system as chylomicrons (Green, P. H. &amp; Riley, J. W. (1981)  Aust. N.Z.J. Med.  11:84-90). Fatty acids are liberated from lipoproteins by the enzyme lipoprotein lipase, which is bound to the luminal side of endothelial cells (Scow, R. O. &amp; Blachette-Mackie, E. J. (1992)  Mol. Cell. Biochem  116:181-191). “Free” fatty acids in the circulation are bound to serum albumin (Spector, A. A. (1984)  Clin. Physiol. Biochem  2:123-134) and are rapidly incorporated by adipocytes, hepatocytes, and cardiac muscle cells. The latter derive 60-90% of their energy through the oxidation of LCFAs (Neely, J. F. Rovetto, M. J. &amp; Oram, J. F. (1972)  Prog. Cardiovasc. Dis:  15:289-329). Although saturable and specific uptake of LCFAs has been demonstrated for intestinal cells, hepatocytes, cardiac myocytes, and adipocytes, the molecular mechanisms of LCFA transport across the plasma membrane have remained controversial (Hui, T. Y. &amp; Bernlohr, D. A. (1997)  Front. Biosci.  15:d222-3 1-d231; Schaffer, J. E. &amp; Lodish, H. F, (1995)  Trends Cardiovasc. Med.  5:218-224). Described herein is a large family of highly homologous mammalian LCFA transporters which show wide expression, including in all tissues relevant to fatty acid metabolism. Further described are novel members of this family in other species, including mycobacterial and nematode FATPs which, like their mammalian counterparts, are functional fatty acid transporters.  
     [0144] The discovery of a diverse but highly homologous family of FATPs is reminiscent of the glucose transporter family. In a manner similar to the FATPs, the glucose transporters have very divergent patterns of tissue expression (McGowan, K. M., Long, S. D. &amp; Pekala, P. H. (1995)  Pharmacol. Ther.  66:465-505). The FATPs, like glucose transporters, may also differ in their substrate specificities, uptake kinetics, and hormonal regulation (Thorens, B. (1996)  Am. J. Physiol.  270:G541-G553). Indeed, the levels of fatty acids in the blood, like those of glucose, can be regulated by insulin and are dysregulated in diseases such as noninsulin-dependent diabetes and obesity (Boden, G. (1997) Diabetes 46:3-10). The underlying mechanisms for the regulation of free fatty acid concentrations in the blood are not understood, but could be explained by hormonal modulation of FATPs.  
     [0145] Insulin-resistance is thought to be the major defect in non insulin-dependent diabetes mellitus (NIDDM) and is one of the earliest manifestations of NIDDM (McGarry (1992) Science 258:766-770). Free fatty acids (FFAs) may provide an explanation for why obesity is a risk factor for NIDDM. Plasma levels of FFAs are elevated in diabetic patients (Reaven et al. (1988)  Diabetes  37:1020). Elevated plasma free fatty acids (FFAs) have been demonstrated to induce insulin-resistance in whole animals and humans (Boden (1998)  Front. Biosci.  3:D169-D175). This insulin-resistance is likely mediated by effects of FFAs on a variety of issues. FFAs added to adipocytes in vitro induce insulin resistance in this cell type as evidenced by inhibition of insulin-induced glucose transport (Van Epps-Fung et al. (1997)  Endocrinology  138:4338-4345). Rats fed a high fat diet developed skeletal muscle insulin resistance as evidenced by a decrease in insulin-induced glucose uptake by skeletal muscle (Han et al., (1997)  Diabetes  46:1761-1767). In addition, elevated plasma FFAs increase insulin-suppressed endogenous glucose production in the liver (Boden (1998)  Front. Biosci.  3:D169-D175), thus increasing hepatic glucose output. It has been postulated that the adverse effects of plasma free fatty acids are due to the FFAs being taken up into the cell, leading to an increase in intracellular long chain fatty acyl .CoA; intracellular long chain acyl CoAs are thought to mediate the effects of FFAs inside the cell. Thus, fatty acid induced insulin-resistance may be prevented by blocking uptake of FFAs into select tissues, in particular liver (by blocking FATP2 and/or FATP5), adipocyte (by blocking FATP1), and skeletal muscle (by blocking FATP1). Blocking intestinal fat absorption (by blocking FATP4) is also expected to reduce plasma FFA levels and thus improve insulin resistance.  
     [0146] During the pathogenesis of NIDDM insulin-resistance can initially be counteracted by increasing insulin output by the pancreatic beta cell. Ultimately, this compensation fails, beta cell function decreases and overt diabetes results (McGarry (1992)  Science  258: 766-770). Manipulating beta cell function is a second point where fatty acid transporter blockers may be beneficial for diabetes. While no FATP homolog has been identified so far that is expressed in the beta cell of the pancreas, the data described below suggest the existence of such a transporter and the sequence information included herein provides the means to identify such a transporter by degenerate PCR, using primers to regions conserved in all FATP family members or by low stringency hybridization. It has been demonstrated that exposure of pancreatic beta-cells to FFAs increases the basal rate of insulin secretion; this in turn leads to a decrease in the intracellular stores of insulin, resulting in decreased capacity for insulin secretion after chronic exposure (Bollheimer et al., (1998)  J. Clin. Invest.  10 1:1094-1101). The effects of FFAs are again likely to be mediated by intracellular long chain fatty acyl CoA molecules (Liu et al., (1998)  J. Clin. Invest.  101:1870-1875). FFAs have also been demonstrated to increase beta cell apoptosis (Shimabukuro et al., (1998)  Proc. Nat. Acad. Sci. USA  95:2498-2502), possibly contributing to the decrease in beta cell numbers in late stage NIDDM.  
     [0147] Another finding with potentially broad implications is the identification of a FATP homologue in  M. tuberculosis . Tuberculosis causes more deaths. worldwide than any other infectious agent and drug-resistant tuberculosis is re-emerging as a problem in industrialized nations (Bloom, B. R. &amp; Small, P. M. (1998)  N. Engl. J. Med.  338:677-678).  Mycobacterium tuberculosis  has about 250 enzymes involved in fatty acid metabolism, compared with only about 50 in  E. coli . It has been suggested that, living as a pathogen, the mycobacteria are largely lipolytic, rather than lipogenic, relying on the lipids within mammalian cells and the tubercle (Cole, S. T. et al.,  Nature  393:537-544 (1998)). The de novo synthesis of fatty acids in  Mycobacterium leprae  is insufficient to maintain growth (Wheeler, P. R., Bulmer, K &amp; Ratledge, C. (1990)  J. Gene. Microbiol.  136:211-217). Thus, it is reasonable to expect that inhibitors of mtFATP will serve as therapeutics for tuberculosis. FATPs expressed in mycobacteria can be targeted to reduce or prevent replication of mycobacteria (e.g., to reduce or prevent replication of  M. tuberculosis ) and, thus, reduce or prevent their adverse effects. For example, a FATP or FATPs expressed by  M. tuberculosis  can be targeted and inhibited, thus reducing or preventing growth of this pathogen (and tuberculosis in humans and other mammals). An inhibitor of an  M. tuberculosis  FATP can be identified, using methods described herein (e.g., expressing the FATP in an appropriate host cell, such as  E. coli  or COS cells; contacting the cells with an agent or drug to be assessed for its ability to inhibit the FATP and, as a result, mycobacterial growth, and assessing its effects on growth). A drug or agent identified in this manner can be further tested for its ability to inhibit a  M. tuberculosis  FATP and  M. tuberculosis  infection in an appropriate animal model or in humans. A method of inhibiting mycobacterial growth, particularly growth of  M. tuberculosis , and compounds useful as drugs for doing so are also the subject of this invention.  
     [0148] An isolated polynucleotide encoding mtFATP, like other polynucleotides encoding FATPs of the FATP family, can be incorporated into vectors, nucleic acids of viruses, and other nucleic acid constructs that can be used in various types of host cells to produce mtFATP. This mtFATP can be used, as it appears on the surface of cells, or in various artificial membrane systems, to assess fatty acid transport function, to identify ligands and molecules that are modulators of fatty acid transport activity. Molecules found to be inhibitors of mtFATP function can be incorporated into pharmaceutical compositions to administer to a human for the treatment of tuberculosis.  
     [0149] Particular embodiments of the invention are polynucleotides encoding a FATP of  Cochliobolus  ( Helminthosporium )  heterostrophus  or portions or variants thereof, the isolated or recombinantly produced FATP, methods for assessing whether an agent binds to the chFATP, and further methods for assessing the effect of an agent being tested for its ability to modulate fatty acid transport activity.  Cochliobolus heterostrophus  is an ascomycete that is the cause of southern corn leaf blight, an economically important threat to the corn crop in the United States. The related species  C. sativus  causes crown rot and common root rot in wheat and barley. One or more FATPs of  C. heterostrophus  can be targeted for the identification of an inhibitor of chFATP function, which can be then be used as an agent effective against infection of plants by  C. heterostrophus  and related organisms. Methods described herein that were applied in studying the expression of a FATP gene and the function of the FATP in its natural site of expression or in a host cell, can be used in the study of the chFATP gene and protein.  
     [0150] Magnaporthe grisea  (rice blast) is an economically important fungal pathogen of rice. Further embodiments of the invention are nucleic acid molecules encoding a FATP of  Magnaporthe grisea , portions thereof, or variants thereof, isolated mgFATP, nucleic acid constructs, and engineered cells expressing mgFATP. Other aspects of the invention are assays to identify an agent which binds to mgFATP and assays to identify an agent which modulates the function of mgFATP in cells in which mgFATP is expressed or in artificial membrane systems. Agents identified as inhibiting mgFATP activity can be developed into anti-fungal agents to be used to treat rice infected with rice blast.  
     [0151] Caenorhabditis elegans  is a nematode related to plant pathogens and human parasites. An isolated polynucleotide which encodes ceFATP, like other polynucleotides encoding FATPs of the FATP family described herein, can be incorporated into nucleic acid vectors and other constructs that can be used in various types of cells to produce ceFATP. ceFATP as it occurs in cells or as it can be isolated or incorporated into various artificial or reconstructed membrane systems, can be used to assess fatty acid transport, and to identify ligands and agents that modulate fatty acid transport activity. Agents found by such assays to be inhibitors of ceFATP activity can be incorporated into compositions for the treatment of diseases caused by genetically related organisms with a FATP of similar sensitivity to the agents.  
     [0152] Aspergillus nidulans  is one of a family of fungal species that can infect humans. Further embodiments of the invention of the family of polynucleotides encoding FATPs are polynucleotides encoding a FATP of  Aspergillus nidulans , and vectors and host cells that can be constructed to comprise such polynucleotides. Further embodiments are a polypeptide encoded by such polynucleotides, portions thereof having one or more functions characteristic of a FATP, and various methods. The methods include those for identifying agents that bind to a FATP and those for assessing the effect of an agent being tested for its ability to modulate fatty acid transport activity. Those agents found to inhibit fatty acid transport function can be used in compositions as anti-fungal pharmaceuticals, or can be modified for greater effectiveness as a pharmaceutical.  
     [0153] One aspect of the invention relates to isolated nucleic acids that encode a FATP as described herein, such as those FATPs having an amino acid sequence in FIG. 45 (SEQ ID NO:47), FIG. 47 (SEQ ID NO:49), FIG. 112 (SEQ ID NO: 117), FIG. 51 (SEQ ID NO:53), FIG. 53 (SEQ ID NO:55), and FIG. 55 (SEQ ID NO:57) and nucleic acids closely related thereto as described herein.  
     [0154] Using the information provided herein, such as a nucleic acid sequence set forth in FIGS.  44 A- 44 C (SEQ ID NO:46), FIGS. 46A and 46B (SEQ ID NO:48), FIG. 112 (SEQ ID NO:116), FIGS.  50 A- 50 C (SEQ ID NO:52), FIG. 52 (SEQ ID NO:54), and FIGS.  54 A- 54 C (SEQ ID NO:56), a nucleic acid of the invention encoding a FATP polypeptide has been obtained using standard cloning and screening methods, such as those for cloning and sequencing cDNA library fragments, followed by obtaining a full length clone. For example, to obtain a nucleic acid of the invention, a library of clones of cDNA of human or other mammalian DNA can be probed with a labeled oligonucleotide, such as a radiolabeled oligonucleotide, preferably about 17 nucleotides or longer, derived from a partial sequence. Clones carrying DNA identical to that of the probe can then be distinguished using stringent (also, “high stringency”) hybridization conditions. By sequencing the individual clones thus identified with sequencing primers designed from the original sequence it is then possible to extend the sequence in both directions to determine the full length sequence. Suitable techniques are described, for example, in  Current Protocols in Molecular Biology  (F. M. Ausubel et al, eds), containing supplements through Supplement 42, 1998, John Wiley and Sons, Inc., especially chapters 5, 6 and 7.  
     [0155] Embodiments of the invention include isolated nucleic acid molecules comprising any of the following nucleotide sequences: 1.) a nucleotide sequence which encodes a protein comprising the amino acid sequence of hsFATP1 (SEQ ID NO:47), the amino acid sequence of hsFATP2 (SEQ ID NO:49), the amino acid sequence of hsFATP3 (SEQ ID NO:117), the amino acid sequence of hsFATP4 (SEQ ID NO: 53), the amino acid sequence of hsFATP5 (SEQ ID NO:55) or the amino acid sequence of hsFATP6 (SEQ ID NO:57); 2.) nucleotide sequences of hsFATP1, hsFATP2, hsFATP3, hsFATP4, hsFATP5, or hsFATP6 (SEQ ID NO:46, 48, 116, 52, 54, or 56, respectively); 3.) a nucleotide sequence which is complementary to the nucleotide sequence of hsFATP1 (SEQ ID NO:46), hsFATP2 (SEQ ID NO:48), hsFATP3 (SEQ ID NO:116), hsFATP4 (SEQ ID NO:52), hsFATP5 (SEQ ID NO:54) or hsFATP6 (SEQ ID NO:56); 4.) a nucleotide sequence which consists of the coding region of hsFATP1 (SEQ ID NO:46), the coding region of hsFATP2 (SEQ ID NO:48), the coding region of hsFATP3 (SEQ ID NO:116), the coding region of hsFATP4 (SEQ ID NO:52), the coding region of hsFATP5 (SEQ ID NO:54), or the coding region of hsFATP6 (SEQ ID NO:56).  
     [0156] The invention further relates to nucleic acids (nucleic acid molecules or polynucleotides) having nucleotide sequences identical over their entire length to those shown in the figures, for instance FIGS.  44 A- 44 C (SEQ ID NO:46), FIGS. 46A and 46B (SEQ ID NO:48), FIGS.  111 A-B (SEQ ID NO:116), FIGS.  50 A- 50 C (SEQ ID NO:52), FIG. 52 (SEQ ID NO:54), and FIGS.  54 A- 54 C (SEQ ID NO:56). It further relates to DNA, which due to the degeneracy of the genetic code, encodes a FATP encoded by one of the FATP-encoding DNAs, whose amino acid sequence is provided herein. Also provided by the invention are nucleic acids having the coding sequences for the mature polypeptides or fragments in reading frame with other coding sequences, such as those encoding a leader or secretory sequence, a pre-, or pro- or prepro-protein sequence. The nucleic acids of the invention encompass nucleic acids that include a single continuous region or discontinuous regions encoding the polypeptide, together with additional regions, that may also contain coding or non-coding sequences. The nucleic acids may also contain non-coding sequences, including, for example, but not limited to, non-coding 5′ and 3′ sequences, such as the transcribed, non-translated sequences, termination signals, ribosome binding sites, sequences that stabilize mRNA, introns, polyadenylation signals, and additional coding sequences which encode additional amino acids. For example, a marker sequence that facilitates purification of the fused polypeptide can be encoded. In certain embodiments of the invention, the marker sequence can be a hexa-histidine peptide, as provided in the pQE vector (Qiagen, Inc., Venlo, The Netherlands) and described in Gentz et al.,  Proc. Natl. Acad. Sci. USA  86: 821-824 (1989), or an HA tag (Wilson et al.,  Cell  37: 767 (1984)), or a sequence encoding glutathione S-transferase of  Schistosoma japonicum  (vectors available from Pharmacia; see Smith, D. B. and Johnson K. S.,  Gene  67:31 (1988) and Kaelin, W. G. et al.,  Cell  70:351 (1992)). Nucleic acids of the invention also include, but are not limited to, nucleic acids comprising a structural gene and its naturally associated sequences that control gene expression.  
     [0157] The invention further relates to nucleic acids (nucleic acid molecules or polynucleotides) that encode a FATP polypeptide. In a particular embodiment, a nucleic acid encodes a portion of a FATP which includes a motif or domain, for example, a lipocalin domain or an AMP-binding domain. Such a polypeptide portion can be a functional portion of a FATP protein. The term “lipocalin domain” is an art recognized term and as used herein refers to a particular domain present in FATP proteins. This domain is described as including regions of sequence homology as well as a common tertiary structure represented as an eight stranded antiparallel beta-barrel. (see Banaszak, L. et al.,  Advances in Protein Chemistry,  45: 89-151). Many lipocalin domains can be identified structurally as a sequence contained within the general formula: [DENG]-X-[DENQGSTARK]-X(0,2)-[DENQARK]-[LIVFY]-{CP}-G-{C}-W-[FYWLRH-X]-[LIVMTA], e.g., the lipocalin signature sequence or consensus pattern (SEQ ID NO: 125). One skilled in the art will recognize that a lipocalin domain for a particular FATP protein can vary in sequence from this general formula. A FATP lipocalin domain can be, for example, identical to the lipocalin signature sequence or can exhibit 60, 65, 70, 75, 80, 85, 90, 95 or greater per cent sequence identity compared to the general formula provided that it retains lipocalin binding function. For example, a lipocalin domain for each of the human FATPs, hsFATP   1   (SEQ ID NO:126), hsFATP2 (SEQ ID NO:127), hsFATP3 (SEQ ID NO:128), hsFATP4 (SEQ ID NO:129), hsFATP5 (SEQ ID NO: 130), and hsFATP6 (SEQ ID NO:131) has been identified. The pattern of these lipocalin domains are highly conserved across the FATP family.  
     [0158] A nucleic acid encoding a portion of a FATP polypeptide can encode one or more domains, and also can include additional nucleotides. For example, the nucleic acid can also include nucleotide sequences that encode a portion of a FATP protein that is upstream from a lipocalin domain. As the term “upstream” or “upstream sequences” is used herein in relation to the lipocalin domain, it is intended to refer to the nucleotide sequence which encodes all or a portion of a FATP protein located between the signal peptide (when one is present) and the lipocalin domain. In the absence of a signal peptide, the term refers to the nucleotide sequence which encodes all or a portion of a FATP protein between the lipocalin domain and the amino terminus (see FIG. 115).  
     [0159] The invention further relates to variants, including naturally-occurring allelic variants, of those nucleic acids described specifically herein by DNA sequence, that encode variants of such polypeptides as those having the amino acid sequences shown in FIG. 45 (SEQ ID NO:47), FIG. 47 (SEQ ID NO:49), FIG. 112 (SEQ ID NO: 117), FIG. 51 (SEQ ID NO:53) FIG. 53 (SEQ ID NO:55), or FIG. 55 (SEQ ID NO:57). Such variants include nucleic acids encoding variants of the above-listed amino acid sequences, wherein those variants have several, such as 5 to 10, 1 to 5, or 3, 2 or 1 amino acids substituted, deleted, or added, in any combination. Variants include polynucleotides encoding polypeptides with at least 95% but less than 100% amino acid sequence identity to the polypeptides described herein by amino acid sequence. Variant polynucleotides hybridize, under low to high stringency conditions, to the alleles described herein by DNA sequence. In one embodiment, variants have silent substitutions, additions and deletions that do not alter the properties and activities of the FATP. Allelic variants of the polynucleotides encoding hsFATP1 (FIG. 45; SEQ ID NO:47), hsFATP2 (FIG. 47; SEQ ID NO:49), hsFATP3 (FIG. 112; SEQ ID NO:117), hsFATP4 (FIG. 51; SEQ ID NO:53), hsFATP5 (FIG. 53; SEQ ID NO:55) and hsFATP6 (FIG. 55; SEQ ID NO:57) will be identified as mapping to chromosomal locations listed for the corresponding wild type genes in Table 2 in Example 1.  
     [0160] Orthologous genes are gene loci in different species that are sufficiently similar to each other in their nucleotide sequences to suggest that they originated from a common ancestral gene. Orthologous genes arise when a lineage splits into two species, rather than when a gene is duplicated within a genome. Proteins that are orthologs are encoded by genes of two different species, wherein the genes are said to be orthologous.  
     [0161] The invention further relates to polynucleotides encoding polypeptides which are orthologous to those polypeptides having a specific amino acid sequence described herein, such as the amino acid sequences shown in FIG. 45 (SEQ ID NO:47), FIG. 47 (SEQ ID NO:49), FIG. 112 (SEQ ID NO: 117), FIG. 51 (SEQ ID NO:53), FIG. 53 (SEQ ID NO:55), or FIG. 55 (SEQ ID NO:57). These polynucleotides, which can be called ortholog polynucleotides, encode orthologous polypeptides that can range in amino acid sequence identity to a reference amino acid sequence described herein, from about 65% to less than 100%, but preferably 70% to 80%, more preferably 80% to 90%, and still more preferably 90% to less than 100%. Orthologous polypeptides can also be those polypeptides that range in amino acid sequence similarity to a reference amino acid sequence described herein from about 75% to 100%, within the signature sequence. The amino acid sequence similarity between the signature sequences of orthologous polypeptides is preferably 80%, more preferably 90%, and still more preferably, 95%. The ortholog polynucleotides encode polypeptides that have similar functional characteristics (e.g., fatty acid transport activity) and similar tissue distribution, as appropriate to the organism from which the ortholog polynucleotides can be isolated.  
     [0162] Ortholog polynucleotides can be isolated from (e.g., by cloning or nucleic acid amplification methods) a great number of species, as shown by the sample of FATPs from evolutionarily divergent species described herein (see, e.g., FIGS.  44 A-C through FIG. 89). Ortholog polynucleotides corresponding to those in FIG. 45 (SEQ ID NO:47), FIG. 47 (SEQ ID NO:49), FIGS.  111 A-B (SEQ ID NO:116), FIG. 51 (SEQ ID NO:53), FIG. 52 (SEQ ID NO:55) and FIG. 55 (SEQ ID NO:57) are those which can be isolated from mammals such as rat, dog, chimpanzee, monkey, baboon, pig, rabbit and guinea pig, for example.  
     [0163] Further variants that are fragments of the nucleic acids of the invention may be used to synthesize full-length nucleic acids of the invention, such as by use as primers in a polymerase chain reaction. As used herein, the term primer refers to a single-stranded oligonucleotide which acts as a point of initiation of template-directed DNA synthesis under appropriate conditions (e.g., in the presence of four different nucleoside triphosphates and an agent for polymerization, such as DNA or RNA polymerase or reverse transcriptase) in an appropriate buffer and at a suitable temperature. The appropriate length of a primer depends on the intended use of the primer, but typically ranges from 15 to 30 nucleotides. Short primer molecules generally require cooler temperatures to form sufficiently stable hybrid complexes with the template. A primer need not reflect the exact sequence of the template, but must be sufficiently complementary to hybridize with a template. The term primer site refers to the area of the target DNA to which a primer hybridizes. The term primer pair refers to a set of primers including a 5′ (upstream) primer that hybridizes with the 5′ end of the DNA sequence to be amplified and a 3′ (downstream) primer that hybridizes with the complement of the 3′ end of the sequence to be amplified.  
     [0164] Further embodiments of the invention are nucleic acids that are at least 80% identical over their entire length to a nucleic acid described herein, for example a nucleic acid having the nucleotide sequence in FIGS.  44 A- 44 C (SEQ ID NO:46), FIGS.  46 A- 46 B (SEQ ID NO:48), FIGS.  111 A-B (SEQ ID NO:116), FIGS.  50 A- 50 C (SEQ ID NO:52), FIG. 52 (SEQ ID NO:54), and FIGS.  54 A- 54 C (SEQ ID NO:56). Additional embodiments are nucleic acids, and the complements of such nucleic acids, having at least 90% nucleotide sequence identity to the above-described sequences, and nucleic acids having at least 95% nucleotide sequence identity. In preferred embodiments, DNA of the present invention has 97% nucleotide sequence identity, 98% nucleotide sequence identity, or at least 99% nucleotide sequence identity with the DNA whose sequences are presented herein.  
     [0165] Other embodiments of the invention are nucleic acids that are at least 80% identical in nucleotide sequence to a nucleic acid encoding a polypeptide having an amino acid sequence as set forth in FIG. 45 (SEQ ID NO:47), FIG. 47 (SEQ ID NO:49), FIG. 112 (SEQ ID NO:1 17), FIG. 51 (SEQ ID NO:53), FIG. 53 (SEQ ID NO:55) or FIG. 55 (SEQ ID NO:57), or as such amino acid sequences are set forth elsewhere herein, and nucleic acids that are complementary to such nucleic acids. Specific embodiments are nucleic acids having at least 90% nucleotide sequence identity to a nucleic acid encoding a polypeptide having an amino acid sequence as described in the list above, nucleic acids having at least 95% sequence identity, and nucleic acids having at least 97% sequence identity.  
     [0166] The terms “complementary” or “complementarity” as used herein, refer to the natural binding of polynucleotides under permissive salt and temperature conditions by base-pairing. Complementarity between two single-stranded molecules may be “partial” in which only some of the nucleic acids bind, or it may be complete when total complementarity exists between the single-stranded molecules (that is, when A-T and G-C base pairing is 100% complete). The degree of complementarity between nucleic acid strands has significant effects on the efficiency and strength of hybridization between nucleic acid strands. This is of particular importance in amplification reactions, which depend on binding between nucleic acid strands.  
     [0167] The invention further includes nucleic acids that hybridize to the above-described nucleic acids, especially those nucleic acids that hybridize under stringent hybridization conditions. “Stringent hybridization conditions” or “high stringency conditions” generally occur within a range from about T m  minus 5° C. (5° C. below the strand dissociation temperature or melting temperature (T m ) of the probe nucleic acid molecule) to about 20° C. to 25° C. below T m . As will be understood by those of skill in the art, the stringency of hybridization may be altered in order to identify or detect molecules having identical or related polynucleotide sequences. An example of high stringency hybridization follows. Hybridization solution is (6× SSC/10 mM EDTA/0.5% SDS/5× Denhardt&#39;s solution/100 μg/ml sheared and denatured salmon sperm DNA). Hybridization is at 64-65° C. for 16 hours. The hybridized blot is washed two times with 2× SSC/0.5% SDS solution at room temperature for 15 minutes each, and two times with 0.2× SSC/0.5% SDS at 65° C., for one hour each. Further examples of high stringency conditions can be found on pages 2.10.1-2.10.16 (see particularly 2.10.8-11) and pages 6.3.1-6 in  Current Protocols in Molecular Biology  (Ausubel, F. M. et al., eds., containing supplements up through Supplement 42, 1998). Examples of high, medium, and low stringency conditions can be found on pages 36 and 37 of WO 98/40404, which are incorporated herein by reference.  
     [0168] The invention further relates to nucleic acids obtainable by screening an appropriate library with a probe having a nucleotide sequence such as that set forth in FIGS.  44 A- 44 C (SEQ ID NO:46), FIGS.  46 A- 46 B (SEQ ID NO:48), FIG. 111 (SEQ ID NO:116), FIGS.  50 A- 50 C (SEQ ID NO:52), FIG. 52 (SEQ ID NO:54) or FIGS.  54 A- 54 C (SEQ ID NO:56), or a probe which is a sufficiently long fragment of any of the above; and isolating the nucleic acid. Such probes generally can comprise at least 15 nucleotides. Nucleic acids obtainable by such screenings may include RNAs, cDNAs and genomic DNA, for example, encoding FATPs of the FATP family described herein.  
     [0169] Further uses for the nucleic acid molecules of the invention, whether encoding a full-length FATP or whether comprising a contiguous portion of a nucleic acid molecule such as one given in SEQ ID NO:46, 48, 116, 52, 54, or 56, include use as markers for tissues in which the corresponding protein is preferentially expressed (to identify constitutively expressed proteins or proteins produced at a particular stage of tissue differentiation or stage of development of a disease state); as molecular weight markers on southern gels; as chromosome markers or tags (when labeled, for example with biotin, a radioactive label or a fluorescent label) to identify chromosomes or to map related gene positions; to compare with endogenous DNA sequences in a mammal to identify potential genetic disorders; as probes to hybridize and thus identify, related DNA sequences; as a source of information to derive PCR primers for genetic fingerprinting; as a probe to “subtract-out” known sequences in the process of discovering other novel nucleic acid molecules; for selecting and making oligomers for attachment to a “gene chip” or other support, to be used, for example, for examination of expression patterns; to raise anti-protein antibodies using DNA immunization techniques; and as an antigen to raise anti-DNA antibodies or to elicit another immune response.  
     [0170] In certain embodiments, a contiguous portion can be about 15, 25, 30, 40, 50, 75, 100, 200, 300, 400, 500, 750, 1000, 1100, 1250, 1500 or more nucleotides in length. In a particular embodiment, the contiguous portion encompasses the signature sequence of a FATP and is about 1080 nucleotides in length.  
     [0171] Further methods to obtain nucleic acids encoding FATPs of the FATP family include PCR and variations thereof (e.g., “RACE” PCR and semi-specific PCR methods). Portions of the nucleic acids having a nucleotide sequence set forth in FIGS.  44 A- 44 C (SEQ ID NO:46), FIGS.  46 A- 46 B (SEQ ID NO:48), FIGS.  111 A-B (SEQ ID NO:116), FIGS.  50 A- 50 C (SEQ ID NO:52), FIG. 52 (SEQ ID NO:54) or FIGS.  54 A- 54 C (SEQ ID NO:56), (especially “flanking sequences” on either side of a coding region) can be used as primers in methods using the polymerase chain reaction, to produce DNA from an appropriate template nucleic acid.  
     [0172] Once a fragment of the FATP gene is generated by PCR, it can be sequenced, and the sequence of the product can be compared to other DNA sequences, for example, by using the BLAST Network Service at the National Center for Biotechnology Information. The boundaries of the open reading frame can then be identified using semi-specific PCR or other suitable methods such as library screening. Once the 5′ initiator methionine codon and the 3′ stop codon have been identified, a PCR product encoding the full-length gene can be generated using genomic DNA as a template, with primers complementary to the extreme 5′ and 3′ ends of the gene or to their flanking sequences. The full-length genes can then be cloned into expression vectors for the production of functional proteins.  
     [0173] The invention also relates to isolated proteins or polypeptides such as those encoded by nucleic acids of the present invention. Isolated proteins can be purified from a natural source or can be made recombinantly. Proteins or polypeptides referred to herein as “isolated” are proteins or polypeptides that exist in a state different from the state in which they exist in cells in which they are normally expressed in an organism, and include proteins or polypeptides obtained by methods described herein, similar methods or other suitable methods, and also include essentially pure proteins or polypeptides, proteins or polypeptides produced by chemical synthesis or by combinations of biological and chemical methods, and recombinant proteins or polypeptides which are isolated. Thus, the term “isolated” as used herein, indicates that the polypeptide in question exists in a physical milieu distinct from that in which it occurs in nature. Thus, “isolated” includes existing in membrane fragments and vesicles membrane fractions, liposomes, lipid bilayers and other artificial membrane systems. An isolated FATP may be substantially isolated with respect to the complex cellular milieu in which it naturally occurs, and may even be purified essentially to homogeneity, for example as determined by PAGE or column chromatography (for example, HPLC), but may also have further cofactors or molecular stabilizers, such as detergents, added to the purified protein to enhance activity. In one embodiment, proteins or polypeptides are isolated to a state at least about 75% pure; more preferably at least about 85% pure, and still more preferably at least about 95% pure, as determined by Coomassie blue staining of proteins on SDS-polyacrylamide gels. Proteins or polypeptides referred to herein as “recombinant” are proteins or polypeptides produced by the expression of recombinant nucleic acids.  
     [0174] In a preferred embodiment, an isolated polypeptide comprising a FATP, a functional portion thereof, or a functional equivalent of the FATP, has at least one function characteristic of a FATP, for example, transport activity, binding function (e.g., a domain which binds to AMP), or antigenic function (e.g., binding of antibodies that also bind to a naturally-occurring FATP, as that function is found in an antigenic determinant). Functional equivalents can have activities that are quantitatively similar to, greater than, or less than, the reference protein. These proteins include, for example, naturally occurring FATPs that can be purified from tissues in which they are produced (including polymorphic or allelic variants), variants (e.g., mutants) of those proteins and/or portions thereof. Such variants include mutants differing by the addition, deletion or substitution of one or more amino acid residues, or modified polypeptides in which one or more residues are modified, and mutants comprising one or more modified residues. Portions or fragments of a FATP can range in size from four amino acid residues to the entire amino acid sequence minus one amino acid and include contiguous portions or fragments about 4, 5, 6, 7, 8, 9, 10, 15, 25, 30, 40, 50, 75, 100, 150, 200, 300, 400, 500, 600 or more amino acid residues in length. In one particular embodiment, the portion or fragment includes the signature sequence of a FATP polypeptide and is about 360 amino acid residues in length.  
     [0175] The isolated proteins of the invention preferably include mammalian fatty acid transport proteins of the FATP family of homologous proteins. In one embodiment, the extent of amino acid sequence similarity between a polypeptide having one of the amino acid sequences shown in FIG. 45 (SEQ ID NO:47), FIG. 47 (SEQ ID NO:49), FIG. 112 (SEQ ID NO:117), FIG. 51 (SEQ ID NO:53), FIG. 53 (SEQ ID NO:55), or FIG. 55 (SEQ ID NO:57), and the respective functional equivalents of these polypeptides is at least about 88%. In other embodiments, the degree of amino acid sequence similarity between a FATP and its respective functional equivalent is at least about 91%, at least about 94%, or at least about 97%.  
     [0176] The polypeptides of the invention also include those FATPs encoded by polynucleotides which are orthologous to those polynucleotides, the sequences of which are described herein in whole or in part. FATPs which are orthologs to those described herein by amino acid sequence, in whole or in part, are, for example, fatty acid transport proteins 1-6 of dog, rat, chimpanzee, monkey, rabbit, guinea pig, baboon and pig, and are also embodiments of the invention.  
     [0177] To determine the percent identity or similarity of two amino acid sequences or of two nucleic acid sequences, the sequences are aligned for optimal comparison purposes (e.g., gaps can be introduced in one or both of a first and a second amino acid or nucleic acid sequence for optimal alignment, and non-homologous (dissimilar) sequences can be disregarded for comparison purposes). In a preferred embodiment, the length of a reference sequence aligned for comparison purposes is at least 30%, preferably at least 40%, more preferably at least 50%, even more preferably at least 60%, and even more preferably at least 70%, 80%, or 90% of the length of the reference sequence. The amino acid residues or nucleotides at corresponding amino acid positions or nucleotide positions are then compared. When a position in the first sequence is occupied by the same amino acid residue or nucleotide as the corresponding position in the second sequence, then the molecules are identical at that position (as used herein, amino acid or nucleic acid “identity” is equivalent to amino acid or nucleic acid “similarity”). The percent identity between the two sequences is a function of the number of identical positions shared by the sequences, taking into account the number of gaps, and the length of each gap, which need to be introduced for optimal alignment of the two sequences.  
     [0178] The invention also encompasses polypeptides having a lower degree of identity but having sufficient similarity so as to perform one or more of the same functions performed by the polypeptides described herein by amino acid sequence. Similarity for a polypeptide is determined by conserved amino acid substitution. Such substitutions are those that substitute a given amino acid in a polypeptide by another amino acid of like characteristics. Conservative substitutions are likely to be phenotypically silent. Typically seen as conservative substitutions are the replacements, one for another, among the aliphatic amino acids Ala, Val, Leu, and Ile; interchange of the hydroxyl residues Ser and Thr, exchange of the acidic residues Asp and Glu, substitution between the amide residues Asn and Gln, exchange of the basic residues Lys and Arg and replacements among the aromatic residues Phe and Tyr. Guidance concerning which amino acid changes are likely to be phenotypically silent is found in Bowie et al.,  Science  247:1306-1310 (1990).  
               TABLE 1                       Conservative Amino Acid Substitutions                                                Aromatic   Phenylalanine               Tryptophan               Tyrosine           Hydrophobic   Leucine               Isoleucine               Valine           Polar   Glutamine               Asparagine           Basic   Arginine               Lysine               Histidine           Acidic   Aspartic Acid               Glutamic Acid           Small   Alanine               Serine               Threonine               Methionine               Glycine                      
 
     [0179] The comparison of sequences and determination of percent identity and similarity between two sequences can be accomplished using a mathematical algorithm. ( Computational Molecular Biology , Lesk, A. M., ed., Oxford University Press, New York, 1988 ; Biocomputing: Informatics and Genome Projects , Smith, D. W., ed., Academic Press, New York, 1993 ; Computer Analysis of Sequence Data, Part  1, Griffin, A. M., and Griffin, H. G., eds., Humana Press, New Jersey, 1994 ; Sequence Analysis in Molecular Biology , von Heinje, G., Academic Press, 1987; and  Sequence Analysis Primer , Gribskov, M. and Devereaux, J., eds., M. Stockton Press, New York, 1991). In a preferred embodiment, the percent identity between two amino acid sequences is determined using the Needleman and Wunsch ( J. Mol. Biol . (48):444-453 (1970)) algorithm which has been incorporated into the GAP program in the GCG software package (available on the worldwide web at gcg.com), using either a Blossom 62 matrix or a PAM250 matrix, and a gap weight of 16, 14, 12, 10, 8, 6, or 4 and a length weight of 1, 2, 3, 4, 5, or 6. In yet another preferred embodiment, the percent identity between two nucleotide sequences is determined using the GAP program in the GCG software package (Devereux, J., et al.,  Nucleic Acids Res.  12(1):387 (1984)), (available on the worldwide web at gcg.com), using a NWSgapdna.CMP matrix and a gap weight of 40, 50, 60, 70, or 80 and a length weight of 1, 2, 3, 4, 5, or 6. In another embodiment, the percent identity between two amino acid or nucleotide sequences is determined using the algorithm of E. Meyers and W. Miller ( CABIOS,  4:11-17 (1989)) which has been incorporated into the ALIGN program (version 2.0), using a PAM120 weight residue table, a gap length penalty of 12 and a gap penalty of 4.  
     [0180] The nucleic acid and protein sequences of the present invention can further be used as a “query sequence” to perform a search against databases to, for example, identify other family members or related sequences. Such searches can be performed using the NBLAST and XBLAST programs (version 2.0) of Altschul, et al. ( J. Mol. Biol.  215:403-10 (1990)). BLAST nucleotide searches can be performed with the NBLAST program, score=100, word length=12 to obtain nucleotide sequences homologous to (with calculatably significant similarity to) the nucleic acid molecules of the invention. BLAST protein searches can be performed with the XBLAST program, score=50, word length=3 to obtain amino acid sequences homologous to the proteins of the invention. To obtain gapped alignments for comparison purposes, Gapped BLAST can be utilized as described in Altschul et al., ( Nucleic Acids Res.  25(17):3389-3402 (1997)). When utilizing BLAST and gapped BLAST programs, the default parameters of the respective programs (e.g., XBLAST and NBLAST) can be used. (see the worldwide web at ncbi.nlm.nih.gov)  
     [0181] Similarity for nucleotide and amino acid sequences can be defined in terms of the parameters set by the Advanced Blast search available from NCBI (the National Center for Biotechnology Information (see, for Advanced BLAST the worldwide web at ncbi.nlm.nih.gov/cgi-bin/BLAST/nph-newblast?Jform=1). These default parameters, recommended for a query molecule of length greater than 85 amino acid residues or nucleotides have been set as follows: gap existence cost, 11, per residue gap cost, 1; lambda ratio, 0.85. Further explanation of version 2.0 of BLAST can be found on related website pages and in Altschul, S. F. et al,  Nucleic Acids Res.  25:3389-3402 (1997).  
     [0182] In certain embodiments, a contiguous portion can be about 4, 5, 6, 7, 8, 9, 10, 15, 25, 30, 40, 50, 75, 100, 150, 200, 300, 400, 500, 600 or more amino acid residues in length. In one particular embodiment, the portion or fragment includes the signature sequence of a FATP polypeptide and is about 360 amino acid residues in length.  
     [0183] The invention further relates to fusion proteins, comprising a FATP or functional portion thereof (as described above) as a first moiety, linked to a second moiety not occurring in the FATP as found in nature. Thus, the second moiety can be an amino acid, peptide or polypeptide. The first moiety can be in an N-terminal location, C-terminal location or internal to the fusion protein. In one embodiment, the fusion protein comprises a FATP as the first moiety, and a second moiety comprising a linker sequence and an affinity ligand. Fusion proteins can be produced by a variety of methods. For example, a fusion protein can be produced by the insertion of a FATP gene or portion thereof into a suitable expression vector, such as Bluescript SK +/− (Stratagene, La Jolla, Calif.), pGEX-4T-2 (Pharmacia, Peapack, N.J.), pET-24(+) (Novagen, Madison, Wis.), or vectors of similar construction. The resulting construct can be introduced into a suitable host cell for expression. Upon expression, fusion protein can be purified from cells by means of a suitable affinity matrix (See e.g.,  Current Protocols in Molecular  Biology, Ausubel, F. M. et al., eds., Vol. 2, pp. 16.4.1-16.7.8, containing supplements up through Supplement 42, 1998).  
     [0184] The invention also relates to enzymatically produced, synthetically produced, or recombinantly produced portions of a fatty acid transport protein. Portions of a FATP can be made which have full or partial function on their own, or which when mixed together (though fully, partially, or nonfunctional alone), spontaneously assemble with one or more other polypeptides to reconstitute a functional protein having at least one function characteristic of a FATP.  
     [0185] Fragments of a FATP can be produced by direct peptide synthesis, for example those using solid-phase techniques (Roberge, J. Y. et al.,  Science  269:202-204 (1995); Merrifield, J.,  J. Am. Chem. Soc.  85:2149-2154 (1963)). Protein synthesis can be performed using manual techniques or by automation. Automated synthesis can be carried out using, for instance, an Applied Biosystems 431A Peptide Synthesizer (Perkin Elmer). Various fragments of a FATP can be synthesized separately and combined using chemical methods.  
     [0186] One aspect of the invention is a peptide or polypeptide having the amino acid sequence of a portion of a fatty acid transport protein which is hydrophilic rather than hydrophobic, and ordinarily can be detected as facing the outside of the cell membrane. Such a peptide or polypeptide can be thought of as being an extracellular domain of the FATP, or a mimetic of said extracellular domain. It is known, for example, that a portion of human FATP4 that includes a highly conserved motif is involved in AMP-CoA binding function (Stuhlsatz-Krouper, S. M. et al.,  J. Biol. Chem.  44:28642-28650 (1998)).  
     [0187] The term “mimetic” as used herein, refers to a molecule, the structure of which is developed from knowledge of the structure of the FATP of interest, or one or more portions thereof, and, as such, is able to effect some or all of the functions of a FATP.  
     [0188] Portions of a FATP can be prepared by enzymatic cleavage of the isolated protein, or can be made by chemical synthesis methods. Portions of a FATP can also be made by recombinant DNA methods in which restriction fragments, or fragments that may have undergone further enzymatic processing, or synthetically made DNAs are joined together to construct an altered FATP gene. The gene can be made such that it encodes one or more desired portions of a FATP. These portions of FATP can be entirely homologous to a known FATP, or can be altered in amino acid sequence relative to naturally occurring FATPs to enhance or introduce desired properties such as solubility, stability, or affinity to a ligand. A further feature of the gene can be a sequence encoding an N-terminal signal peptide directed to the plasma membrane.  
     [0189] An extracellular domain can be determined by a hydrophobicity plot, such as those shown in FIGS. 28A, 29A, and  35 A, or by a hydrophilicity plot such as those shown in FIGS. 28C, 29C,  35 C,  91 ,  92  and  93 . A polypeptide or peptide comprising all or a portion of a FATP extracellular domain can be used in a pharmaceutical composition. When administered to a mammal by an appropriate route, the polypeptide or peptide can bind to fatty acids and compete with the native FATPs in the membrane of cells, thereby making fewer fatty acid molecules available as substrates for transport into cells, and reducing the amount of fatty acids taken up by, for example, the heart, in the case of FATP6.  
     [0190] Another aspect of the invention relates to a method of producing a fatty acid transport protein, variants or portions thereof, and to expression systems and host cells containing a vector appropriate for expression of a fatty acid transport protein.  
     [0191] Cells that express a FATP, a variant or a portion thereof, or an ortholog of a FATP described herein by amino acid sequence, can be made and maintained in culture, under conditions suitable for expression, to produce protein in the cells for cell-based assays, or to produce protein for isolation. These cells can be procaryotic or eucaryotic. Examples of procaryotic cells that can be used for expression include  Escherichia coli, Bacillus subtilis  and other bacteria. Examples of eucaryotic cells that can be used for expression include yeasts such as  Saccharomyces cerevisiae, Schizosaccharomyces pombe, Pichia pastoris  and other lower eucaryotic cells, and cells of higher eucaryotes such as those from insects and mammals, such as primary cells and cell lines such as CHO, HeLa, 3T3 and BHK cells, preferably COS cells and human kidney 293 cells, and more preferably Jurkat cells. (See, e.g., Ausubel, F. M. et al., eds.  Current Protocols in Molecular Biology , Greene Publishing Associates and John Wiley &amp; Sons, Inc., containing Supplements up through Supplement 42, 1998)).  
     [0192] In one embodiment, host cells that produce a recombinant FATP, or a portion thereof, a variant, or an ortholog of a FATP described herein by amino acid sequence, can be made as follows. A gene encoding a FATP, variant or a portion thereof can be inserted into a nucleic acid vector, e.g., a DNA vector, such as a plasmid, phage, cosmid, phagemid, virus, virus-derived vector (e.g., SV40, vaccinia, adenovirus, fowl pox virus, pseudorabies viruses, retroviruses) or other suitable replicon, which can be present in a single copy or multiple copies, or the gene can be integrated in a host cell chromosome. A suitable replicon or integrated gene can contain all or part of the coding sequence for a FATP or variant, operably linked to one or more expression control regions whereby the coding sequence is under the control of transcription signals and linked to appropriate translation signals to permit translation. The vector can be introduced into cells by a method appropriate to the type of host cells (e.g., transfection, electroporation, infection). For expression from the FATP gene, the host cells can be maintained under appropriate conditions (e.g., in the presence of inducer, normal growth conditions, etc.). Proteins or polypeptides thus produced can be recovered (e.g., from the cells, as in a membrane fraction, from the periplasmic space of bacteria, from culture medium) using suitable techniques. Appropriate membrane targeting signals may be incorporated into the expressed polypeptide. These signals may be endogenous to the polypeptide or they may be heterologous signals.  
     [0193] Polypeptides of the invention can be recovered and purified from cell cultures (or from their primary cell source) by well-known methods including ammonium sulfate or ethanol precipitation, acid extraction, anion or cation exchange chromatography, phosphocellulose chromatography, hydrophobic interaction chromatography, affinity chromatography, hydroxylapatite chromatography and high performance liquid chromatography. Known methods for refolding protein can be used to regenerate active conformation if the polypeptide is denatured during isolation or purification.  
     [0194] In a further aspect of the invention are methods for assessing the transport function of any of the fatty acid transport proteins or polypeptides described herein, including orthologs, and in variations of these, methods for identifying an inhibitor (or an enhancer) of such function and methods for assessing the transport function in the presence of a candidate inhibitor or a known inhibitor.  
     [0195] A variety of systems comprising living cells can be used for these methods. Cells to be used in fatty acid transport assays, and further in methods for identifying an inhibitor or enhancer of this function, express one or more FATPs. See Examples 3, 6, 9, 12 and 14 for data on tissue distribution of expression of FATPs, and Examples 10 and 11 describing recombinant cells expressing FATP. Cells for use in cell-based assays described herein can be drawn from a variety of sources, such as isolated primary cells of various organs and tissues wherein one or more FATPs are naturally expressed. In some cases, the cells can be from adult organs, and in some cases, from embryonic or fetal organs, such as heart, lung, liver, intestine, skeletal muscle, kidney and the like. Cells for this purpose can also include cells cultured as fragments of organs or in conditions simulating the cell type and/or tissue organization of organs, in which artificial materials may be used as substrates for cell growth. Other types of cells suitable for this purpose include cells of a cell strain or cell line (ordinarily comprising cells considered to be “transformed”) transfected to express one or more FATPs.  
     [0196] A further embodiment of the invention is a method for detecting, in a sample of cells, a fatty acid transport protein, a portion or fragment thereof, a fusion protein comprising a FATP or a portion thereof, or an ortholog as described herein, wherein the cells can be, for instance, cells of a tissue, primary culture cells, or cells of a cell line, including cells into which nucleic acid has been introduced. The method comprises adding to the sample an agent that specifically binds to the protein, and detecting the agent specifically bound to the protein. Appropriate washing steps can be added to reduce nonspecific binding to the agent. The agent can be, for example, an antibody, a ligand or a substrate mimic. The agent can have incorporated into it, or have bound to it, covalently or by high affinity non-covalent interactions, for instance, a label that facilitates detection of the agent to which it is bound, wherein the label can be, but is not limited to, a phosphorescent label, a fluorescent label, a biotin or avidin label, or a radioactive label. The means of detection of a fatty acid transport protein can vary, as appropriate to the agent and label used. For example, for an antibody that binds to the fatty acid transport protein, the means of detection may call for binding a second antibody, which has been conjugated to an enzyme, to the antibody which binds the fatty acid transport protein, and detecting the presence of the second antibody by means of the enzymatic activity of the conjugated enzyme.  
     [0197] Similar principles can also be applied to a cell lysate or a more purified preparation of proteins from cells that may comprise a fatty acid transport protein of interest, for example in the methods of immunoprecipitation, immunoblotting, immunoaffinity methods, that in addition to detection of the particular FATP, can also be used in purification steps, and qualitative and quantitative immunoassays. See, for instance, chapters 11 through 14 in  Antibodies: A Laboratory Manual , E. Harlow and D. Lane, eds., Cold Spring Harbor Laboratory, 1988.  
     [0198] Isolated fatty acid transport protein or, an antigenically similar portion thereof, especially a portion that is soluble, can be used in a method to select and identify molecules which bind specifically to the FATP. Fusion proteins comprising all of, or a portion of, the fatty acid transport protein linked to a second moiety not occurring in the FATP as found in nature, can be prepared for use in another embodiment of the method. Suitable fusion proteins for this purpose include those in which the second moiety comprises an affinity ligand (e.g., an enzyme, antigen, epitope). FATP fusion proteins can be produced by the insertion of a gene encoding the FATP or a variant thereof, or a suitable portion of such gene into a suitable expression vector, which encodes an affinity ligand (e.g., pGEX-4T-2 and pET-15b, encoding glutathione S-transferase and His-Tag affinity ligands, respectively). The expression vector can be introduced into a suitable host cell for expression. Host cells are lysed and the lysate, containing fusion protein, can be bound to a suitable affinity matrix by contacting the lysate with an affinity matrix.  
     [0199] In a particular embodiment, a nucleic acid encodes a portion of a FATP polypeptide which includes a motif or domain, for example, a lipocalin domain or an AMP-binding domain. Such a polypeptide portion can be a functional portion of a FATP protein. The term “lipocalin domain” is an art recognized term and as used herein refers to a particular domain present in FATP proteins. This domain is described as including regions of sequence homology as well as a common tertiary structure represented as an eight stranded antiparallel beta-barrel. (see Banaszak, L. et al.,  Advances in Protein Chemistry,  45: 89-151). Many lipocalin domains can be identified structurally as a sequence contained within the general formula: [DENG]-X-[DENQGSTARK]-X(0,2)-[DENQARK]-[LIVFY]-{CP}-G-{C}-W-[FYWLRH-X]-[LIVMTA], e.g., the lipocalin signature sequence or consensus pattern (SEQ ID NO: 125). One skilled in the art will recognize that a lipocalin domain for a particular FATP protein can vary in sequence from this general formula. A FATP lipocalin domain can be, for example, identical to the lipocalin signature sequence, or, can exhibit 60, 65, 70, 75, 80, 85, 90, 95 or greater sequence percent identity in comparison to the general formula provided that it still retains the necessary lipocalin binding function.  
     [0200] For example, a lipocalin domain for each of the human FATPs, hsFATP1 (SEQ ID NO: 126), hsFATP2 (SEQ ID NO: 127), hsFATP3 (SEQ ID NO: 128), hsFATP4 (SEQ ID NO: 129), hsFATP5 (SEQ ID NO: 130), and hsFATP6 (SEQ ID NO: 131) has been identified. These particular lipocalin domains are located near the N-terminal portion of the specified proteins (see FIG. 118). The sequences of these lipocalin domains are highly conserved across the FATP family. A search using the lipocalin signature sequence conducted on a public database (worldwide web at ebi.ac.uk/interpro/), indicated that the lipocalin domains of hsFATP1 and hsFATP4 share identity with signature sequence. In addition, a search directed to identifying sequences having at least 80% identity to the lipocalin signature sequence identified three additional human FATPs, hsFATP3, hsFATP5 and hsFATP6.  
     [0201] A lipocalin domain can also be identified functionally since, for example, it has been identified as a binding motif capable of binding fatty acids. In particular, the studies described in Experiment 20 demonstrated that fusion proteins including the lipocalin domains from hsFATP4 bound long chain fatty acids such as oleates and palmitates with great specificity. Other fatty acids can also be used to assess binding in FATP4 and other members of the FATP family.  
     [0202] Polypeptides, including fusion polypeptides, which contain a lipocalin domain can also include additional components. For example, fusion polypeptides containing a lipocalin domain can include amino acid residues from the portion of the protein which is located upstream, i. e., in the direction of the N-terminal end of a FATP protein, from the lipocalin domain. As the term “upstream sequences” is used herein in relation to the lipocalin domain, it is intended to refer to the amino acid residues of a FATP protein which are located between the signal peptide (when one is present) and the lipocalin domain. In the absence of a signal peptide, the term refers to the portion of a FATP protein between the lipocalin domain and the amino terminus (see FIG. 115).  
     [0203] Fusion polypeptides which contain a lipocalin domain can also include additional domains or motifs, for example, an AMP binding domain can be included. For example, an AMP binding domain for each of the human FATPs, hsFATP1 (SEQ ID NO: 132), hsFATP2 (SEQ ID NO: 133), hsFATP3 (SEQ ID NO: 134), hsFATP4 (SEQ ID NO: 135), hsFATP5 (SEQ ID NO: 136) and hsFATP6 (SEQ ID NO: 137) has been identified (see FIG. 118).  
     [0204] In one embodiment, the fusion protein can be immobilized on a suitable affinity matrix under conditions sufficient to bind the affinity ligand portion of the fusion protein to the matrix, and is contacted with one or more candidate binding agents (e.g., a mixture of peptides) to be tested, under conditions suitable for binding of the binding agents to the FATP portion of the bound fusion protein. Next, the affinity matrix with bound fusion protein can be washed with a suitable wash buffer to remove unbound candidate binding agents and non-specifically bound candidate binding agents. Those agents which remain bound can be released by contacting the affinity matrix with fusion protein bound thereto with a suitable elution buffer. Wash buffer can be formulated to permit binding of the fusion protein to the affinity matrix, without significantly disrupting binding of specifically bound binding agents. In this aspect, elution buffer can be formulated to permit retention of the fusion protein by the affinity matrix, but can be formulated to interfere with binding of the candidate binding agents to the target portion of the fusion protein. For example, a change in the ionic strength or pH of the elution buffer can lead to release of specifically bound agent, or the elution buffer can comprise a release component or components designed to disrupt binding of specifically bound agent to the target portion of the fusion protein.  
     [0205] Immobilization can be performed prior to, simultaneous with, or after, contacting the fusion protein with candidate binding agent, as appropriate. Various permutations of the method are possible, depending upon factors such as the candidate molecules tested, the affinity matrix-ligand pair selected, and elution buffer formulation. For example, after the wash step, fusion protein with binding agent molecules bound thereto can be eluted from the affinity matrix with a suitable elution buffer (a matrix elution buffer, such as glutathione for a GST fusion). Where the fusion protein comprises a cleavable linker, such as a thrombin cleavage site, cleavage from the affinity ligand can release a portion of the fusion with the candidate agent bound thereto. Bound agent molecules can then be released from the fusion protein or its cleavage product by an appropriate method, such as extraction.  
     [0206] One or more candidate binding agents can be tested simultaneously. Where a mixture of candidate binding agents is tested, those found to bind by the foregoing processes can be separated (as appropriate) and identified by suitable methods (e.g., PCR, sequencing, chromatography). Large libraries of candidate binding agents (e.g., peptides, RNA oligonucleotides) produced by combinatorial chemical synthesis or by other methods can be tested (see e.g., Ohlmeyer, M. H. J. et al.,  Proc. Natl. Acad. Sci. USA  90:10922-10926 (1993) and DeWitt, S. H. et al.,  Proc. Natl. Acad. Sci. USA  90:6909-6913 (1993), relating to tagged compounds; see also Rutter, W. J. et al. U.S. Pat. No. 5,010,175; Huebner, V. D. et al., U.S. Pat. No. 5,182,366; and Geysen, H. M., U.S. Pat. No. 4,833,092). Random sequence RNA libraries (see Ellington, A. D. et al.,  Nature  346:818-822 (1990); Bock, L. C. et al.,  Nature  355:584-566 (1992); and Szostak, J. W.,  Trends in Biochem. Sci.  17:89-93 (March, 1992)) can also be screened according to the present method to select RNA molecules which bind to a target FATP or FATP fusion protein. Where binding agents selected from a combinatorial library by the present method carry unique tags, identification of individual biomolecules by chromatographic methods is possible. Where binding agents do not carry tags, chromatographic separation, followed by mass spectrometry to ascertain structure, can be used to identify binding agents selected by the method, for example.  
     [0207] The invention also comprises a method for identifying an agent which inhibits interaction between a fatty acid transport protein (e.g., one comprising the amino acid sequence in SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:117, SEQ ID NO:53, SEQ ID NO:55, or SEQ ID NO:57), and a ligand of said protein. The FATP can be one described by an amino acid sequence herein, a portion or fragment thereof, a variant thereof, or an ortholog thereof, or a FATP fusion protein. Here, a ligand can be, for instance, a substrate, or a substrate mimic, an antibody, or a compound, such as a peptide, that binds with specificity to a site on the protein. The method comprises combining, not limited to a particular order, the fatty acid protein, the ligand of the protein, and a candidate agent to be assessed for its ability to inhibit interaction between the protein and the ligand, under conditions appropriate for interaction between the protein and the ligand (e.g., pH, salt, temperature conditions conducive to appropriate conformation and molecular interactions); determining the extent to which the protein and ligand interact; and comparing (1) the extent of protein-ligand interaction in the presence of candidate agent with (2) the extent of protein-ligand interaction in the absence of candidate agent, wherein if (1) is less than (2), then the candidate agent is one which inhibits interaction between the protein and the ligand.  
     [0208] The method can be facilitated, for example, by using an experimental system which employs a solid support (column chromatography matrix, wall of a plate, microtiter wells, column pore glass, pins to be submerged in a solution, beads, etc.) to which the protein can be attached. Accordingly, in one embodiment, the protein can be fixed to a solid phase directly or indirectly, by a linker. The candidate agent to be tested is added under conditions conducive for interaction and binding to the protein. The ligand is added to the solid phase system under conditions appropriate for binding. Excess ligand is removed, as by a series of washes done under conditions that do not disrupt protein-ligand interactions. Detection of bound ligand can be facilitated by using a ligand that carries a label (e.g., fluorescent, chemiluminescent, radioactive). In a control experiment, protein and ligand are allowed to interact in the absence of any candidate agent, under conditions otherwise identical to those used for the “test” conditions where candidate inhibiting agent is present, and any washes used in the test conditions are also used in the control. The extent to which ligand binds to the protein in the presence of candidate agent is compared to the extent to which ligand binds to the protein in the absence of the candidate agent. If the extent to which interaction of the protein and the ligand occurs is less in the presence of the candidate agent than in the absence of the candidate agent, the candidate agent is an agent which inhibits interaction between the protein and the ligand of the protein.  
     [0209] In a further embodiment, an inhibitor (or an enhancer) of a fatty acid transport protein can be identified. The method comprises steps which are, or are variations of the following: contacting the cells with fatty acid, wherein the fatty acid can be labeled for convenience of detection; contacting a first aliquot of the cells with an agent being tested as an inhibitor (or enhancer) of fatty acid uptake while maintaining a second aliquot of cells under the same conditions but without contact with the agent; and measuring (e.g., quantitating) fatty acid in the first and second aliquots of cells; wherein a lesser quantity of fatty acid in the first aliquot compared to that in the second aliquot is indicative that the agent is an inhibitor of fatty acid uptake by a fatty acid transport protein. A greater quantity of fatty acid in the first aliquot compared to that in the second aliquot is indicative that the agent is an enhancer of fatty acid uptake by a fatty acid transport protein.  
     [0210] A particular embodiment of identifying an inhibitor or enhancer of fatty acid transport function employs the above steps, but also employs additional steps preceding those given above: introducing into cells of a cell strain or cell line (“host cells” for the intended introduction of, or after the introduction of, a vector) a vector comprising a fatty acid transport protein gene, wherein expression of the gene can be regulatable or constitutive, and providing conditions to the host cells under which expression of the gene can occur.  
     [0211] The terms “contacting” and “combining” as used herein in the context of bringing molecules into close proximity to each other, can be accomplished by conventional means. For example, when referring to molecules that are soluble, contacting is achieved by adding the molecules together in a solution. “Contacting” can also be adding an agent to a test system, such as a vessel containing cells in tissue culture.  
     [0212] The term “inhibitor” or “antagonist”, as used herein, refers to an agent which blocks, diminishes, inhibits, hinders, limits, decreases, reduces, restricts or interferes with fatty acid transport into the cytoplasm of a cell, or alternatively and additionally, prevents or impedes the cellular effects associated with fatty acid transport. The term “enhancer” or “agonist”, as used herein, refers to an agent which augments, enhances, or increases fatty acid transport into the cytoplasm of a cell. An antagonist will decrease fatty acid concentration, fatty acid metabolism and byproduct levels in the cell, leading to phenotypic and molecular changes.  
     [0213] In order to produce a “host cell” type suitable for fatty acid uptake assays and for assays derived therefrom for identifying inhibitors or enhancers thereof, a nucleic acid vector can be constructed to comprise a gene encoding a fatty acid transport protein, for example, human FATP1, FATP2, FATP3, FATP4, FATP5, FATP6, a mutant or variant thereof, an ortholog of the human proteins, such as mouse orthologs or orthologs found in other mammals, or a FATP family protein of origin in an organism other than a mammal. The gene of the vector can be regulatable, such as by the placement of the gene under the control of an inducible or repressible promoter in the vector (e.g., inducible or repressible by a change in growth conditions of the host cell harboring the vector, such as addition of inducer, binding or functional removal of repressor from the cell millieu, or change in temperature) such that expression of the FATP gene can be turned on or initiated by causing a change in growth conditions, thereby causing the protein encoded by the gene to be produced, in host cells comprising the vector, as a plasma membrane protein. Alternatively, the FATP gene can be constitutively expressed.  
     [0214] A vector comprising a FATP gene, such as a vector described herein, can be introduced into host cells by a means appropriate to the vector and to the host cell type. For example, commonly used methods such as electroporation, transfection, for instance, transfection using CaCl 2 , and transduction (as for a virus or bacteriophage) can be used. Host cells can be, for example, mammalian cells such as primary culture cells or cells of cell lines such as COS cells, 293 cells or Jurkat cells. Host cells can also be, in some cases, cells derived from insects, cells of insect cell lines, bacterial cells, such as  E. coli , or yeast cells, such as  S. cerevisiae . It is preferred that the fatty acid transport protein whose function is to be assessed, with or without a candidate inhibitor or enhancer, be produced in host cells whose ancestor cells originated in a species related to the species of origin of the FATP gene encoding the fatty acid transport protein. For example, it is preferable that tests of function or of inhibition or enhancement of a mammalian FATP be carried out in host mammalian cells producing the FATP, rather than bacterial cells or yeast cells.  
     [0215] Host cells comprising a vector comprising a regulatable FATP gene can be treated so as to allow expression of the FATP gene and production of the encoded protein (e.g., by contacting the cells with an inducer compound that effects transcription from an inducible promoter operably linked to the FATP gene).  
     [0216] Alternatively, host cells containing an endogenous FATP gene can be engineered to activate or deactivate expression of the FATP gene and production of the encoded protein. For example, homologous recombination, often referred to as targeting, can be utilized to alter the regulatory region associated with the FATP gene to increase or decrease the level of expression. Alteration of the regulatory region can include disablement of the regulatory region associated with the FATP gene and/or replacement of the region or a portion of the region. A variety of regulatory regions are known which can be transfected into cells to cause an endogenous gene to display a pattern of induction or expression that differs from that of the cell prior to transfection.  
     [0217] The test agent (e.g., an agonist or antagonist) is added to the cells to be used in a fatty acid transport assay, in the presence or absence of test agent, under conditions suitable for production and/or maintenance of the expressed FATP in a conformation appropriate for association of the FATP with test agent and substrate. For example, conditions under which an agent is assessed, such as media and temperature requirements, can, initially, be similar to those necessary for transport of typical fatty acid substrates across the plasma membrane. One of ordinary skill in the art will know how to vary experimental conditions depending upon the biochemical nature of the test agent. The test agent can be added to the cells in the presence of fatty acid, or in the absence of fatty acid substrate, with the fatty acid substrate being added following the addition of the test agent. The concentration at which the test agent can be evaluated can be varied, as appropriate, to test for an increased effect with increasing concentrations.  
     [0218] Test agents to be assessed for their effects on fatty acid transport can be any chemical (element, molecule, compound), made synthetically, made by recombinant techniques or isolated from a natural source. For example, test agents can be peptides, polypeptides, peptoids, sugars, hormones, or nucleic acid molecules, such as antisense nucleic acid molecules. In addition, test agents can be small molecules or molecules of greater complexity made by combinatorial chemistry, for example, and compiled into libraries. These libraries can comprise, for example, alcohols, alkyl halides, amines, amides, esters, aldehydes, ethers and other classes of organic compounds. Test agents can also be natural or genetically engineered products isolated from lysates of cells, bacterial, animal or plant, or can be the cell lysates themselves. Presentation of test compounds to the test system can be in either an isolated form or as mixtures of compounds, especially in initial screening steps.  
     [0219] Thus, the invention relates to a method for identifying agents which alter fatty acid transport, the method comprising providing the test agent to the cell (wherein “cell” includes the plural, and can include cells of a cell strain, cell line or culture of primary cells or organ culture, for example), under conditions suitable for binding to its target, whether to the FATP itself or to another target on or in the cell, wherein the transformed cell comprises a FATP.  
     [0220] In greater detail, to test one or more agents or compounds (e.g., a mixture of compounds can conveniently be screened initially) for inhibition of the transport function of a fatty acid transport protein, the agent(s) can be contacted with the cells. The cells can be contacted with a labeled fatty acid. The fatty acid can be, for example, a known substrate of the fatty acid transport protein such as oleate or palmitate. The fatty acid can itself be labeled with a radioactive isotope, (e.g.,  3 H or 14C) or can have a radioactively labeled adduct attached. In other variations, the fatty acid can have chemically attached to it a fluorescent label, or a substrate for an enzyme occurring within the cells, wherein the substrate yields a detectable product, such as a highly colored or fluorescent product. Addition of candidate inhibitors and labeled substrate to the cells comprising fatty acid transport protein can be in either order or can be simultaneous.  
     [0221] A second aliquot of cells, which can be called “control” cells (a “first” aliquot of cells can be called “test” cells), is treated, if necessary (as in the case of transformed “host” cells), so as to allow expression of the FATP gene, and is contacted with the labeled substrate of the fatty acid transport protein. The second aliquot of cells is not contacted with one or more agents to be tested for inhibition of the transport function of the protein produced in the cells, but is otherwise kept under the same culture conditions as the first aliquot of cells.  
     [0222] In a further step of a method to identify inhibitors of a fatty acid transport protein, the labeled fatty acid is measured in the first and second aliquots of cells. A preliminary step of this measurement process can be to separate the external medium from the cells so as to be able to distinguish the labeled fatty acid external to the cells from that which has been transported inside the cells. This can be accomplished, for instance, by removing the cells from their growth container, centrifuging the cell suspension, removing the supernatant and performing one or more wash steps to extensively dilute the remaining medium which may contain labeled fatty acid. Detection of the labeled fatty acid can be by a means appropriate to the label used. For example, for a radioactive label, detection can be by scintillation counting of appropriately prepared samples of cells (e.g., lysates or protein extracts); for a fluorescent label, by measuring fluorescence in the cells by appropriate instrumentation.  
     [0223] If a compound tested as a candidate inhibitor of transport function causes the test cells to have less labeled fatty acid detected in the cells than that detected in the control cells, then the compound is an inhibitor of the fatty acid transport protein. Procedures analogous to those above can be devised for identifying enhancers (agonists of FATPs) of fatty acid transport function wherein if the test cells contain more labeled fatty acid than that detected in the control cells, or if the fatty acid is taken up at a higher rate, then the compound being tested can be concluded to be an enhancer of the fatty acid transport protein.  
     [0224] Example 13 describes use of an assay of this type to identify an inhibitor of a FATP. In Example 13, an antisense oligonucleotide which specifically inhibits biosynthesis of mmFATP4 was demonstrated to inhibit fatty acid uptake into mouse enterocytes. Similarly, antisense oligonucleotides directed towards specifically inhibiting the biosynthesis of FATP6 in heart cells, FATP5 in liver cells, FATP3 in lung cells, and FATP2 in colon cells, can be demonstrated as examples of “test agents” that inhibit fatty acid transport.  
     [0225] Another assay to determine whether an agent is an inhibitor (or enhancer) of fatty acid transport employs animals, one or more of which are administered the agent, and one or more of which are maintained under similar conditions, but are not administered the agent. Both groups of animals are given fatty acids (e.g., orally, intravenously, by tube inserted into stomach or intestine), and the fatty acids taken up into a bodily fluid (e.g., serum) or into an organ or tissue of interest are measured from comparable samples taken from each group of animals. The fatty acids may carry a label (e.g., radioactive) to facilitate detection and quantitation of fatty acids taken up into the fluid or tissue being sampled. This type of assay can be used alone or can be used in addition to in vitro assays of a candidate inhibitor or enhancer.  
     [0226] An agent determined to be an inhibitor (or enhancer) of FATP function, such as fatty acid binding and/or fatty acid uptake, can be administered to cells in culture, or in vivo, to a mammal (e.g. human) to inhibit (or enhance) FATP function. Such an agent may be one that acts directly on the FATP (for example, by binding) or can act on an intermediate in a biosynthetic pathway to produce FATP, such as transcription of the FATP gene, processing of the mRNA, or translation of the mRNA. An example of such an agent is antisense oligonucleotide.  
     [0227] Antisense methods similar to those illustrated in Example 13 can be used to determine the target FATP of a compound or agent that has an inhibitory or enhancing effect on fatty acid uptake. For example, antisense oligonucleotide directed to the inhibition of FATP4 biosynthesis can be added to lung cells or cell lines derived from lung cells. In addition, antisense oligonucleotides directed to the inhibition of other FATPs, except for FATP3, can also be added to the lung cells. The administration of antisense oligonucleotides in this manner ensures that the predominant FATP activity remaining in the cells comes from FATP3. After a period of incubation of the cells with the antisense oligonucleotides sufficient to deplete the plasma membrane of the FATPs whose biosynthesis has been inhibited, a test agent, preferably one that has been shown by some preliminary test to have an inhibitory or enhancing activity on fatty acid transport, can be added to the lung cells. If the test agent is now demonstrated, after treatment of the cells with antisense oligonucleotides, to have an inhibitory or enhancing activity on fatty acid transport in the lung cells, it can be concluded that the target of the test agent is FATP3, or a molecule involved in the biosynthesis or activity of FATP3.  
     [0228] In another type of cell-based assay for uptake of fatty acids, a change of intracellular pH resulting from the uptake of fatty acids can be followed by an indicator fluorophore. The fluorophore can be taken up by the cells in a preincubation step. Fatty acids can be added to the cell medium, and after some period of incubation to allow FATP-mediated uptake of fatty acids, the change in λ max  of fluorescence can be measured, as an indicator of a change in intracellular pH, as the λ max  of fluorescence of the fluorophore changes with the pH of its environment, thereby indicating uptake of fatty acids. One such fluorophore is BCECF (2′, 7′-bis(2-carboxyethyl)-5(6)-carboxyfluorescein; Rink, T. J. et al.,  J Cell. Biol.  95: 189 (1982)).  
     [0229] In assays similar to those described above, a candidate inhibitor or enhancer of fatty acid transport function can be added (or mock-added, for control cultures) to cultures of cells engineered to express a desired FATP to which fatty acid substrate is also added. Inhibition of fatty acid uptake is indicated by a lack of the drop in pH, indicating fatty acid uptake, that is seen in control cells. Enhancement of fatty acid uptake is indicated by a decrease in intracellular pH, as compared to control cells not receiving the candidate enhancer of fatty acid transport function.  
     [0230] Yeast cells can be used in a similar cell-based assay for the uptake of fatty acids mediated by a FATP, and such an assay can be adapted to a screening assay for the identification of agents that inhibit or enhance fatty acid uptake by an FATP. Yeast cells lacking an endogenous FATP activity (mutated, disrupted or deleted for FAT1; Faergeman, N. J. et al.,  J. Biol. Chem.  272(13):8531-8538 (1997); Watkins, P. A. et al.,  J. Biol. Chem.  273(29):18210-18219 (1998)) can be engineered to harbor a related gene of the family of FATP-encoding genes, such as a mammalian FATP (e.g., human FATP4).  
     [0231] Examples of expression vectors include pEG (Mitchell, D. A., et al.,  Yeast  9:715-723 (1993)) and pDAD1 and pDAD2, which contain a GAL1 promoter (Davis, L. I. and Fink, G. R.,  Cell  61:965-978 (1990)). A variety of promoters are suitable for expression. Available yeast vectors offer a choice of promoters. In one embodiment, the inducible GAL1 promoter is used. In another embodiment, the constitutive ADH1 promoter (alcohol dehydrogenase; Bennetzen, J. L. and Hall, B. D.,  J. Biol. Chem.  257:3026-3031 (1982)) can be used to express an inserted gene on glucose-containing media. An example of a vector suitable for expression of a heterologous FATP gene in yeast is pQB169.  
     [0232] With the introduced FATP gene providing the only fatty acid transport protein function for the yeast cells, it is possible to study effect of the heterologous FATP on fatty acid transport into the yeast cells in isolation. Assays for the uptake of fatty acids into the yeast cells can be devised that are similar to those described above and/or those assays that have been illustrated in the Examples. Tests for candidate inhibitors or enhancers of the heterologous FATP can be done in cultures of yeast cells, wherein the yeast cells are incubated with fatty acid substrate and an agent to be tested as an inhibitor or enhancer of FATP function. FATP uptake after a period of time can be measured by analyzing the contents of the yeast cells for fatty acid substrate, as compared with control yeast cells incubated with the fatty acid, but not with the test agent. Yeast cells have the additional advantage, over mammalian cells in culture, for example, that yeast cells can be forced to rely upon fatty acids as their only source of carbon, if the growth medium supplied to the yeast cells is formulated to contain no other source of carbon. Thus, the effect of the heterologous FATP on fatty acid uptake and metabolism in the engineered yeast cells can be amplified. An agent that efficiently blocks transport function of the heterologous FATP could result in death of the yeast cells. Thus, in this case, inhibition of function of the heterologous FATP can result in loss of viability. A simple measure of viability is turbidity of the yeast suspension culture, which can be adapted to a high throughput screening assay for effects of various agents to be tested, using microtiter plates or similar devices for small-volume cultures of the engineered yeast cells.  
     [0233] Cell-free assays can also be used to measure the transport of fatty acids across a membrane, and therefor also to assess a test treatment or test agent for its effect on the rate or extent of fatty acid transport. An isolated FATP, for example in the presence of a detergent that preserves the native 3-dimensional structure of the FATP, or partially purified FATP, can be used in an artificial membrane system typically used to preserve the native conformation and activity of membrane proteins. Such systems include liposomes, artificial bilayers of phospholipids, isolated plasma membrane such as cell membrane fragments, cell membrane fractions, or cell membrane vesicles, and other systems in which the FATP can be properly oriented within the membrane to have transport activity. Assays for transport activity can be performed using methods analogous to those that can be used in cells engineered to predominantly express one FATP whose function is to be measured. A labeled (e.g., radioactively labeled) fatty acid substrate can be incubated with one side of a bilayer or in a suspension of liposomes constructed to integrate a properly oriented FATP. The accumulation of fatty acids with time can be measured, using appropriate means to detect the label (e.g., scintillation counting of medium on each side of the bilayer, or of the contents of liposomes isolated from the surrounding medium). Assays such as these can be adapted to use for the testing of agents which might interact with the FATP to produce an inhibitory or an enhancing effect on the rate or extent of fatty acid transport. That is, the above-described assay can be done in the presence or absence of the agent to be tested, and the results compared.  
     [0234] For examples of isolation of membrane proteins (ADP/ATP carrier and uncoupling protein), reconstitution into phospholipid vesicles, and assays of transport, see Klingenberg, M. et al.,  Methods Enzymol.  260:369-389 (1995). For an example of a membrane protein (phosphate carrier of  Saccharomyces cerevisiae ) that was purified and solubilized from  E. coli  inclusion bodies, see Schroer, A. et al.,  J. Biol. Chem.  273: 14269-14276 (1998). The Glut1 glucose transporter of rat has been expressed in yeast. A crude membrane fraction of the yeast was prepared and reconstituted with soybean phospholipids into liposomes. Glucose transport activity could be measured in the liposomes (Kasahara, T. and Kasahara, M.,  J. Biol. Chem.  273: 29113-29117 (1998)). Similar methods can be applied to the proteins and polypeptides of the invention.  
     [0235] Another embodiment of the invention is a method for inhibiting fatty acid uptake in a mammal (e.g., a human), comprising administering to the mammal a therapeutically effective amount of an inhibitor of the transport function of one or more of the fatty acid transport proteins, thereby decreasing fatty acid uptake by cells comprising the fatty acid protein(s). Where it is desirable to reduce the uptake of fatty acids, for example, in the treatment of chronic obesity or as a part of a program of weight control or hyperlipidemia control in a human, one or more inhibitors of one or more of the fatty acid transport proteins can be administered in an effective dose, and by an effective route, for example, orally, or by an indwelling device that can deliver doses to the small intestine. The inhibitor can be one identified by methods described herein, or can be one that is, for instance, structurally related to an inhibitor identified by methods described herein (e.g., having chemical adducts to better stabilize or solubilize the inhibitor). The invention further relates to compositions comprising inhibitors of fatty acid uptake in a mammal, which may further comprise pharmaceutical carriers suitable for administration to a subject mammal, such as sterile solubilizing or emulsifying agents.  
     [0236] A further embodiment of the present invention is a method of enhancing or increasing fatty acid uptake, such as enhancing or increasing LCFA uptake in the small intestine (e.g., to treat or prevent a malabsorption syndrome or other wasting condition) or in the liver (e.g., by an enhancer of FATP5 transport activity to treat acute liver failure) or in the kidney (e.g., by an enhancer of FATP2 transport activity to treat kidney failure). In this embodiment, a therapeutically effective amount of an enhancer of the transport function of one or more of the fatty acid transport proteins can be administered to a mammalian subject, with the result that fatty acid uptake in the small intestine is enhanced. In this embodiment, one or more enhancers of one or more of fatty acid transport proteins is administered in an effective dose and by a route (e.g., orally or by a device, such as an indwelling catheter or other device) which can deliver doses to the gut. The enhancer of FATP function (e.g., an enhancer of FATP4 function) can be identified by methods described herein or can be one that is structurally similar to an enhancer identified by methods described herein.  
     [0237] Aerobic reperfusion of ischemic myocardium is a common clinical event which can occur during such treatments as cardiac surgery, angioplasty, and thrombolytic therapy after a myocardial infarction. During reperfusion, a rapid recovery of myocardial energy production is essential for the complete recovery of contractile function. Not only the extent of recovery of myocardial energy metabolism but also the type of energy substrate used by the heart during reperfusion are important determinants of functional recovery. Circulating fatty acid levels increase following acute myocardial infarction or during cardiac surgery, such that during and following ischemia the heart muscle can be exposed to very high concentrations of fatty acids (Lopaschuk, G. D. and W. C. Stanley,  Science and Medicine  (November/December 1997)). High plasma fatty acid concentrations increase the severity of ischemic damage in a number of experimental models of cardiac ischemia and have been linked to depression of mechanical function during aerobic reperfusion of previously ischemic hearts. Further data show that modifying fatty acid utilization can be beneficial for heart function in ischemia and can be a useful approach for the treatment of angina. See, e.g., Desideri and Celegon,  Am. J. Cardiol.  82(5A):50K-53K; Lopaschuk,  Am. J. Cardiol.  82(5A):14K-1 7K. Plasma fatty acid concentrations can be reduced by administering to a human subject or other mammal an effective amount of an inhibitor of a FATP such as FATP2 or FATP4, thereby providing a way of reducing fatty acid utilization by the heart.  
     [0238] In a further embodiment of the invention, a therapeutically effective amount of an inhibitor of hsFATP6 can be administered to a human patient by a suitable route, to reduce the uptake of fatty acids by cardiac muscle. This treatment is desirable in patients who are diagnosed as having, or who are at risk of, abnormal accumulations of fatty acids in the heart or a detrimentally high rate of uptake of fatty acids into the heart, because of ischemic heart disease, or following ischemia or trauma to the heart.  
     [0239] The invention further relates to antibodies that bind to an isolated or recombinant fatty acid transport protein of the FATP family, including portions of antibodies, which can specifically recognize and bind to one or more FATPs. The antibodies and portions thereof of the invention include those which bind to one or more FATPs of mouse or other mammalian species. In a preferred embodiment, the antibodies specifically bind to a naturally occurring FATP of humans. The antibodies can be used in methods to detect or to purify a protein of the present invention or a portion thereof by various methods of immunoaffinity chromatography, to inhibit the function of a protein in a method of therapy, or to selectively inactivate an active site, or to study other aspects of the structure of these proteins, for example.  
     [0240] The antibodies of the present invention can be polyclonal or monoclonal. The term antibody is intended to encompass both polyclonal and monoclonal antibodies. Antibodies of the present invention can be raised against an appropriate immunogen, including proteins or polypeptides of the present invention, such as an isolated or recombinant FATP1, FATP2, FATP3, FATP4, FATP5, FATP6, mtFATP, ceFATPa, ceFATPb, scFATP or portions thereof, or synthetic molecules, such as synthetic peptides (e.g., conjugated to a suitable carrier). Preferred embodiments are antibodies that bind to any of the following: hsFATP 1, hsFATP2, hsFATP3, hsFATP4, hsFATP5 or hsFATP6. The immunogen can be a polypeptide comprising a portion of a FATP and having at least one function of a fatty acid transport protein, as described herein.  
     [0241] The term antibody is also intended to encompass single chain antibodies, chimeric, humanized or primatized (CDR-grafted) antibodies and the like, as well as chimeric or CDR-grafted single chain antibodies, comprising portions from more than one species. For example, the chimeric antibodies can comprise portions of proteins derived from two different species, joined together chemically by conventional techniques or prepared as a single contiguous protein using, genetic engineering techniques (e.g., DNA encoding the protein portions of the chimeric antibody can be expressed to produce a contiguous protein chain. See, e.g., Cabilly et al., U.S. Pat. No. 4,816,567; Cabilly et al., European Patent No. 0,125,023 B1; Boss et al., U.S. Pat. No. 4,816,397; Boss et al., European Patent No. 0,120,694 B1; Neuberger, M. S. et al., WO 86/01533; Neuberger, M. S. et al., European Patent No. 0,194,276 B1; Winter, U.S. Pat. No. 5,225,539; Winter, European Patent No. 0,239,400 B1; Queen et al., U.S. Pat. No. 5,585,089; and Queen et al., European Patent No. EP 0 451 216 B1. See also, Newman, R. et al.,  BioTechnology,  10: 1455-1460 (1992), regarding primatized antibody, and Ladner et al., U.S. Pat. No. 4,946,778 and Bird, R. E. et al.,  Science,  242:423-426 (1988) regarding single chain antibodies.)  
     [0242] Whole antibodies and biologically functional fragments thereof are also encompassed by the term antibody. Biologically functional antibody fragments which can be used include those fragments sufficient for binding of the antibody fragment to a FATP to occur, such as Fv, Fab, Fab′ and F(ab′) 2  fragments. Such fragments can be produced by enzymatic cleavage or by recombinant techniques. For instance, papain or pepsin cleavage can generate Fab or F(ab′) 2  fragments, respectively. Antibodies can also be produced in a variety of truncated forms using antibody genes in which one or more stop codons have been introduced upstream of the natural stop site. For example, a chimeric gene encoding a F(ab′) 2  heavy chain portion can be designed to include DNA sequences encoding the CH 1  domain and hinge region of the heavy chain.  
     [0243] Preparation of immunizing antigen (whole cells comprising FATP on the cell surface or purified FATP), and polyclonal and monoclonal antibody production can be performed using any suitable technique. A variety of methods have been described (See e.g., Kohler et al.,  Nature,  256: 495-497 (1975) and  Eur. J. Immunol.  6: 511-519 (1976); Milstein et al.,  Nature  266: 550-552 (1977); Koprowski et al., U.S. Pat. No. 4,172,124; Harlow, E. and D. Lane, 1988 , Antibodies: A Laboratory Manual , (Cold Spring Harbor Laboratory: Cold Spring Harbor, N.Y.); Chapter 11 In  Current Protocols In Molecular Biology , Vol. 2 (containing supplements up through Supplement 42, 1998), Ausubel, F. M. et al., eds., (John Wiley &amp; Sons: New York, N.Y.)). Generally, a hybridoma can be produced by fusing a suitable immortal cell line (e.g., a myeloma cell line such as SP2/0) with antibody producing cells. The antibody producing cells, preferably those obtained from the spleen or lymph nodes, can be obtained from animals immunized with the antigen of interest. Immunization of animals can be by introduction of whole cells comprising fatty acid transport protein on the cell surface. The fused cells (hybridomas) can be isolated using selective culture conditions, and cloned by limiting dilution. Cells which produce antibodies with the desired specificity can be selected by a suitable assay (e.g., ELISA).  
     [0244] Other suitable methods of producing or isolating antibodies (including human antibodies) of the requisite specificity can used, including, for example, methods which select recombinant antibody from a library (e.g., Hoogenboom et al., WO 93/06213; Hoogenboom et al., U.S. Pat. No. 5,565,332; WO 94/13804, published Jun. 23, 1994; and Dower, W. J. et al., U.S. Pat. No. 5,427,908), or which rely upon immunization of transgenic animals (e.g., mice) capable of producing a full repertoire of human antibodies (see e.g., Jakobovits et al.,  Proc. Natl. Acad. Sci. USA,  90: 2551-2555 (1993); Jakobovits et al.,  Nature,  362:255-258 (1993); Lonberg et al., U.S. Pat. No. 5,569,825; Lonberg et al., U.S. Pat. No. 5,545,806; Surani et al., U.S. Pat. No. 5,545,807; and Kucherlapati, R. et al., European Patent No. EP 0 463 151 B1).  
     [0245] Another aspect of the invention is a method for directing an agent to cardiac muscle. The differential expression of FATP6 in cardiac muscle but not in other tissue types allows for the specific targeting of drugs, diagnostic agents, tagging labels, histological stains or other substances specifically to cardiac muscle. A targeting vehicle can be used for the delivery of such a substance. Targeting vehicles which bind specifically to FATP6 can be linked to a substance to be delivered to the cells of cardiac muscle. The linkage can be, for instance, via one or more covalent bonds, or by high affinity non-covalent bonds. A targeting vehicle can be an antibody, for instance, or other compound (e.g., a fatty acid or fatty acid analog) which binds to FATP6 with high specificity.  
     [0246] Targeting vehicles specific to the heart-specific protein FATP6 have in vivo (e.g., therapeutic and diagnostic) applications. For example, an antibody which specifically binds to FATP6 can be conjugated to a drug to be targeted to the heart (e.g., a cardiac glycoside to treat congestive heart failure, or β-adrenergic agents, sodium channel blockers or calcium channel blockers to treat arrhythmias). A substance (e.g., a radioactive substance) which can be detected (e.g., a label) in vivo can also be linked to a targeting vehicle which specifically binds to a heart-specific protein such as FATP6, and the conjugate can be used as a labeling agent to identify cardiac muscle cells.  
     [0247] Targeting vehicles specific to FATP6 find further applications in vitro. For example, an FATP6-specific targeting vehicle, such as an antibody (a polyclonal preparation or monoclonal) which specifically binds to FATP6, can be linked to a substance which can be used as a stain for a tissue sample (e.g., horseradish peroxidase) to provide a method for the identification of cardiac muscle in a sample, as can be used in embryology studies, for example.  
     [0248] In a similar manner, an agent can be directed to the liver of a mammal, as FATP5 is expressed in liver but not in other tissue types. A targeting vehicle which specifically binds to FATP5 can be conjugated to a drug for delivery of the drug to the liver, such as a drug to treat hepatitis, Wilson&#39;s disease, lipid storage diseases and liver cancer. As with targeting vehicles specific to FATP6, targeting vehicles specific to FATP5 can be used in studying tissue samples in vitro.  
     [0249] The invention also relates to compositions comprising a modulator of FATP function. The term “modulate” as used herein refers to the ability of a molecule to alter the function of another molecule. Thus, modulate could mean, for example, inhibit, antagonize, agonize, upregulate, downregulate, induce, or suppress. A modulator has the capability of altering function of its target. Such alteration can be accomplished at any stage of the transcription, translation, expression or function of the protein, so that, for example, modulation of a target gene can be accomplished by modulation of the DNA or RNA encoding the protein, and the protein itself.  
     [0250] Antagonists or agonists (inhibitors or enhancers) of the FATPs of the invention, antibodies that bind a FATP, or mimetics of a FATP can be employed in combination with a non-sterile or sterile carrier or carriers for use with cells, tissues or organisms, such as a pharmaceutical carrier suitable for administration to a mammalian subject. Such compositions comprise, for instance, a media additive or a therapeutically effective amount of an inhibitor or enhancer compound to be identified by an assay of the invention and a pharmaceutically acceptable carrier or excipient. Such carriers may include, but are not limited to, saline, buffered saline, dextrose, water, ethanol, surfactants, such as glycerol, excipients such as lactose and combinations thereof. The formulation can be chosen by one of ordinary skill in the art to suit the mode of administration. The chosen route of administration will be influenced by the predominant tissue or organ location of the FATP whose function is to be inhibited or enhanced. For example, for affecting the function of FATP4, a preferred administration can be oral or through a tube inserted into the stomach (e.g., direct stomach tube or nasopharyngeal tube), or through other means to accomplish delivery to the small intestine. The invention further relates to diagnostic and pharmaceutical packs and kits comprising one or more containers filled with one or more of the ingredients of the aforementioned compositions of the invention.  
     [0251] Compounds of the invention which are FATPs, FATP fusion proteins, FATP mimetics, FATP gene-specific antisense poly- or oligonucleotides, inhibitors or enhancers of a FATP may be employed alone or in conjunction with other compounds, such as therapeutic compounds. The pharmaceutical compositions may be administered in any effective, convenient manner, including administration by topical, oral, anal, vaginal, intravenous, intraperitoneal, intramuscular, subcutaneous, intranasal, transdermal or intradermal routes, among others. In therapy or as a prophylactic, the active agent may be administered to an individual as an injectable composition, for example as a sterile aqueous dispersion, preferably isotonic.  
     [0252] Alternatively, the composition may be formulated for topical application, for example, in the form of ointments, creams, lotions, eye ointments, eye drops, ear drops, mouthwash, impregnated dressings and sutures and aerosols, and may contain appropriate conventional additives, including, for example, preservatives, solvents to assist drug penetration, and emollients in ointments and creams. Such topical formulations may also contain compatible conventional carriers, for example cream or ointment bases, and ethanol or oleyl alcohol for lotions.  
     [0253] In addition, the amount of the compound will vary depending on the size, age, body weight, general health, sex, and diet of the host, and the time of administration, the biological half-life of the compound, and the particular characteristics and symptoms of the disorder to be treated. Adjustment and manipulation of established dose ranges are well within the ability of those of skill in the art.  
     [0254] A further aspect of the invention is a method to identify a polymorphism, or the presence of an alternative or variant allele of a gene in the genome of an organism (of interest here, genes encoding FATPs). As used herein, polymorphism refers to the occurrence of two or more genetically determined alternative sequences or alleles in a population. A polymorphic locus may be as small as a base pair. Polymorphic markers include restriction fragment length polymorphisms, variable number of tandem repeats (VNTR&#39;s), hypervariable regions, minisatellites, dinucleotide repeats, trinucleotide repeats, tetranucleotide repeats, simple sequence repeats, and insertion elements such as Alu. The first identified alleleic form, or the most frequently occurring form can be arbitrarily designated as the reference (usually, “wildtype”) form, and other allelic forms are designated as alternative (sometimes, “mutant” or “variant”). Dipolid organisms may be homozygous or heterozygous for allelic forms.  
     [0255] An “allele” or “allelic sequence” is an alternative form of a gene which may result from at least one mutation in the nucleotide sequence. Alleles may result in altered mRNAs or polypeptides whose structure or function may or may not be altered. Any given gene may have none, one, or many allelic forms (polymorphism). Common mutational changes which give rise to alleles are generally ascribed to natural deletions, additions, or substitutions of nucleotides. Each of these types of changes may occur alone, or in combination with the others, one or more times in a given sequence.  
     [0256] Several different types of polymorphisms have been reported. A restriction fragment length polymorphism (RFLP) is a variation in DNA sequence that alters the length of a restriction fragment (Botstein et al.,  Am. J. Hum. Genet.  32:314-331 (1980)). The restriction fragment length polymorphism may create or delete a restriction site, thus changing the length of the restriction fragment. RFLPs have been widely used in, human and animal genetic analyses (see WO 90/13668; WO 90/11369; Donis-Keller,  Cell  51:319-337 (1987); Lander et al.,  Genetics  121:85-99 (1989)). When a heritable trait can be linked to a particular RFLP, the presence of the RFLP in an individual can be used to predict the likelihood that the individual will also exhibit the trait.  
     [0257] Other polymorphisms take the form of short tandem repeats (STRs) that include tandem di-, tri- and tetra-nucleotide repeated motifs. These tandem repeats are also referred to as variable number tandem repeat (VNTR) polymorphisms. VNTRs have been used in identity and paternity analysis (U.S. Pat. No. 5,075,217; Armour et al.,  FEBS Lett.  307:113-115 (1992); Horn et al., WO 91/14003; Jeffreys, EP 370,719), and in a large number of genetic mapping studies.  
     [0258] Other polymorphisms take the form of single nucleotide variations between individuals of the same species. Such polymorphisms are far more frequent than RFLPs, STRs (short tandem repeats) and VNTRs (variable number tandem repeats). Some single nucleotide polymorphisms occur in protein-coding sequences, in which case, one of the polymorphic forms may give rise to the expression of a defective or other variant protein and, potentially, a genetic disease. Other single nucleotide polymorphisms occur in noncoding regions. Some of these polymorphisms may also result in defective protein expression (e.g., as a result of defective splicing). Other single nucleotide polymorphisms have no phenotypic effects.  
     [0259] Many of the methods described below require amplification of DNA from target samples and purification of the amplified products. This can be accomplished by PCR, for instance. See generally,  PCR Technology, Principles and Applications for DNA Amplification  (ed. H. A. Erlich), Freeman Press, New York, N.Y., 1992 ; PCR Protocols. A Guide to Methods and Applications  (eds. Innis, et al.), Academic Press, San Diego, Calif., 1990; Mattila et al.,  Nucleic Acids Res.  19:4967 (1991); Eckert et al.,  PCR Methods and Applications  1:17 (1991); PCR (eds. McPherson et al., IRS Press, Oxford); and U.S. Pat. No. 4,683,202.  
     [0260] Other suitable amplification methods include the ligase chain reaction (LCR) (see Wu and Wallace,  Genomics  4:560 (1989); Landegren et al.,  Science  241:1077 (1988)), transcription amplification (Kwoh et al.,  Proc. Natl. Acad. Sci. USA  86:1173 (1989), self-sustained sequence replication (Guatelli et al.,  Proc. Natl. Acad. Sci. USA  87:1874 (1990), and nucleic acid based sequence amplification (NASBA). The latter two amplification methods involve isothermal reactions based on isothermal transcription, which produce both single stranded RNA (ssRNA) and double stranded DNA (dsDNA) as the amplification products in a ratio of about 30 or 100 to 1, respectively.  
     [0261] Another aspect of the invention is a method for detecting a variant allele of a human FATP gene, comprising preparing amplified, purified FATP DNA from a reference human and amplified, purified, FATP DNA from a “test” human to be compared to the reference as having a variant allele, using the same or comparable amplification procedures, and determining whether the reference DNA and test DNA differ in DNA sequence in the FATP gene, whether in a coding or a noncoding region, wherein, if the test DNA differs in sequence from the reference DNA, the test DNA comprises a variant allele of a human FATP gene. The following is a discussion of some of the methods by which it can be determined whether the reference FATP DNA and test FATP DNA differ in sequence.  
     [0262] Direct Sequencing.  
     [0263] The direct analysis of the sequence of variant alleles of the present invention can be accomplished using either the dideoxy chain termination method or the Maxam and Gilbert method (see Sambrook et al.,  Molecular Cloning: A Laboratory Manual,  2nd ed., Cold Spring Harbor Press, New York 1989; Zyskind et al.,  Recombinant DNA Laboratory Manual , Acad. Press, 1988)).  
     [0264] Denaturing Gradient Gel Electrophoresis.  
     [0265] Amplification products generated using the polymerase chain reaction can be analyzed by the use of denaturing gradient gel eletrophoresis. Different alleles can be identified based on the different sequence-dependent strand dissociation properties and electrophoretic migration of DNA in solution (chapter 7 in Erlich, ed.  PCR Technology, Principles and Applications for DNA Amplification , W. H. Freeman and Co., New York, 1992).  
     [0266] Single-Strand Conformation Polymorphism Analysis.  
     [0267] Alleles of target sequences can be differentiated using single-strand conformation polymorphism analysis, which identifies base differences by alteration in electrophoretic migration of single stranded PCR products, as described in Orita et al.,  Proc. Natl. Acad. Sci. USA  86:2766-2770 (1989). Amplified PCR products can be generated as described above, and heated or otherwise denatured, to form single-stranded amplification products. Single-stranded nucleic acids may refold or form secondary structures which are partially dependent on the base sequence. The different electrophoretic mobilities of single-stranded amplification products can be related to base-sequence differences between alleles of target sequences.  
     [0268] Detection of Binding by Protein that Binds to Mismatches.  
     [0269] Amplified DNA comprising the FATP gene or portion of the gene of interest from genomic DNA, for example, of a normal individual is prepared, using primers designed on the basis of the DNA sequences provided herein. Amplified DNA is also prepared, in a similar manner, from genomic DNA of an individual to be tested for bearing a distinguishable allele. The primers used in PCR carry different labels, for example, primer 1 with biotin, and primer 2 with  32 P. Unused primers are separated from the PCR products, and the products are quantitated. The heteroduplexes are used in a mismatch detection assay using immobilized mismatch binding protein (MutS) bound to nitrocellulose. The presence of biotin-labeled DNA wherein mismatched regions are bound to the nitrocellulose via MutS protein, is detected by visualizing the binding of streptavidin to biotin. See WO 95/12689. MutS protein has also been used in the detection of point mutations in a gel-mobility-shift assay (Lishanski, A. et al.,  Proc. Natl. Acad. Sci. USA  91:2674-2678 (1994)).  
     [0270] Other methods, such as those described below, can be used to distinguish a FATP allele from a reference allele, once a particular allele has been characterized as to DNA sequence.  
     [0271] Allele-Specific Probes.  
     [0272] The design and use of allele-specific probes for analyzing polymorphims is described by e.g., Saiki et al.,  Nature  324:163-166 (1986); Dattagupta, EP 235,726, Saiki, WO 89/11548. Allele-specific probes can be designed so that they hybridize to a segment of a target DNA from one individual but do not hybridize to the corresponding segment from another individual due to the presence of different polymorphic forms in the respective segments from the two individuals. Hybridization conditions should be sufficiently stringent that there is a significant difference in hybridization intensity between alleles, and preferably an essentially binary response, whereby a probe hybridizes to only one of the alleles. Some probes are designed to hybridize to a segment of target DNA such that the polymorphic site aligns with a central position (e.g., in a 15-mer at the 7 position; in a 16-mer, at either the 8 or 9 position) of the probe. This design of probe achieves good discrimination in hybridization between different allelic forms.  
     [0273] Allele-specific probes are often used in pairs, one member of a pair showing a perfect match to a reference form of a target sequence and the other member showing a perfect match to a variant form. Several pairs of probes can then be immobilized on the same support for simultaneous analysis of multiple polymorphisms within the same target sequence.  
     [0274] Allele-Specific Primers.  
     [0275] An allele-specific primer hybridizes to a site on target DNA overlapping a polymorphism, and only primes amplification of an allelic form to which the primer exhibits perfect complementarity. See Gibbs,  Nucleic Acid Res.  17:2427-2448 (1989). This primer is used in conjunction with a second primer which hybridizes at a distal site. Amplification proceeds from the two primers, resulting in a detectable product which indicates the particular allelic form is present. A control is usually performed with a second pair of primers, one of which shows a single base mismatch at the polymorphic site and the other of which exhibits perfect complementarity to a distal site. The single-base mismatch prevents amplification and no detectable product is formed. The method works best when the mismatch is included in the 3′-most position of the oligonucleotide aligned with the polymorphism because this position is most destabilizing to elongation from the primer (see, e.g., WO 93/22456).  
     [0276] Gene Chips.  
     [0277] Allelic variants can also be identified by hybridization to nucleic acids immobilized on solid supports (gene chips), as described, for example, in WO 95/11995 and U.S. Pat. No. 5,143,854, both of which are incorporated herein by reference. WO 95/11995 describes subarrays that are optimized for detection of a characterized variant allele. Such a subarray contains probes designed to be complementary to a second reference sequence, which is an allelic variant of the first reference sequence.  
     [0278] The present method is illustrated by the following examples, which are not intended to be limiting in any way.  
     EXAMPLES  
     Materials and Methods  
     [0279] The following Materials and Methods were used in the work described in Examples 1-5.  
     [0280] Sequence Alignment of FATP Clones.  
     [0281] The DNA sequence for mouse FATP1 was obtained from the National Center for Biotechnology Information nonredundant database. cDNAs for mmFATP2, 3, 4, and 5 were obtained by screening mouse expression libraries (purchased from GIBCO/BRL, Rockville, Md.) with probes derived from the cloned expressed sequence tags (ESTs) (Research Genetics, Huntsville, Ala.). Full-length clones were obtained for mmFATP2 and 5 and partial sequences for mmFATP3 and 4. The sequences described herein have been deposited in the GenBank database (Accession Nos. FATP2, AF072760; FATP3, AF072759; FATP4, AF072758; FATP5, AF072757).  
     [0282] Neither FATP2 nor FATP5 contains an in-frame stop codon upstream of the putative initiator methionine; initiator methionines were assigned by homology with that in mmFATP 1 and by the presence of a signal sequence immediately after it. The  Mycobacterium tuberculosis, Caenorhabditis elegans , and  Saccharomyces cerevisiae  sequences were present in the dbEST database as part of the sequencing projects for these organisms. Sequences were aligned utilizing a ClustalX algorithm and the resulting alignment exported to SeqVu. Homologous amino acid substitutions are boxed in FIG. 1 and were determined using the Dayhoff 250 method with a 50% homology cutoff.  
     [0283] Cell Transfection and LCFA Uptake.  
     [0284] COS cells were cotransfected using the DEAE-dextran method with the mammalian expression vector pCDNA 3.1 (Invitrogen, Carlsbad, Calif.) expressing the gene for CD2 (pCDNA-CD2) in combination with either a pCDNA 3.1 or pCMVSPORT2 (GIBCO/BRL, Rockville, Md.) expression vector containing one of the murine or nematode FATP genes (pCDNA-mmFATP1, pCDNA-FATP2, pCMVSPORT-FATP5, pCDNA-ceFATPb). Two days after transfection, cells were assayed for CD2 expression with a phycoerythrin-coupled anti-CD2(PE-CD2) monoclonal antibody (PharMingen, Franklin Lakes, N.J.), and fatty acid uptake was assayed with a BODIPY-labeled fatty acid analogue (Molecular Probes). Briefly, cells were washed twice with PBS (phosphate buffered saline) and stained with PE-CD2 at 4° C. for 30 min in PBS containing 10% fetal calf serum. They were then washed three times with PBS/fetal calf serum for 5 min followed by an incubation for 2 min at 37° C. in fatty acid uptake solution, which contained 0.1 μM BODIPY-FA and 0.1% fatty acid-free BSA (bovine serum albumin) in PBS (Schaffer, J. E. &amp; Lodish, H. F. (1994)  Cell  79:427-436). After 2 min, the cells were washed four times with ice-cold PBS/0.1% BSA. The cells were then removed from the plates with PBS containing 5 mM EDTA and resuspended in PBS containing 10% fetal calf serum and 10 mM EDTA. PE-CD2 and BODIPY-FA fluorescence were measured using a FACScan (Becton Dickinson, Franklin Lakes, N.J.). COS cells were gated on forward scatter (FSC) and side scatter (SS). Cells exhibiting more than 300 CD2 fluorescence units (dsim) representing 15% of all cells were deemed CD2 positive and their BODIPY-FA fluorescence was quantitated.  
     [0285] E. coli -Based LCFA Uptake Assay.  
     [0286] The full-length coding region of mtFATP and a control protein, the mammalian transcription factor TFE3, were subcloned into the inducible, prokaryotic expression vector pET (Novagen, Madison, Wis.). Expression was induced with 1 mM isopropyl β-D-thiogalactoside (IPTG) for 1 hour, or cells were left uninduced. Cells were washed in PBS/0.1% BSA and resuspended in 1 ml PBS/0. 1% BSA containing 0.1 μM [ 3 H]palmitate (NEN) at 37° C. Uptake was stopped after the indicated incubation time by transferring the cells onto filter paper using a cell harvester (Brandel, Bethesda, Md.). Filters were washed extensively with ice-cold PBS/0.1% BSA, and [ 3 H]palmitate was quantitated by scintillation counting.  
     [0287] Northern Blots.  
     [0288] Northern blot analysis of murine FATP expression was done using poly(A) mRNA blots (Clontech, Palo Alto, Calif.). Probes of each of the FATPs were derived from the 3′ untranslated regions of each gene and were &lt;60% identical in sequence. Probes were labeled by random priming (Boehringer Mannheim, Indianapolis, Ind.) and hybridized at 65° C. Blots were extensively washed in 0.2% SSC/0.1% SDS at 65° C.  
     [0289] Generation of Phylogenetic Trees.  
     [0290] Complete and partial sequences for FATP genes from human, rat, mouse, puffer fish,  Drosophila melanogaster, C. elegans, S. cerevisiae , and  M. tuberculosis  were aligned using ClustalX. A homologous region of 48 amino acids (residues 472-519 in mmFATP1) from all of the genes was used to determine phylogenetic relationship within ClustalX. Based on these data a phylogenetic tree was generated using Tree View PPC (FIG. 5).  
     [0291] Nomenclature.  
     [0292] It is proposed that the FATP genes be given a species specific prefix (mm,  Mus musculus ; hs,  Homo sapiens ; mt,  M tuberculosis ; dm,  D. melanogaster ; ce,  C. elegans , sc,  S. cerevisiae ) and numbered such that mammalian homologues in different species share the same number but differ in their prefix. Since the two  C. elegans  genes cannot be paired with a specific human or mouse FATP, they have been designated ceFATPa and ceFATPb.  
     Example 1  
     Identification of Novel Mammalian FATPs  
     [0293] The National Center for Biotechnology Information EST database was screened, using the mouse FATP protein sequence (mmFATP1), to identify novel FATPs. This strategy led to the identification of more than 50 murine EST sequences which could be assembled into five distinct contiguous DNA sequences (contigs). One contig was identical to the previously cloned FATP, which has been renamed FATP1. Another, which has been renamed FATP2, is the murine homologue of a rat gene previously identified by others as a very long chain acyl-CoA synthase (Uchiyama, A., Aoyama, T., Kamijo, K., Uchida, Y., Kondo, N., Orii, T. &amp; Hashimoto, T. (1996)  J. Biol. Chem.  271:30360-30365). The other three contigs represented novel genes (FATP3, 4, and 5). Full-length clones for FATP2 and FATP5 and nearly complete sequences for FATP3 and 4 (FIG. 1) were obtained by screening cDNA libraries made from mouse day 10.5 embryos and adult liver. Also identified were human homologues for each of the murine genes in the EST database. A sixth human gene was also identified; whether this gene is also present in the mouse will require additional studies. Map positions are given in Tables 2 and 3.  
     [0294] The genetic loci for all of the human genes, with the exception of FATP5 which was already mapped as an unknown EST, were determined using the radiation hybrid panels. The map positions given below show the distance (in centiRays) from the closest framework marker. As a guideline, there are approximately 300 kb/cR.  
               TABLE 2                       Mapping Data for Human Genes                                                hsFATP1   Chromosome Chr19               places 13.35 cR from WI-6344 (lod &gt; 3.0)           hsFATP2   Chromosome Chr15               places 4.92 cR from D15S126 (lod &gt; 3.0)           hsFATP3   Chromosome Chr1               places 13.24 cR from WI-2862 (lod &gt; 3.0)           hsFATP4   Chromosome Chr9               places 7.80 cR from WI-9685 (lod &gt; 3.0)           hsFATP5   unknown EST previously mapped to near D19S418           hsFATP6   Chromosome Chr5               places 1.41 cR from WI-4907 (lod &gt; 3.0)                      
 
     [0295] The mouse map is an internal backcross panel consisting of 188 mouse backcross DNA&#39;s plus 4 controls (B6, Spretus, F1, Water). The backcross was constructed by crossing B6 by Spretus animals and then crossing those F1&#39;s back to B6. Mapping is accomplished by taking advantage of recombinational events during meiosis, and the use of PCR primers to detect the differences (by size or re-annealing events) at any given locus between the B6 and Spretus allele.  
     [0296] For the purposes of mapping, a novel set of primers (gene of interest) is used to amplify from all 188 DNA&#39;s and then typed as being a B6 (“B”) or a Spretus (“S”). This string of B&#39;s and S&#39;s is entered into the Map Manager program, which does a best fit calculation by comparing the string of 188 typings from the gene of interest to all loci already extant in the panel, for all 20 chromosomes. The gene of interest is then assigned to a particular area on a particular chromosome according to a number of parameters, including the minimalization of double cross-overs, and the highest LOD scores. Indicated in Table 3 are distances to the closest markers on either side of the FATP locus.  
               TABLE 3                       Mapping Data for Mouse Genes                                        mmFATP1   Chromosome 8           places 2.82 cM from D8Mit132 (lod 43.4) and 1.81 cM           from D8Mit74 (lod 43.5)       mmFATP2   Chromosome 2           places 1.29 cM from D2Mit258 (lod 47.9) and 1.75 cM           from D2NDS3 (lod 44.9)       mmFATP3   Chromosome 3           places 2.54 cM from D3Mit22 (lod 29.5) and 19.62 cM           from D3Mit42 (lod 13.6)       mmFATP4   Chromosome 2           places 13.78 cM from D2Mit1 (lod 22.9) and 3.85 cM           from D2Mit65 (lod 41.9)       mmFATP5   Chromosome 7           places 7.28 cM proximal of D7Mit21 (lod 28.3)                  
 
     Example 2  
     Assessment of Function  
     [0297] The ability of the newly identified mouse genes to function as fatty acid transporters was assessed using a fluorescence-activated cell sorting-based assay. COS cells were transiently cotransfected with expression vectors encoding the cell surface protein CD2 and either mmFATP1, mmFATP2, or mmFATP5, respectively. Two days after transfection, COS cells were stained with an antibody to CD2 and then incubated with a BODIPY-labeled fatty acid [BODIPY-FA, (Schaffer, J. E. &amp; Lodish, H. F. (1994)  Cell  79:427-436)]. The cells were then washed extensively, lifted off the dish, and analyzed by fluorescence-activated cell sorting. As judged by the number of CD2-positive cells, the transfection efficiency was approximately 20-30%. Fatty acid uptake was quantitated in the transiently transfected COS cells by measuring the BODIPY-FA fluorescence of the CD2-positive cells. Expression of CD2 had no effect on fatty acid uptake as shown by the finding that COS cells expressing only the transfected CD2 cDNA (CD2-positive) had the same low level of BODIPY-FA uptake as did untransfected (CD2-negative) control cells (FIG. 2A, control). In COS cells cotransfected with CD2 and mmFATP1, mmFATP2, or mmFATP5, uptake of BODIPY-FA by the transfected (CD2-positive) cells was increased between 15- to 90-fold over control (CD2 cDNA only) cells (FIGS.  2 A- 2 D).  
     Example 3  
     Expression Patterns of Murine FATPs  
     [0298] Expression patterns of members of the murine FATP gene family were characterized by Northern blot analysis; to avoid cross-hybridization, the probes used were from the 3′ untranslated region of these genes, which are less than 60% identical in sequence. The expression pattern of FATP1 agrees with that previously found (Schaffer, J. E. &amp; Lodish, H. F. (1994)  Cell  79:427-436). Here, expression was seen primarily in heart and kidney. FATP2 is expressed almost exclusively in liver and kidney, which corresponds to the reported tissue distribution of the rat homologue [very long chain acyl-CoA (VLACS)] as assessed by Western blotting (Uchiyama, A., Aoyama, T., Kamijo, K., Uchida, Y., Kondo, N., Orii, T. &amp; Hashimoto, T. (1996)  J. Biol. Chem.  271:30360-30365). FATP3 is present in lung, liver, and testis. FATP5 is expressed only in liver and cannot be detected in other tissues even when the blot is overexposed. The human homologue of FATP5 is also liver specific and is not expressed in a wide array of other tissues tested, including fetal liver.  
     Example 4  
     FATPs Are Evolutionarily Conserved  
     [0299] The EST database was searched, using sequences conserved among the five murine FATP genes, for FATP genes in other organisms. Two homologues were found in  C. elegans  and one in  M. tuberculosis . One of the  C. elegans  genes was cloned from a cDNA library and expressed in COS cells, as described for the murine FATPs. Overexpression of the nematode FATP resulted in a 15-fold increase of BODIPY-FA uptake compared with control cells (FIG. 3). The mycobacterial FATP gene was isolated from a phage library and assessed for its ability to facilitate fatty acid uptake.  E. coli  transformed with a prokaryotic, isopropyl P-D-thiogalactoside-inducible expression vector containing the mycobacterial FATP gene demonstrated a significant increase in the rate of [ 3 H]palmitate uptake after induction, compared with uninduced bacteria or  E. coli  transformed with a control protein (FIG. 4). Novel FATP genes were also identified in  F. rubripes  (puffer fish) and  D. melanogaster.    
     Example 5  
     Phylogenetic Tree of FATPs  
     [0300] Faergeman et al. (Faergeman, N. J., DiRusso. C. C., Elberger, A., Knudsen, J. &amp; Black, P. N. (1997)  J. Biol. Chem.  272:8531-8538) identified three regions of very strong conservation between the scFATP and mmFATP1 genes. The sequences of the FATPS were compared over a 311-amino acid FATP “signature sequence” which includes these conserved regions corresponding to amino acids 246-557 in mmFATP1 (underlined in FIG. 1). When compared with the National Center for Biotechnology Information nonredundant database, only one region of the “FATP signature sequence” shows significant homology to other proteins. This small stretch of amino acids (underlined in FIG. 1) is an AMP-binding motif found in a multitude of other proteins, such as acyl-CoA synthase, several CoA lipases, and gramicidin S synthetase component II (Schaffer, J. E. &amp; Lodish, H. F. (1994)  Cell  79:427-436). The relevance of this motif to fatty acid transport is unclear. Other highly conserved regions among the FATPs, including long stretches of amino acids &gt;90% identical from mycobacteria to humans, are not found in any other class of proteins. A 48-amino acid segment of the FATP signature sequence was used to construct a phylogenetic tree (FIG. 5). Each of the human and mouse genes form their own branch; hsFATP6, which as yet has no murine homologue, is most closely related to hsFATP3 and mmFATP3. As expected, mVLACS is closer in sequence to mmFATP2 than to hsFATP2. The FATP genes of invertebrates i.e.,  C. elegans  and  D. melanogaster , are most closely related to each other. Surprisingly, the mycobacteral gene is more closely related to the human and mouse FATP5 genes than to the FATPs of any of the lower organisms. Whether this reflects coevolution of the mycobacterial and human genes awaits further study.  
     [0301] Materials and Methods  
     [0302] The following materials and methods were used in the work described in Examples 6-10.  
     [0303] Isolation of full-length human FATP 1 and 4  
     [0304] Full-length clones encoding human FATP1 and human FATP4 were identified by searching databases for sequences similar to murine FATP1-5 coding regions using the BlastX algorithm (Altschul et al.,  J. Mol. Biol.  215: 403-410, 1990).  
     [0305] A concatamer of nucleotide sequences comprising the coding sequences of mmFATP1 (Genbank Accession U15976), mmFATP2, mmFATP3 (SEQ ID NO:6), mmFATP4 (SEQ ID NO:8) and mmFATP5 (SEQ ID NO:10) was used to search the Millennium database using the BLASTX algorithm. Sequences with a score &gt;150 were evaluated for whether they represented known FATP coding sequences.  
     [0306] Human clones with similarity to the 5′ end of murine FATP sequences were sequenced completely. Clones encoding full-length human FATP1 were obtained from a heart cDNA library constructed in the mammalian expression vector pMET7 (Tartaglia et al.,  Cell,  83: 1263-1271, 1995). Clones encoding full-length human FATP4 were obtained from a spleen cDNA library constructed in the mammalian expression vector pMET7.  
     [0307] Isolation of Full-Length Human FATP6  
     [0308] Several clones encoding human FATP6 were identified by searching public databases as described above. Five clones were analyzed further by restriction digestion and DNA sequencing. One of these clones (Genbank Accession # AA412064) appeared to be full-length and its entire insert was sequenced.  
     [0309] DNA Sequence Analysis  
     [0310] Sequences were aligned with the DNAStar program using the Clustal method. Hydrophobicity plots were generated with DNA Strider using the Kyte Doolittle method.  
     [0311] In situ Hybridization  
     [0312] Tissues were collected from 8 week old C57/B16 mice. Tissues were fresh frozen, cut on a cryostat at 10 μm thickness and mounted on Superfrost Plus slides (VWR). Sections were air dried for 20 minutes and then incubated with ice cold 4% paraformaldehyde (PFA)/phosphate buffered saline (PBS) for 10 minutes. Slides were washed 2 times 5 minutes with PBS, incubated with 0.25% acetic anhydride/1 M triethanolamine for 10 minutes, washed with PBS for 5 minutes and dehydrated with 70%, 80%, 95% and 100% ethanol for 1 minute each. Sections were incubated with chloroform for 5 minutes. Hybridizations were performed with  35 S-radiolabeled (5×10 7  cpm/ml) cRNA probes generated from the 3′ untranslated regions of mouse FATPs by PCR followed by in vitro transcription in the presence of 50% formamide, 10% dextran sulfate, 1× Denhardt&#39;s solution, 600 mM NaCl, 10 mM DTT, 0.25% SDS and 10 μg/ml tRNA for 18 hours at 55° C. After hybridization, slides were washed with 10 mM Tris-HC1 pH 7.6, 500 mM NaCl, 1 mM EDTA (TNE) for 10 minutes, incubated in 40 μg/ml RNase A in TNE at 37° C. for 30 minutes, washed in TNE for 10 minutes, incubated once in 2× SSC at 60° C. for 1 hour, once in 0.2× SSC at 60° C. for 1 hour, once in 0.2× SSC at 65° C. for 1 hour and dehydrated with 50%, 70%, 80%, 90% and 100% ethanol. Localization of mRNA transcripts was detected by dipping slides in Kodak NBT-2 photoemulsion and exposing for 7 days at 4° C., followed by development with Kodak Dektol developer. Slides were counter stained with haematoxylon and eosin and photographed. Controls for the in situ hybridization experiments include the use of a sense probe which showed no signal above background in all cases.  
     [0313] Northern Blotting  
     [0314] Human mRNA blots were obtained from Invitrogen or Clontech. PCR fragments from the 3′ untranslated regions of human FATPs were used as probes. Blots were probed with  32 P-labeled DNA probes using the Rapid-Hyb buffer (Amersham, Buckinghamshire, UK) according to the manufacturer&#39;s instructions.  
     [0315] Cell transfection and LCFA uptake. COS cells were cotransfected, using lipofectamine (GIBCO BRL, Rockville, Md.) according to the manufacturer&#39;s instructions, with the mammalian expression vector pCDNA3.1 (Invitrogen, Carlsbad, Calif.) expressing the gene for CD2 in combination with a pMET7 expression vector (Tartaglia et al.,  Cell,  83:1263-1271, 1995) containing hsFATP1 (pMET7-hsFATP1) or hsFATP4 (pMET7-hsFATP4) or pMET7 alone. Two days after transfection, cells were assayed for CD2 expression with a phycoerythrin-coupled anti-CD2 (PE-CD2) monoclonal antibody (PharMingen, Franklin Lakes, N.J.), and fatty acid uptake was assayed with a BODIPY-labeled fatty acid analog (Molecular Probes) as described above.  
     Example 6  
     Determination of Expression of mmFATPs  
     [0316] mmFATP4, and to lesser extent mmFATP2, are expressed at high levels in the brush border layer of the small intestine.  
     [0317] Cell transfection and LCFA uptake. COS cells were cotransfected, using lipofectamine (GIBCO BRL, Rockville, Md.) according to the manufacturer&#39;s instructions, with the mammalian expression vector pCDNA3.1 (Invitrogen, Carlsbad, Calif.) expressing the gene for CD2 in combination with a pMET7 expression vector (Tartaglia et al.,  Cell,  83:1263-1271, 1995) containing hsFATP1 (pMET7-hsFATP1) or hsFATP4 (pMET7-hsFATP4) or pMET7 alone. Two days after transfection, cells were assayed for CD2 expression with a phycoerythrin-coupled anti-CD2 (PE-CD2) monoclonal antibody (PharMingen, Franklin Lakes, N.J.), and fatty acid uptake was assayed with a BODIPY-labeled fatty acid analog (Molecular Probes) as described above.  
     [0318] Absorption of dietary fat requires transport of free fatty acids across the apical membrane of epithelial cells in the small intestine. Previous studies suggested that this transport is protein-mediated; however, the transport protein had not yet been identified. In situ hybridization was performed on each of the three regions of the small intestine—duodenum, jejunum and ileum—as well as the colon, using probes from the 3′ untranslated regions of mmFATP1, mmFATP2, mmFATP3, mmFATP4 and mmFATP5, to determine whether any of the mouse FATPs are expressed in the small intestine. It was expected that a protein involved in fatty acid absorption would be expressed in the epithelial cells of the small intestine, but absent from the colon.  
     [0319] Expression of mmFATPs in the jejunum was identical to that in the ileum in all cases. High levels of mmFATP4 mRNA were present in the epithelial cells of the jejunum and ileum, and lower, but significant, amounts were detected in the epithelial cells of the duodenum. Significantly, FATP4 mRNA was absent from other cell types of the small intestine and no FATP4 mRNA could be detected in any of the cells of the colon. FATP2 mRNA was present in the epithelial cells of the duodenum at a level similar to that of FATP4, but was present at lower levels in the jejunum and ileum. No signals above background were detected for mmFATP1, mmFATP3 and mmFATP5 in any of the intestinal tissues. mmFATP3 and FATP5 were clearly detectable by in situ hybridization in adult liver and mmFATP1 could be detected in a variety of tissues on a whole embryo in situ, indicating that the FATP1, 3, and 5 probes were working.  
     [0320] mmFATP4 expression is predominant in the small intestine compared to the other organs of the mouse embryo. In the small intestine, FATP4 expression is limited to differentiated enterocytes, while no signal is detected in the connective tissue or the undifferentiated epithelial cells in the crypts. Differentiated enterocytes are known to be the cells that mediate the uptake of fatty acids. FATP4 is specifically and strongly expressed in the epithelial cells of adult murine duodenum and ileum but not colon. Other FATPs, such as FATP5, are not expressed in the small intestine. Thus, FATP4 is the major FATP in the mouse small intestine. Given its high level of expression, it is likely that FATP4, and to a lesser extent FATP2, play an important role in the absorption of fatty acids.  
     [0321] mmFATP2, and mmFATP5 are Expressed in Hepatocytes  
     [0322] Northern analysis of mmFATP2, mmFATP3, mmFATP4 and mmFATP5 showed expression in the liver. To determine whether these proteins are present in hepatocytes or other cells types present in liver homogenates, in situ hybridizations were performed. mmFATP2, and mmFATP5 mRNA was clearly present in hepatocytes, and was not concentrated in other cell types such as endothelial cells or macrophages. No signal above background was detected for mmFATP 1 in any of the cell types in the liver, consistent with the results of the Northern blotting.  
     Example 7  
     Isolation and Sequence Analysis of Full-Length Human FATP 1 and Full-Length Human FATP4  
     [0323] To identify human cDNA clones encoding FATP family members, Millennium databases were searched for sequences similar to murine FATP1-5 coding regions. Two clones were. analyzed in detail; inspection of the entire DNA sequence of these two clones showed that they encode the human orthologs of mmFATP1 and mm FATP4, respectively. These two clones were designated hsFATP1 and hsFATP4, and their DNA and predicted protein sequences are shown in FIGS.  44 A- 44 C and  45 , and  50 A- 50 C and  51 . hsFATP1 is predicted to encode a 646 amino acid, 71 kD protein with multiple membrane-spanning domains (FIG. 28A). HsFATP4 is predicted to encode a 643 amino acid, 72 kD protein with multiple membrane spanning domains (See FIG. 29A). A comparison of the DNA sequences of mouse and human FATP1 and mouse and human FATP4 (FIGS.  30 A- 30 B and  31 A- 31 B) shows that the mouse and human orthologs are 85% (FATP1) and 87% (FATP4) identical to each other within the coding sequences given in these figures. At the amino acid level, hsFATP1 and hsFATP4 are ˜90% identical to their respective mouse orthologs within the coding region shown in these figures (FIGS. 32 and 33). The sequence identities between mouse and human FATP1 and FATP4 are considerably higher than the ones observed between different FATP family members within one species (˜40%-60%) and are present in the N-terminal part of the protein, a region that is poorly conserved between different FATP family members. This high degree of sequence conservation clearly demonstrates that the newly identified human FATPs are orthologs of mouse FATP1 and FATP4 rather than novel FATP family members.  
     [0324] Table 4 is an identity/similarity matrix comparing the amino acid sequences of FATP1 and 4 from human and mouse. This shows that the gene whose sequence is shown in FIG. 43A is indeed human FATP4, since it is 91% identical with the murine FATP4 but only 62% identical with the closest related human FATP, which is FATP1.  
               TABLE 4                          Identity/Similarity Matrix                                     hsFATP4   mmFATP4   hsFATP1   mmFATP1                                             hsFATP4   —   93.2   72.3   72.0       mmFATP4   91.0   —   71.2   71.1       hsFATP1   61.9   61.0   —   92.4       mmFATP1   60.7   59.6   89.5   —                  
 
     Example 8  
     Isolation and Sequence Analysis of Full-Length Human FATP6  
     [0325] A search of EST databases identified a set of overlapping human sequences that were similar to FATPs, but did not have a clear mouse ortholog. One of these EST clones was found to encode a full-length cDNA. The entire insert of this clone was sequenced and designated hsFATP6. The DNA and predicted protein sequences of hsFATP6 are shown in FIGS.  54 A- 54 C and  55 . HsFATP6 is predicted to encode a 619 amino acid, 70 kD protein with multiple membrane-spanning domains (FIG. 35A). A comparison of the amino acid sequences of hsFATP6 with other human FATPs shows about 37% identity to either hsFATP1 or hsFATP4 (FIG. 36). This degree of sequence identity is similar to what is observed between different mouse FATPs. The phylogenetic analysis described above clearly demonstrates that hsFATP6 is a member of the FATP family, but not an ortholog of any of the mouse FATPs. Comparisons were done with “ALIGN” (E. Myers and W. Miller, “Optimal Alignments in Linear Space,”  CABIOS  4:11-17 (1988) using standard settings.  
     Example 9  
     Tissue Distribution of Human FATPs  
     [0326] The tissue distribution of human FATPs was assessed by Northern blotting. Human FATP3 was expressed in a large variety of tissues. In contrast, human FATP5 was present at high levels in the liver, but was undetectable in all other tissues examined. Thus, both hsFATP3 and hsFATP5 recapitulate the expression pattern of their mouse orthologs (see above). HsFATP6 is a novel FATP with no mouse ortholog as yet. Northern blotting shows that hsFATP6 is expressed at high levels in the heart, but is undetectable in other tissues, including skeletal and smooth muscle. This tissue distribution suggests that human FATP6 performs an important role in energy metabolism in the heart; blocking FATP6-mediated fatty acid transport may therefore be beneficial for a number of heart diseases, e.g., ischemic heart disease.  
     [0327] To identify the major FATP expressed in the human small intestine, Northern blotting was performed on a blot containing mRNA from human stomach, jejunum, ileum, colon, rectum and lung. hsFATP5 and hsFATP6 were undetectable in any of these tissues. FATP5 is only expressed in liver and FATP6 only in heart. hsFATP2 was weakly expressed in the colon, and an even weaker signal was detectable in jejunum, ileum and lung lanes. hsFATP3 was expressed well in the lung, but was only weakly expressed in the other tissues tested. Importantly, no difference was seen in the expression of hsFATP3 between small intestine and stomach or colon, suggesting that the expression observed is not related to fatty acid absorption in the small intestine. hsFATP4 was clearly expressed in both jejunum and ileum; expression was significantly lower in the colon and was absent in the stomach. This expression pattern is consistent with a major role for FATP4 in absorption of fatty acids in the human gut.  
     Example 10  
     Expression of hsFATP1 and hsFATP4 Promotes Transport of Fatty Acids  
     [0328] COS cells were cotransfected using lipofectamine with the mammalian expression vector pCDNA-CD2 in combination with one of the FATP-containing expression vectors (pMET7-hsFATP1 or pMET7-hsFATP4) or an insertless expression vector (pMET7, control) as described in Materials and Methods for Examples 6-10. COS cells were gated on forward scatter and side scatter. Cells exhibiting more than 400 CD2 fluorescence units representing −30% of all cells were deemed CD2-positive. The percent of CD2-positive cells exhibiting a BODIPY-fluorescence of &gt;300 is plotted for the three different vectors tested (FIG. 37).  
     Example 11  
     Stable Expression of Human FATP4 in 293 Cells  
     [0329] Stable cell lines were generated as follows. A DNA fragment containing the entire hsFATP4 coding sequence as well as 100 nucleotides of 5′ and 50 nucleotides of 3′ untranslated region was inserted into the vector pIRES-neo (Clontech, Palo Alto, Calif.) using standard cloning techniques. The resulting construct or a vector control (pIRES-neo) was transfected into 293 cells using the lipofectamine method (Gibco BRL, Rockville, Md.) according to the manufacturer&#39;s directions. Cells that had taken up the DNA were selected with 1 mg/ml G418 (Gibco BRL, Rockville, Md.). Single colonies were picked 1 to 2 weeks after transfection and grown in medium containing 0.8 mg/ml G418. Colonies were screened for the ability to take up fatty acids by measuring uptake of a fluorescently labeled fatty acid (BODIPY-FA). About 40 colonies transfected with the pIRES-neo containing FATP4 and ˜20 colonies transfected with pIRES-neo control were analyzed. All 20 of the vector control clones showed amounts of BODIFY-FA uptake similar to each other and to untransfected 293 cells. In contrast, among the 40 FATP4 transfected clones, 3 had a 5- to 10-fold increased BODIPY-FA uptake compared to any of the vector controls, and a large number (˜20) showed an approximately two-fold increase in BODIPY-FA levels. This distribution is consistent with FATP4 conferring increased fatty acid uptake in these cells. One of the cell lines with the highest amount of BODIPY-FA uptake was selected to be used for measuring uptake of tritiated fatty acid.  
     [0330] The uptake of tritiated oleate over time by either FATP4 expressing or control cells was assayed over time. Expression of FATP4 increases the rate of fatty acid uptake by over 3-fold, demonstrating that FATP4 is, like the other FATPs, a functional fatty acid transporter (FIG. 38).  
     Example 12  
     Immuno-Staining with FATP4-Specific Antiserum  
     [0331] A polyclonal antiserum against the C-terminus of mmFATP4 was raised using a GST-fusion protein having mmFATP4-specific amino acid sequence 552-643 (AVASP . . . GEEKL). In western blot experiments, the purified antibody reacted strongly with a synthetic peptide matching the C-terminus of mmFATP4, but not with a corresponding region of mmFATP2, mmFATP3, or mmFATP5. The mmFATP4 specific polyclonal antiserum detects, in western blot experiments with enterocyte lysates from 3 different mice, a ˜70 kDa protein, which is in accordance with mmFATP4&#39;s predicted molecular weight of 72 kDa. The binding is specific for mmFATP4, since it can be completely abolished by preincubation of the antiserum with the GST-fusion peptide used to raise the antibody.  
     [0332] Immunofluorescence experiments were performed using the anti-mmFATP4 antiserum on fresh frozen sections of murine small intestine. The antibody binding demonstrates strong expression of mmFATP4 in enterocytes, confirming the results of the in situ hybridization experiments. At higher magnifications it is apparent that mmFATP4 is expressed at the apical side of the enterocyte, indicating that the transporter is present in the brush border membrane, which is known to mediate the uptake of fatty acids from the intestinal lumen.  
     [0333] Immuno-electron microscopy studies were performed on fresh frozen murine intestinal cells. The gold particles used, appearing as black specks on the electron micrographs, indicate the subcellular localization of mmFATP4 to be on the microvilli of the enterocyte. It can be seen from electron micrographs that mmFATP4 is localized exclusively in membranes, preferentially the apical plasma membrane, confirming that it is indeed a membrane protein.  
     [0334] Methods for Immunofluorescence and Immunogold Electron Microscopy  
     [0335] Unfixed mouse small intestine was washed with Hank&#39;s buffered salt solution containing 1 mM EDTA, infused with 2.3 M sucrose solution, and embedded in O.C.T., 4583 compound. The material was thick sectioned (15 μM -40 μM). The sections were washed in PBS containing 1% BSA and 0.075% glycine to block non-specific binding. Primary and secondary antibodies were diluted in PBS with 10% FCS and incubated for 1 h. The sections were mounted in 90% glycerol/PBS containing 1 mg/ml paraphenylinediamine, and examined with a Bio-Rad MRC 600 confocal, mounted on a Zeiss Axioscop.  
     [0336] For the immunogold labeling, the tissue was fixed with 2% paraformaldehyde in PBS for 10 minutes, after which it was cryoprotected by infiltration with 2.3 M sucrose in 0.1 M phosphate buffer (pH 7.4) containing 20% polyvinylpyrrolidone, and then mounted on aluminum cryo nails and frozen in liquid nitrogen (Tokuyasu, K. T.,  J. Microscop.  143:139-149, 1986). Ultrathin sections were collected on carbon/formvar-coated nickel grids. The primary antibody (anti-FATP4) was diluted in 10% FCS in PBS and incubated overnight at 4° C., followed by donkey anti-rabbit IgG-gold (12 nm) (Jackson Labs) for 1 h. The sections were stained in 2% neutral uranyl acetate (20 minutes) and absorption stained with 2% uranyl acetate in 0.2% methylcellulose containing 3.2% polyvinyl alcohol. The sections were examined with a Philips EM 410 electron microscope.  
     Example 13  
     Inhibition of Fatty Acid Uptake Specific to FATP4 Demonstrated in Isolated Mouse Enterocytes  
     [0337] Phosphorothioate derivatives of the following oligonucleotides were synthesized:  
                                  FATP4-AS2   CCCCCACCAGAGAGGCTCC   (SEQ ID NO:103)                   FATP4-AS2MM   CCACCCCCGGAAAGCCTGC   (SEQ ID NO:104)               FATP4-S2   GGAGCCTCTCTGGTGGGGG   (SEQ ID NO:105)          
 
     [0338] FATP4 AS2 is the antisense oligo; it is designed to be complementary to the sequence extending from nucleotide 10 to nucleotide 28 of the mouse FATP4 coding sequence. FATP4-AS2MM is a control oligo; in the oligo every third nucleotide was changed creating mismatches; the overall nucleotide composition is identical to FATP4-AS2 (same number of G, A, T, C). FATP4-S2 is the sense control.  
     [0339] Enterocytes were isolated from the small intestine of mice and incubated for 48 h in tissue culture (FIG. 40) either without oligonucleotides (squares) or with 100 μM FATP4 specific sense (circles) or antisense (diamonds) oligonucleotides. The uptake over time of 25 μM oleate was then measured. While the FATP4 sense oligonucleotide did not significantly influence the uptake, the antisense oligonucleotide inhibited fatty acid uptake by ˜50%.  
     [0340] The effect of either FATP4 sense, antisense or mismatch sequence oligonucleotides on the uptake of fatty acids was measured in enterocytes. Isolated enterocytes were incubated with increasing concentrations of FATP4 antisense oligonucleotides (solid bars in FIG. 41), or a mismatch control oligonucleotide with identical nucleotide composition (stippled bars), or with 100 μM of the FATP4 sense-oligonucleotide (lined bar). The medium for this incubation was Dulbecco&#39;s modified Eagle&#39;s medium with 4.5 g/L glucose, I mM sodium pyruvate, 0.01 mg/ml human transferrin and 10% fetal bovine serum. After 48 hours of incubation the uptake of oleate by enterocytes was measured over a 5 minute time interval. Measurements were done in quadruplicate. The uptake assay was done in Hank&#39;s buffered salt solution with 10 mM taurocholate. Only the enterocytes given FATP4 antisense oligonucleotide showed a concentration dependent decrease of fatty acid uptake, inhibiting it at a 100 μM concentration by ˜50%. This effect was FATP4 specific, since only the antisense oligonucleotide which can bind to the FATP4 mRNA and block its translation inhibited uptake, but not a control oligonucleotide differing only in the sequence but not the nucleotide content, ruling out a toxic or otherwise nonspecific inhibitory effect of this oligonucleotide due to its chemical composition.  
     [0341] As a further control experiment, the uptake of oleate was measured along with the uptake of methionine in the same cultured enterocytes. Antisense oligonucleotide, mismatch sequence oligonucleotide, or no oligonucleotide was added to a concentration of 100 μM to cultures of enterocytes. After incubation for 48 hours, the uptake of both  3 H-labeled oleate and  35 S-labeled methionine was assayed. Results are shown in FIG. 42. Fatty acid uptake is at the left side of the paired bars; methionine uptake is on the right side of the paired bars. The fact that amino acid uptake was not influenced by the antisense oligonucleotide treatment further supports the conclusion that the antisense oligonucleotide causes a specific reduction in translation of FATP4-specific mRNA.  
     Example 14  
     mmFATP2 is Expressed in Proximal Renal Tubule Epithelium  
     [0342] Northern analysis showed that mmFATP1, mmFATP2, and mmFATP4 are present in the kidney. In situ hybridization (methods as for Example 6) was performed to determine which cell type(s) of the kidney these mRNAs are expressed in. mmFATP1 mRNA was present in virtually all cells throughout the kidney with no obvious preference for a particular cell type. In contrast, mmFATP2 was expressed only in the renal cortex. Within the cortex, expression of mmFATP2 was restricted to the epithelial cells of the proximal renal tubules. The primary function of proximal renal tubule cells is the reabsorption of filtered salts and nutrients (e.g., glucose), a process that requires mitochondrial oxidation and that can utilize fatty acids as energy substrates. Based on the localization of mmFATP2, it is possible that mmFATP2 is important for reabsorption in the kidney by allowing uptake of an energy source (fatty acids) from the blood into renal epithelial cells. Alternatively, if fatty acids need to be reabsorbed in the kidney, similarly to glucose, FATP2 could be involved in the reabsorption of fatty acids. Determination of the subcellular localization of FATP2 will distinguish between these two possibilities.  
               TABLE 5                          Mouse FATP mRNA Expression                                     Mouse Probes   mFATP1   mFATP2   mFATP3   mFATP4   mFATP5               E18.5 embryo   everywhere,   liver   —   Brain, small   Mouse Probes       expression   brain = thymus&gt;   (hepatocytes)       intestine,           heart&gt; brown           superior           fat, others           cervical                       ganglion                       (SCG), dorsal                       root ganglion                       (DRG), other                       regions have                       lower                       expression       Duodenum   —   villi (surface   —   villi (surface               epithelium)           epithelium)       Jejunum   —   villi (surface   —   villi (surface               epithelium)           epithelium)       Ileum   —   villi (surface   —   villi (surface               epithelium)           epithelium)       Colon   low expression   very low level   —           in the crypt   in the crypt       Kidney   cortex and   proximal   —           medulla   tubules       Liver   —   hepatocytes   hepatocytes   —   hepatocytes       Pancreas   exocrine   exocrine   —   —   —           secretory units   secretory units           or acinar cells;   or acinar cells;           endocrine   endocrine           pancreas (islet)   pancreas (islet)           are negative   are negative       Brain   Neuronal   —   —   Neuronal   —           expression           expression           throughout the           throughout the           brain including           brain including           hypothalamus           hypothalamus       Heart   myocytes   —   —       Testis   seminiferous   —   seminiferous           tubules       tubules       Lung   bronchiole   —   —       Adipose   adipocyte   adipocyte   —                  
 
     Example 15  
     Isolation of Full-Length Human FATP3  
     [0343] Full-length clones encoding human FATP3 were identified by searching databases for sequences similar to the murine FATP 1-5 coding regions using the BlastX algorithm (Altschul et al.,  J. Mol. Biol.  215: 403-410, 1990). Human clones with similarity to the 5′ end of murine FATP sequences were sequenced completely. A clone encoding full-length human FATP3 was obtained from a human bone library constructed in the mammalian expression vector pMET7 (Tartaglia, L. A. et al.,  Cell  83: 1263-1271, 1995). To identify human cDNA clones encoding FATP family members, databases were searched for sequences similar to murine FATP1-5 coding regions. One clone was found to encode the human ortholog of mmFATP3 and was designated hsFATP3. The DNA and predicted protein sequences of hsFATP3 are shown in FIGS. 94A and 94B. hsFATP3 is predicted to encode a 702 amino acid 75.6 kD protein with multiple membrane-spanning domains. A comparison of the DNA sequences of mouse and human FATP3 shows that the mouse and human orthologs are 81% identical to each other within the coding region. At the amino acid level, hsFATP3 is ˜86% identical to mm FATP3 within the coding region. The sequence identities between mouse and human FATP3 are considerably higher than those observed between different FATP family members within one species (˜40%) and are present in the N-terminal part of the protein, a region that is poorly conserved between different FATP family members.  
     Example 16  
     Substrate Specificity of Fatty Acid Transport in hsFATP-Transfected Clones  
     [0344] Using a mammalian expression vector, we generated 40 stable 239 cell lines expressing hsFATP4 and 20 cell lines transfected with a control plasmid. The ability of the different cell lines to take up FA, as assessed by uptake assays using the fluorescently labeled Bodipy-palmitate, correlated well with their FATP4 expression levels determined by Western blotting (FIG. 95). All 20 vector control clones showed amounts of Bodipy-FA uptake similar to each other and to untransfected 239 cells. In contrast, among the 40 FATP4 transfected clones, a large number (˜20) showed an approximately 2-fold increase in Bodipy-FA uptake compared to any of the vector controls, and three had a 5- to 10-fold increase in Bodipy-FA uptake.  
     [0345] Several of the cell lines with the highest amount of Bodipy-FA uptake as well as isolated primary enterocytes were used to measure the uptake of radiolabeled FAs. Short-term uptake by 293 cells and enterocytes of all FAs tested was linear (FIG. 97). hsFATP4 expression enhanced the rate of palmitate uptake approximately 3 fold over 293 cells transfected with vector alone (FIG. 97) and also accelerated the uptake of oleate but not of linolate, arachidonate, octanoate, butyrate or cholesterol (Table 6). Isolated primary enterocytes showed a similar preference for palmitate and oleate, and absence of transport of arachidonate, octanoate, and butyrate, but displayed a more robust transport of linolate and cholesterol than the transfected 293 cells.  
     [0346] To further characterize the substrate specificity of FATP4, we measured the uptake by stably transfected 293 cells of 5 μM Bodipy-FA in the presence of a 20 fold molar excess (i.e., 100 μM) of FAs, FA-derivatives and lipid soluble vitamins and hormones. Both saturated and non-saturated fatty acids containing 10 to 26 C atoms strongly competed for uptake of Bodipy-palmitate (FIG. 96 and Table 7) and thus are presumed to be substrates of FATP4. In contrast, fatty acids with eight or fewer C atoms did not compete and thus are presumed not to be FATP4 substrates. Similarly, esters of long chain FAs and other hydrophobic molecules tested had no effect on uptake of Bodipy-palmitate.  
     [0347] LCFA Uptake Assays (Methods)  
     [0348] Bodipy-FA uptake assays using FACS were performed, adapted to a 96-well format. LCFA uptake assays with enterocytes or with stably transfected 293 cells were done as follows. Mixed micelles of radiolabeled FA (NEN) and taurocholate (Sigma) in HBS were generated by brief sonication at 37° C. Equal volumes of cells and micelle solution were mixed, resulting in a final FA concentration of 25 μM for antisense assays and 10 μM for substrate specificity assays. Final taurocholate concentration was 5 mM. Cells were incubated for the indicated amount of time at 37° C. The assay was stopped by transferring the cells onto filter paper followed by extensive washes with ice-cold HBS containing 0.1% BSA using a cell harvester (Brandell). Incorporated oleate was then determined by β-scintillation counting (Beckman).  
               TABLE 6                          Uptake of Different Substrates by FATP4       Expressing Cell Lines and Enterocytes                                         293 Cells                       Stably               293 Cells   Expressing   FATP4       Fatty Acid   Control*   FATP4   specific   Enterocytes*                                         Palmitate   564   1695   1131   3036       Oleate   662   1122   459   117       Linolate   640   673   33   116       Arachidonate   3   5   2   0       Octanoate   0   0   0   5       Butyrate   0   50   50   73       Cholesterol   319   345   26   531                                  
 
     [0349]               TABLE 7                          Competition of Bodipy-FA Uptake by FATP4 Expressing Cells                         Fatty Acids   Formula   Competition               Butyric Acid   C 4 H 8 O 2     −       Caproic Acid   C 6 H 12 O 2     −       Caprylic Acid   C 8 H 16 O 2     −       Capric Acid   C 10 H 20 O 2     ++       Lauric Acid   C 12 H 24 O 2     ++       Myristic Acid   C 14 H 28 O 2     ++       Palmitic Acid   C 16 H 32 O 2     ++       Stearic Acid   C 18 H 36 O 2     +       Oleic Acid   C 18 H 34 O 2     ++       Linoleic Acid   C 18 H 32 O 2     ++       Arachidic Acid   C 20 H 40 O 2     ++       Lignoceric Acid   C 24 H 48 O 2     ++       Cerotic Acid   C 26 H 52 O 2     ++                 Fatty Acid Derivatives                         Palmitic Acid Methyl   C 17 H 34 O 2     −       Ester       Stearic Acid Methyl Ester   C 19 H 38 O 2     −       Oleic Acid Ethyl Ester   C 20 H 38 O 2     −       Oleic Acid Oley Ester   C 36 H 68 O 2     −       Oleoyl CoA   C 39 H 68 N 7 O 17 P 3 S   −       Cholesteryl Oleate   C 45 H 78 O 2     −                 Lipid-Soluble Vitamins &amp; Hormones                         Retinoic Acid (Pro-Vitamin A)   C 20 H 28 O 2     ±       Ergocalciferol (Vitamin D2)   C 28 H 44 O 2     −       Tocopherol (Vitamin E)   C 29 H 50 O 2     −       3-Phytylamenadione (Vitamin   C 31 H 46 O 2     −       K1)       Prostaglandin E2   C 20 H 32 O 5     −                                                            
     Example 17  
     Identification and Characterization of the FATP5 Promoter  
     [0350] Methods  
     [0351] BAC Isolation and Luciferase Constructs  
     [0352] An arrayed BAC library was screened by PCR for FATP5 genomic clones. PCR primers designed by a program from the Whitehead Institute&#39;s Genome Center specifically amplified a single band of the correct size from mouse genomic DNA. Two putative BACs containing the FATP5 genomic sequence were identified and the presence of FATP5 sequence was confirmed by dot hybridization of the BAC with the mmFATP5 cDNA.  
     [0353] After isolation of positive BACs, large amounts of bacteria were grown and DNA prepared using a Qiagen maxi-prep kit (Qiagen, Venlo, The Netherlands). The BAC was digested with Sac I and ligated into pZero-2 (Invitrogen, Carlsbad, Calif.). Inserts containing mmFATP5 genomic sequence were identified by screening colony lifts of the ligation with an β- 32 P-ATP radiolabeled, random primed (Boehringer-Mannheim, Indianapolis, Ind.) mmFATP5 cDNA as a probe. Positive colonies were picked and restriction analysis with Sac I revealed them to contain an identical, large insert of 8-10 kb. Digestion of the Sac I fragment with BstX I yielded three pieces that were subsequently subcloned into pZero and sequenced using an ABI sequencer (Research Genetics). A 1.3 kb piece containing sequence immediately upstream of the FATP5 initiator methionine was subcloned into the Xho I and Bgl II sites of the promoter-less pGL3 luciferase reporter vector (Promega Corp., Madison, Wis.). 7 kb of additional upstream sequence was subcloned into the Xho I and Sac I sites of the prior construct to yield a final construct containing approximately 8 kb of genomic sequence upstream of the initiator methionine. Deletions of the FATP5 promoter were constructed using PCR with the 1.3 promoter construct as the template. Products were amplified with primers containing Hind III (5′ primer) and Xho 1 (3′ primer) sites using Elongase (Gibco, Rockville, Md.). The resulting fragments were cut with Hind III and Xho I and subcloned into the corresponding sites of the promoter-less pGL3 luciferase reporter vector. The internal 30 base pair deletions, GC box mutations, and 10 nucleotide linker scan were all created with the Quickchange mutagenesis kit (Stratagene, La Jolla, Calif.) according to the manufacturer&#39;s instructions. At least two different bacterial colonies were picked for each construct. The inserts from both colonies were sequenced to check for unintended point mutations and both constructs were assayed for luciferase activity.  
     [0354] Cell Culture, Transfection, and Luciferase Measurements  
     [0355] HepG2, Hep3B, HT1080, 3T3-L1, BOSC, and HACAT cells were grown in DMEM supplemented with 10% fetal calf serum, 1× penicillin-streptomycin and glutamine (Gibco, Rockville, Md.). Mink lung cells were grown in MEM supplemented with 10% fetal calf serum, 1× minimal essential amino acids, 1× penicillin-streptomycin and glutamine. The evening prior to transfection, cells were plated at 50-60% confluence in 24 well dishes. The following morning, cells were placed in 2 mls of fresh media and 250 μL of a CaPO 4  solution (Invitrogen, Carlsbad, Calif.) containing 2 μg of a luciferase reporter construct and 0.5 μg of pCMV-p-gal was added to the cells. pCMV-β-gal constitutively expresses β-galactosidase and was used to normalize transfection efficiency (Hua et al., 1998). After 12 hours, the cells were washed twice with DMEM and placed in fresh media. Thirty six hours later, the media over the cells was removed and 250 μL of 1× reporter lysis buffer (Promega Corp., Madison, Wis.) was added. After vigorous shaking for 15 minutes at room temperature, the supernatants were transferred to Eppendorf tubes and briefly centrifuged to remove particulates. 20 μL from these tubes was used for determination of luciferase activity (Promega Corp., Madison, Wis.) and 20 μL was used for the measurement of β-galactosidase activity (Clontech, Palo Alto, Calif.). All luciferase values were normalized to β-galactosidase to control for transfrection efficiency and expressed as relative luciferase units (RLU). For experiments comparing different cell lines, promoter activity was computed as a fold induction by dividing the RLU activity of either the −8 or −271 promoter constructs by the RLU activity a promoter-less construct. Each data point was done in triplicate and each experiment was repeated a minimum of three times.  
     [0356] Northern Blots, Preparation of Nuclear Extracts, and Gel Shift Assays  
     [0357] Human poly-A northern blots were purchased from a commercial vendor (Clontech, Palo Alto, Calif.) and probed with a piece of the human FATP5 3′ untranslated region specific for FATP5. Nuclear lysates from HepG2 and BOSC cells were essentially prepared according to the method of Hua et al. and stored at −80° C. (Hua et al., 1998). Probes for gel shift assays were end labeled using T4 polynucleotide kinase (Boehringer-Mannheirn, Indianapolis, Ind.) and gel purified. Gel shifts were performed at room temperature in 30 μL reactions comprised of 6 μL 5 × binding buffer (100 mM Tris 8.0, 300 mM KCl, 5 mM EDTA, 8 mM MgCl 2 , and 36% glycerol), 0.5 μL of 100 mM DTT, 1 μL of 10 mg/ml BSA, 2 μL of 2 mg/ml poly dI/dC, and 5 μL nuclear lysate. Ten minutes after the addition of nuclear lysate, 40,000 cpm of  32 P-labeled probe were added. After 20 minutes at room temperature, loading dye was added and the reaction run on a 4% non-denaturing gel.  
     [0358] Results  
     [0359] Human FATP5 mRNA is Only Expressed in Adult Liver  
     [0360] We had previously reported that mmFATP5 mRNA was only expressed in the liver (Hirsch et al., 1998). To determine if the human isoform of FATP5 was also liver specific, we performed northern analysis using a probe from the 3′ transcribed but untranslated region of the human gene. Similar to the mouse homolog, hsFATP5 is liver specific. Interestingly, hsFATP5 was not expressed in fetal liver suggesting that it may be developmentally regulated.  
     [0361] Identification of a FATP5 Promoter  
     [0362] We next set out to determine the cis-acting elements responsible for liver specific expression of FATP5. We identified BACs containing the FATP5 genomic locus and subcloned a 10 kb Sac I fragment which was subsequently sequenced. The Sac I fragment contains approximately 8 kb of genomic sequence upstream of the FATP5 initiator methionine. Blast searches using the 5′ end of the Sac I sequence revealed that it contained coding sequence for an unknown gene immediately upstream of FATP5. Since the FATP5 promoter is unlikely to overlap the coding sequence of another gene, we hypothesized that the 10 kb Sac I fragment contained the FATP5 promoter. To test this hypothesis, 8 kb of genomic DNA upstream of the translational initiator of FATP was subcloned into the promoter-less pGL3 luciferase reporter vector. This construct was transiently transfected into the HepG2 liver cell line and luciferase activity was determined. The −8 kb piece of DNA resulted in a 35 fold induction of luciferase activity when compared to a pGL3 vector without the FATP5 genomic sequence (FIG. 100). To determine if this activity reflected tissue specific transcription, the −8 kb luciferase reporter construct was transfected into a variety of additional cell types. While promoter activity was also detected in the Hep3b hepatoma cell line, non-liver cell lines did not express luciferase above the level of the promoter-less vector. Thus, the 8 kb upstream genomic element recapitulated liver specific expression in vitro.  
     [0363] The FATP5 Promoter Resides within the 261 Base Pairs Upstream of the Initiator Methionine and Requires a Single GC Box  
     [0364] To determine the cis-acting elements in the −8 kb of genomic sequence responsible for transcriptional activity, serial 5′ deletions of the promoter were constructed and transfected into HepG2 cells. Surprisingly, greater than 90% of the −8 kb was dispensable for promoter activity. A construct containing only 261 base pairs upstream of the initiator methionine resulted in promoter activity equivalent to that of the −8 kb construct (FIG. 101). Identical results were obtained when the deletion series was transfected into Hep3b cells (data not shown). We next determined if promoter activity of a small genetic element was tissue specific. Transfection of a construct containing 271 base pairs upstream of the initiator methionine into a variety of cell lines essentially replicated the results of the −8 kb construct in that expression was observed only in liver derived cell lines (FIG. 102).  
     [0365] Since deletion analysis revealed that bases between −261 and −218 were required for promoter activity, we closely examined this region for binding sites of known transcription factors and found the sequence GGGGCGGGG between nucleotides −241 and −232 (FIG. 103A). This sequence binds the Sp1 family of transcription factors and is termed a GC box. To determine if the activity of the −271 construct required the GC box, we mutated the GC box. The first construct deleted nucleotides −241 to −222 which removed the GC box and additional downstream sequence which, although less optimal, might also bind the Sp1 family of transcription factors(SEQ ID NO: 107). The second construct had three G to A point mutations in the GC box between nucleotides −241 to −232(SEQ ID NO: 108). Such mutations had previously been shown to abolish transcriptional activity of GC boxes (Rodenburg et al., 1997). In contrast to the wild type −271 promoter, both of the mutated constructs were transcriptionally inactive in HepG2 cells (FIG. 103B). Identical results were also obtained in Hep3B cells (data not shown). This suggests that the GC box between −241 to −232 is essential for transcriptional activity of the FATP5 promoter. We next examined whether the sequences necessary for luciferase activity also bound proteins in nuclear extracts from HepG2 cells. Two different oligonucleotides were used for gel shift analysis. One oligonucleotide (AF-1) contained nucleotides −250 to −230(SEQ ID NO: 111) and the other (AF-2) spanned nucleotides ˜260 to ˜−200(SEQ ID NO: 109) (FIG. 104). Both oligonucleotides yielded three significant complexes from HepG2 nuclear extracts. All complexes were specific as 100 fold excess of the same unlabeled oligonucleotide could compete for binding of the radiolabeled oligonucleotide. Mutant AF-1 oligonucleotides containing three point mutations in the GC box did not bind any proteins in HepG2 nuclear extracts or compete for binding of nuclear proteins to the AF-1 or AF-2 oligonucleotides (data not shown). Oligonucleotides AF-1 and AF-2 also bound recombinant Spi (Promega Corp, Madison, Wis., data not shown). However, nuclear extract from BOSC cells, a kidney cell line, and HepG2 cells had identical patterns of complex formation (data not shown).  
     [0366] Identification of Novel Sequences Required for Transcriptional Activity of the FATP5 Promoter  
     [0367] While the GC box between nucleotides 241 and 232 is essential for transcriptional activity, additional sequences downstream of the GC box might also be required for transcription. To determine if such sequences existed, we created 30 base pair internal deletions in the ˜−271 construct downstream of the GC box. Constructs that had deletions in sequences between 240 and 180 nucleotides upstream of the FATP5 translational initiator had greatly reduced transcriptional activity in HepG2 cells (FIG. 105). To identify the specific sequences within this region required for FATP5 transcription, a 10 nucleotide linker (CTAACAGGAG) (SEQ ID NO: 1-13) was exchanged for wild type sequence within the context of the −271 base pair construct (FIG. 106). Inadvertently, the 210 to 200 construct had a single nucleotide insertion and the 190 to 180 construct had a two nucleotide insertion relative to the wild type sequence. However, several other linker constructs that also had equivalent insertions (230 to 220 or 170 to 160 for example) had high levels of luciferase activity. Thus the decrease in luciferase activity in the 190 to 180 and 210 to 200 constructs is due to changes in the nucleotide sequence and not the result of the nucleotide additions. Transfection of these DNA into HepG2 cells revealed two regions important for transcription. Mutating sequences between nucleotides −210 and ˜−200 or between nucleotides −190 and −180 drastically reduced luciferase activity (FIG. 106).  
     [0368] In both humans and mice, FATP5 is only expressed in the liver. To determine the promoter elements mediating liver specific transcription, we isolated a BAC encoding the mouse FATP5 genomic locus and sequenced 10 kb upstream of the transcriptional start. Since this 10 kb of genomic DNA did not contain either a TATA box or GC rich regions found in TATA-less promoters, FATP5 may utilize non-canonical sequences for transcription initiation. Unfortunately, attempts to identify the transcriptional start using primer extension were unsuccessful, perhaps due to secondary structure in the 5′ UTR. Since we did not unambiguously determine the transcriptional start site, the nucleotide numbering in all of the promoter constructs refers to the distance from the translational start codon.  
     [0369] GC Box and Sp1 Transcription Factors  
     [0370] Since another gene was situated approximately 8 kb upstream of the FATP5 initiator methionine, we hypothesized that promoter elements were likely within this region of DNA. A luciferase reporter construct containing this sequence was transcriptionally active in two liver cell lines but was inactive in cell lines derived from lung, muscle, kidney, skin, or fibroblasts. Deletion analysis of the −8 kb reporter construct revealed that the FATP5 promoter was contained within the 261 nucleotides upstream of the initiator methionine. Promoter activity in this −261 base pair piece required the presence of a single GC box. Gel shift assays with oligonucleotides containing this GC box revealed the presence of three distinct complexes that required a functional GC box for binding. GC boxes bind the Sp1 family of transcription factors and the multiple complexes could reflect the binding of different members of the Sp1 protein family or different post-translational modifications of Sp1 in HepG2 cells (Rodenburg et al., 1997). Although the Sp1 family of transcription factors is widely expressed, Sp1 has been shown to be important for the transcription of several liver specific genes and is upregulated in liver after birth (Rodenburg et al., 1997). In some cases, Sp1 will facilitate the binding of a tissue specific transcription factor to DNA. For example, Sp1 binding to DNA enhances the binding of C/EBPβ to an adjacent site in the liver specific CYP2D5 promoter (Lee et al., 1994). Since the C/EBPβ binding site in the CYP2D5 promoter is suboptimal, C/EBPβ binding to this site requires the presence of Sp 1 or nuclear extract. A similar situation could occur in the FATP5 promoter. Although mutations in the 10 nucleotides downstream of the GC box had no effect on luciferase activity, we did not test mutations immediately upstream of the GC box for effects on promoter activity. It is also possible that Sp1 might bind an unknown liver specific transcription factor and recruit it to the FATP5 promoter. Although, there is no experimental evidence for this, Sp1 has recently been shown to bind to a transcriptional activator so additional interacting proteins are possible (Ryu et al., 1999). Other liver specific transcription factors  
     [0371] Alternatively, since the Sp1 gene family is important for the transcription of many genes which are not liver specific, liver specific promoter elements in the FATP5 promoter might be located elsewhere (Boisclair et al., 1993; Rongnoparut et al., 1991; Sorensen and Wintersberger, 1999). Analysis of the sequence downstream of the GC box using TFSearch (http://pdap1.trc.rwcp.orjp/research/db/TFSEARCH.html) did not reveal any additional transcription factor binding sites of relevance (Heinemeyer et al., 1999; Heinemeyer et al., 1998). Further, we were unable to visually identify binding sites for known liver specific transcription factors in this sequence (De Simone and Cortese, 1992; Hanson and Reshef, 1997; Lai, 1992). Thus, we looked experimentally for additional promoter elements by mutating the sequence downstream of the GC box and identified two additional sites downstream of the GC box that were essential for FATP5 transcription. The sequences of these sites do not conform to any known transcription factor binding sites suggesting the either novel proteins bind these elements or that these elements bind known proteins in a novel manner. Preliminary gel shift data using oligonucleotides spanning these site suggests that these two elements may comprise a binding site for a single complex. Further additional data suggests that the complex which binds to these two sites interacts with the GC box 30 base pairs upstream. Interestingly, we noted a palindromic sequence equally split between these two sites (FIG. 107). Since many transcription factors bind palindromic DNA elements, it is intriguing to speculate that these two sequences contribute to the binding site for a novel transcription factor. Current investigations are focused on identifying the proteins binding to these novel elements and how this element interacts with the GC box.  
     [0372] Several studies have shown that the FATP gene family is regulated by a variety of substances including LPS, cytokines, insulin, and diet (Frohnert et al., 1999; Hui et al., 1998; Memon et al., 1999). Especially intriguing has been a recent report that FATP1 is upregulated by PPARα ligands in liver cell lines (Martin et al., 1997; Motojima et al., 1998). Since fatty acids may be endogenous activators of PPAR&#39;s, transcriptional regulation of FATP1 by PPAR&#39;s may represent a physiologic feedback loop (Gottlicher et al., 1992; Grimaldi et al., 1999; Schoonjans et al., 1996). Given that liver also expresses FATP5, it will be interesting to see whether this genes is also regulated by PPARα and the tools developed here should help address this question.  
     [0373] Several factors make the FATP5 promoter amenable to further study. First, liver specific transcription of FATP5 can be recapitulated using immortalized cell lines in vitro. Second, the minimal required promoter element that confers liver specific transcription is very small. Third, transcriptional activity of this promoter is very robust. Thus, further study of the FATP5 promoter may provide additional insight into the mechanisms of liver specific transcription and regulation of the FATP gene family.  
     Example 18  
     [0374] Materials and Methods  
     [0375] Polyclonal antibodies were raised against proteins containing the N-terminal domain of mouse FATP2 or the C-terminal domain of mouse FATP5 fused to glutathione-S-transferase (GS). Tissues for immunofluorescence were collected from 8 week old mice and a 2 year old chimpanzee. Tissues were fresh frozen, cut on a cryostat and mounted on slides. Immunofluorescence was performed as previously described (Stahl et al., 1999). Pictures were taken on a Zeiss confocal microscope.  
     [0376] To determine FATP2 expression in the gall bladder, mouse gall bladder was incubated with anti-FATP2 antibody as the primary antibody and rhodamine-labeled anti-rabbit IG as the secondary antibody. FATP2 antibody clearly stained the gall bladder epithelium, but did not result in significant staining of other cell types. (FIG. 108)  
     [0377] To further study FATP2 expression, chimpanzee liver was costained with anti-FATP2 antibody(green) and anti CD31 antibody(red). CD31 is expressed on endothelial cells and is used as a marker for blood vessels. FATP2 immunoreactivity was present in large patches which overlap with CD31 positive areas, suggesting that FATP2 protein was present in the space of Diss, the area where hepatocytes exchange nutrients with the blood. This implicates FATP2 in the uptake of fatty acids into hepatocytes. In addition to areas which overlap with CD31 immunoreactivity, FATP2 protein was also present on the cell surface of hepatocytes in a small bead pattern. Immunoelectronmicroscopy of similar sections showed that FATP2 immunoreactivity was localized in the walls of bile caniculi which are formed by the liver cells. (FIG. 109) The presence of FATP2 in bile caniculi in the liver as well as its presence in the gall bladder epithelium suggests a role for FATP2 in either absorption or secretion of fatty acids into the bile. The levels of free fatty acids in the bile have been associated with the frequency of all stone formation.  
     [0378] To further study FATP5 expression, chimpanzee liver was costained with anti-FATP5 antibody(green) and anti CD31 antibody(red). CD31 is expressed on endothelial cells and is used as a marker for blood vessels. FATP5 immunoreactivity was present in large patches which overlap with CD31 positive areas, suggesting that FATP5 protein was present in the space of Diss, the area where hepatocytes exchange nutrients with the blood. (FIG. 110) This implicates FATP5 in the uptake of fatty acids into hepatocytes.  
     Example 19  
     Identification and Characterization of Human FATP3 Proteins  
     [0379] Isolation of Additional HumanFATP3 Clones  
     [0380] An additional clone encoding human FATP3 was identified by searching for sequences similar to murine or human FATP3 coding regions using the BlastX algorithm in a proprietary database, (Altschul, et al, J. Mol. Bio. 215: 403-410, 1990). One clone, which was identified by random library sequencing, is described as johni003f04 (SEQ ID NO:116) extends the open reading frame of the hsFATP3 polypeptide sequence by 30 amino acids at the N-terminus when compared to previously discovered sequences. The DNA sequence of this clone is shown in FIGS. 111A and 111B, and the predicted protein sequence (SEQ ID NO: 117) is shown in FIG. 112. The open reading frame of this clone begins at the initial nucleotide and includes nucleotide 2240. The first ATG is located at nucleotide number 51, resulting in a predicted protein which includes 730 amino acids. An FATP signature sequence (see Hirsch et al., PNAS, 95:8625-8629, 1998) is clearly present between amino acids 331 and 640 of hsFATP3. Within this signature sequence hsFATP3 is 48% identical to hsFATP1 at the amino acid level. A consensus AMP-binding motif has been identified (amino acid 333-334). Thus, hsFATP3 is clearly a member of the fatty acid family.  
     [0381] Functional Analysis of FATP3 Clones  
     [0382] SEQ ID NO: 116 is contained in the mammalian expression vector pMET7 (Tartaglia, et a.., Cell, 83: 1263-1271, 1995). To determine if the protein encoded by this DNA sequence can mediate fatty acid uptake, SEQ ID NO: 116 was transfected into COS cells. Uptake of a BODIPY-labeled fatty acid was determined as described in previous experiments (Hirsch, et al., PNAS, 95: 8625-8629, 1998). Transfection with SEQ ID NO: 116 resulted in a dramatic increase in fatty acid uptake when compared to transfection with vector control. In this experiment, CD31 served as a marker for transfected cells. Only CD31 positive cells were considered for analysis (see Hirsch, et al., PNAS, 95: 8625-8629, 1998 for details). The results (FIG. 113) demonstrate that SEQ ID NO: 116 encodes a functional fatty acid transport protein.  
     [0383] Tissue Distribution of Human FATP3  
     [0384] Polyclonal antibodies were raised by immunizing rabbits with GST fused to the most C-terminal 89 amino acids of mmFATP3-(RPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRMANEGFDP SVLSDPLYVLDQDIGAYLPLTPARYSALLSGDLRI) (SEQ ID NO: 120). Western blotting experiments with murine tissue lysates using the anti-FATP3 antiserum closely confirmed the unique expression pattern of FATP3 as judged by northern blot experiments. This, together with the fact that the serum reacted only weakly with lysates from cell lines expressing either FATP1, -2, -4 or -5, indicates that the antibody recognizes preferentially FATP3, but not other FATP family members.  
     [0385] FATP3 protein was detected in mouse liver, spleen, heart, kidney, testis, white adipose tissue, and most notably in the lung. Further FATP3 expression in the lung was examined by immunofluorescence microscopy. 5 to 10 μM thick fresh frozen unfixed sections of murine and chimpanzee lungs were blocked with 10% FCS/1% donkey serum/1% BSA in HBS and incubated overnight with anti-FATP3 serum in blocking solution. After washing the sections Alexa 488 conjugated donkey anti-rabbit secondary antibodies were used to detect bound anti-FATP3 primary antibodies and nuclei were stained TOTO3. In later experiments, chimpanzee lung was incubated with a mixture of rabbit anti-FATP3 and mouse monoclonal anti-CD31 to visualize FATP3 as well as blood vessels. Sections were imaged on a Zeiss LSM510 confocal microscope. Experiments carried out once with mouse and three times with chimpanzee lung tissue showed that FATP3 is present at high levels in type-II pneumocytes, a cell type responsible for secretion of surfactant, a phospholipid-rich film critical for lung function. The exact function of FAT3 in type II pneumocytes is not yet clear. One hypothesis is that FATP3 is responsible for supplying fatty acid substrates for the symthesis of surfactant.  
     [0386] PCR-based experiments showed that the exocrine as well as endocrine pancreas expresses FATP3. This fact was confirmed by immunofluorescence performed as described above for the lung sections, on chimpanzee pancreas which showed FATP3 localized to the plasma membrane of acinar cells and a punctate expression pattern on the plasma membrane and in the cytosol of alpha and beta cells of the pancreatic islands. The identification of a fatty acid transporter in the insulin producing cells of the pancreas has potentially broad implications for the treatment of type II diabetes and obesity. In both diseases, fatty acid levels in the blood are elevated and, in later stages of the disease, lead to diminished insulin secretion by the pancreas due to the induction of apoptosis in insulin-producing beta cells (Shimabukuro, et al., PNAS, 95: 2498-2502, 1988). Blocking fatty acid uptake into the beta cells could possibly prevent apoptosis and maintain insulin secretion thus preventing the progression from obesity to diabetes.  
     Example 20  
     Identification of a Fatty Acid Binding Domain in FATP4  
     [0387] GST fusion proteins were constructed in pGEX for four regions of hsFATP4 (SEQ ID NO: 52; FIG. 51) which were generated by PCR and verified by sequencing. The first three fusion proteins were constructed from regions near the N-terminal portion of the protein. SP1 (SEQ ID NO: 121) contained amino acid residues 43-239 of the hsFATP4 sequence as shown in FIG. 114A. This portion of hsFATP4 contains a lipocalin domain (as shown in FIG. 117) as well as a number of residues which in hsFATP4 are upstream of the lipocalin domain. SP2 (SEQ ID NO: 122) contained residues 43-290 of the hsFATP4 sequence as shown in FIG. 114B. This portion of the hsFATP4 contains a lipocalin domain and an AMP binding domain as well as a number of residues which are upstream of the lipocalin domain. SP3 (SEQ ID NO: 123) contained amino acid residues 125-290 of the hsFATP4 sequence as shown in FIG. 114C). This portion of the hsFATP4 contains a lipocalin domain and an AMP binding domain, but does not contain the upstream residues. The fourth fusion protein was constructed from a region at the C-terminal end of the hsFATP4 polypeptide. SP5 contained amino acid residues 417-643 of hsFATP4 polypeptide as show in FIG. 114D (SEQ ID NO: 124).  
     [0388] Proteins were expressed in  E. coli  and purified on glutathione affinity beads using standard techniques. To determine fatty acid binding, beads were mixed with 100 μM 14C-labeled fatty acids in mixed micelles with taurocholate (10 mM, Sigma) and incubated for 30 minutes at room temperature. The beads were subsequently washed with PBS containing 10 mM taurocholate and radioactivity associated with beads was assessed by scintillation counting. A fusion to the C-terminal domain of hsFATP4 (SP5) did not show any oleate (ARC) binding compared to GST protein alone, while 2 N-terminal fusions (SP1 and 2) bound significant amounts of oleate. (FIG. 116).  
                                                   FATTY ACID   SP1   SP2   SP3   SP5   GST                  Oleate   25772 ± 1326   16172 ± 1639   4206 ± 631   2413 ± 186   1511 ± 525                  
 
     [0389] Similar results were obtained using maltose-binding protein fusions. MBP fusion constructs were generated by digesting the pGEX-SP constructs with EcoRI/XhoI and ligated into pMAL digested with EcoRI/SaII. MBP fusion proteins were expressed in  E. coli  and were purified under non-denaturing conditions following the manufacturer&#39;s instructions. To determine fatty acid binding, beads were mixed with 100 μM 14C-labeled fatty acids in mixed micelles with taurocholate (10 mM, Sigma) and incubated for 30 minutes at room temperature. The beads were subsequently washed with HBS containing 10 mM taurocholate. The proteins were subsequently eluted from the resin with maltose and the amount of fatty acid binding to MBP-SP1, -2, -3, and -5 was assessed by determining the radioactivity associated with the elute by β-scintillation counting.  
     [0390] Unlike GST fusion proteins, MBP fusion proteins are not self-dimerizing. Further, long-chain fatty acids (such as oleate and palmitate), but not short-chain fatty acids (such as butyrate), were specifically bound by SP1 (FIG. 117). This selective binding is consistent with previous reports of the substrate specificity of FATP4 (Stahl, et al., Mol. Cell, 4, 299-308, 1999). The identification of a fatty acid binding domain in FATP4 will be useful in the development of small molecules that inhibit the binding and transport of fatty acids by FATP4 and may provide useful information on the mechanism of fatty acid transport.  
     [0391] Results of Fatty Acid Binding  
                                                   binding to           FATTY ACID   Composition   MBP-SP1   binding to MBP-SP5                                                Oleate   C18H3402   3968   2800       Palmitate   C16H3202   4588   844       Arachidonate   C20H4002   1942   1147       Butyrate   C4H802   142   633                  
 
     [0392] These experiments demonstrate that the FATPs of the present invention contain domains that bind various long chain fatty acids. Thus, polypeptides containing these domains can be prepared and utilized to assess the modulation of binding and transport function by a variety of agents. The polypeptides with the highest binding capacities were shown to be those containing a lipocalin domain (such as those shown in FIG. 118) with additional upstream residues, such as those associated with this domain in the N-terminal portion of hsFATP4. Polypeptides containing domains in addition to the lipocalin domain (for example, those containing an AMP binding domain) were also shown to bind fatty acids at significant levels.  
     [0393]FIG. 118 contains an alignment depicting the consensus sequences for the six human FATP, hsFATP1, hsFATP2, hsFATP3, hsFATP4, hsFATP5 and hsFATP6 polypeptides. A lipocalin domain and an AMP binding domain for each polypeptide are both identifed and compared. A search using the lipocalin signature sequence [DENG]-X-[DENQGSTARK]-X(0,2)-[DENQARK]-[LIVFY]-{CP}-G-{C}-W-[FYWLRH-X]-[LIVMTA] conducted on a public database (www.ebi.ac.uk/interpro/), indicated that the lipocalin domains of hsFATP1 and hsFATP4 are identical to the lipocalin signature sequence. In addition, a search directed to identifying sequences having at least 80% identity to the lipocalin signature sequence identified three additional human FATPs, hsFATP3, hsFATP5 and hsFATP6.  
     [0394] The following is the result of comparing individual hsFATP protein sequences with the lipocalin domain identified for hsFATP 1 and hsFATP4. The comparison was made using the BLAST Network Service at the National Center for Biotechnology Information. (Capitalized AA agree with the lipocalin signature sequence.)  
                                  FATP6:   114 to 125 NEpDFVhVWFGL. 76% similarity   (SEQ ID NO: 138)               AATGAGCCGGACTTCGTTCACGTGTGGTTCGGCCTC               FATP5:   182 to 194 sQAVpaLcMWLGL. 53% similarity   (SEQ ID NO: 139)           TCCCAGGCCGTTCCAGCCCTGTGTATGTGGCTGGGGCTG               FATP4:   134 to 146 ENRNEFVGLWLGM. Identity   (SEQ ID NO: 129)           GAGAACCGCAATGAGTTCGTGGGCCTATGGCTGGGCATG               FATP3:   221 to 234 IPAGPEFLwLWTGL. 69% similarity   (SEQ ID NO: 140)           CTCCCCGCTGGCCCAGAGTTTCTGTGGCTCTGGTTCGGGCTG               FATP2:   112 to 124 GNEPAYVwLWLGL. 80% similarity   (SEQ ID NO: 127)           GGTAACGAGCCGGCCTACGTGTGGCTGTGGCTGGGGCTG               FATP1:   136 to 148 EGRPEFVGLWLGL. Identity   (SEQ ID NO: 126)           GAGGGCCGGCCGGAGTTCGTGGGGCTGTGGCTGGGCCTG          
 
     [0395] References  
     [0396] Abumrad, N., Coburn, C., and Ibrahimi, A. (1999). Membrane proteins implicated in long-chain fatty acid uptake by mammalian cells: CD36, FATP and FABPm. Biochim Biophys Acta 1441, 4-13.  
     [0397] Berk, P. D., Bradbury, M., Zhou, S. L., Stump, D., and Han, N. I. (1996). Characterization of membrane transport processes: lessons from the study of BSP, bilirubin, and fatty acid uptake. Semin Liver Dis 16, 107-20.  
     [0398] Berk, P. D., and Stump, D. D. (1999). Mechanisms of cellular uptake of long chain free fatty acids. Mol Cell Biochem 192, 17-31.  
     [0399] Boisclair, Y. R., Brown, A. L., Casola, S., and Rechler, M. M. (1993). Three clustered Sp1 sites are required for efficient transcription of the TATA-less promoter of the gene for insulin-like growth factor-binding protein-2 from the rat. J Biol Chem 268, 24892-901.  
     [0400] De Simone, V., and Cortese, R. (1992). Transcription factors and liver-specific genes. Biochim Biophys Acta 1132, 119-26.  
     [0401] Fitscher, B. A., Elsing, C., Riedel, H. D., Gorski, J., and Stremmel, W. (1996). Protein-mediated facilitated uptake processes for fatty acids, bilirubin, and other amphipathic compounds [see comments]. Proc Soc Exp Biol Med 212, 15-23.  
     [0402] Frohnert, B. I., Hui, T. Y., and Bernlohr, D. A. (1999). Identification of a functional peroxisome proliferator-responsive element in the murine fatty acid transport protein gene. J Biol Chem 274, 3970-7.  
     [0403] Glatz, J. F., Luiken, J. J., van Nieuwenhoven, F. A., and Van der Vusse, G. J. (1997). Molecular mechanism of cellular uptake and intracellular translocation of fatty acids. Prostaglandins Leukot Essent Fatty Acids 5 7, 3-9.  
     [0404] Gottlicher, M., Widmark, E., Li, Q., and Gustafsson, J. A. (1992). Fatty acids activate a chimera of the clofibric acid-activated receptor and the glucocorticoid receptor. Proc Natl Acad Sci U S A 89, 4653-7.  
     [0405] Grimaldi, P. A., Teboul, L., Gaillard, D., Armengod, A. V., and Amri, E. Z. (1999). Long chain fatty acids as modulators of gene transcription in preadipose cells. Mol Cell Biochem 192, 63-8.  
     [0406] Hamilton, J. A. (1998). Fatty acid transport: difficult or easy? J Lipid Res 39, 467-81.  
     [0407] Hanson, R. W., and Reshef, L. (1997). Regulation of phosphoenolpyruvate carboxykinase (GTP) gene expression. Annu Rev Biochem 66, 581-611.  
     [0408] Heinemeyer, T., Chen, X., Karas, H., Kel, A. E., Kel, O. V., Liebich, I., Meinhardt, T., Reuter, I., Schacherer, F., and Wingender, E. (1999). Expanding the TRANSFAC database towards an expert system of regulatory molecular mechanisms. Nucleic Acids Res 27, 318-22.  
     [0409] Heinemeyer, T., Wingender, E., Reuter, I., Hermjakob, H., Kel, A. E., Kel, O. V., Ignatieva, E. V., Ananko, E. A., Podkolodnaya, O. A., Kolpakov, F. A., Podkolodny, N. L., and Kolchanov, N. A. (1998). Databases on transcriptional regulation: TRANSFAC, TRRD and COMPEL. Nucleic Acids Res 26, 362-7.  
     [0410] Hirsch, D., Stahl, A., and Lodish, H. F. (1998). A family of fatty acid transporters conserved from mycobacterium to man. Proc Natl Acad Sci U S A 95, 8625-9.  
     [0411] Hua, X., Liu, X., Ansari, D. O., and Lodish, H. F. (1998). Synergistic cooperation of TFE3 and smad proteins in TGF-beta-induced transcription of the plasminogen activator inhibitor-1 gene. Genes Dev 12, 3084-95.  
     [0412] Hui, T. Y., Frohnert, B. I., Smith, A. J., Schaffer, J. E., and Bemlohr, D. A. (1998). Characterization of the murine fatty acid transport protein gene and its insulin response sequence. J Biol Chem 273, 27420-9.  
     [0413] Lai, E. (1992). Regulation of hepatic gene expression and development. Semin Liver Dis 12, 246-51.  
     [0414] Lee, Y. H., Yano, M., Liu, S. Y., Matsunaga, E., Johnson, P. F., and Gonzalez, F. J. (1994). A novel cis-acting element controlling the rat CYP2D5 gene and requiring cooperativity between C/EBP beta and an Sp1 factor. Mol Cell Biol 14, 1383-94.  
     [0415] Martin, G., Schoonjans, K., Lefebvre, A. M., Staels, B., and Auwerx, J. (1997). Coordinate regulation of the expression of the fatty acid transport protein and acyl-CoA synthetase genes by PPARalpha and PPARgamma activators. J Biol Chem 272, 28210-7.  
     [0416] Memon, R. A., Fuller, J., Moser, A. H., Smith, P. J., Grunfeld, C., and Feingold, K. R. (1999). Regulation of putative fatty acid transporters and Acyl-CoA synthetase in liver and adipose tissue in ob/ob mice. Diabetes 48, 121-7.  
     [0417] Motojima, K., Passilly, P., Peters, J. M., Gonzalez, F. J., and Latruffe, N. (1998). Expression of putative fatty acid transporter genes are regulated by peroxisome proliferator-activated receptor alpha and gamma activators in a tissue- and inducer-specific manner. J Biol Chem 273, 16710-4.  
     [0418] Rodenburg, R. J., Holthuizen, P. E., and Sussenbach, J. S. (1997). A functional Sp1 binding site is essential for the activity of the adult liver-specific human insulin-like growth factor II promoter. Mol Endocrinol 11, 237-50.  
     [0419] Rongnoparut, P., Verdon, C. P., Gehnrich, S. C., and Sul, H. S. (1991). Isolation and characterization of the transcriptionally regulated mouse liver (B-type) phosphofructokinase gene and its promoter. J Biol Chem 266, 8086-91.  
     [0420] Ryu, S., Zhou, S., Ladumer, A. G., and Tjian, R. (1999). The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1. Nature 397, 446-50.  
     [0421] Schaffer, J., and Lodish, H. F. (1995). Molecular mechanisms of long-chain fatty acid uptake. Trends in Cardiovascular Medicine 5, 218-224.  
     [0422] Schaffer, J. E., and Lodish, H. F. (1994). Expression cloning and characterization of a novel adipocyte long chain fatty acid transport protein [see comments]. Cell 79, 427-36.  
     [0423] Schoonjans, K., Staels, B., and Auwerx, J. (1996). The peroxisome proliferator activated receptors (PPARS) and their effects on lipid metabolism and adipocyte differentiation. Biochim Biophys Acta 1302, 93-109.  
     [0424] Sorensen, P., and Wintersberger, E. (1999). Sp1 and NF-Y are necessary and sufficient for growth-dependent regulation of the hamster thymidine kinase promoter [In Process Citation]. J Biol Chem 274, 30943-9.  
     [0425] Stahl, A., Hirsch, D. J., Gimeno, R. E., Punreddy, S., Ge, P., Watson, N., Patel, S., Kotler, M., Raimondi, A., Tartaglia, L. A., and Lodish, H. F. (1999). Identification of the major intestinal fatty acid transport protein [In Process Citation]. Mol Cell 4, 299-308.  
     [0426] Stremmel, W. (1989). Mechanism of hepatic fatty acid uptake. Journal of Hepatology 9, 374-382.  
     [0427] All references cited herein are incorporated by reference in their entirety.  
     [0428] While this invention has been particularly shown and described with references to preferred embodiments thereof, it will be understood by those skilled in the art that various changes in form and details may be made therein without departing from the spirit and scope of the invention as defined by the appended claims.  
 
    
     
       
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                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
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                 Phe Ile Phe Thr Ser Gly Thr Thr Gly Leu Pro Lys Pro Ala Ile Leu  
               
               
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                 &lt;213&gt; ORGANISM: Caenorhabditis elegans  
               
               
                   
               
               
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                 Arg Leu Met Trp Gly Asn Gly Leu Arg Gly Gln Ile Trp Lys Glu Phe  
               
               
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                 Val Gly Arg Phe Gly Ile Lys Lys Ile Gly Glu Leu Tyr Gly Ser Thr  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Glu Gly Asn Ser Asn Ile Val Asn Val Asp Asn His Val Gly Ala Cys  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Gly Phe Met Pro Ile Tyr Pro His Ile Gly Ser Leu Tyr Pro Val Arg  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Leu Ile Lys Val Asp Arg Ala Thr Gly Glu Leu Glu Arg Asp Lys Asn  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Gly Leu Cys Val Pro Cys Val Pro Gly Glu Thr Gly Glu Met Val Gly  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Val Ile Lys Glu Lys Asp Ile Leu Leu Lys Phe Glu Gly Tyr Val Ser  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Glu Gly Asp Thr Ala Lys Lys Ile Tyr Arg Asp Val Phe Lys His Gly  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asp Lys Val Phe Ala Ser Gly Asp Ile Leu His Trp Asp Asp Leu Gly  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Tyr Leu Tyr Phe Val Asp Arg Cys Gly Asp Thr Phe Arg Trp Lys Gly  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Glu Asn Val Ser Thr Thr Glu Val Glu Gly Ile Leu Gln Pro Val Met  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Asp Val Glu Asp Ala Thr Val Tyr Gly Val Thr Val Gly Lys Met Glu  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Gly Arg Ala Gly Met Ala Gly Ile Val Val Lys Asp Gly Thr Asp Val  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Glu Lys Phe Ile Ala Asp Ile Thr Ser Arg Leu Thr Glu Asn Leu Ala  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ser Tyr Ala Ile Pro Val Phe Ile Arg  
               
               
                             340                 345  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 4  
               
               
                 &lt;211&gt; LENGTH: 356  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Saccharomyces cerevisiae  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 4  
               
               
                   
               
               
                 Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala Ile Val  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val His Ser Arg Tyr Tyr Arg Ile Ala Ala Phe Gly His His Ser Tyr  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Ser Met Arg Ala Ala Asp Val Leu Tyr Asp Cys Leu Pro Leu Tyr His  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ser Ala Gly Asn Ile Met Gly Val Gly Gln Cys Val Ile Tyr Gly Leu  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Thr Val Val Leu Arg Lys Lys Phe Ser Ala Ser Arg Phe Trp Asp Asp  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Cys Val Lys Tyr Asn Cys Thr Val Val Gln Tyr Val Gly Glu Val Cys  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Arg Tyr Leu Leu His Thr Pro Ile Ser Lys Tyr Glu Lys Met His Lys  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Val Lys Val Ala Tyr Gly Asn Gly Leu Arg Pro Asp Ile Trp Gln Asp  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Phe Arg Lys Arg Phe Asn Ile Glu Val Ile Gly Glu Phe Tyr Ala Ala  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Thr Glu Ala Pro Phe Ala Thr Thr Thr Phe Gln Lys Gly Asp Phe Gly  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Ile Gly Ala Cys Arg Asn Tyr Gly Thr Ile Ile Gln Trp Phe Leu Ser  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Phe Gln Gln Thr Leu Val Arg Met Asp Pro Asn Asp Asp Ser Val Ile  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Tyr Arg Asn Ser Lys Gly Phe Cys Glu Val Ala Pro Val Gly Glu Pro  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Glu Met Leu Met Arg Ile Phe Phe Pro Lys Lys Pro Glu Thr Ser  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Phe Gln Gly Tyr Leu Gly Asn Ala Lys Glu Thr Lys Ser Lys Val Val  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Arg Asp Val Phe Arg Arg Gly Asp Ala Trp Tyr Arg Cys Gly Asp Leu  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Leu Lys Ala Asp Glu Tyr Gly Leu Trp Tyr Phe Leu Asp Arg Met Gly  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Asp Thr Phe Arg Trp Lys Ser Glu Asn Val Ser Thr Thr Glu Val Glu  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Asp Gln Leu Thr Ala Ser Asn Lys Glu Gln Tyr Ala Gln Val Leu Val  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Val Gly Ile Lys Val Pro Lys Tyr Glu Gly Arg Ala Gly Phe Ala Val  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Ile Lys Leu Thr Asp Asn Ser Leu Asp Ile Thr Ala Lys Thr Lys Leu  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Leu Asn Asp Ser Leu Ser Arg Leu Asn Leu Pro Ser Tyr Ala Met Pro  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Leu Phe Val Lys  
               
               
                         355  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 5  
               
               
                 &lt;211&gt; LENGTH: 334  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mycobacterium tuberculosis  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 5  
               
               
                   
               
               
                 Tyr Ile Phe Thr Ser Gly Thr Thr Gly Phe Pro Lys Ala Ser Val Met  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Thr His His Arg Trp Leu Arg Ala Leu Ala Val Phe Gly Gly Met Gly  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Leu Arg Leu Lys Gly Ser Asp Thr Leu Tyr Ser Cys Leu Pro Leu Tyr  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 His Asn Asn Ala Leu Thr Val Ala Val Ser Ser Val Ile Asn Ser Gly  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Ala Thr Leu Ala Leu Gly Lys Ser Phe Ser Ala Ser Arg Phe Trp Asp  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Glu Val Ile Ala Asn Arg Ala Thr Ala Phe Val Tyr Ile Gly Glu Ile  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Cys Arg Tyr Leu Leu Asn Gln Pro Ala Lys Pro Thr Asp Arg Ala His  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Gln Val Arg Val Ile Cys Gly Asn Gly Leu Arg Pro Glu Ile Trp Asp  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Glu Phe Thr Thr Arg Phe Gly Val Ala Arg Val Cys Glu Phe Tyr Ala  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ala Ser Glu Gly Asn Ser Ala Phe Ile Asn Ile Phe Asn Val Pro Arg  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Thr Ala Gly Val Ser Pro Met Pro Leu Ala Phe Val Glu Tyr Asp Leu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asp Thr Gly Asp Pro Leu Arg Asp Ala Ser Gly Arg Val Arg Arg Val  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Pro Asp Gly Glu Pro Gly Leu Leu Leu Ser Arg Val Asn Arg Leu Gln  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Pro Phe Asp Gly Tyr Thr Asp Pro Val Ala Ser Glu Lys Lys Leu Val  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Arg Asn Ala Phe Arg Asp Gly Asp Cys Trp Phe Asn Thr Gly Asp Val  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Met Ser Pro Gln Gly Met Gly His Ala Ala Phe Val Asp Arg Leu Gly  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala Thr Thr Gln Val Glu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Ala Ala Leu Ala Ser Asp Gln Thr Val Glu Glu Cys Thr Val Tyr Gly  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Val Gln Ile Pro Arg Thr Gly Gly Arg Ala Gly Met Ala Ala Ile Thr  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Leu Arg Ala Gly Ala Glu Phe Asp Gly Gln Ala Leu Ala Arg Thr Val  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Tyr Gly His Leu Pro Gly Tyr Ala Leu Pro Leu Phe Val Arg  
               
               
                                 325                 330  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 6  
               
               
                 &lt;211&gt; LENGTH: 2087  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 6  
               
               
                   
               
               
                 acgactcact atagggagag agctatgacg tcgcatgcac gcgtaagctt gggcccctcg     60  
               
               
                   
               
               
                 agggatcctc tagagcggcc gccgaccccg aaagctctga gagcgggtgc agtctggcct    120  
               
               
                   
               
               
                 ggcgtctcgc gtacctggcc cgggagcagc cgacacacac cttcctcatc cacggcgcgc    180  
               
               
                   
               
               
                 agcgctttag ctacgcggag gctgagcgcg agagcaaccg gattgctcgc gcctttctgc    240  
               
               
                   
               
               
                 gcgcacgggg ctggaccggg ggccgccgag gctcgggcag gggcagcact gaggaaggcg    300  
               
               
                   
               
               
                 cacgcgtggc gcctccggct ggagatgcgg ctgctagagg gacgaccgcg ccccctctgg    360  
               
               
                   
               
               
                 cacccggggc gaccgtggcg ctgctcctcc cagcgggccc ggatttcctt tggatttggt    420  
               
               
                   
               
               
                 tcggactggc caaagctggc ctgcgcacgg cctttgtgcc caccgcttta cgccgaggac    480  
               
               
                   
               
               
                 ccctgctgca ctgcctccgc agctgcggtg cgagtgcgct cgtgctggcc acagagttcc    540  
               
               
                   
               
               
                 tggagtccct ggagccggac ctgccggcct tgagagccat ggggctccac ctatgggcga    600  
               
               
                   
               
               
                 cgggccctga aactaatgta gctggaatca gcaatttgct atcggaagca gcagaccaag    660  
               
               
                   
               
               
                 tggatgagcc agtgccgggg tacctctctg ccccccagaa cataatggac acctgcctgt    720  
               
               
                   
               
               
                 acatcttcac ctctggcact actggcctgc ccaaggctgc tcgaatcagt catctgaagg    780  
               
               
                   
               
               
                 ttctacagtg ccagggattc taccatctgt gtggagtcca ccaggaggac gtgatctacc    840  
               
               
                   
               
               
                 tcgcactccc actgtaccac atgtctggct cccttctggg cattgtgggc tgcttgggca    900  
               
               
                   
               
               
                 ttggggccac cgtggtgctg aaacccaagt tctcagctag ccagttctgg gacgattgcc    960  
               
               
                   
               
               
                 agaaacacag ggtgacagtg ttccagtaca ttggggagtt gtgccgatac ctcgtcaacc   1020  
               
               
                   
               
               
                 agcccccgag caaggcagag tttgaccata aggtgcgctt ggcagtgggc agtgggttgc   1080  
               
               
                   
               
               
                 gcccagacac ctgggagcgt ttcctgcggc gatttggacc tctgcagata ctggagacgt   1140  
               
               
                   
               
               
                 atggcatgac agagggcaac gtagctacgt tcaattacac aggacggcag ggtgcagtgg   1200  
               
               
                   
               
               
                 ggcgagcttc ctggctttac aagcacatct tccccttctc cttgattcga tacgatgtca   1260  
               
               
                   
               
               
                 tgacagggga gcctattcgg aatgcccagg ggcactgcat gaccacatct ccaggtgagc   1320  
               
               
                   
               
               
                 caggcctact ggtggcccca gtgagccagc agtccccctt cctgggctat gctggggctc   1380  
               
               
                   
               
               
                 cggagctggc caaggacaag ctgctgaagg atgtcttctg gtctggggac gttttcttca   1440  
               
               
                   
               
               
                 atactgggga cctcttggtc tgtgatgagc aaggctttct tcacttccac gatcgtactg   1500  
               
               
                   
               
               
                 gagacaccat caggtggaag ggagagaatg tggccacaac tgaagtggct gaggtcttgg   1560  
               
               
                   
               
               
                 agaccctgga cttccttcag gaggtgaaca tctatggagt cacggtgcca gggcacgaag   1620  
               
               
                   
               
               
                 gcagggcagg catggcggcc ttggctctgc ggcccccgca ggctctgaac ctggtgcagc   1680  
               
               
                   
               
               
                 tctacagcca tgtttctgag aacttgccac cgtatgcccg acctcggttt ctcaggctcc   1740  
               
               
                   
               
               
                 aggaatcttt ggccactact gagaccttca aacagcagaa ggttaggatg gccaatgagg   1800  
               
               
                   
               
               
                 gctttgaccc cagtgtactg tctgacccac tctatgttct ggaccaagat ataggggcct   1860  
               
               
                   
               
               
                 acctgcccct cacacctgcc cggtacagtg ccctcctgtc tggagacctt cgaatctgaa   1920  
               
               
                   
               
               
                 accttccact tgagggaggg gctcggaggg tacaggccac catggctgca ccagggaggg   1980  
               
               
                   
               
               
                 ttttcgggta tcttttgtat atggagtcat tattttgtaa taaacagctg gagcttaaaa   2040  
               
               
                   
               
               
                 aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaa                 2087  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 7  
               
               
                 &lt;211&gt; LENGTH: 613  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 7  
               
               
                   
               
               
                 Ala Ala Asp Pro Glu Ser Ser Glu Ser Gly Cys Ser Leu Ala Trp Arg  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Ala Tyr Leu Ala Arg Glu Gln Pro Thr His Thr Phe Leu Ile His  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Ala Gln Arg Phe Ser Tyr Ala Glu Ala Glu Arg Glu Ser Asn Arg  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ile Ala Arg Ala Phe Leu Arg Ala Arg Gly Trp Thr Gly Gly Arg Arg  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Gly Ser Gly Arg Gly Ser Thr Glu Glu Gly Ala Arg Val Ala Pro Pro  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Gly Asp Ala Ala Ala Arg Gly Thr Thr Ala Pro Pro Leu Ala Pro  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Ala Thr Val Ala Leu Leu Leu Pro Ala Gly Pro Asp Phe Leu Trp  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ile Trp Phe Gly Leu Ala Lys Ala Gly Leu Arg Thr Ala Phe Val Pro  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Thr Ala Leu Arg Arg Gly Pro Leu Leu His Cys Leu Arg Ser Cys Gly  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ala Ser Ala Leu Val Leu Ala Thr Glu Phe Leu Glu Ser Leu Glu Pro  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asp Leu Pro Ala Leu Arg Ala Met Gly Leu His Leu Trp Ala Thr Gly  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Pro Glu Thr Asn Val Ala Gly Ile Ser Asn Leu Leu Ser Glu Ala Ala  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Asp Gln Val Asp Glu Pro Val Pro Gly Tyr Leu Ser Ala Pro Gln Asn  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Ile Met Asp Thr Cys Leu Tyr Ile Phe Thr Ser Gly Thr Thr Gly Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Pro Lys Ala Ala Arg Ile Ser His Leu Lys Val Leu Gln Cys Gln Gly  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Phe Tyr His Leu Cys Gly Val His Gln Glu Asp Val Ile Tyr Leu Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Leu Pro Leu Tyr His Met Ser Gly Ser Leu Leu Gly Ile Val Gly Cys  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Leu Gly Ile Gly Ala Thr Val Val Leu Lys Pro Lys Phe Ser Ala Ser  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Gln Phe Trp Asp Asp Cys Gln Lys His Arg Val Thr Val Phe Gln Tyr  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ile Gly Glu Leu Cys Arg Tyr Leu Val Asn Gln Pro Pro Ser Lys Ala  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Glu Phe Asp His Lys Val Arg Leu Ala Val Gly Ser Gly Leu Arg Pro  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Asp Thr Trp Glu Arg Phe Leu Arg Arg Phe Gly Pro Leu Gln Ile Leu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Glu Thr Tyr Gly Met Thr Glu Gly Asn Val Ala Thr Phe Asn Tyr Thr  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Gly Arg Gln Gly Ala Val Gly Arg Ala Ser Trp Leu Tyr Lys His Ile  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Phe Pro Phe Ser Leu Ile Arg Tyr Asp Val Met Thr Gly Glu Pro Ile  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Arg Asn Ala Gln Gly His Cys Met Thr Thr Ser Pro Gly Glu Pro Gly  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Leu Leu Val Ala Pro Val Ser Gln Gln Ser Pro Phe Leu Gly Tyr Ala  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Gly Ala Pro Glu Leu Ala Lys Asp Lys Leu Leu Lys Asp Val Phe Trp  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Ser Gly Asp Val Phe Phe Asn Thr Gly Asp Leu Leu Val Cys Asp Glu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gln Gly Phe Leu His Phe His Asp Arg Thr Gly Asp Thr Ile Arg Trp  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Lys Gly Glu Asn Val Ala Thr Thr Glu Val Ala Glu Val Leu Glu Thr  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Leu Asp Phe Leu Gln Glu Val Asn Ile Tyr Gly Val Thr Val Pro Gly  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 His Glu Gly Arg Ala Gly Met Ala Ala Leu Ala Leu Arg Pro Pro Gln  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ala Leu Asn Leu Val Gln Leu Tyr Ser His Val Ser Glu Asn Leu Pro  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Tyr Ala Arg Pro Arg Phe Leu Arg Leu Gln Glu Ser Leu Ala Thr  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Thr Glu Thr Phe Lys Gln Gln Lys Val Arg Met Ala Asn Glu Gly Phe  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Asp Pro Ser Val Leu Ser Asp Pro Leu Tyr Val Leu Asp Gln Asp Ile  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Gly Ala Tyr Leu Pro Leu Thr Pro Ala Arg Tyr Ser Ala Leu Leu Ser  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Gly Asp Leu Arg Ile  
               
               
                     610  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 8  
               
               
                 &lt;211&gt; LENGTH: 2301  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 8  
               
               
                   
               
               
                 cccacgcgtc cgcccacgcg tccggcatgg ccaagctggg cgtggaggcg gctctcatca     60  
               
               
                   
               
               
                 acaccaacct taggcgggat gccctgcgcc actgtcttga cacctcaaag gcacgagctc    120  
               
               
                   
               
               
                 tcatctttgg cagtgagatg gcctcagcta tctgtgagat ccatgctagc ctggagccca    180  
               
               
                   
               
               
                 cactcagcct cttctgctct ggatcctggg agcccagcac agtgcccgtc agcacagagc    240  
               
               
                   
               
               
                 atctggaccc tcttctggaa gatgccccga agcacctgcc cagtcaccca gacaagggtt    300  
               
               
                   
               
               
                 ttacagataa gctcttctac atctacacat cgggcaccac ggggctaccc aaagctgcca    360  
               
               
                   
               
               
                 ttgtggtgca cagcaggtat tatcgtatgg cttccctggt gtactatgga ttccgcatgc    420  
               
               
                   
               
               
                 ggcctgatga cattgtctat gactgcctcc ccctctacca ctcaagcagg aaacatcgtg    480  
               
               
                   
               
               
                 gggattggca gtgcttactc cacggcatga ctgtggtgat ccggaagaag ttctcagcct    540  
               
               
                   
               
               
                 cccggttctg ggatgattgt atcaagtaca actgcacagt ggtacagtac attggcgagc    600  
               
               
                   
               
               
                 tctgccgcta cctcctgaac cagccacccc gtgaggctga gtctcggcac aaggtgcgca    660  
               
               
                   
               
               
                 tggcactggg caacggtctc cggcagtcca tctggaccga cttctccagc cgtttccaca    720  
               
               
                   
               
               
                 tcccccaggt ggctgagttc tatggggcca ctgaatgcaa ctgtagcctg ggcaactttg    780  
               
               
                   
               
               
                 acagccgggt gggggcctgt ggcttcaata gccgcatcct gtcctttgtg taccctatcc    840  
               
               
                   
               
               
                 gtttggtacg tgtcaatgag gataccatgg aactgatccg gggacccgat ggagtctgca    900  
               
               
                   
               
               
                 ttccctgtca accaggtcag ccaggccagc tggtgggtcg catcatccag caggaccctc    960  
               
               
                   
               
               
                 tgcgccgttt cgacgggtac ctcaaccagg gtgccaacaa caagaagatt gctaatgatg   1020  
               
               
                   
               
               
                 tcttcaagaa gggggaccaa gcctacctca ctggtgacgt cctggtgatg gatgagctgg   1080  
               
               
                   
               
               
                 gttacctgta cttccgagat cgcactgggg acacgttccg ctggaaaggg gagaatgtat   1140  
               
               
                   
               
               
                 ctaccactga ggtggagggc acactcagcc gcctgcttca tatggcagat gtggcagttt   1200  
               
               
                   
               
               
                 atggtgttga ggtgccagga actgaaggcc gagcaggaat ggctgccgtt gcaagtccca   1260  
               
               
                   
               
               
                 tcagcaactg tgacctggag agctttgcac agaccttgaa aaaggagctg cctctgtatg   1320  
               
               
                   
               
               
                 cccgccccat cttcctgcgc ttcttgcctg agctgcacaa gacagggacc ttcaagttcc   1380  
               
               
                   
               
               
                 agaagacaga gttgcggaag gagggctttg acccatctgt tgtgaaagac ccgctgttct   1440  
               
               
                   
               
               
                 atctggatgc tcggaagggc tgctacgttg cactggacca ggaggcctat acccgcatcc   1500  
               
               
                   
               
               
                 aggcaggcga ggagaagctg tgatttcccc ctacatccct ctgagggcca gaagatgctg   1560  
               
               
                   
               
               
                 gattcagagc cctagcgtcc accccagagg gtcctgggca atgccagacc aaagctagca   1620  
               
               
                   
               
               
                 gggcccgcac ctccgcccct aggtgctgat ctcccctctc ccaaactgcc aagtgactca   1680  
               
               
                   
               
               
                 ctgccgcttc cccgaccctc cagaggcttt ctgtgaaagt ctcatccaag ctgtgtcttc   1740  
               
               
                   
               
               
                 tggtccaggc gtggcccctg gccccagggt ttctgatagg ctcctttagg atggtatctt   1800  
               
               
                   
               
               
                 gggtccagcg ggccagggtg tgggagagga gtcactaaga tccctccaat cagaagggag   1860  
               
               
                   
               
               
                 cttacaaagg aaccaaggca aagcctgtag actcaggaag ctaagtggcc agagactata   1920  
               
               
                   
               
               
                 gtggccagtc atcccatgtc cacagaggat cttggtccag agctgccaaa gtgtcacctc   1980  
               
               
                   
               
               
                 tccctgcctg cacctctggg gaaaagagga cagcatgtgg ccactgggca cctgtctcaa   2040  
               
               
                   
               
               
                 gaagtcagga tcacacactc agtccttgtt tctccaggtt cccttgttct tgtctcgggg   2100  
               
               
                   
               
               
                 agggagggac gagtgtcctg tctgtccttc ctgcctgtct gtgagtctgt gttgcttctc   2160  
               
               
                   
               
               
                 catctgtcct agcctgagtg tgggtggaac aggcatgagg agagtgtggc tcaggggcca   2220  
               
               
                   
               
               
                 ataaactctg ccttgactcc tcttaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa   2280  
               
               
                   
               
               
                 aaaaaaaaaa aaaaaaaaaa a                                             2301  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 9  
               
               
                 &lt;211&gt; LENGTH: 506  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 9  
               
               
                   
               
               
                 His Ala Ser Ala His Ala Ser Gly Met Ala Lys Leu Gly Val Glu Ala  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ala Leu Ile Asn Thr Asn Leu Arg Arg Asp Ala Leu Arg His Cys Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Asp Thr Ser Lys Ala Arg Ala Leu Ile Phe Gly Ser Glu Met Ala Ser  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ala Ile Cys Glu Ile His Ala Ser Leu Glu Pro Thr Leu Ser Leu Phe  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Cys Ser Gly Ser Trp Glu Pro Ser Thr Val Pro Val Ser Thr Glu His  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Leu Asp Pro Leu Leu Glu Asp Ala Pro Lys His Leu Pro Ser His Pro  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Lys Gly Phe Thr Asp Lys Leu Phe Tyr Ile Tyr Thr Ser Gly Thr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Thr Gly Leu Pro Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Met Ala Ser Leu Val Tyr Tyr Gly Phe Arg Met Arg Pro Asp Asp Ile  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Val Tyr Asp Cys Leu Pro Leu Tyr His Ser Ser Arg Lys His Arg Gly  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asp Trp Gln Cys Leu Leu His Gly Met Thr Val Val Ile Arg Lys Lys  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Phe Ser Ala Ser Arg Phe Trp Asp Asp Cys Ile Lys Tyr Asn Cys Thr  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Val Val Gln Tyr Ile Gly Glu Leu Cys Arg Tyr Leu Leu Asn Gln Pro  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Pro Arg Glu Ala Glu Ser Arg His Lys Val Arg Met Ala Leu Gly Asn  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Gly Leu Arg Gln Ser Ile Trp Thr Asp Phe Ser Ser Arg Phe His Ile  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Pro Gln Val Ala Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Leu  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Gly Asn Phe Asp Ser Arg Val Gly Ala Cys Gly Phe Asn Ser Arg Ile  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Leu Ser Phe Val Tyr Pro Ile Arg Leu Val Arg Val Asn Glu Asp Thr  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Met Glu Leu Ile Arg Gly Pro Asp Gly Val Cys Ile Pro Cys Gln Pro  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Gly Gln Pro Gly Gln Leu Val Gly Arg Ile Ile Gln Gln Asp Pro Leu  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Arg Arg Phe Asp Gly Tyr Leu Asn Gln Gly Ala Asn Asn Lys Lys Ile  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ala Asn Asp Val Phe Lys Lys Gly Asp Gln Ala Tyr Leu Thr Gly Asp  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Val Leu Val Met Asp Glu Leu Gly Tyr Leu Tyr Phe Arg Asp Arg Thr  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ser Thr Thr Glu Val  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Glu Gly Thr Leu Ser Arg Leu Leu His Met Ala Asp Val Ala Val Tyr  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Val Glu Val Pro Gly Thr Glu Gly Arg Ala Gly Met Ala Ala Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Ala Ser Pro Ile Ser Asn Cys Asp Leu Glu Ser Phe Ala Gln Thr Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Lys Lys Glu Leu Pro Leu Tyr Ala Arg Pro Ile Phe Leu Arg Phe Leu  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Pro Glu Leu His Lys Thr Gly Thr Phe Lys Phe Gln Lys Thr Glu Leu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Arg Lys Glu Gly Phe Asp Pro Ser Val Val Lys Asp Pro Leu Phe Tyr  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Leu Asp Ala Arg Lys Gly Cys Tyr Val Ala Leu Asp Gln Glu Ala Tyr  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Thr Arg Ile Gln Ala Gly Glu Glu Lys Leu  
               
               
                             500                 505  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 10  
               
               
                 &lt;211&gt; LENGTH: 2277  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 10  
               
               
                   
               
               
                 cactcatcag agctaagaga gactacacgc tctcatctac ttcagaaaga gccaatgcca     60  
               
               
                   
               
               
                 tgggtatttg gaagaaacta accttactgc tgttgctgct tctgctggtt ggcctggggc    120  
               
               
                   
               
               
                 agcccccatg gccagcagct atggctctgg ccctgcgttg gttcctggga gaccccacat    180  
               
               
                   
               
               
                 gccttgtgct gcttggcttg gcattgctgg gcagaccctg gatcagctcc tggatgcccc    240  
               
               
                   
               
               
                 actggctgag cctggtagga gcagctctta ccttattcct attgcctcta cagccacccc    300  
               
               
                   
               
               
                 cagggctacg ctggctgcat aaagatgtgg ctttcacctt caagatgctt ttctatggcc    360  
               
               
                   
               
               
                 taaagttcag gcgacgcctt aacaaacatc ctccagagac ctttgtggat gctttagagc    420  
               
               
                   
               
               
                 ggcaagcact ggcatggcct gaccgggtgg ccttggtgtg tactgggtct gagggctcct    480  
               
               
                   
               
               
                 caatcacaaa tagccagctg gatgccaggt cctgtcaggc agcatgggtc ctgaaagcaa    540  
               
               
                   
               
               
                 agctgaagga tgccgtaatc cagaacacaa gagatgctgc tgctatctta gttctcccgt    600  
               
               
                   
               
               
                 ccaagaccat ttctgctttg agtgtgtttc tggggttggc caagttgggc tgccctgtgg    660  
               
               
                   
               
               
                 cctggatcaa tccacacagc cgagggatgc ccttgctaca ctctgtacgg agctctgggg    720  
               
               
                   
               
               
                 ccagtgtgct gattgtggat ccagacctcc aggagaacct ggaagaagtc cttcccaagc    780  
               
               
                   
               
               
                 tgctagctga gaacattcac tgcttctacc ttggccacag ctcacccacc ccgggagtag    840  
               
               
                   
               
               
                 aggctctggg agcttccctg gatgctgcac cttctgaccc agtacctgcc agccttcgag    900  
               
               
                   
               
               
                 ctacgattaa gtggaaatct cctgccatat tcatctttac ttcagggacc actggactcc    960  
               
               
                   
               
               
                 caaagccagc catcttatca catgagcggg tcatacaagt gagcaacgtg ctgtccttct   1020  
               
               
                   
               
               
                 gtggatgcag agctgatgat gtggtctatg acgtcctacc tctgtaccat acgatagggc   1080  
               
               
                   
               
               
                 ttgtccttgg attccttggc tgcttacaag ttggagccac ctgtgtcctg gcccccaagt   1140  
               
               
                   
               
               
                 tctctgcctc ccgattctgg gctgagtgcc ggcagcatgg cgtaacagtg atcttgtatg   1200  
               
               
                   
               
               
                 tgggtgaaat cctgcggtac ttgtgtaacg tccctgagca accagaagac aagatacata   1260  
               
               
                   
               
               
                 cagtgcgctt ggccatggga actggacttc gggcaaatgt gtggaaaaac ttccagcaac   1320  
               
               
                   
               
               
                 gctttggtcc cattcggatc tgggaattct acggatccac agagggcaat gtgggcttaa   1380  
               
               
                   
               
               
                 tgaactatgt gggccactgc ggggctgtgg gaaggaccag ctgcatcctt cgaatgctga   1440  
               
               
                   
               
               
                 ctccctttga gcttgtacag ttcgacatag agacagcaga gcctctgagg gacaaacagg   1500  
               
               
                   
               
               
                 gtttttgcat tcctgtggag ccaggaaagc caggacttct tttgaccaag gttcgaaaga   1560  
               
               
                   
               
               
                 accaaccctt cctgggctac cgtggttccc aggccgagtc caatcggaaa cttgttgcga   1620  
               
               
                   
               
               
                 atgtacgacg cgtaggagac ctgtacttca acactgggga cgtgctgacc ttggaccagg   1680  
               
               
                   
               
               
                 aaggcttctt ctactttcaa gaccgccttg gtgacacctt ccggtggaag ggcgaaaacg   1740  
               
               
                   
               
               
                 tatctactgg agaggtggag tgtgttttgt ctagcctaga cttcctagag gaagtcaatg   1800  
               
               
                   
               
               
                 tctatggtgt gcctgtgcca gggtgtgagg gtaaggttgg catggctgct gtgaaactgg   1860  
               
               
                   
               
               
                 ctcctgggaa gacttttgat gggcagaagc tataccagca tgtccgctcc tggctccctg   1920  
               
               
                   
               
               
                 cctatgccac acctcatttc atccgtatcc aggattccct ggagatcaca aacacctaca   1980  
               
               
                   
               
               
                 agctggtaaa gtcacggctg gtgcgtgagg gttttgatgt ggggatcatt gctgaccccc   2040  
               
               
                   
               
               
                 tctacatact ggacaacaag gcccagacct tccggagtct gatgccagat gtgtaccagg   2100  
               
               
                   
               
               
                 ctgtgtgtga aggaacctgg aatctctgac cacctagcca actggaaggc aatccaaaag   2160  
               
               
                   
               
               
                 tgtagagatt gacactagtc agcttcacaa agttgtccgg gttccagatg cccatggccc   2220  
               
               
                   
               
               
                 agtagtactt agagaataaa cttgaatgtg tatacaaaaa aaaaaaaaaa aaaaaaa      2277  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 11  
               
               
                 &lt;211&gt; LENGTH: 662  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 11  
               
               
                   
               
               
                 Met Ala Leu Ala Leu Arg Trp Phe Leu Gly Asp Pro Thr Cys Leu Val  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Leu Gly Leu Ala Leu Leu Gly Arg Pro Trp Ile Ser Ser Trp Met  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Pro His Trp Leu Ser Leu Val Gly Ala Ala Leu Thr Leu Phe Leu Leu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Pro Leu Gln Pro Pro Pro Gly Leu Arg Trp Leu His Lys Asp Val Ala  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Phe Thr Phe Lys Met Leu Phe Tyr Gly Leu Lys Phe Arg Arg Arg Leu  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Asn Lys His Pro Pro Glu Thr Phe Val Asp Ala Leu Glu Arg Gln Ala  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Leu Ala Trp Pro Asp Arg Val Ala Leu Val Cys Thr Gly Ser Glu Gly  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Ser Ile Thr Asn Ser Gln Leu Asp Ala Arg Ser Cys Gln Ala Ala  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Trp Val Leu Lys Ala Lys Leu Lys Asp Ala Val Ile Gln Asn Thr Arg  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Asp Ala Ala Ala Ile Leu Val Leu Pro Ser Lys Thr Ile Ser Ala Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Ser Val Phe Leu Gly Leu Ala Lys Leu Gly Cys Pro Val Ala Trp Ile  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asn Pro His Ser Arg Gly Met Pro Leu Leu His Ser Val Arg Ser Ser  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Gly Ala Ser Val Leu Ile Val Asp Pro Asp Leu Gln Glu Asn Leu Glu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Glu Val Leu Pro Lys Leu Leu Ala Glu Asn Ile His Cys Phe Tyr Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Gly His Ser Ser Pro Thr Pro Gly Val Glu Ala Leu Gly Ala Ser Leu  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asp Ala Ala Pro Ser Asp Pro Val Pro Ala Ser Leu Arg Ala Thr Ile  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Trp Lys Ser Pro Ala Ile Phe Ile Phe Thr Ser Gly Thr Thr Gly  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Leu Pro Lys Pro Ala Ile Leu Ser His Glu Arg Val Ile Gln Val Ser  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Asn Val Leu Ser Phe Cys Gly Cys Arg Ala Asp Asp Val Val Tyr Asp  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Val Leu Pro Leu Tyr His Thr Ile Gly Leu Val Leu Gly Phe Leu Gly  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Cys Leu Gln Val Gly Ala Thr Cys Val Leu Ala Pro Lys Phe Ser Ala  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ser Arg Phe Trp Ala Glu Cys Arg Gln His Gly Val Thr Val Ile Leu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Tyr Val Gly Glu Ile Leu Arg Tyr Leu Cys Asn Val Pro Glu Gln Pro  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Glu Asp Lys Ile His Thr Val Arg Leu Ala Met Gly Thr Gly Leu Arg  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Ala Asn Val Trp Lys Asn Phe Gln Gln Arg Phe Gly Pro Ile Arg Ile  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Trp Glu Phe Tyr Gly Ser Thr Glu Gly Asn Val Gly Leu Met Asn Tyr  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Val Gly His Cys Gly Ala Val Gly Arg Thr Ser Cys Ile Leu Arg Met  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Leu Thr Pro Phe Glu Leu Val Gln Phe Asp Ile Glu Thr Ala Glu Pro  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Arg Asp Lys Gln Gly Phe Cys Ile Pro Val Glu Pro Gly Lys Pro  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gly Leu Leu Leu Thr Lys Val Arg Lys Asn Gln Pro Phe Leu Gly Tyr  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Arg Gly Ser Gln Ala Glu Ser Asn Arg Lys Leu Val Ala Asn Val Arg  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Arg Val Gly Asp Leu Tyr Phe Asn Thr Gly Asp Val Leu Thr Leu Asp  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Gln Glu Gly Phe Phe Tyr Phe Gln Asp Arg Leu Gly Asp Thr Phe Arg  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Trp Lys Gly Glu Asn Val Ser Thr Gly Glu Val Glu Cys Val Leu Ser  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Ser Leu Asp Phe Leu Glu Glu Val Asn Val Tyr Gly Val Pro Val Pro  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Gly Cys Glu Gly Lys Val Gly Met Ala Ala Val Lys Leu Ala Pro Gly  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Lys Thr Phe Asp Gly Gln Lys Leu Tyr Gln His Val Arg Ser Trp Leu  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Pro Ala Tyr Ala Thr Pro His Phe Ile Arg Ile Gln Asp Ser Leu Glu  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ile Thr Asn Thr Tyr Lys Leu Val Lys Ser Arg Leu Val Arg Glu Gly  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Phe Asp Val Gly Ile Ile Ala Asp Pro Leu Tyr Ile Leu Asp Asn Lys  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Ala Gln Thr Phe Arg Ser Leu Met Pro Asp Val Tyr Gln Ala Val Cys  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Glu Gly Thr Trp Asn Leu  
               
               
                             660  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 12  
               
               
                 &lt;211&gt; LENGTH: 1622  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: (1)...(1622)  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 998, 1022, 1027, 1078, 1094, 1121, 1128, 1202, 1275,  
               
               
                       1292,1308  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 12  
               
               
                   
               
               
                 atgggattga ctctttcctg gacaaagtgg atgaagtatc aactgaacct atcccagagt     60  
               
               
                   
               
               
                 catggaggtc tgaagtcact ttttccactc ctgccttata catttatact tctggaacca    120  
               
               
                   
               
               
                 caggtcttcc aaaagcagcc atgatcactc atcagcgcat atggtatgga actggcctca    180  
               
               
                   
               
               
                 cttttgtaag cggattgaag gcagatgatg tcatctatat cactctgccc ttttaccaca    240  
               
               
                   
               
               
                 gtgctgcact actgattggc attcacggat gtattgtggc tggtgctact cttgccttgc    300  
               
               
                   
               
               
                 ggactaaatt ttcagccagc cagttttggg atgactgcag aaaatacaac gtcactgtca    360  
               
               
                   
               
               
                 ttcagtatat cggtgaactg cttcggtatt tatgcaactc accacagaaa ccaaatgacc    420  
               
               
                   
               
               
                 gtgatcataa agtgagactg gcactgggaa atggcttacg aggagatgtg tggagacaat    480  
               
               
                   
               
               
                 ttgtcaagag atttggggac atatgcatct atgagttcta tgctgccact gaaggcaata    540  
               
               
                   
               
               
                 ttggatttat gaattatgcg agaaaagttg gtgctgttgg aagagtaaac tacctacaga    600  
               
               
                   
               
               
                 aaaaaatcat aacttatgac ctgattaaat atgatgtgga gaaagatgaa cctgtccgtg    660  
               
               
                   
               
               
                 atgaaaatgg atattgcgtc agagttccca aaggtgaagt tggacttctg gtttgcaaaa    720  
               
               
                   
               
               
                 tcacacaact tacaccattt aatggctatg ctggagcaaa ggctcagaca gagaagaaaa    780  
               
               
                   
               
               
                 aactgagaga tgtctttaag aaaggagacc tctatttcaa cagtggagat ctcttaatgg    840  
               
               
                   
               
               
                 ttgaccatga aaatttcatc tatttccacg acagagttgg agatacattc cggtggaaag    900  
               
               
                   
               
               
                 gggaaaatgt ggccaccact gaagttgctg atatagttgg actggttgat ttttttccaa    960  
               
               
                   
               
               
                 ggaagtaaaa tgtttatggg agtgcatggg ccaagatnat ggaggttcga attggcatgg   1020  
               
               
                   
               
               
                 cnttccnttc aaaatggaaa gaaaaccatg gaatttgatg gaaagaaatt ttttcagnac   1080  
               
               
                   
               
               
                 attgctgata accnacctag ttatgcaagg ccccggtttt ntaagaanac aggacaccat   1140  
               
               
                   
               
               
                 tgagatcact ggaattttta aacaccgcaa aatgaccttt ggtggaggag ggctttaacc   1200  
               
               
                   
               
               
                 cngctgtcat caaagatgcc ttgtattttc ttggatgaca cagcaaaaat gtatgtgcct   1260  
               
               
                   
               
               
                 atgactgagg acatntataa tgccataagt gntaaaaccc tgaaattntg aatattccca   1320  
               
               
                   
               
               
                 ggaggataat tcaacatttc cagaaagaaa ctgaatggac agccacttga tataatccaa   1380  
               
               
                   
               
               
                 ctttaatttg attgaagatt gtgaggaaat tttgtaggaa atttgcatac ccgtaaaggg   1440  
               
               
                   
               
               
                 agactttttt aaataacagt tgagtctttg caagtaaaaa gatttagaga ttattatttt   1500  
               
               
                   
               
               
                 tcagtgtgca cctactgttt gtatttgcaa actgagcttg ttggagggaa ggcattattt   1560  
               
               
                   
               
               
                 tttaaaatac ttagtaaatt aaagaacacc aacatgtgaa aaaaaaaaaa aaaaaaaaaa   1620  
               
               
                   
               
               
                 aa                                                                  1622  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 13  
               
               
                 &lt;211&gt; LENGTH: 286  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 13  
               
               
                   
               
               
                 Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala Met Ile  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Thr His Gln Arg Ile Trp Tyr Gly Thr Gly Leu Thr Phe Val Ser Gly  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Leu Lys Ala Asp Asp Val Ile Tyr Ile Thr Leu Pro Phe Tyr His Ser  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ala Ala Leu Leu Ile Gly Ile His Gly Cys Ile Val Ala Gly Ala Thr  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Leu Ala Leu Arg Thr Lys Phe Ser Ala Ser Gln Phe Trp Asp Asp Cys  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Arg Lys Tyr Asn Val Thr Val Ile Gln Tyr Ile Gly Glu Leu Leu Arg  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Tyr Leu Cys Asn Ser Pro Gln Lys Pro Asn Asp Arg Asp His Lys Val  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Arg Leu Ala Leu Gly Asn Gly Leu Arg Gly Asp Val Trp Arg Gln Phe  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Val Lys Arg Phe Gly Asp Ile Cys Ile Tyr Glu Phe Tyr Ala Ala Thr  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Glu Gly Asn Ile Gly Phe Met Asn Tyr Ala Arg Lys Val Gly Ala Val  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Gly Arg Val Asn Tyr Leu Gln Lys Lys Ile Ile Thr Tyr Asp Leu Ile  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Lys Tyr Asp Val Glu Lys Asp Glu Pro Val Arg Asp Glu Asn Gly Tyr  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Cys Val Arg Val Pro Lys Gly Glu Val Gly Leu Leu Val Cys Lys Ile  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Thr Gln Leu Thr Pro Phe Asn Gly Tyr Ala Gly Ala Lys Ala Gln Thr  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Glu Lys Lys Lys Leu Arg Asp Val Phe Lys Lys Gly Asp Leu Tyr Phe  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asn Ser Gly Asp Leu Leu Met Val Asp His Glu Asn Phe Ile Tyr Phe  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 His Asp Arg Val Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Thr Thr Glu Val Ala Asp Ile Val Gly Leu Val Asp Phe Phe  
               
               
                         275                 280                 285  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 14  
               
               
                 &lt;211&gt; LENGTH: 753  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 14  
               
               
                   
               
               
                 caattcggga cccccagggg cactgtatgg ccacatctcc aggtgagcca ggggaagttg     60  
               
               
                   
               
               
                 ctaaaggatg tcttccggcc tggggatgtt ttcttcaaca ctggggacct gctggtctgc    120  
               
               
                   
               
               
                 gatgaccaag gttttctccg cttccatgat cgtactggag acaccttcag gtggaaaggg    180  
               
               
                   
               
               
                 gagaatgtgg ccacaaccga ggtggcagag gtcttcgagg ccctagattt tcttcaggag    240  
               
               
                   
               
               
                 gtgaacgtct atggagtcac tgtgccaggg catgaaggca gggctggaat ggcagcccta    300  
               
               
                   
               
               
                 gttctgcgtc ccccccacgc tttggacctt atgcagctct acacccacgt gtctgagaac    360  
               
               
                   
               
               
                 ttgccacctt atgcccggcc ccgattcctc aggctccagg agtctttggc caccacagag    420  
               
               
                   
               
               
                 accttcaaac agcagaaagt tcggatggca aatgagggct tcgaccccag caccctgtct    480  
               
               
                   
               
               
                 gacccactgt acgttctgga ccaggctgta ggtgcctacc tgcccctcac aactgcccgg    540  
               
               
                   
               
               
                 tacagcgccc tcctggcagg aaaccttcga atctgagaac ttccacacct gaggcacctg    600  
               
               
                   
               
               
                 agagaggaac tctgtggggt gggggccgtt gcaggtgtac tgggctgtca gggatctttt    660  
               
               
                   
               
               
                 ctataccaga actgcggtca ctattttgta ataaatgtgg ctggagctga tccagctgtc    720  
               
               
                   
               
               
                 tctgacctac aaaaaaaaaa aaaaaaaaaa aaa                                 753  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 15  
               
               
                 &lt;211&gt; LENGTH: 191  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 15  
               
               
                   
               
               
                 Gln Phe Gly Thr Pro Arg Gly Thr Val Trp Pro His Leu Gln Val Ser  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Gln Gly Lys Leu Leu Lys Asp Val Phe Arg Pro Gly Asp Val Phe Phe  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Asn Thr Gly Asp Leu Leu Val Cys Asp Asp Gln Gly Phe Leu Arg Phe  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 His Asp Arg Thr Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Thr Thr Glu Val Ala Glu Val Phe Glu Ala Leu Asp Phe Leu Gln Glu  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Val Asn Val Tyr Gly Val Thr Val Pro Gly His Glu Gly Arg Ala Gly  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Met Ala Ala Leu Val Leu Arg Pro Pro His Ala Leu Asp Leu Met Gln  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Leu Tyr Thr His Val Ser Glu Asn Leu Pro Pro Tyr Ala Arg Pro Arg  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Phe Leu Arg Leu Gln Glu Ser Leu Ala Thr Thr Glu Thr Phe Lys Gln  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Gln Lys Val Arg Met Ala Asn Glu Gly Phe Asp Pro Ser Thr Leu Ser  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asp Pro Leu Tyr Val Leu Asp Gln Ala Val Gly Ala Tyr Leu Pro Leu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Thr Thr Ala Arg Tyr Ser Ala Leu Leu Ala Gly Asn Leu Arg Ile  
               
               
                             180                 185                 190  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 16  
               
               
                 &lt;211&gt; LENGTH: 734  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: (1)...(734)  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 27, 46  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 16  
               
               
                   
               
               
                 tcaagtacaa ctgcacgatt gtcatancat tggtgaactg tgccgntacc tcctgaacca     60  
               
               
                   
               
               
                 gccaccgcgg gaggcagaaa accagcacca ggttcgcatg gcactaggca atggcctccg    120  
               
               
                   
               
               
                 gcagtccatc tggaccaact tttccagccg cttccacata ccccaggtgg ctgagttyta    180  
               
               
                   
               
               
                 cggggccaca gagtgcaact gtagcctggg caacttcgac agccaggtgg gggcctgtgg    240  
               
               
                   
               
               
                 tttcaatagc cgcatcctgt ccttcgtgta ccccatccgg ttggtacgtg tcaacgagga    300  
               
               
                   
               
               
                 caccatggag ctgatccggg ggcccgacgg cgtctgcatt ccctgccagc caggtgagcc    360  
               
               
                   
               
               
                 gggccagctg gtgggccgca tcatccagaa agaccccctg cgccgcttcg atggctacct    420  
               
               
                   
               
               
                 caaccagggc gccaacaaca agaagattgc caaggatgtc ttcaagaagg gggaccaggc    480  
               
               
                   
               
               
                 ctaccttact ggtgatgtgc tggtgatgga cgagctgggc tacctgtact tccgagaccg    540  
               
               
                   
               
               
                 cactggggac acgttccgct ggaaaggtga gaacgtgtcc accaccgagg tggaaggcac    600  
               
               
                   
               
               
                 actcagccgc ctgctggaca tggctgacgt ggccgtgtat ggtgtcgagg tgccaggaac    660  
               
               
                   
               
               
                 cgagggccgg gccggaatgg ctgctgtggc cagccccact ggcaactgtg acctgggagc    720  
               
               
                   
               
               
                 gctttgctca ggtc                                                      734  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 17  
               
               
                 &lt;211&gt; LENGTH: 213  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 17  
               
               
                   
               
               
                 Ile Gly Glu Leu Cys Arg Tyr Leu Leu Asn Gln Pro Pro Arg Glu Ala  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Glu Asn Gln His Gln Val Arg Met Ala Leu Gly Asn Gly Leu Arg Gln  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Ser Ile Trp Thr Asn Phe Ser Ser Arg Phe His Ile Pro Gln Val Ala  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Leu Gly Asn Phe Asp  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Ser Gln Val Gly Ala Cys Gly Phe Asn Ser Arg Ile Leu Ser Phe Val  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Tyr Pro Ile Arg Leu Val Arg Val Asn Glu Asp Thr Met Glu Leu Ile  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Arg Gly Pro Asp Gly Val Cys Ile Pro Cys Gln Pro Gly Glu Pro Gly  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Gln Leu Val Gly Arg Ile Ile Gln Lys Asp Pro Leu Arg Arg Phe Asp  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Gly Tyr Leu Asn Gln Gly Ala Asn Asn Lys Lys Ile Ala Lys Asp Val  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Phe Lys Lys Gly Asp Gln Ala Tyr Leu Thr Gly Asp Val Leu Val Met  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asp Glu Leu Gly Tyr Leu Tyr Phe Arg Asp Arg Thr Gly Asp Thr Phe  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Arg Trp Lys Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Thr Leu  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Arg Leu Leu Asp Met Ala Asp Val Ala Val Tyr Gly Val Glu Val  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Pro Gly Thr Glu Gly  
               
               
                     210  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 18  
               
               
                 &lt;211&gt; LENGTH: 1278  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: (1)...(1278)  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 2, 165, 292  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 18  
               
               
                   
               
               
                 cntgcctctt gtaccacgtg atgggacttt gtcgttggga tcctcggctg cttagatctc     60  
               
               
                   
               
               
                 ggagccacct gtgttctggc ccccaagttc tctacttcct gcttctggga tgactgtcgg    120  
               
               
                   
               
               
                 cagcatggcg tgacagtgat cctgtatgtg ggcgagctcc tgcgntactt gtgtaacatt    180  
               
               
                   
               
               
                 ccccagcaac cagaggaccg gacacataca gtccgcctgg caatgggcaa tggactacgg    240  
               
               
                   
               
               
                 gctgatgtgt ggggagacct tccagcagcg tttcggtcct atttcggatc tngggaagtc    300  
               
               
                   
               
               
                 ttacgggcty ccacagaagg gcaacatggg gctttagttc aactattgtt gggggcgctg    360  
               
               
                   
               
               
                 cggggscctg grggcaaaga tggagcttgc ctcctccgaa tgctgtcccc ctttgagctg    420  
               
               
                   
               
               
                 gtgcagttcg acatggaggc ggcggagcct gtgagggaca atcagggctt ctgcatccct    480  
               
               
                   
               
               
                 gtagggctag gggagccggg gctgctgttg accaaggtgg taagccagca acccttcgtg    540  
               
               
                   
               
               
                 ggctaccgcg gcccccgaga gctgtcggaa cggaagctgg tgcgcaacgt gcggcaatcg    600  
               
               
                   
               
               
                 ggcgacgttt actacaacac cggggacgta ctggccatgg accgcgaagg cttcctctac    660  
               
               
                   
               
               
                 ttccgcgacc gactcgggga caccttccga tggaagggcg agaacgtgtc cacgcacgag    720  
               
               
                   
               
               
                 gtggagggcg tgttgtcgca ggtggacttc ttgcaacagg ttaacgtgta tggcgtgtgc    780  
               
               
                   
               
               
                 gtgccaggtt gtgagggtaa ggtgggcatg gctgctgtgg cattagcccc cggccagact    840  
               
               
                   
               
               
                 ttcgacgggg agaagttgta ccagcacgtt cgcgcttggc tccctgccta cgctaccccc    900  
               
               
                   
               
               
                 catttcatcc gcatccagga cgccatggag gtcaccagca cgttcaaact gatgaagacc    960  
               
               
                   
               
               
                 cggttggtgc gtgagggctt caatgtgggg atcgtggttg accctctgtt tgtactggac   1020  
               
               
                   
               
               
                 aaccgggccc agtccttccg gcccctgacg gcagaaatgt accaggctgt gtgtgaggga   1080  
               
               
                   
               
               
                 acctggaggc tctgatcacc tggccaaccc actggggtag ggatcaaagc cagccacccc   1140  
               
               
                   
               
               
                 caccccaaca cactcggtgt ccctttcatc ctgggcctgt gtgaatccca gcctggccat   1200  
               
               
                   
               
               
                 accctcaacc tcagtgggct ggaaatgaca gtgggccctg tagcagtggc agaataaact   1260  
               
               
                   
               
               
                 cagmtgygtt cacagaaa                                                 1278  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 19  
               
               
                 &lt;211&gt; LENGTH: 199  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 19  
               
               
                   
               
               
                 Glu Gly Gln His Gly Ala Leu Val Gln Leu Leu Leu Gly Ala Leu Arg  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Gly Pro Gly Gly Lys Asp Gly Ala Cys Leu Leu Arg Met Leu Ser Pro  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Glu Leu Val Gln Phe Asp Met Glu Ala Ala Glu Pro Val Arg Asp  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Asn Gln Gly Phe Cys Ile Pro Val Gly Leu Gly Glu Pro Gly Leu Leu  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Leu Thr Lys Val Val Ser Gln Gln Pro Phe Val Gly Tyr Arg Gly Pro  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Arg Glu Leu Ser Glu Arg Lys Leu Val Arg Asn Val Arg Gln Ser Gly  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Val Tyr Tyr Asn Thr Gly Asp Val Leu Ala Met Asp Arg Glu Gly  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Phe Leu Tyr Phe Arg Asp Arg Leu Gly Asp Thr Phe Arg Trp Lys Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Glu Asn Val Ser Thr His Glu Val Glu Gly Val Leu Ser Gln Val Asp  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Phe Leu Gln Gln Val Asn Val Tyr Gly Val Cys Val Pro Gly Cys Glu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Gly Lys Val Gly Met Ala Ala Val Ala Leu Ala Pro Gly Gln Thr Phe  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asp Gly Glu Lys Leu Tyr Gln His Val Arg Ala Trp Leu Pro Ala Tyr  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ala Thr Pro His Phe Ile Arg  
               
               
                         195  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 20  
               
               
                 &lt;211&gt; LENGTH: 1361  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 20  
               
               
                   
               
               
                 cgcttgtgtg ttaaagaaga aattttcagc aagccagttt tggagtgact gcaagaagta     60  
               
               
                   
               
               
                 tgatgtgact gtgtttcagt atattggaga actttgtcgc tacctttgca aacaatctaa    120  
               
               
                   
               
               
                 gagagaagga gaaaaggatc ataaggtgcg tttggcaatt ggaaatggca tacggagtga    180  
               
               
                   
               
               
                 tgtatggaga gaatttttag acagatttgg aaatataaag gtgtgtgaac tttatgcagc    240  
               
               
                   
               
               
                 taccgaatca agcatatctt tcatgaacta cactgggaga attggagcaa ttgggagaac    300  
               
               
                   
               
               
                 aaatttgttt tacaaacttc tttccacttt tgacttaata aagtatgact ttcagaaaga    360  
               
               
                   
               
               
                 tgaacccatg agaaatgagc agggttgggt attcatgaga aaaaggagac ctggacttct    420  
               
               
                   
               
               
                 catttctcga gtgaatgcaa aaaatccctt ctttggctat gctgggcctt ataagcacac    480  
               
               
                   
               
               
                 aaaagacaaa ttgctttgtg atgtttttaa gaagggagat gtttacctta atactggaga    540  
               
               
                   
               
               
                 cttaatagtc caggatcagg acaatttcct ttatttttgg gaccgtactg gagacacttt    600  
               
               
                   
               
               
                 cagatggaaa ggagaaaatg tcgcaaccac tgaggttgct gatgttattg gaatgttgga    660  
               
               
                   
               
               
                 tttcatacag gaagcaaacg tctatggtgt ggctatatca ggttatgaag gaagagcagg    720  
               
               
                   
               
               
                 aatggcttct attattttaa aaccaaatac atctttagat ttggaaaaag tttatgaaca    780  
               
               
                   
               
               
                 agttgtaaca tttctaccag cttatgcttg tccacgattt ttaagaattc aggaaaaaat    840  
               
               
                   
               
               
                 ggaagcaaca ggaacattca aactattgaa gcatcagttg gtggaagatg gatttaatcc    900  
               
               
                   
               
               
                 actgaaaatt tctgaaccac tttacttcat ggataacttg aaaaagtctt atgttctact    960  
               
               
                   
               
               
                 gaccagggaa ctttatgatc aaataatgtt aggggaaata aaactttaag atttttatat   1020  
               
               
                   
               
               
                 ctagaacttt catatgcttt cttaggaaga gtgagagggg ggtatatgat tctttatgaa   1080  
               
               
                   
               
               
                 atggggaaag ggagctaaca ttaattatgc atgtactata tttccttaat atgagagata   1140  
               
               
                   
               
               
                 attttttaat tgcataagaa ttttaatttc ttttaattga tataaacaga gttgattatt   1200  
               
               
                   
               
               
                 ctttttatct atttggagat tcagtgcata actaagtatt ttccttaata ctaaagattt   1260  
               
               
                   
               
               
                 taaataataa atagtggcta gcggtttgga caatcactaa aaatgtactt tctaataagt   1320  
               
               
                   
               
               
                 aaaatttcta attttgaata aaagattaaa ttttactgaa a                       1361  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 21  
               
               
                 &lt;211&gt; LENGTH: 335  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 21  
               
               
                   
               
               
                 Ala Cys Val Leu Lys Lys Lys Phe Ser Ala Ser Gln Phe Trp Ser Asp  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Cys Lys Lys Tyr Asp Val Thr Val Phe Gln Tyr Ile Gly Glu Leu Cys  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Arg Tyr Leu Cys Lys Gln Ser Lys Arg Glu Gly Glu Lys Asp His Lys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Val Arg Leu Ala Ile Gly Asn Gly Ile Arg Ser Asp Val Trp Arg Glu  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Phe Leu Asp Arg Phe Gly Asn Ile Lys Val Cys Glu Leu Tyr Ala Ala  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Thr Glu Ser Ser Ile Ser Phe Met Asn Tyr Thr Gly Arg Ile Gly Ala  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Ile Gly Arg Thr Asn Leu Phe Tyr Lys Leu Leu Ser Thr Phe Asp Leu  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ile Lys Tyr Asp Phe Gln Lys Asp Glu Pro Met Arg Asn Glu Gln Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Trp Val Phe Met Arg Lys Arg Arg Pro Gly Leu Leu Ile Ser Arg Val  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Asn Ala Lys Asn Pro Phe Phe Gly Tyr Ala Gly Pro Tyr Lys His Thr  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Lys Asp Lys Leu Leu Cys Asp Val Phe Lys Lys Gly Asp Val Tyr Leu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asn Thr Gly Asp Leu Ile Val Gln Asp Gln Asp Asn Phe Leu Tyr Phe  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Trp Asp Arg Thr Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Thr Thr Glu Val Ala Asp Val Ile Gly Met Leu Asp Phe Ile Gln Glu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Asn Val Tyr Gly Val Ala Ile Ser Gly Tyr Glu Gly Arg Ala Gly  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Met Ala Ser Ile Ile Leu Lys Pro Asn Thr Ser Leu Asp Leu Glu Lys  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Val Tyr Glu Gln Val Val Thr Phe Leu Pro Ala Tyr Ala Cys Pro Arg  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Phe Leu Arg Ile Gln Glu Lys Met Glu Ala Thr Gly Thr Phe Lys Leu  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Leu Lys His Gln Leu Val Glu Asp Gly Phe Asn Pro Leu Lys Ile Ser  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Glu Pro Leu Tyr Phe Met Asp Asn Leu Lys Lys Ser Tyr Val Leu Leu  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Thr Arg Glu Leu Tyr Asp Gln Ile Met Leu Gly Glu Ile Lys Leu  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 22  
               
               
                 &lt;211&gt; LENGTH: 2007  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mycobacterium tuberculosis  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 22  
               
               
                   
               
               
                 tagtcgataa cgtcaaggac gctctgcggg cctgcgcacc ttcctgaggt tggtcgacaa     60  
               
               
                   
               
               
                 ccaattcgac atttcgcaaa cgaatcgagg gcttacgtgt ccgattacta cggcggcgca    120  
               
               
                   
               
               
                 cacacaacgg tcaggctgat cgacctggca actcggatgc cgcgagtgtt ggcggacacg    180  
               
               
                   
               
               
                 ccggtgattg tgcgtggggc aatgaccggg ctgctggccc ggccgaattc caaggcgtcg    240  
               
               
                   
               
               
                 atcggcacgg tgttccagga ccgggccgct cgctacggtg accgagtctt cctgaaattc    300  
               
               
                   
               
               
                 ggcgatcagc agctgaccta ccgcgacgct aacgccaccg ccaaccggta cgccgcggtg    360  
               
               
                   
               
               
                 ttggccgccc gcggcgtcgg ccccggcgac gtcgttggca tcatgttgcg taactcaccc    420  
               
               
                   
               
               
                 agcacagtct tggcgatgct ggccacggtc aagtgcggcg ctatcgccgg catgctcaac    480  
               
               
                   
               
               
                 taccaccagc gcggcgaggt gttggcgcac agcctgggtc tgctggacgc gaaggtactg    540  
               
               
                   
               
               
                 atcgcagagt ccgacttggt cagcgccgtc gccgaatgcg gcgcctcgcg cggccgggta    600  
               
               
                   
               
               
                 gcgggcgacg tgctgaccgt cgaggacgtg gagcgattcg ccacaacggc gcccgccacc    660  
               
               
                   
               
               
                 aacccggcgt cggcgtcggc ggtgcaagcc aaagacaccg cgttctacat cttcacctcg    720  
               
               
                   
               
               
                 ggcaccaccg gatttcccaa ggccagtgtc atgacgcatc atcggtggct gcgggcgctg    780  
               
               
                   
               
               
                 gccgtcttcg gagggatggg gctgcggctg aagggttccg acacgctcta cagctgcctg    840  
               
               
                   
               
               
                 ccgctgtacc acaacaacgc gttaacggtc gcggtgtcgt cggtgatcaa ttctggggcg    900  
               
               
                   
               
               
                 accctggcgc tgggtaagtc gttttcggcg tcgcggttct gggatgaggt gattgccaac    960  
               
               
                   
               
               
                 cgggcgacgg cgttcgtcta catcggcgaa atctgccgtt atctgctcaa ccagccggcc   1020  
               
               
                   
               
               
                 aagccgaccg accgtgccca ccaggtgcgg gtgatctgcg gtaacgggct gcggccggag   1080  
               
               
                   
               
               
                 atctgggatg agttcaccac ccgcttcggg gtcgcgcggg tgtgcgagtt ctacgccgcc   1140  
               
               
                   
               
               
                 agcgaaggca actcggcctt tatcaacatc ttcaacgtgc ccaggaccgc cggggtatcg   1200  
               
               
                   
               
               
                 ccgatgccgc ttgcctttgt ggaatacgac ctggacaccg gcgatccgct gcgggatgcg   1260  
               
               
                   
               
               
                 agcgggcgag tgcgtcgggt acccgacggt gaacccggcc tgttgcttag ccgggtcaac   1320  
               
               
                   
               
               
                 cggctgcagc cgttcgacgg ctacaccgac ccggttgcca gcgaaaagaa gttggtgcgc   1380  
               
               
                   
               
               
                 aacgcttttc gagatggcga ctgttggttc aacaccggtg acgtgatgag cccgcagggc   1440  
               
               
                   
               
               
                 atgggccatg ccgccttcgt cgatcggctg ggcgacacct tccgctggaa gggcgagaat   1500  
               
               
                   
               
               
                 gtcgccacca ctcaggtcga agcggcactg gcctccgacc agaccgtcga ggagtgcacg   1560  
               
               
                   
               
               
                 gtctacggcg tccagattcc gcgcaccggc gggcgcgccg gaatggccgc gatcacactg   1620  
               
               
                   
               
               
                 cgcgctggcg ccgaattcga cggccaggcg ctggcccgaa cggtttacgg tcacttgccc   1680  
               
               
                   
               
               
                 ggctatgcac ttccgctctt tgttcgggta gtggggtcgc tggcgcacac cacgacgttc   1740  
               
               
                   
               
               
                 aagagtcgca aggtggagtt gcgcaaccag gcctatggcg ccgacatcga ggatccgctg   1800  
               
               
                   
               
               
                 tacgtactgg ccggcccgga cgaaggatat gtgccgtact acgccgaata ccctgaggag   1860  
               
               
                   
               
               
                 gtttcgctcg gaaggcgacc gcagggctag cggattccgg gcgcagtctc gatacccgca   1920  
               
               
                   
               
               
                 ctggacgctc gacggtaacc aggcactatg gatgcgtgcg ttcaacaccg ccggcctcag   1980  
               
               
                   
               
               
                 ccggtcgttc aacaccgccg gcgttag                                       2007  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 23  
               
               
                 &lt;211&gt; LENGTH: 597  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mycobacterium tuberculosis  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 23  
               
               
                   
               
               
                 Met Ser Asp Tyr Tyr Gly Gly Ala His Thr Thr Val Arg Leu Ile Asp  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Ala Thr Arg Met Pro Arg Val Leu Ala Asp Thr Pro Val Ile Val  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Arg Gly Ala Met Thr Gly Leu Leu Ala Arg Pro Asn Ser Lys Ala Ser  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ile Gly Thr Val Phe Gln Asp Arg Ala Ala Arg Tyr Gly Asp Arg Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Phe Leu Lys Phe Gly Asp Gln Gln Leu Thr Tyr Arg Asp Ala Asn Ala  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Thr Ala Asn Arg Tyr Ala Ala Val Leu Ala Ala Arg Gly Val Gly Pro  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Asp Val Val Gly Ile Met Leu Arg Asn Ser Pro Ser Thr Val Leu  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ala Met Leu Ala Thr Val Lys Cys Gly Ala Ile Ala Gly Met Leu Asn  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Tyr His Gln Arg Gly Glu Val Leu Ala His Ser Leu Gly Leu Leu Asp  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ala Lys Val Leu Ile Ala Glu Ser Asp Leu Val Ser Ala Val Ala Glu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Cys Gly Ala Ser Arg Gly Arg Val Ala Gly Asp Val Leu Thr Val Glu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asp Val Glu Arg Phe Ala Thr Thr Ala Pro Ala Thr Asn Pro Ala Ser  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ala Ser Ala Val Gln Ala Lys Asp Thr Ala Phe Tyr Ile Phe Thr Ser  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Thr Thr Gly Phe Pro Lys Ala Ser Val Met Thr His His Arg Trp  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Leu Arg Ala Leu Ala Val Phe Gly Gly Met Gly Leu Arg Leu Lys Gly  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Ser Asp Thr Leu Tyr Ser Cys Leu Pro Leu Tyr His Asn Asn Ala Leu  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Thr Val Ala Val Ser Ser Val Ile Asn Ser Gly Ala Thr Leu Ala Leu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly Lys Ser Phe Ser Ala Ser Arg Phe Trp Asp Glu Val Ile Ala Asn  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Arg Ala Thr Ala Phe Val Tyr Ile Gly Glu Ile Cys Arg Tyr Leu Leu  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Asn Gln Pro Ala Lys Pro Thr Asp Arg Ala His Gln Val Arg Val Ile  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Cys Gly Asn Gly Leu Arg Pro Glu Ile Trp Asp Glu Phe Thr Thr Arg  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Phe Gly Val Ala Arg Val Cys Glu Phe Tyr Ala Ala Ser Glu Gly Asn  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Ser Ala Phe Ile Asn Ile Phe Asn Val Pro Arg Thr Ala Gly Val Ser  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Pro Met Pro Leu Ala Phe Val Glu Tyr Asp Leu Asp Thr Gly Asp Pro  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Leu Arg Asp Ala Ser Gly Arg Val Arg Arg Val Pro Asp Gly Glu Pro  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Leu Leu Leu Ser Arg Val Asn Arg Leu Gln Pro Phe Asp Gly Tyr  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Thr Asp Pro Val Ala Ser Glu Lys Lys Leu Val Arg Asn Ala Phe Arg  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Asp Gly Asp Cys Trp Phe Asn Thr Gly Asp Val Met Ser Pro Gln Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Met Gly His Ala Ala Phe Val Asp Arg Leu Gly Asp Thr Phe Arg Trp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Lys Gly Glu Asn Val Ala Thr Thr Gln Val Glu Ala Ala Leu Ala Ser  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Asp Gln Thr Val Glu Glu Cys Thr Val Tyr Gly Val Gln Ile Pro Arg  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Thr Gly Gly Arg Ala Gly Met Ala Ala Ile Thr Leu Arg Ala Gly Ala  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Glu Phe Asp Gly Gln Ala Leu Ala Arg Thr Val Tyr Gly His Leu Pro  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Gly Tyr Ala Leu Pro Leu Phe Val Arg Val Val Gly Ser Leu Ala His  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Thr Thr Thr Phe Lys Ser Arg Lys Val Glu Leu Arg Asn Gln Ala Tyr  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Gly Ala Asp Ile Glu Asp Pro Leu Tyr Val Leu Ala Gly Pro Asp Glu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Gly Tyr Val Pro Tyr Tyr Ala Glu Tyr Pro Glu Glu Val Ser Leu Gly  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Arg Arg Pro Gln Gly  
               
               
                         595  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 24  
               
               
                 &lt;211&gt; LENGTH: 3704  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: CDS  
               
               
                 &lt;222&gt; LOCATION: (175)...(2112)  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 24  
               
               
                   
               
               
                 tcgacccacg gcgtccggga ccccaaagca gaagcccgca cagtaggcac agcgcaccca     60  
               
               
                   
               
               
                 agaagggtcc aggagtctgc agaaacagaa aggtccccgg cctcagcctc ctagtccctg    120  
               
               
                   
               
               
                 cctgcctcct gcctgagctt ctgggagact gaaggcacgg cttgcagctt cagg atg      177  
               
               
                                                                             Met  
               
               
                                                                              1  
               
               
                   
               
               
                 cgg gct ccg ggt gcg ggc gcg gcc tcg gtg gtc tcg ctg gcg ctg ttg      225  
               
               
                 Arg Ala Pro Gly Ala Gly Ala Ala Ser Val Val Ser Leu Ala Leu Leu  
               
               
                              5                   10                  15  
               
               
                   
               
               
                 tgg ctg ctg ggg ctg ccg tgg acc tgg agc gcg gca gcg gcg ctc ggc      273  
               
               
                 Trp Leu Leu Gly Leu Pro Trp Thr Trp Ser Ala Ala Ala Ala Leu Gly  
               
               
                          20                  25                  30  
               
               
                   
               
               
                 gtg tac gtg ggc agc ggc ggc tgg cgc ttc ctg cgc atc gtc tgc aag      321  
               
               
                 Val Tyr Val Gly Ser Gly Gly Trp Arg Phe Leu Arg Ile Val Cys Lys  
               
               
                      35                  40                  45  
               
               
                   
               
               
                 acc gcg agg cga gac ctc ttc ggt ctc tct gtg ctg atc cgc gtg cgc      369  
               
               
                 Thr Ala Arg Arg Asp Leu Phe Gly Leu Ser Val Leu Ile Arg Val Arg  
               
               
                  50                  55                  60                  65  
               
               
                   
               
               
                 ctg gag ctg cgg cgg cac cag cgt gcc ggc cac acc atc ccg cgc atc      417  
               
               
                 Leu Glu Leu Arg Arg His Gln Arg Ala Gly His Thr Ile Pro Arg Ile  
               
               
                                  70                  75                  80  
               
               
                   
               
               
                 ttt cag gcg gta gtg cag cga cag ccc gag cgc ctg gcg ctg gtg gat      465  
               
               
                 Phe Gln Ala Val Val Gln Arg Gln Pro Glu Arg Leu Ala Leu Val Asp  
               
               
                              85                  90                  95  
               
               
                   
               
               
                 gcc ggg acc ggc gag tgc tgg acc ttt gcg cag ctg gac gcc tac tcc      513  
               
               
                 Ala Gly Thr Gly Glu Cys Trp Thr Phe Ala Gln Leu Asp Ala Tyr Ser  
               
               
                         100                 105                 110  
               
               
                   
               
               
                 aat gcg gta gcc aac ctc ttc cgc cag ctg ggc ttc gcg ccg ggc gac      561  
               
               
                 Asn Ala Val Ala Asn Leu Phe Arg Gln Leu Gly Phe Ala Pro Gly Asp  
               
               
                     115                 120                 125  
               
               
                   
               
               
                 gtg gtg gcc atc ttc ctg gag ggc cgg ccg gag ttc gtg ggg ctg tgg      609  
               
               
                 Val Val Ala Ile Phe Leu Glu Gly Arg Pro Glu Phe Val Gly Leu Trp  
               
               
                 130                 135                 140                 145  
               
               
                   
               
               
                 ctg ggc ctg gcc aag gcg ggc atg gag gcc gcg ctg ctc aac gtg aac      657  
               
               
                 Leu Gly Leu Ala Lys Ala Gly Met Glu Ala Ala Leu Leu Asn Val Asn  
               
               
                                 150                 155                 160  
               
               
                   
               
               
                 ctg cgg cgc gag ccc ctg gcc ttc tgc ctg ggc acc tcg ggc gct aag      705  
               
               
                 Leu Arg Arg Glu Pro Leu Ala Phe Cys Leu Gly Thr Ser Gly Ala Lys  
               
               
                             165                 170                 175  
               
               
                   
               
               
                 gcc ctg atc ttt gga gga gaa atg gtg gcg gcg gtg gcc gaa gtg agc      753  
               
               
                 Ala Leu Ile Phe Gly Gly Glu Met Val Ala Ala Val Ala Glu Val Ser  
               
               
                         180                 185                 190  
               
               
                   
               
               
                 ggg cat ctg ggg aaa agt ttg atc aag ttc tgc tct gga gac ttg ggg      801  
               
               
                 Gly His Leu Gly Lys Ser Leu Ile Lys Phe Cys Ser Gly Asp Leu Gly  
               
               
                     195                 200                 205  
               
               
                   
               
               
                 ccc gag ggc atc ttg ccg gac acc cac ctc ctg gac ccg ctg ctg aag      849  
               
               
                 Pro Glu Gly Ile Leu Pro Asp Thr His Leu Leu Asp Pro Leu Leu Lys  
               
               
                 210                 215                 220                 225  
               
               
                   
               
               
                 gag gcc tct act gcc ccc ttg gca cag atc ccc agc aag ggc atg gac      897  
               
               
                 Glu Ala Ser Thr Ala Pro Leu Ala Gln Ile Pro Ser Lys Gly Met Asp  
               
               
                                 230                 235                 240  
               
               
                   
               
               
                 gat cgt ctt ttc tac atc tac acg tcg ggg acc acc ggg ctg ccc aag      945  
               
               
                 Asp Arg Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys  
               
               
                             245                 250                 255  
               
               
                   
               
               
                 gct gcc att gtc gtg cac agc agg tac tac cgc atg gca gcc ttc ggc      993  
               
               
                 Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ala Phe Gly  
               
               
                         260                 265                 270  
               
               
                   
               
               
                 cac cac gcc tac cgc atg cag gcg gct gac gtg ctc tat gac tgc ctg     1041  
               
               
                 His His Ala Tyr Arg Met Gln Ala Ala Asp Val Leu Tyr Asp Cys Leu  
               
               
                     275                 280                 285  
               
               
                   
               
               
                 ccc ctg tac cac tcg gca gga aac atc atc ggc gtg ggg cag tgt ctc     1089  
               
               
                 Pro Leu Tyr His Ser Ala Gly Asn Ile Ile Gly Val Gly Gln Cys Leu  
               
               
                 290                 295                 300                 305  
               
               
                   
               
               
                 atc tat ggg ctg aca gtc gtc ctc cgc aag aaa ttc tcg gcc agc cgc     1137  
               
               
                 Ile Tyr Gly Leu Thr Val Val Leu Arg Lys Lys Phe Ser Ala Ser Arg  
               
               
                                 310                 315                 320  
               
               
                   
               
               
                 ttc tgg gac gac tgc atc aag tac aac tgc acg gtg gtt cag tac atc     1185  
               
               
                 Phe Trp Asp Asp Cys Ile Lys Tyr Asn Cys Thr Val Val Gln Tyr Ile  
               
               
                             325                 330                 335  
               
               
                   
               
               
                 ggg gag atc tgc cgc tac ctg ctg aag cag ccg gtg cgc gag gcg gag     1233  
               
               
                 Gly Glu Ile Cys Arg Tyr Leu Leu Lys Gln Pro Val Arg Glu Ala Glu  
               
               
                         340                 345                 350  
               
               
                   
               
               
                 agg cga cac cgc gtg cgc ctg gcg gtg ggg aac ggg ctg cgt cct gcc     1281  
               
               
                 Arg Arg His Arg Val Arg Leu Ala Val Gly Asn Gly Leu Arg Pro Ala  
               
               
                     355                 360                 365  
               
               
                   
               
               
                 atc tgg gag gag ttc acg gag cgc ttc ggc gta cgc caa atc ggg gag     1329  
               
               
                 Ile Trp Glu Glu Phe Thr Glu Arg Phe Gly Val Arg Gln Ile Gly Glu  
               
               
                 370                 375                 380                 385  
               
               
                   
               
               
                 ttc tac ggc gcc acc gag tgc aac tgc agc att gcc aac atg gac ggc     1377  
               
               
                 Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Ile Ala Asn Met Asp Gly  
               
               
                                 390                 395                 400  
               
               
                   
               
               
                 aag gtc ggc tcc tgt ggt ttc aac agc cgc atc ctg ccc cac gtg tac     1425  
               
               
                 Lys Val Gly Ser Cys Gly Phe Asn Ser Arg Ile Leu Pro His Val Tyr  
               
               
                             405                 410                 415  
               
               
                   
               
               
                 ccc atc cgg ctg gtg aag gtc aat gag gac aca atg gag ctg ctg cgg     1473  
               
               
                 Pro Ile Arg Leu Val Lys Val Asn Glu Asp Thr Met Glu Leu Leu Arg  
               
               
                         420                 425                 430  
               
               
                   
               
               
                 gat gcc cag ggc ctc tgc atc ccc tgc cag gcc ggg gag cct ggc ctc     1521  
               
               
                 Asp Ala Gln Gly Leu Cys Ile Pro Cys Gln Ala Gly Glu Pro Gly Leu  
               
               
                     435                 440                 445  
               
               
                   
               
               
                 ctt gtg ggt cag atc aac caa cag gac ccg ctg cgc cgc ttc gat ggc     1569  
               
               
                 Leu Val Gly Gln Ile Asn Gln Gln Asp Pro Leu Arg Arg Phe Asp Gly  
               
               
                 450                 455                 460                 465  
               
               
                   
               
               
                 tat gtc agc gag agc gcc acc agc aag aag atc gcc cac agc gtc ttc     1617  
               
               
                 Tyr Val Ser Glu Ser Ala Thr Ser Lys Lys Ile Ala His Ser Val Phe  
               
               
                                 470                 475                 480  
               
               
                   
               
               
                 agc aag ggc gac agc gcc tac ctc tca ggt gac gtg cta gtg atg gat     1665  
               
               
                 Ser Lys Gly Asp Ser Ala Tyr Leu Ser Gly Asp Val Leu Val Met Asp  
               
               
                             485                 490                 495  
               
               
                   
               
               
                 gag ctg ggc tac atg tac ttc cgg gac cgt agc ggg gac acc ttc cgc     1713  
               
               
                 Glu Leu Gly Tyr Met Tyr Phe Arg Asp Arg Ser Gly Asp Thr Phe Arg  
               
               
                         500                 505                 510  
               
               
                   
               
               
                 tgg cga ggg gag aac gtc tcc acc acc gag gtg gag ggc gtg ctg agc     1761  
               
               
                 Trp Arg Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Val Leu Ser  
               
               
                     515                 520                 525  
               
               
                   
               
               
                 cgc ctg ctg ggc cag aca gac gtg gcc gtc tat ggg gtg gct gtt cca     1809  
               
               
                 Arg Leu Leu Gly Gln Thr Asp Val Ala Val Tyr Gly Val Ala Val Pro  
               
               
                 530                 535                 540                 545  
               
               
                   
               
               
                 gga gtg gag ggt aag gca ggg atg gcg gcc gtc gca gac ccc cac agc     1857  
               
               
                 Gly Val Glu Gly Lys Ala Gly Met Ala Ala Val Ala Asp Pro His Ser  
               
               
                                 550                 555                 560  
               
               
                   
               
               
                 ctg ctg gac ccc aac gcg ata tac cag gag ctg cag aag gtg ctg gca     1905  
               
               
                 Leu Leu Asp Pro Asn Ala Ile Tyr Gln Glu Leu Gln Lys Val Leu Ala  
               
               
                             565                 570                 575  
               
               
                   
               
               
                 ccc tat gcc cgg ccc atc ttc ctg cgc ctc ctg ccc cag gtg gac acc     1953  
               
               
                 Pro Tyr Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Gln Val Asp Thr  
               
               
                         580                 585                 590  
               
               
                   
               
               
                 aca ggc acc ttc aag atc cag aag acg agg ctg cag cga gag ggc ttt     2001  
               
               
                 Thr Gly Thr Phe Lys Ile Gln Lys Thr Arg Leu Gln Arg Glu Gly Phe  
               
               
                     595                 600                 605  
               
               
                   
               
               
                 gac cca cgc cag acc tca gac cgg ctc ttc ttc ctg gac ctg aag cag     2049  
               
               
                 Asp Pro Arg Gln Thr Ser Asp Arg Leu Phe Phe Leu Asp Leu Lys Gln  
               
               
                 610                 615                 620                 625  
               
               
                   
               
               
                 ggc cac tac ctg ccc tta aat gag gca gtc tac act cgc atc tgc tcg     2097  
               
               
                 Gly His Tyr Leu Pro Leu Asn Glu Ala Val Tyr Thr Arg Ile Cys Ser  
               
               
                                 630                 635                 640  
               
               
                   
               
               
                 ggc gcc ttc gcc ctc tgaagctgtt cctctactgg ccacaaactc tgggcctggt     2152  
               
               
                 Gly Ala Phe Ala Leu  
               
               
                             645  
               
               
                   
               
               
                 gggagaggcc agcttgagcc agacagcgct gcccaggggt ggccgcctag tacacaccca   2212  
               
               
                   
               
               
                 cctggccgag ctgtacctgg cacggcccat cctggactga gaaactggaa cctcagagga   2272  
               
               
                   
               
               
                 acccgtgcct ctctgctgcc ttggtgcccc tgtgtctgcc tcctctccct gcttttcagc   2332  
               
               
                   
               
               
                 ctctgtctcc ttccatccct gtccctgtct ggccttaact cttccctctc tttcttttct   2392  
               
               
                   
               
               
                 ttctttcttt cttttttttt aagatagagt ctcactctgc tgcccgggct agagtgcagt   2452  
               
               
                   
               
               
                 ggtgggatct cggctcactg caacctctgc ctcctggggt tcaagtgatc ctcccacctc   2512  
               
               
                   
               
               
                 agcctcctga gtagctggga ttacaggcac ccgccaccac gtccagctaa tttttatatt   2572  
               
               
                   
               
               
                 tttagtagag acggggtttc accatgttgg tcaggctggt cttgaactcc tgacctcagg   2632  
               
               
                   
               
               
                 tgatccgctg gcctcggcct cccagagtgc tgggattata ggcgtgagcc tctggcccgg   2692  
               
               
                   
               
               
                 cctttccttt ttcctctcct ctcctgccga gagtggaaca cacgtgtcct gggagctgca   2752  
               
               
                   
               
               
                 tcttgtgtag ggtccagctg cttttgggga ctgcaggaat catctcccct gggccctgga   2812  
               
               
                   
               
               
                 ctcggactgg ggcctcccca cctccctctc ggctgtgcct tacggagccc caatccaggc   2872  
               
               
                   
               
               
                 ctcctgtggc tgttgggttc cagatgctgc agctccatgt gacttccaag caggccctcc   2932  
               
               
                   
               
               
                 gccctccctg ctgaatggag gagccggggg tcccccaggc caactggaaa atctcccagg   2992  
               
               
                   
               
               
                 ctaggccaat tgccttttgc acttccccgt tcctgtcaca tttccccagc cccaccttcc   3052  
               
               
                   
               
               
                 cctcctgatg ccctgaaagc ttccggaatt gactgtgacc acttggatgt caccactgtc   3112  
               
               
                   
               
               
                 agcccctgcc ttgatgtccc catttagcca tctccatgga gctcctgctg gagggccctg   3172  
               
               
                   
               
               
                 aaccctgcac tgcgtggctg cccagccagc tgcctcctgt cctgggagga ggcctcctgg   3232  
               
               
                   
               
               
                 gtgtcctcat ctggtgtgtc tactggaggg tcccacagga gaggcagcag aggggtcagg   3292  
               
               
                   
               
               
                 ggaggtctcc tgccgggggt tggcctctca agcctcaggg gttctagcct gttgaatata   3352  
               
               
                   
               
               
                 ccccacctgg tgggtggccc ctccgatgtc cccactgatg gctctgacac cgtgttggtg   3412  
               
               
                   
               
               
                 gcgatgtccc agacaatccc accaggacgg cccagacatc cctactggct tcgctggtgg   3472  
               
               
                   
               
               
                 ctcatctcga acatccacgc cagcctttct ggggccggcc acccaggccg cctgtccgtc   3532  
               
               
                   
               
               
                 tgtcctccct ccagcagcac cccctggccc ctggagtggt ggggccatgg caagagacac   3592  
               
               
                   
               
               
                 cgtggcgtct catgtgaact ttcctgggca ctgtggtttt atttcctaat tgatttaaga   3652  
               
               
                   
               
               
                 aataaacctg aagaccgtct ggtgaaaaaa aaaaaaaaaa aagggcggcc gc           3704  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 25  
               
               
                 &lt;211&gt; LENGTH: 646  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 25  
               
               
                   
               
               
                 Met Arg Ala Pro Gly Ala Gly Ala Ala Ser Val Val Ser Leu Ala Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Trp Leu Leu Gly Leu Pro Trp Thr Trp Ser Ala Ala Ala Ala Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Val Tyr Val Gly Ser Gly Gly Trp Arg Phe Leu Arg Ile Val Cys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Thr Ala Arg Arg Asp Leu Phe Gly Leu Ser Val Leu Ile Arg Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Arg Leu Glu Leu Arg Arg His Gln Arg Ala Gly His Thr Ile Pro Arg  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ile Phe Gln Ala Val Val Gln Arg Gln Pro Glu Arg Leu Ala Leu Val  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Ala Gly Thr Gly Glu Cys Trp Thr Phe Ala Gln Leu Asp Ala Tyr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Asn Ala Val Ala Asn Leu Phe Arg Gln Leu Gly Phe Ala Pro Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asp Val Val Ala Ile Phe Leu Glu Gly Arg Pro Glu Phe Val Gly Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Trp Leu Gly Leu Ala Lys Ala Gly Met Glu Ala Ala Leu Leu Asn Val  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asn Leu Arg Arg Glu Pro Leu Ala Phe Cys Leu Gly Thr Ser Gly Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Lys Ala Leu Ile Phe Gly Gly Glu Met Val Ala Ala Val Ala Glu Val  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Gly His Leu Gly Lys Ser Leu Ile Lys Phe Cys Ser Gly Asp Leu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Pro Glu Gly Ile Leu Pro Asp Thr His Leu Leu Asp Pro Leu Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Lys Glu Ala Ser Thr Ala Pro Leu Ala Gln Ile Pro Ser Lys Gly Met  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asp Asp Arg Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ala Phe  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly His His Ala Tyr Arg Met Gln Ala Ala Asp Val Leu Tyr Asp Cys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Leu Pro Leu Tyr His Ser Ala Gly Asn Ile Ile Gly Val Gly Gln Cys  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Leu Ile Tyr Gly Leu Thr Val Val Leu Arg Lys Lys Phe Ser Ala Ser  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Arg Phe Trp Asp Asp Cys Ile Lys Tyr Asn Cys Thr Val Val Gln Tyr  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ile Gly Glu Ile Cys Arg Tyr Leu Leu Lys Gln Pro Val Arg Glu Ala  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Glu Arg Arg His Arg Val Arg Leu Ala Val Gly Asn Gly Leu Arg Pro  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ala Ile Trp Glu Glu Phe Thr Glu Arg Phe Gly Val Arg Gln Ile Gly  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Ile Ala Asn Met Asp  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Lys Val Gly Ser Cys Gly Phe Asn Ser Arg Ile Leu Pro His Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Tyr Pro Ile Arg Leu Val Lys Val Asn Glu Asp Thr Met Glu Leu Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Arg Asp Ala Gln Gly Leu Cys Ile Pro Cys Gln Ala Gly Glu Pro Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Leu Val Gly Gln Ile Asn Gln Gln Asp Pro Leu Arg Arg Phe Asp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gly Tyr Val Ser Glu Ser Ala Thr Ser Lys Lys Ile Ala His Ser Val  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Phe Ser Lys Gly Asp Ser Ala Tyr Leu Ser Gly Asp Val Leu Val Met  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Asp Glu Leu Gly Tyr Met Tyr Phe Arg Asp Arg Ser Gly Asp Thr Phe  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Arg Trp Arg Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Val Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ser Arg Leu Leu Gly Gln Thr Asp Val Ala Val Tyr Gly Val Ala Val  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Gly Val Glu Gly Lys Ala Gly Met Ala Ala Val Ala Asp Pro His  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ser Leu Leu Asp Pro Asn Ala Ile Tyr Gln Glu Leu Gln Lys Val Leu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ala Pro Tyr Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Gln Val Asp  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Thr Thr Gly Thr Phe Lys Ile Gln Lys Thr Arg Leu Gln Arg Glu Gly  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Phe Asp Pro Arg Gln Thr Ser Asp Arg Leu Phe Phe Leu Asp Leu Lys  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Gln Gly His Tyr Leu Pro Leu Asn Glu Ala Val Tyr Thr Arg Ile Cys  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Ser Gly Ala Phe Ala Leu  
               
               
                                 645  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 26  
               
               
                 &lt;211&gt; LENGTH: 2917  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: CDS  
               
               
                 &lt;222&gt; LOCATION: (208)...(2136)  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 26  
               
               
                   
               
               
                 cgacccacgc gtccgggcgg gcggggccgg gcggcgggcg gggctggcgg ggcggccggg     60  
               
               
                   
               
               
                 ccatgcaggg cgcagagccg gctaaaccct gctgagaccc ggctccgtgc gtccaggggc    120  
               
               
                   
               
               
                 ggctaatgcc cctcacgctg tctacgctgc tgcaaccggg ccgcatctgg acggggcgcc    180  
               
               
                   
               
               
                 gcgcggcgga gccgacgccg ggccaca atg ctg ctt gga gcc tct ctg gtg ggg    234  
               
               
                                               Met Leu Leu Gly Ala Ser Leu Val Gly  
               
               
                                                1               5  
               
               
                   
               
               
                 gtg ctg ctg ttc tcc aag ctg gtg ctg aaa ctg ccc tgg acc cag gtg      282  
               
               
                 Val Leu Leu Phe Ser Lys Leu Val Leu Lys Leu Pro Trp Thr Gln Val  
               
               
                  10                  15                  20                  25  
               
               
                   
               
               
                 gga ttc tcc ctg ttg ttc ctc tac ttg gga tct ggc ggc tgg cgc ttc      330  
               
               
                 Gly Phe Ser Leu Leu Phe Leu Tyr Leu Gly Ser Gly Gly Trp Arg Phe  
               
               
                                  30                  35                  40  
               
               
                   
               
               
                 atc cgg gtc ttc atc aag acc atc agg cgc gat atc ttt ggc ggc ctg      378  
               
               
                 Ile Arg Val Phe Ile Lys Thr Ile Arg Arg Asp Ile Phe Gly Gly Leu  
               
               
                              45                  50                  55  
               
               
                   
               
               
                 gtc ctc ctg aag gtg aag gca aag gtg cga cag tgc ctg cag gag cgg      426  
               
               
                 Val Leu Leu Lys Val Lys Ala Lys Val Arg Gln Cys Leu Gln Glu Arg  
               
               
                          60                  65                  70  
               
               
                   
               
               
                 cgg aca gtg ccc att ttg ttt gcc tct acc gtt cgg cgc cac ccc gac      474  
               
               
                 Arg Thr Val Pro Ile Leu Phe Ala Ser Thr Val Arg Arg His Pro Asp  
               
               
                      75                  80                  85  
               
               
                   
               
               
                 aag acg gcc ctg atc ttc gag ggc aca gat acc cac tgg acc ttc cgc      522  
               
               
                 Lys Thr Ala Leu Ile Phe Glu Gly Thr Asp Thr His Trp Thr Phe Arg  
               
               
                  90                  95                 100                 105  
               
               
                   
               
               
                 cag ctg gat gag tac tca agc agt gta gcc aac ttc ctg cag gcc cgg      570  
               
               
                 Gln Leu Asp Glu Tyr Ser Ser Ser Val Ala Asn Phe Leu Gln Ala Arg  
               
               
                                 110                 115                 120  
               
               
                   
               
               
                 ggc ctg gcc tcg ggc gat gtg gct gcc atc ttc atg gag aac cgc aat      618  
               
               
                 Gly Leu Ala Ser Gly Asp Val Ala Ala Ile Phe Met Glu Asn Arg Asn  
               
               
                             125                 130                 135  
               
               
                   
               
               
                 gag ttc gtg ggc cta tgg ctg ggc atg gcc aag ctc ggt gtg gag gca      666  
               
               
                 Glu Phe Val Gly Leu Trp Leu Gly Met Ala Lys Leu Gly Val Glu Ala  
               
               
                         140                 145                 150  
               
               
                   
               
               
                 gcc ctc atc aac acc aac ctg cgg cgg gat gct ctg ctc cac tgc ctc      714  
               
               
                 Ala Leu Ile Asn Thr Asn Leu Arg Arg Asp Ala Leu Leu His Cys Leu  
               
               
                     155                 160                 165  
               
               
                   
               
               
                 acc acc tcg cgc gca cgg gcc ctt gtc ttt ggc agc gaa atg gcc tca      762  
               
               
                 Thr Thr Ser Arg Ala Arg Ala Leu Val Phe Gly Ser Glu Met Ala Ser  
               
               
                 170                 175                 180                 185  
               
               
                   
               
               
                 gcc atc tgt gag gtc cat gcc agc ctg gac ccc tcg ctc agc ctc ttc      810  
               
               
                 Ala Ile Cys Glu Val His Ala Ser Leu Asp Pro Ser Leu Ser Leu Phe  
               
               
                                 190                 195                 200  
               
               
                   
               
               
                 tgc tct ggc tcc tgg gag ccc ggt gcg gtg cct cca agc aca gaa cac      858  
               
               
                 Cys Ser Gly Ser Trp Glu Pro Gly Ala Val Pro Pro Ser Thr Glu His  
               
               
                             205                 210                 215  
               
               
                   
               
               
                 ctg gac cct ctg ctg aaa gat gct ccc aag cac ctt ccc agt tgc cct      906  
               
               
                 Leu Asp Pro Leu Leu Lys Asp Ala Pro Lys His Leu Pro Ser Cys Pro  
               
               
                         220                 225                 230  
               
               
                   
               
               
                 gac aag ggc ttc aca gat aaa ctg ttc tac atc tac aca tcc ggc acc      954  
               
               
                 Asp Lys Gly Phe Thr Asp Lys Leu Phe Tyr Ile Tyr Thr Ser Gly Thr  
               
               
                     235                 240                 245  
               
               
                   
               
               
                 aca ggg ctg ccc aag gcc gcc atc gtg gtg cac agc agg tat tac cgc     1002  
               
               
                 Thr Gly Leu Pro Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg  
               
               
                 250                 255                 260                 265  
               
               
                   
               
               
                 atg gct gcc ctg gtg tac tat gga ttc cgc atg cgg ccc aac gac atc     1050  
               
               
                 Met Ala Ala Leu Val Tyr Tyr Gly Phe Arg Met Arg Pro Asn Asp Ile  
               
               
                                 270                 275                 280  
               
               
                   
               
               
                 gtc tat gac tgc ctc ccc ctc tac cac tca gca gga aac atc gtg gga     1098  
               
               
                 Val Tyr Asp Cys Leu Pro Leu Tyr His Ser Ala Gly Asn Ile Val Gly  
               
               
                             285                 290                 295  
               
               
                   
               
               
                 atc ggc cag tgc ctg ctg cat ggc atg acg gtg gtg att cgg aag aag     1146  
               
               
                 Ile Gly Gln Cys Leu Leu His Gly Met Thr Val Val Ile Arg Lys Lys  
               
               
                         300                 305                 310  
               
               
                   
               
               
                 ttc tca gcc tcc cgg ttc tgg gac gat tgt atc aag tac aac tgc acg     1194  
               
               
                 Phe Ser Ala Ser Arg Phe Trp Asp Asp Cys Ile Lys Tyr Asn Cys Thr  
               
               
                     315                 320                 325  
               
               
                   
               
               
                 att gtg cag tac att ggt gaa ctg tgc cgc tac ctc ctg aac cag cca     1242  
               
               
                 Ile Val Gln Tyr Ile Gly Glu Leu Cys Arg Tyr Leu Leu Asn Gln Pro  
               
               
                 330                 335                 340                 345  
               
               
                   
               
               
                 ccg cgg gag gca gaa aac cag cac cag gtt cgc atg gca cta ggc aat     1290  
               
               
                 Pro Arg Glu Ala Glu Asn Gln His Gln Val Arg Met Ala Leu Gly Asn  
               
               
                                 350                 355                 360  
               
               
                   
               
               
                 ggc ctc cgg cag tcc atc tgg acc aac ttt tcc agc cgc ttc cac ata     1338  
               
               
                 Gly Leu Arg Gln Ser Ile Trp Thr Asn Phe Ser Ser Arg Phe His Ile  
               
               
                             365                 370                 375  
               
               
                   
               
               
                 ccc cag gtg gct gag ttc tac ggg gcc aca gag tgc aac tgt agc ctg     1386  
               
               
                 Pro Gln Val Ala Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Leu  
               
               
                         380                 385                 390  
               
               
                   
               
               
                 ggc aac ttc gac agc cag gtg ggg gcc tgt ggt ttc aat agc cgc atc     1434  
               
               
                 Gly Asn Phe Asp Ser Gln Val Gly Ala Cys Gly Phe Asn Ser Arg Ile  
               
               
                     395                 400                 405  
               
               
                   
               
               
                 ctg tcc ttc gtg tac ccc atc cgg ttg gta cgt gtc aac gag gac acc     1482  
               
               
                 Leu Ser Phe Val Tyr Pro Ile Arg Leu Val Arg Val Asn Glu Asp Thr  
               
               
                 410                 415                 420                 425  
               
               
                   
               
               
                 atg gag ctg atc cgg ggg ccc gac ggc gtc tgc att ccc tgc cag cca     1530  
               
               
                 Met Glu Leu Ile Arg Gly Pro Asp Gly Val Cys Ile Pro Cys Gln Pro  
               
               
                                 430                 435                 440  
               
               
                   
               
               
                 ggt gag ccg ggc cag ctg gtg ggc cgc atc atc cag aaa gac ccc ctg     1578  
               
               
                 Gly Glu Pro Gly Gln Leu Val Gly Arg Ile Ile Gln Lys Asp Pro Leu  
               
               
                             445                 450                 455  
               
               
                   
               
               
                 cgc cgc ttc gat ggc tac ctc aac cag ggc gcc aac aac aag aag att     1626  
               
               
                 Arg Arg Phe Asp Gly Tyr Leu Asn Gln Gly Ala Asn Asn Lys Lys Ile  
               
               
                         460                 465                 470  
               
               
                   
               
               
                 gcc aag gat gtc ttc aag aag ggg gac cag gcc tac ctt act ggt gat     1674  
               
               
                 Ala Lys Asp Val Phe Lys Lys Gly Asp Gln Ala Tyr Leu Thr Gly Asp  
               
               
                     475                 480                 485  
               
               
                   
               
               
                 gtg ctg gtg atg gac gag ctg ggc tac ctg tac ttc cga gac cgc act     1722  
               
               
                 Val Leu Val Met Asp Glu Leu Gly Tyr Leu Tyr Phe Arg Asp Arg Thr  
               
               
                 490                 495                 500                 505  
               
               
                   
               
               
                 ggg gac acg ttc cgc tgg aaa ggt gag aac gtg tcc acc acc gag gtg     1770  
               
               
                 Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ser Thr Thr Glu Val  
               
               
                                 510                 515                 520  
               
               
                   
               
               
                 gaa ggc aca ctc agc cgc ctg ctg gac atg gct gac gtg gcc gtg tat     1818  
               
               
                 Glu Gly Thr Leu Ser Arg Leu Leu Asp Met Ala Asp Val Ala Val Tyr  
               
               
                             525                 530                 535  
               
               
                   
               
               
                 ggt gtc gag gtg cca gga acc gag ggc cgg gcc gga atg gct gct gtg     1866  
               
               
                 Gly Val Glu Val Pro Gly Thr Glu Gly Arg Ala Gly Met Ala Ala Val  
               
               
                         540                 545                 550  
               
               
                   
               
               
                 gcc agc ccc act ggc aac tgt gac ctg gag cgc ttt gct cag gtc ttg     1914  
               
               
                 Ala Ser Pro Thr Gly Asn Cys Asp Leu Glu Arg Phe Ala Gln Val Leu  
               
               
                     555                 560                 565  
               
               
                   
               
               
                 gag aag gaa ctg ccc ctg tat gcg cgc ccc atc ttc ctg cgc ctc ctg     1962  
               
               
                 Glu Lys Glu Leu Pro Leu Tyr Ala Arg Pro Ile Phe Leu Arg Leu Leu  
               
               
                 570                 575                 580                 585  
               
               
                   
               
               
                 cct gag ctg cac aaa aca gga acc tac aag ttc cag aag aca gag cta     2010  
               
               
                 Pro Glu Leu His Lys Thr Gly Thr Tyr Lys Phe Gln Lys Thr Glu Leu  
               
               
                                 590                 595                 600  
               
               
                   
               
               
                 cgg aag gag ggc ttt gac ccg gct att gtg aaa gac ccg ctg ttc tat     2058  
               
               
                 Arg Lys Glu Gly Phe Asp Pro Ala Ile Val Lys Asp Pro Leu Phe Tyr  
               
               
                             605                 610                 615  
               
               
                   
               
               
                 cta gat gcc cag aag ggc cgc tac gtc ccg ctg gac caa gag gcc tac     2106  
               
               
                 Leu Asp Ala Gln Lys Gly Arg Tyr Val Pro Leu Asp Gln Glu Ala Tyr  
               
               
                         620                 625                 630  
               
               
                   
               
               
                 agc cgc atc cag gca ggc gag gag aag ctg tgattccccc catccctctg       2156  
               
               
                 Ser Arg Ile Gln Ala Gly Glu Glu Lys Leu  
               
               
                     635                 640  
               
               
                   
               
               
                 agggccggcg gatgctggat ccggagcccc aggttccgcc ccagagcggt cctggacaag   2216  
               
               
                   
               
               
                 gccagaccaa agcaagcagg gcctggcacc tccatcctga ggtgctgccc ctccatccaa   2276  
               
               
                   
               
               
                 aactgccaag tgactcattg ccttcccaac ccttccagag gctttctgtg aaagtctcat   2336  
               
               
                   
               
               
                 gtccaagttc cgtcttctgg gctgggcagg ccctctggtt cccaggctga gactgacggg   2396  
               
               
                   
               
               
                 ttttctcagg atgatgtctt gggtgagggt agggagagga caaggggtca ccgagccctt   2456  
               
               
                   
               
               
                 cccagagagc agggagctta taaatggaac cagagcagaa gtccccagac tcaggaagtc   2516  
               
               
                   
               
               
                 aacagagtgg gcagggacag tggtagcatc catctggtgg ccaaagagaa tcgtagcccc   2576  
               
               
                   
               
               
                 agagctgccc aagttcactg ggctccaccc ccacctccag gaggggagga gaggacctga   2636  
               
               
                   
               
               
                 catctgtagg tggcccctga tgccccatct acagcaggag gtcaggacca cgcccctggc   2696  
               
               
                   
               
               
                 ctctccccac tcccccatcc tcctccctgg gtggctgcct gattatccct caggcagggc   2756  
               
               
                   
               
               
                 ctctcagtcc ttgtgggtct gtgtcacctc catctcagtc ttggcctggc tatgagggga   2816  
               
               
                   
               
               
                 ggaggaatgg gagagggggc tcaggggcca ataaactctg ccttgagtcc tcctaaaaaa   2876  
               
               
                   
               
               
                 aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa agggcggccg c                       2917  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 27  
               
               
                 &lt;211&gt; LENGTH: 643  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 27  
               
               
                   
               
               
                 Met Leu Leu Gly Ala Ser Leu Val Gly Val Leu Leu Phe Ser Lys Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val Leu Lys Leu Pro Trp Thr Gln Val Gly Phe Ser Leu Leu Phe Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Tyr Leu Gly Ser Gly Gly Trp Arg Phe Ile Arg Val Phe Ile Lys Thr  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ile Arg Arg Asp Ile Phe Gly Gly Leu Val Leu Leu Lys Val Lys Ala  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Lys Val Arg Gln Cys Leu Gln Glu Arg Arg Thr Val Pro Ile Leu Phe  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Ser Thr Val Arg Arg His Pro Asp Lys Thr Ala Leu Ile Phe Glu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Thr Asp Thr His Trp Thr Phe Arg Gln Leu Asp Glu Tyr Ser Ser  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Val Ala Asn Phe Leu Gln Ala Arg Gly Leu Ala Ser Gly Asp Val  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Ala Ala Ile Phe Met Glu Asn Arg Asn Glu Phe Val Gly Leu Trp Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Gly Met Ala Lys Leu Gly Val Glu Ala Ala Leu Ile Asn Thr Asn Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Arg Arg Asp Ala Leu Leu His Cys Leu Thr Thr Ser Arg Ala Arg Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Leu Val Phe Gly Ser Glu Met Ala Ser Ala Ile Cys Glu Val His Ala  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Leu Asp Pro Ser Leu Ser Leu Phe Cys Ser Gly Ser Trp Glu Pro  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Ala Val Pro Pro Ser Thr Glu His Leu Asp Pro Leu Leu Lys Asp  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Pro Lys His Leu Pro Ser Cys Pro Asp Lys Gly Phe Thr Asp Lys  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ala Leu Val Tyr Tyr  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly Phe Arg Met Arg Pro Asn Asp Ile Val Tyr Asp Cys Leu Pro Leu  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Tyr His Ser Ala Gly Asn Ile Val Gly Ile Gly Gln Cys Leu Leu His  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Gly Met Thr Val Val Ile Arg Lys Lys Phe Ser Ala Ser Arg Phe Trp  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Asp Asp Cys Ile Lys Tyr Asn Cys Thr Ile Val Gln Tyr Ile Gly Glu  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Leu Cys Arg Tyr Leu Leu Asn Gln Pro Pro Arg Glu Ala Glu Asn Gln  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 His Gln Val Arg Met Ala Leu Gly Asn Gly Leu Arg Gln Ser Ile Trp  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Thr Asn Phe Ser Ser Arg Phe His Ile Pro Gln Val Ala Glu Phe Tyr  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gly Ala Thr Glu Cys Asn Cys Ser Leu Gly Asn Phe Asp Ser Gln Val  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Ala Cys Gly Phe Asn Ser Arg Ile Leu Ser Phe Val Tyr Pro Ile  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Arg Leu Val Arg Val Asn Glu Asp Thr Met Glu Leu Ile Arg Gly Pro  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Asp Gly Val Cys Ile Pro Cys Gln Pro Gly Glu Pro Gly Gln Leu Val  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Gly Arg Ile Ile Gln Lys Asp Pro Leu Arg Arg Phe Asp Gly Tyr Leu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Asn Gln Gly Ala Asn Asn Lys Lys Ile Ala Lys Asp Val Phe Lys Lys  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Gly Asp Gln Ala Tyr Leu Thr Gly Asp Val Leu Val Met Asp Glu Leu  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Gly Tyr Leu Tyr Phe Arg Asp Arg Thr Gly Asp Thr Phe Arg Trp Lys  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Thr Leu Ser Arg Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Leu Asp Met Ala Asp Val Ala Val Tyr Gly Val Glu Val Pro Gly Thr  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Glu Gly Arg Ala Gly Met Ala Ala Val Ala Ser Pro Thr Gly Asn Cys  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Asp Leu Glu Arg Phe Ala Gln Val Leu Glu Lys Glu Leu Pro Leu Tyr  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Glu Leu His Lys Thr Gly  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Thr Tyr Lys Phe Gln Lys Thr Glu Leu Arg Lys Glu Gly Phe Asp Pro  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ala Ile Val Lys Asp Pro Leu Phe Tyr Leu Asp Ala Gln Lys Gly Arg  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Tyr Val Pro Leu Asp Gln Glu Ala Tyr Ser Arg Ile Gln Ala Gly Glu  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Glu Lys Leu  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 28  
               
               
                 &lt;211&gt; LENGTH: 1941  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 28  
               
               
                   
               
               
                 atgcgggctc cgggtgcggg cgcggcctcg gtggtctcgc tggcgctgtt gtggctgctg     60  
               
               
                   
               
               
                 gggctgccgt ggacctggag cgcggcagcg gcgctcggcg tgtacgtggg cagcggcggc    120  
               
               
                   
               
               
                 tggcgcttcc tgcgcatcgt ctgcaagacc gcgaggcgag acctcttcgg tctctctgtg    180  
               
               
                   
               
               
                 ctgatccgcg tgcgcctgga gctgcggcgg caccagcgtg ccggccacac catcccgcgc    240  
               
               
                   
               
               
                 atctttcagg cggtagtgca gcgacagccc gagcgcctgg cgctggtgga tgccgggacc    300  
               
               
                   
               
               
                 ggcgagtgct ggacctttgc gcagctggac gcctactcca atgcggtagc caacctcttc    360  
               
               
                   
               
               
                 cgccagctgg gcttcgcgcc gggcgacgtg gtggccatct tcctggaggg ccggccggag    420  
               
               
                   
               
               
                 ttcgtggggc tgtggctggg cctggccaag gcgggcatgg aggccgcgct gctcaacgtg    480  
               
               
                   
               
               
                 aacctgcggc gcgagcccct ggccttctgc ctgggcacct cgggcgctaa ggccctgatc    540  
               
               
                   
               
               
                 tttggaggag aaatggtggc ggcggtggcc gaagtgagcg ggcatctggg gaaaagtttg    600  
               
               
                   
               
               
                 atcaagttct gctctggaga cttggggccc gagggcatct tgccggacac ccacctcctg    660  
               
               
                   
               
               
                 gacccgctgc tgaaggaggc ctctactgcc cccttggcac agatccccag caagggcatg    720  
               
               
                   
               
               
                 gacgatcgtc ttttctacat ctacacgtcg gggaccaccg ggctgcccaa ggctgccatt    780  
               
               
                   
               
               
                 gtcgtgcaca gcaggtacta ccgcatggca gccttcggcc accacgccta ccgcatgcag    840  
               
               
                   
               
               
                 gcggctgacg tgctctatga ctgcctgccc ctgtaccact cggcaggaaa catcatcggc    900  
               
               
                   
               
               
                 gtggggcagt gtctcatcta tgggctgaca gtcgtcctcc gcaagaaatt ctcggccagc    960  
               
               
                   
               
               
                 cgcttctggg acgactgcat caagtacaac tgcacggtgg ttcagtacat cggggagatc   1020  
               
               
                   
               
               
                 tgccgctacc tgctgaagca gccggtgcgc gaggcggaga ggcgacaccg cgtgcgcctg   1080  
               
               
                   
               
               
                 gcggtgggga acgggctgcg tcctgccatc tgggaggagt tcacggagcg cttcggcgta   1140  
               
               
                   
               
               
                 cgccaaatcg gggagttcta cggcgccacc gagtgcaact gcagcattgc caacatggac   1200  
               
               
                   
               
               
                 ggcaaggtcg gctcctgtgg tttcaacagc cgcatcctgc cccacgtgta ccccatccgg   1260  
               
               
                   
               
               
                 ctggtgaagg tcaatgagga cacaatggag ctgctgcggg atgcccaggg cctctgcatc   1320  
               
               
                   
               
               
                 ccctgccagg ccggggagcc tggcctcctt gtgggtcaga tcaaccaaca ggacccgctg   1380  
               
               
                   
               
               
                 cgccgcttcg atggctatgt cagcgagagc gccaccagca agaagatcgc ccacagcgtc   1440  
               
               
                   
               
               
                 ttcagcaagg gcgacagcgc ctacctctca ggtgacgtgc tagtgatgga tgagctgggc   1500  
               
               
                   
               
               
                 tacatgtact tccgggaccg tagcggggac accttccgct ggcgagggga gaacgtctcc   1560  
               
               
                   
               
               
                 accaccgagg tggagggcgt gctgagccgc ctgctgggcc agacagacgt ggccgtctat   1620  
               
               
                   
               
               
                 ggggtggctg ttccaggagt ggagggtaag gcagggatgg cggccgtcgc agacccccac   1680  
               
               
                   
               
               
                 agcctgctgg accccaacgc gatataccag gagctgcaga aggtgctggc accctatgcc   1740  
               
               
                   
               
               
                 cggcccatct tcctgcgcct cctgccccag gtggacacca caggcacctt caagatccag   1800  
               
               
                   
               
               
                 aagacgaggc tgcagcgaga gggctttgac ccacgccaga cctcagaccg gctcttcttc   1860  
               
               
                   
               
               
                 ctggacctga agcagggcca ctacctgccc ttaaatgagg cagtctacac tcgcatctgc   1920  
               
               
                   
               
               
                 tcgggcgcct tcgccctctg a                                             1941  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 29  
               
               
                 &lt;211&gt; LENGTH: 1938  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 29  
               
               
                   
               
               
                 atgcgggctc ctggagcagg aacagcctct gtggcctcac tggcgctgct ttggtttctg     60  
               
               
                   
               
               
                 ggacttccgt ggacctggag cgcggcggcg gcgttctgtg tgtacgtggg tggcggcggc    120  
               
               
                   
               
               
                 tggcgctttc tgcgtatcgt ctgcaagacg gcgaggcgag acctctttgg cctctctgtt    180  
               
               
                   
               
               
                 ctgattcgtg ttcggctaga gctgcgacga caccggcgag caggagacac gatcccgtgc    240  
               
               
                   
               
               
                 atcttccagg ctgtggcccg gcgacaacca gagcgcctgg cactggtgga cgccagtagt    300  
               
               
                   
               
               
                 ggtatatgct ggaccttcgc acagctggac acctactcca atgctgtagc caacctgttc    360  
               
               
                   
               
               
                 cgccagctgg gctttgcacc aggcgatgtg gtggctgtgt tcctggaggg ccggccggag    420  
               
               
                   
               
               
                 ttcgtgggac tgtggctggg cctggccaag gccggtgtgg tggctgctct tctcaatgtc    480  
               
               
                   
               
               
                 aacctgaggc gggagcccct ggccttctgc ctgggcacat cagctgccaa ggccctcatt    540  
               
               
                   
               
               
                 tatggcgggg agatggcagc ggcggtggcg gaggtgagcg agcagctggg gaagagcctc    600  
               
               
                   
               
               
                 ctcaagttct gctctggaga tctggggcct gagagcatcc tgcctgacac gcagctcctg    660  
               
               
                   
               
               
                 gaccccatgc ttgctgaggc gcccaccaca cccctggcac aagccccagg caagggcatg    720  
               
               
                   
               
               
                 gatgatcggc tgttttacat ctatacttct gggaccaccg ggcttcctaa ggctgccatt    780  
               
               
                   
               
               
                 gtggtgcaca gcaggtacta ccgcattgct gcctttggcc accattccta cagcatgcgt    840  
               
               
                   
               
               
                 gccgccgatg tgctctatga ctgcctgcca ctctaccact ctgcagggaa catcatgggt    900  
               
               
                   
               
               
                 gtggggcagt gcgtcatcta cgggttgacg gtggtactgc gcaagaagtt ctccgccagc    960  
               
               
                   
               
               
                 cgcttctggg atgactgtgt caagtacaat tgcacggtag tgcagtacat aggtgaaatc   1020  
               
               
                   
               
               
                 tgccgctacc tgctgaggca gccggttcgc gacgtggagc agcgacaccg cgtgcgcctg   1080  
               
               
                   
               
               
                 gccgtgggta atgggctgcg gccagccatc tgggaggagt tcacgcagcg cttcggtgtg   1140  
               
               
                   
               
               
                 ccacagatcg gcgagttcta cggcgctacc gagtgcaact gcagcattgc caacatggac   1200  
               
               
                   
               
               
                 ggcaaggtcg gctcctgcgg cttcaacagc cgtatcctca cgcatgtgta ccccatccgt   1260  
               
               
                   
               
               
                 ctggtcaagg tcaatgagga cacgatggag ccactgcggg actccgaggg cctctgcatc   1320  
               
               
                   
               
               
                 ccgtgccagc ccggggaacc cggccttctc gtgggccaga tcaaccagca ggaccctctg   1380  
               
               
                   
               
               
                 cggcgtttcg atggttatgt tagtgacagt gccaccaaca agaagattgc ccacagcgtt   1440  
               
               
                   
               
               
                 ttccgaaagg gcgatagcgc ctacctctca ggtgacgtgc tagtgatgga cgagctgggc   1500  
               
               
                   
               
               
                 tacatgtatt tccgtgaccg cagcggggac accttccgct ggcgcgggga gaacgtgtcc   1560  
               
               
                   
               
               
                 accacggagg tggaagccgt gctgagccgc ctactgggcc agacggacgt ggctgtgtat   1620  
               
               
                   
               
               
                 ggggtggctg tgccaggagt ggaggggaaa gctggcatgg cagccatcgc agatccccac   1680  
               
               
                   
               
               
                 agccagttgg accctaactc aatgtaccag gaattacaga aggttcttgc atcctatgct   1740  
               
               
                   
               
               
                 cggcccatct tcctgcgtct tctgccccag gtggatacca caggcacctt caagatccag   1800  
               
               
                   
               
               
                 aagacccggc tgcagcgtga aggctttgac ccccgtcaga cctcagacag gctcttcttt   1860  
               
               
                   
               
               
                 ctagacctga agcagggacg ctatgtaccc ctggatgaga gagtccatgc ccgcatttgt   1920  
               
               
                   
               
               
                 gcaggcgact tctcactc                                                 1938  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 30  
               
               
                 &lt;211&gt; LENGTH: 1896  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 30  
               
               
                   
               
               
                 ctgttctcca agctggtgct gaaactgccc tggacccagg tgggattctc cctgttgttc     60  
               
               
                   
               
               
                 ctctacttgg gatctggcgg ctggcgcttc atccgggtct tcatcaagac catcaggcgc    120  
               
               
                   
               
               
                 gatatctttg gcggcctggt cctcctgaag gtgaaggcaa aggtgcgaca gtgcctgcag    180  
               
               
                   
               
               
                 gagcggcgga cagtgcccat tttgtttgcc tctaccgttc ggcgccaccc cgacaagacg    240  
               
               
                   
               
               
                 gccctgatct tcgagggcac agatacccac tggaccttcc gccagctgga tgagtactca    300  
               
               
                   
               
               
                 agcagtgtag ccaacttcct gcaggcccgg ggcctggcct cgggcgatgt ggctgccatc    360  
               
               
                   
               
               
                 ttcatggaga accgcaatga gttcgtgggc ctatggctgg gcatggccaa gctcggtgtg    420  
               
               
                   
               
               
                 gaggcagccc tcatcaacac caacctgcgg cgggatgctc tgctccactg cctcaccacc    480  
               
               
                   
               
               
                 tcgcgcgcac gggcccttgt ctttggcagc gaaatggcct cagccatctg tgaggtccat    540  
               
               
                   
               
               
                 gccagcctgg acccctcgct cagcctcttc tgctctggct cctgggagcc cggtgcggtg    600  
               
               
                   
               
               
                 cctccaagca cagaacacct ggaccctctg ctgaaagatg ctcccaagca ccttcccagt    660  
               
               
                   
               
               
                 tgccctgaca agggcttcac agataaactg ttctacatct acacatccgg caccacaggg    720  
               
               
                   
               
               
                 ctgcccaagg ccgccatcgt ggtgcacagc aggtattacc gcatggctgc cctggtgtac    780  
               
               
                   
               
               
                 tatggattcc gcatgcggcc caacgacatc gtctatgact gcctccccct ctaccactca    840  
               
               
                   
               
               
                 gcaggaaaca tcgtgggaat cggccagtgc ctgctgcatg gcatgacggt ggtgattcgg    900  
               
               
                   
               
               
                 aagaagttct cagcctcccg gttctgggac gattgtatca agtacaactg cacgattgtg    960  
               
               
                   
               
               
                 cagtacattg gtgaactgtg ccgctacctc ctgaaccagc caccgcggga ggcagaaaac   1020  
               
               
                   
               
               
                 cagcaccagg ttcgcatggc actaggcaat ggcctccggc agtccatctg gaccaacttt   1080  
               
               
                   
               
               
                 tccagccgct tccacatacc ccaggtggct gagttctacg gggccacaga gtgcaactgt   1140  
               
               
                   
               
               
                 agcctgggca acttcgacag ccaggtgggg gcctgtggtt tcaatagccg catcctgtcc   1200  
               
               
                   
               
               
                 ttcgtgtacc ccatccggtt ggtacgtgtc aacgaggaca ccatggagct gatccggggg   1260  
               
               
                   
               
               
                 cccgacggcg tctgcattcc ctgccagcca ggtgagccgg gccagctggt gggccgcatc   1320  
               
               
                   
               
               
                 atccagaaag accccctgcg ccgcttcgat ggctacctca accagggcgc caacaacaag   1380  
               
               
                   
               
               
                 aagattgcca aggatgtctt caagaagggg gaccaggcct accttactgg tgatgtgctg   1440  
               
               
                   
               
               
                 gtgatggacg agctgggcta cctgtacttc cgagaccgca ctggggacac gttccgctgg   1500  
               
               
                   
               
               
                 aaaggtgaga acgtgtccac caccgaggtg gaaggcacac tcagccgcct gctggacatg   1560  
               
               
                   
               
               
                 gctgacgtgg ccgtgtatgg tgtcgaggtg ccaggaaccg agggccgggc cggaatggct   1620  
               
               
                   
               
               
                 gctgtggcca gccccactgg caactgtgac ctggagcgct ttgctcaggt cttggagaag   1680  
               
               
                   
               
               
                 gaactgcccc tgtatgcgcg ccccatcttc ctgcgcctcc tgcctgagct gcacaaaaca   1740  
               
               
                   
               
               
                 ggaacctaca agttccagaa gacagagcta cggaaggagg gctttgaccc ggctattgtg   1800  
               
               
                   
               
               
                 aaagacccgc tgttctatct agatgcccag aagggccgct acgtcccgct ggaccaagag   1860  
               
               
                   
               
               
                 gcctacagcc gcatccaggc aggcgaggag aagctg                             1896  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 31  
               
               
                 &lt;211&gt; LENGTH: 1896  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 31  
               
               
                   
               
               
                 cttgggtcca agctagtgct gaagctgccc tggacccagg tgggattctc cctgttgctc     60  
               
               
                   
               
               
                 ctgtacttgg ggtctggtgg ctggcgtttc atccgggtct tcatcaagac ggtcaggaga    120  
               
               
                   
               
               
                 gatatctttg gtggcatggt gctcctgaag gtgaagacca aggtgcgacg gtaccttcag    180  
               
               
                   
               
               
                 gagcggaaga cggtgcccct gctgtttgct tcaatggtac agcgccaccc ggacaagaca    240  
               
               
                   
               
               
                 gccctgattt tcgagggcac agacactcac tggaccttcc gccagctgga tgagtactcc    300  
               
               
                   
               
               
                 agtagtgtgg ccaacttcct gcaggcccgg ggcctggcct caggcaatgt agttgccctc    360  
               
               
                   
               
               
                 tttatggaaa accgcaatga gtttgtgggt ctgtggctag gcatggccaa gctgggcgtg    420  
               
               
                   
               
               
                 gaggcggctc tcatcaacac caaccttagg cgggatgccc tgcgccactg tcttgacacc    480  
               
               
                   
               
               
                 tcaaaggcac gagctctcat ctttggcagt gagatggcct cagctatctg tgagatccat    540  
               
               
                   
               
               
                 gctagcctgg agcccacact cagcctcttc tgctctggat cctgggagcc cagcacagtg    600  
               
               
                   
               
               
                 cccgtcagca cagagcatct ggaccctctt ctggaagatg ccccgaagca cctgcccagt    660  
               
               
                   
               
               
                 cacccagaca agggttttac agataagctc ttctacatct acacatcggg caccacgggg    720  
               
               
                   
               
               
                 ctacccaaag ctgccattgt ggtgcacagc aggtattatc gtatggcttc cctggtgtac    780  
               
               
                   
               
               
                 tatggattcc gcatgcggcc tgatgacatt gtctatgact gcctccccct ctaccactca    840  
               
               
                   
               
               
                 agcaggaaac atcgtgggga ttggcagtgc ttactccacg gcatgactgt ggtgatccgg    900  
               
               
                   
               
               
                 aagaagttct cagcctcccg gttctgggat gattgtatca agtacaactg cacagtggta    960  
               
               
                   
               
               
                 cagtacattg gcgagctctg ccgctacctc ctgaaccagc caccccgtga ggctgagtct   1020  
               
               
                   
               
               
                 cggcacaagg tgcgcatggc actgggcaac ggtctccggc agtccatctg gaccgacttc   1080  
               
               
                   
               
               
                 tccagccgtt tccacatccc ccaggtggct gagttctatg gggccactga atgcaactgt   1140  
               
               
                   
               
               
                 agcctgggca actttgacag ccgggtgggg gcctgtggct tcaatagccg catcctgtcc   1200  
               
               
                   
               
               
                 tttgtgtacc ctatccgttt ggtacgtgtc aatgaggata ccatggaact gatccgggga   1260  
               
               
                   
               
               
                 cccgatggag tctgcattcc ctgtcaacca ggtcagccag gccagctggt gggtcgcatc   1320  
               
               
                   
               
               
                 atccagcagg accctctgcg ccgtttcgac gggtacctca accagggtgc caacaacaag   1380  
               
               
                   
               
               
                 aagattgcta atgatgtctt caagaagggg gaccaagcct acctcactgg tgacgtcctg   1440  
               
               
                   
               
               
                 gtgatggatg agctgggtta cctgtacttc cgagatcgca ctggggacac gttccgctgg   1500  
               
               
                   
               
               
                 aaaggggaga atgtatctac cactgaggtg gagggcacac tcagccgcct gcttcatatg   1560  
               
               
                   
               
               
                 gcagatgtgg cagtttatgg tgttgaggtg ccaggaactg aaggccgagc aggaatggct   1620  
               
               
                   
               
               
                 gccgttgcaa gtcccatcag caactgtgac ctggagagct ttgcacagac cttgaaaaag   1680  
               
               
                   
               
               
                 gagctgcctc tgtatgcccg ccccatcttc ctgcgcttct tgcctgagct gcacaagaca   1740  
               
               
                   
               
               
                 gggaccttca agttccagaa gacagagttg cggaaggagg gctttgaccc atctgttgtg   1800  
               
               
                   
               
               
                 aaagacccgc tgttctatct ggatgctcgg aagggctgct acgttgcact ggaccaggag   1860  
               
               
                   
               
               
                 gcctataccc gcatccaggc aggcgaggag aagctg                             1896  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 32  
               
               
                 &lt;211&gt; LENGTH: 646  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 32  
               
               
                   
               
               
                 Met Arg Ala Pro Gly Ala Gly Ala Ala Ser Val Val Ser Leu Ala Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Trp Leu Leu Gly Leu Pro Trp Thr Trp Ser Ala Ala Ala Ala Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Val Tyr Val Gly Ser Gly Gly Trp Arg Phe Leu Arg Ile Val Cys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Thr Ala Arg Arg Asp Leu Phe Gly Leu Ser Val Leu Ile Arg Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Arg Leu Glu Leu Arg Arg His Gln Arg Ala Gly His Thr Ile Pro Arg  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ile Phe Gln Ala Val Val Gln Arg Gln Pro Glu Arg Leu Ala Leu Val  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Ala Gly Thr Gly Glu Cys Trp Thr Phe Ala Gln Leu Asp Ala Tyr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Asn Ala Val Ala Asn Leu Phe Arg Gln Leu Gly Phe Ala Pro Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asp Val Val Ala Ile Phe Leu Glu Gly Arg Pro Glu Phe Val Gly Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Trp Leu Gly Leu Ala Lys Ala Gly Met Glu Ala Ala Leu Leu Asn Val  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asn Leu Arg Arg Glu Pro Leu Ala Phe Cys Leu Gly Thr Ser Gly Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Lys Ala Leu Ile Phe Gly Gly Glu Met Val Ala Ala Val Ala Glu Val  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Gly His Leu Gly Lys Ser Leu Ile Lys Phe Cys Ser Gly Asp Leu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Pro Glu Gly Ile Leu Pro Asp Thr His Leu Leu Asp Pro Leu Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Lys Glu Ala Ser Thr Ala Pro Leu Ala Gln Ile Pro Ser Lys Gly Met  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asp Asp Arg Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ala Phe  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly His His Ala Tyr Arg Met Gln Ala Ala Asp Val Leu Tyr Asp Cys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Leu Pro Leu Tyr His Ser Ala Gly Asn Ile Ile Gly Val Gly Gln Cys  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Leu Ile Tyr Gly Leu Thr Val Val Leu Arg Lys Lys Phe Ser Ala Ser  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Arg Phe Trp Asp Asp Cys Ile Lys Tyr Asn Cys Thr Val Val Gln Tyr  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ile Gly Glu Ile Cys Arg Tyr Leu Leu Lys Gln Pro Val Arg Glu Ala  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Glu Arg Arg His Arg Val Arg Leu Ala Val Gly Asn Gly Leu Arg Pro  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ala Ile Trp Glu Glu Phe Thr Glu Arg Phe Gly Val Arg Gln Ile Gly  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Ile Ala Asn Met Asp  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Lys Val Gly Ser Cys Gly Phe Asn Ser Arg Ile Leu Pro His Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Tyr Pro Ile Arg Leu Val Lys Val Asn Glu Asp Thr Met Glu Leu Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Arg Asp Ala Gln Gly Leu Cys Ile Pro Cys Gln Ala Gly Glu Pro Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Leu Val Gly Gln Ile Asn Gln Gln Asp Pro Leu Arg Arg Phe Asp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gly Tyr Val Ser Glu Ser Ala Thr Ser Lys Lys Ile Ala His Ser Val  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Phe Ser Lys Gly Asp Ser Ala Tyr Leu Ser Gly Asp Val Leu Val Met  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Asp Glu Leu Gly Tyr Met Tyr Phe Arg Asp Arg Ser Gly Asp Thr Phe  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Arg Trp Arg Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Val Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ser Arg Leu Leu Gly Gln Thr Asp Val Ala Val Tyr Gly Val Ala Val  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Gly Val Glu Gly Lys Ala Gly Met Ala Ala Val Ala Asp Pro His  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ser Leu Leu Asp Pro Asn Ala Ile Tyr Gln Glu Leu Gln Lys Val Leu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ala Pro Tyr Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Gln Val Asp  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Thr Thr Gly Thr Phe Lys Ile Gln Lys Thr Arg Leu Gln Arg Glu Gly  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Phe Asp Pro Arg Gln Thr Ser Asp Arg Leu Phe Phe Leu Asp Leu Lys  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Gln Gly His Tyr Leu Pro Leu Asn Glu Ala Val Tyr Thr Arg Ile Cys  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Ser Gly Ala Phe Ala Leu  
               
               
                                 645  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 33  
               
               
                 &lt;211&gt; LENGTH: 646  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 33  
               
               
                   
               
               
                 Met Arg Ala Pro Gly Ala Gly Thr Ala Ser Val Ala Ser Leu Ala Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Trp Phe Leu Gly Leu Pro Trp Thr Trp Ser Ala Ala Ala Ala Phe  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Cys Val Tyr Val Gly Gly Gly Gly Trp Arg Phe Leu Arg Ile Val Cys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Thr Ala Arg Arg Asp Leu Phe Gly Leu Ser Val Leu Ile Arg Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Arg Leu Glu Leu Arg Arg His Arg Arg Ala Gly Asp Thr Ile Pro Cys  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ile Phe Gln Ala Val Ala Arg Arg Gln Pro Glu Arg Leu Ala Leu Val  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Ala Ser Ser Gly Ile Cys Trp Thr Phe Ala Gln Leu Asp Thr Tyr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Asn Ala Val Ala Asn Leu Phe Arg Gln Leu Gly Phe Ala Pro Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asp Val Val Ala Val Phe Leu Glu Gly Arg Pro Glu Phe Val Gly Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Trp Leu Gly Leu Ala Lys Ala Gly Val Val Ala Ala Leu Leu Asn Val  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asn Leu Arg Arg Glu Pro Leu Ala Phe Cys Leu Gly Thr Ser Ala Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Lys Ala Leu Ile Tyr Gly Gly Glu Met Ala Ala Ala Val Ala Glu Val  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Glu Gln Leu Gly Lys Ser Leu Leu Lys Phe Cys Ser Gly Asp Leu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Pro Glu Ser Ile Leu Pro Asp Thr Gln Leu Leu Asp Pro Met Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Glu Ala Pro Thr Thr Pro Leu Ala Gln Ala Pro Gly Lys Gly Met  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asp Asp Arg Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Ile Ala Ala Phe  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly His His Ser Tyr Ser Met Arg Ala Ala Asp Val Leu Tyr Asp Cys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Leu Pro Leu Tyr His Ser Ala Gly Asn Ile Met Gly Val Gly Gln Cys  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Val Ile Tyr Gly Leu Thr Val Val Leu Arg Lys Lys Phe Ser Ala Ser  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Arg Phe Trp Asp Asp Cys Val Lys Tyr Asn Cys Thr Val Val Gln Tyr  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ile Gly Glu Ile Cys Arg Tyr Leu Leu Arg Gln Pro Val Arg Asp Val  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Glu Gln Arg His Arg Val Arg Leu Ala Val Gly Asn Gly Leu Arg Pro  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ala Ile Trp Glu Glu Phe Thr Gln Arg Phe Gly Val Pro Gln Ile Gly  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Ile Ala Asn Met Asp  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Lys Val Gly Ser Cys Gly Phe Asn Ser Arg Ile Leu Thr His Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Tyr Pro Ile Arg Leu Val Lys Val Asn Glu Asp Thr Met Glu Pro Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Arg Asp Ser Glu Gly Leu Cys Ile Pro Cys Gln Pro Gly Glu Pro Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Leu Val Gly Gln Ile Asn Gln Gln Asp Pro Leu Arg Arg Phe Asp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gly Tyr Val Ser Asp Ser Ala Thr Asn Lys Lys Ile Ala His Ser Val  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Phe Arg Lys Gly Asp Ser Ala Tyr Leu Ser Gly Asp Val Leu Val Met  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Asp Glu Leu Gly Tyr Met Tyr Phe Arg Asp Arg Ser Gly Asp Thr Phe  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Arg Trp Arg Gly Glu Asn Val Ser Thr Thr Glu Val Glu Ala Val Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ser Arg Leu Leu Gly Gln Thr Asp Val Ala Val Tyr Gly Val Ala Val  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Gly Val Glu Gly Lys Ala Gly Met Ala Ala Ile Ala Asp Pro His  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ser Gln Leu Asp Pro Asn Ser Met Tyr Gln Glu Leu Gln Lys Val Leu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ala Ser Tyr Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Gln Val Asp  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Thr Thr Gly Thr Phe Lys Ile Gln Lys Thr Arg Leu Gln Arg Glu Gly  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Phe Asp Pro Arg Gln Thr Ser Asp Arg Leu Phe Phe Leu Asp Leu Lys  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Gln Gly Arg Tyr Val Pro Leu Asp Glu Arg Val His Ala Arg Ile Cys  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Ala Gly Asp Phe Ser Leu  
               
               
                                 645  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 34  
               
               
                 &lt;211&gt; LENGTH: 632  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 34  
               
               
                   
               
               
                 Leu Phe Ser Lys Leu Val Leu Lys Leu Pro Trp Thr Gln Val Gly Phe  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ser Leu Leu Phe Leu Tyr Leu Gly Ser Gly Gly Trp Arg Phe Ile Arg  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Val Phe Ile Lys Thr Ile Arg Arg Asp Ile Phe Gly Gly Leu Val Leu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Leu Lys Val Lys Ala Lys Val Arg Gln Cys Leu Gln Glu Arg Arg Thr  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Val Pro Ile Leu Phe Ala Ser Thr Val Arg Arg His Pro Asp Lys Thr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Leu Ile Phe Glu Gly Thr Asp Thr His Trp Thr Phe Arg Gln Leu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Glu Tyr Ser Ser Ser Val Ala Asn Phe Leu Gln Ala Arg Gly Leu  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ala Ser Gly Asp Val Ala Ala Ile Phe Met Glu Asn Arg Asn Glu Phe  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Val Gly Leu Trp Leu Gly Met Ala Lys Leu Gly Val Glu Ala Ala Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ile Asn Thr Asn Leu Arg Arg Asp Ala Leu Leu His Cys Leu Thr Thr  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Ser Arg Ala Arg Ala Leu Val Phe Gly Ser Glu Met Ala Ser Ala Ile  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Cys Glu Val His Ala Ser Leu Asp Pro Ser Leu Ser Leu Phe Cys Ser  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Gly Ser Trp Glu Pro Gly Ala Val Pro Pro Ser Thr Glu His Leu Asp  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Pro Leu Leu Lys Asp Ala Pro Lys His Leu Pro Ser Cys Pro Asp Lys  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Gly Phe Thr Asp Lys Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Leu Pro Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Ala Leu Val Tyr Tyr Gly Phe Arg Met Arg Pro Asn Asp Ile Val Tyr  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Asp Cys Leu Pro Leu Tyr His Ser Ala Gly Asn Ile Val Gly Ile Gly  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Gln Cys Leu Leu His Gly Met Thr Val Val Ile Arg Lys Lys Phe Ser  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ala Ser Arg Phe Trp Asp Asp Cys Ile Lys Tyr Asn Cys Thr Ile Val  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Gln Tyr Ile Gly Glu Leu Cys Arg Tyr Leu Leu Asn Gln Pro Pro Arg  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Glu Ala Glu Asn Gln His Gln Val Arg Met Ala Leu Gly Asn Gly Leu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Arg Gln Ser Ile Trp Thr Asn Phe Ser Ser Arg Phe His Ile Pro Gln  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Val Ala Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Leu Gly Asn  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Phe Asp Ser Gln Val Gly Ala Cys Gly Phe Asn Ser Arg Ile Leu Ser  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Phe Val Tyr Pro Ile Arg Leu Val Arg Val Asn Glu Asp Thr Met Glu  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Leu Ile Arg Gly Pro Asp Gly Val Cys Ile Pro Cys Gln Pro Gly Glu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Pro Gly Gln Leu Val Gly Arg Ile Ile Gln Lys Asp Pro Leu Arg Arg  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Phe Asp Gly Tyr Leu Asn Gln Gly Ala Asn Asn Lys Lys Ile Ala Lys  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Asp Val Phe Lys Lys Gly Asp Gln Ala Tyr Leu Thr Gly Asp Val Leu  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Val Met Asp Glu Leu Gly Tyr Leu Tyr Phe Arg Asp Arg Thr Gly Asp  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Thr Phe Arg Trp Lys Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Thr Leu Ser Arg Leu Leu Asp Met Ala Asp Val Ala Val Tyr Gly Val  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Glu Val Pro Gly Thr Glu Gly Arg Ala Gly Met Ala Ala Val Ala Ser  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Thr Gly Asn Cys Asp Leu Glu Arg Phe Ala Gln Val Leu Glu Lys  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Glu Leu Pro Leu Tyr Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Glu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu His Lys Thr Gly Thr Tyr Lys Phe Gln Lys Thr Glu Leu Arg Lys  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Glu Gly Phe Asp Pro Ala Ile Val Lys Asp Pro Leu Phe Tyr Leu Asp  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ala Gln Lys Gly Arg Tyr Val Pro Leu Asp Gln Glu Ala Tyr Ser Arg  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Ile Gln Ala Gly Glu Glu Lys Leu  
               
               
                 625                 630  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 35  
               
               
                 &lt;211&gt; LENGTH: 632  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 35  
               
               
                   
               
               
                 Leu Gly Ser Lys Leu Val Leu Lys Leu Pro Trp Thr Gln Val Gly Phe  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ser Leu Leu Leu Leu Tyr Leu Gly Ser Gly Gly Trp Arg Phe Ile Arg  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Val Phe Ile Lys Thr Val Arg Arg Asp Ile Phe Gly Gly Met Val Leu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Leu Lys Val Lys Thr Lys Val Arg Arg Tyr Leu Gln Glu Arg Lys Thr  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Val Pro Leu Leu Phe Ala Ser Met Val Gln Arg His Pro Asp Lys Thr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Leu Ile Phe Glu Gly Thr Asp Thr His Trp Thr Phe Arg Gln Leu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Glu Tyr Ser Ser Ser Val Ala Asn Phe Leu Gln Ala Arg Gly Leu  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ala Ser Gly Asn Val Val Ala Leu Phe Met Glu Asn Arg Asn Glu Phe  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Val Gly Leu Trp Leu Gly Met Ala Lys Leu Gly Val Glu Ala Ala Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ile Asn Thr Asn Leu Arg Arg Asp Ala Leu Arg His Cys Leu Asp Thr  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Ser Lys Ala Arg Ala Leu Ile Phe Gly Ser Glu Met Ala Ser Ala Ile  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Cys Glu Ile His Ala Ser Leu Glu Pro Thr Leu Ser Leu Phe Cys Ser  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Gly Ser Trp Glu Pro Ser Thr Val Pro Val Ser Thr Glu His Leu Asp  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Pro Leu Leu Glu Asp Ala Pro Lys His Leu Pro Ser His Pro Asp Lys  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Gly Phe Thr Asp Lys Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Leu Pro Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Ser Leu Val Tyr Tyr Gly Phe Arg Met Arg Pro Asp Asp Ile Val Tyr  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Asp Cys Leu Pro Leu Tyr His Ser Ser Arg Lys His Arg Gly Asp Trp  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Gln Cys Leu Leu His Gly Met Thr Val Val Ile Arg Lys Lys Phe Ser  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ala Ser Arg Phe Trp Asp Asp Cys Ile Lys Tyr Asn Cys Thr Val Val  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Gln Tyr Ile Gly Glu Leu Cys Arg Tyr Leu Leu Asn Gln Pro Pro Arg  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Glu Ala Glu Ser Arg His Lys Val Arg Met Ala Leu Gly Asn Gly Leu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Arg Gln Ser Ile Trp Thr Asp Phe Ser Ser Arg Phe His Ile Pro Gln  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Val Ala Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Leu Gly Asn  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Phe Asp Ser Arg Val Gly Ala Cys Gly Phe Asn Ser Arg Ile Leu Ser  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Phe Val Tyr Pro Ile Arg Leu Val Arg Val Asn Glu Asp Thr Met Glu  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Leu Ile Arg Gly Pro Asp Gly Val Cys Ile Pro Cys Gln Pro Gly Gln  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Pro Gly Gln Leu Val Gly Arg Ile Ile Gln Gln Asp Pro Leu Arg Arg  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Phe Asp Gly Tyr Leu Asn Gln Gly Ala Asn Asn Lys Lys Ile Ala Asn  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Asp Val Phe Lys Lys Gly Asp Gln Ala Tyr Leu Thr Gly Asp Val Leu  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Val Met Asp Glu Leu Gly Tyr Leu Tyr Phe Arg Asp Arg Thr Gly Asp  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Thr Phe Arg Trp Lys Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Thr Leu Ser Arg Leu Leu His Met Ala Asp Val Ala Val Tyr Gly Val  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Glu Val Pro Gly Thr Glu Gly Arg Ala Gly Met Ala Ala Val Ala Ser  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Ile Ser Asn Cys Asp Leu Glu Ser Phe Ala Gln Thr Leu Lys Lys  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Glu Leu Pro Leu Tyr Ala Arg Pro Ile Phe Leu Arg Phe Leu Pro Glu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu His Lys Thr Gly Thr Phe Lys Phe Gln Lys Thr Glu Leu Arg Lys  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Glu Gly Phe Asp Pro Ser Val Val Lys Asp Pro Leu Phe Tyr Leu Asp  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ala Arg Lys Gly Cys Tyr Val Ala Leu Asp Gln Glu Ala Tyr Thr Arg  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Ile Gln Ala Gly Glu Glu Lys Leu  
               
               
                 625                 630  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 36  
               
               
                 &lt;211&gt; LENGTH: 2885  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 36  
               
               
                   
               
               
                 aacggcaagt aagcgcaacg caattaatgt gagtagctca ctcattaggc accccaggct     60  
               
               
                   
               
               
                 ttacacttta tgcttccggg ctcgtatgtt gtgtggaatt gtgagcggat accaatttca    120  
               
               
                   
               
               
                 cacaggaacc agctatgaca tgattacgaa tttaatacga ctcactatag ggaatttggc    180  
               
               
                   
               
               
                 cctcgaggcc aagaattcgg cacgaggggt gctgagcccc tgcgcggttt ctggtgcgta    240  
               
               
                   
               
               
                 gagactgtaa atcgctgcgc ttctcagtca tcatcatccc agcttttccc ggctcgaatt    300  
               
               
                   
               
               
                 cagcctccaa ctcaagctcg cgggaaagac tacctgagag gagaaaagct tctgtccctg    360  
               
               
                   
               
               
                 gaccttcttc tgagggtgga gtcggaggct ccctgctttc cagccgccca gtgacccaag    420  
               
               
                   
               
               
                 cttaatcttc agcaccactt ggggcgacct tttcggtgca aacctacgat tctgtttctc    480  
               
               
                   
               
               
                 aggattcctc cccatcccgc ttcgccccgg aaaagctgac aagaacttca ggtgtaagcc    540  
               
               
                   
               
               
                 ctgagtagtg aggatctgcg gtctccgtgg agagctgtgc ctggaagaga aggacgctgg    600  
               
               
                   
               
               
                 tgggggctga gatcagagct gtcttctggc ccagttgccc ccatgcttct gtcatggcta    660  
               
               
                   
               
               
                 acagttctag gggctggaat ggtcgtcctg cacttcttgc agaaactcct gttcccttac    720  
               
               
                   
               
               
                 ttttgggatg acttctggtt cgtgttgaag gtggtgctca ttataattcg gctgaagaag    780  
               
               
                   
               
               
                 tatgaaaaga gaggggagct ggtgactgtg ctggataaat tcttgagtca tgccaaaaga    840  
               
               
                   
               
               
                 caacctcgga aacctttcat catctatgag ggagacatct acacctatca ggatgtagac    900  
               
               
                   
               
               
                 aaaaggagca gcagagtggc ccatgtcttc ctgaaccatt cctctctgaa aaagggggac    960  
               
               
                   
               
               
                 acggtggctc tgctgatgag caatgagccg gacttcgttc acgtgtggtt cggcctcgcc   1020  
               
               
                   
               
               
                 aagctgggct gcgtggtggc ctttctcaac accaacattc gctccaactc cctcctgaat   1080  
               
               
                   
               
               
                 tgcatccgcg cctgtgggcc cagagcccta gtggtgggcg cagatttgct tggaacggta   1140  
               
               
                   
               
               
                 gaagaaatcc ttccaagcct ctcagaaaat atcagtgttt gggggatgaa agattctgtt   1200  
               
               
                   
               
               
                 ccacaaggtg taatttcact caaagaaaaa ctgagcacct cacctgatga gcccgtgcca   1260  
               
               
                   
               
               
                 cgcagccacc atgttgtctc actcctcaag tctacttgtc tttacatttt tacctctgga   1320  
               
               
                   
               
               
                 acaacaggtc taccaaaagc agctgtgatt agtcagctgc aggttttaag gggttctgct   1380  
               
               
                   
               
               
                 gtcctgtggg cttttggttg tactgctcat gacattgttt atataaccct tcctctgtat   1440  
               
               
                   
               
               
                 catagttcag cagctatcct gggaatttct ggatgtgttg agttgggtgc cacttgtgtg   1500  
               
               
                   
               
               
                 ttaaagaaga aattttcagc aagccagttt tggagtgact gcaagaagta tgatgtgact   1560  
               
               
                   
               
               
                 gtgtttcagt atattggaga actttgtcgc tacctttgca aacaatctaa gagagaagga   1620  
               
               
                   
               
               
                 gaaaaggatc ataaggtgcg tttggcaatt ggaaatggca tacggagtga tgtatggaga   1680  
               
               
                   
               
               
                 gaatttttag acagatttgg aaatataaag gtgtgtgaac tttatgcagc taccgaatca   1740  
               
               
                   
               
               
                 agcatatctt tcatgaacta cactgggaga attggagcaa ttgggagaac aaatttgttt   1800  
               
               
                   
               
               
                 tacaaacttc tttccacttt tgacttaata aagtatgact ttcagaaaga tgaacccatg   1860  
               
               
                   
               
               
                 agaaatgagc agggttggtg tattcatgtg aaaaaaggag aacctggact tctcatttct   1920  
               
               
                   
               
               
                 cgagtgaatg caaaaaatcc cttctttggc tatgctgggc cttataagca cacaaaagac   1980  
               
               
                   
               
               
                 aaattgcttt gtgatgtttt taagaaggga gatgtttacc ttaatactgg agacttaata   2040  
               
               
                   
               
               
                 gtccaggatc aggacaattt cctttatttt tgggaccgta ctggagacac tttcagatgg   2100  
               
               
                   
               
               
                 aaaggagaaa atgtcgcaac cactgaggtt gctgatgtta ttggaatgtt ggatttcata   2160  
               
               
                   
               
               
                 caggaagcaa acgtctatgg tgtggctata tcaggttatg aaggaagagc aggaatggct   2220  
               
               
                   
               
               
                 tctattattt taaaaccaaa tacatcttta gatttggaaa aagtttatga acaagttgta   2280  
               
               
                   
               
               
                 acatttctac cagcttatgc ttgtccacga tttttaagaa ttcaggaaaa aatggaagca   2340  
               
               
                   
               
               
                 acaggaacat tcaaactatt gaagcatcag ttggtggaag atggatttaa tccactgaaa   2400  
               
               
                   
               
               
                 atttctgaac cactttactt catggataac ttgaaaaagt cttatgttct actgaccagg   2460  
               
               
                   
               
               
                 gaactttatg atcaaataat gttaggggaa ataaaacttt aagattttta tatctagaac   2520  
               
               
                   
               
               
                 tttcatatgc tttcttagga agagtgagag gggggtatat gattctttat gaaatgggga   2580  
               
               
                   
               
               
                 aagggagcta acattaatta tgcatgtact atatttcctt aatatgagag ataatttttt   2640  
               
               
                   
               
               
                 aattgcataa gaattttaat ttcttttaat tgatataaac attagttgat tattcttttt   2700  
               
               
                   
               
               
                 atctatttgg agattcagtg cataactaag tattttcctt aatactaaag attttaaata   2760  
               
               
                   
               
               
                 ataaatagtg gctagcggtt tggacaatca ctaaaaatgt actttctaat aagtaaaatt   2820  
               
               
                   
               
               
                 tctaattttg aataaaagat taaattttac tgaaaaaaaa aaaaaaaaaa aaaattggcg   2880  
               
               
                   
               
               
                 gccgc                                                               2885  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 37  
               
               
                 &lt;211&gt; LENGTH: 619  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 37  
               
               
                   
               
               
                 Met Leu Leu Ser Trp Leu Thr Val Leu Gly Ala Gly Met Val Val Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 His Phe Leu Gln Lys Leu Leu Phe Pro Tyr Phe Trp Asp Asp Phe Trp  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Val Leu Lys Val Val Leu Ile Ile Ile Arg Leu Lys Lys Tyr Glu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Arg Gly Glu Leu Val Thr Val Leu Asp Lys Phe Leu Ser His Ala  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Lys Arg Gln Pro Arg Lys Pro Phe Ile Ile Tyr Glu Gly Asp Ile Tyr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Thr Tyr Gln Asp Val Asp Lys Arg Ser Ser Arg Val Ala His Val Phe  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Leu Asn His Ser Ser Leu Lys Lys Gly Asp Thr Val Ala Leu Leu Met  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Asn Glu Pro Asp Phe Val His Val Trp Phe Gly Leu Ala Lys Leu  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Gly Cys Val Val Ala Phe Leu Asn Thr Asn Ile Arg Ser Asn Ser Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Leu Asn Cys Ile Arg Ala Cys Gly Pro Arg Ala Leu Val Val Gly Ala  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asp Leu Leu Gly Thr Val Glu Glu Ile Leu Pro Ser Leu Ser Glu Asn  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Ile Ser Val Trp Gly Met Lys Asp Ser Val Pro Gln Gly Val Ile Ser  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Leu Lys Glu Lys Leu Ser Thr Ser Pro Asp Glu Pro Val Pro Arg Ser  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 His His Val Val Ser Leu Leu Lys Ser Thr Cys Leu Tyr Ile Phe Thr  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala Val Ile Ser Gln Leu Gln  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Val Leu Arg Gly Ser Ala Val Leu Trp Ala Phe Gly Cys Thr Ala His  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Asp Ile Val Tyr Ile Thr Leu Pro Leu Tyr His Ser Ser Ala Ala Ile  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Leu Gly Ile Ser Gly Cys Val Glu Leu Gly Ala Thr Cys Val Leu Lys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Lys Lys Phe Ser Ala Ser Gln Phe Trp Ser Asp Cys Lys Lys Tyr Asp  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Val Thr Val Phe Gln Tyr Ile Gly Glu Leu Cys Arg Tyr Leu Cys Lys  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Gln Ser Lys Arg Glu Gly Glu Lys Asp His Lys Val Arg Leu Ala Ile  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Gly Asn Gly Ile Arg Ser Asp Val Trp Arg Glu Phe Leu Asp Arg Phe  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Gly Asn Ile Lys Val Cys Glu Leu Tyr Ala Ala Thr Glu Ser Ser Ile  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ser Phe Met Asn Tyr Thr Gly Arg Ile Gly Ala Ile Gly Arg Thr Asn  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Leu Phe Tyr Lys Leu Leu Ser Thr Phe Asp Leu Ile Lys Tyr Asp Phe  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gln Lys Asp Glu Pro Met Arg Asn Glu Gln Gly Trp Cys Ile His Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Lys Lys Gly Glu Pro Gly Leu Leu Ile Ser Arg Val Asn Ala Lys Asn  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Pro Phe Phe Gly Tyr Ala Gly Pro Tyr Lys His Thr Lys Asp Lys Leu  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Cys Asp Val Phe Lys Lys Gly Asp Val Tyr Leu Asn Thr Gly Asp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Leu Ile Val Gln Asp Gln Asp Asn Phe Leu Tyr Phe Trp Asp Arg Thr  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala Thr Thr Glu Val  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Ala Asp Val Ile Gly Met Leu Asp Phe Ile Gln Glu Ala Asn Val Tyr  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Gly Val Ala Ile Ser Gly Tyr Glu Gly Arg Ala Gly Met Ala Ser Ile  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ile Leu Lys Pro Asn Thr Ser Leu Asp Leu Glu Lys Val Tyr Glu Gln  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Val Val Thr Phe Leu Pro Ala Tyr Ala Cys Pro Arg Phe Leu Arg Ile  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Gln Glu Lys Met Glu Ala Thr Gly Thr Phe Lys Leu Leu Lys His Gln  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu Val Glu Asp Gly Phe Asn Pro Leu Lys Ile Ser Glu Pro Leu Tyr  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Phe Met Asp Asn Leu Lys Lys Ser Tyr Val Leu Leu Thr Arg Glu Leu  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Tyr Asp Gln Ile Met Leu Gly Glu Ile Lys Leu  
               
               
                     610                 615  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 38  
               
               
                 &lt;211&gt; LENGTH: 646  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 38  
               
               
                   
               
               
                 Met Arg Ala Pro Gly Ala Gly Ala Ala Ser Val Val Ser Leu Ala Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Trp Leu Leu Gly Leu Pro Trp Thr Trp Ser Ala Ala Ala Ala Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Val Tyr Val Gly Ser Gly Gly Trp Arg Phe Leu Arg Ile Val Cys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Thr Ala Arg Arg Asp Leu Phe Gly Leu Ser Val Leu Ile Arg Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Arg Leu Glu Leu Arg Arg His Gln Arg Ala Gly His Thr Ile Pro Arg  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ile Phe Gln Ala Val Val Gln Arg Gln Pro Glu Arg Leu Ala Leu Val  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Ala Gly Thr Gly Glu Cys Trp Thr Phe Ala Gln Leu Asp Ala Tyr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Asn Ala Val Ala Asn Leu Phe Arg Gln Leu Gly Phe Ala Pro Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asp Val Val Ala Ile Phe Leu Glu Gly Arg Pro Glu Phe Val Gly Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Trp Leu Gly Leu Ala Lys Ala Gly Met Glu Ala Ala Leu Leu Asn Val  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asn Leu Arg Arg Glu Pro Leu Ala Phe Cys Leu Gly Thr Ser Gly Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Lys Ala Leu Ile Phe Gly Gly Glu Met Val Ala Ala Val Ala Glu Val  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Gly His Leu Gly Lys Ser Leu Ile Lys Phe Cys Ser Gly Asp Leu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Pro Glu Gly Ile Leu Pro Asp Thr His Leu Leu Asp Pro Leu Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Lys Glu Ala Ser Thr Ala Pro Leu Ala Gln Ile Pro Ser Lys Gly Met  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asp Asp Arg Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ala Phe  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly His His Ala Tyr Arg Met Gln Ala Ala Asp Val Leu Tyr Asp Cys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Leu Pro Leu Tyr His Ser Ala Gly Asn Ile Ile Gly Val Gly Gln Cys  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Leu Ile Tyr Gly Leu Thr Val Val Leu Arg Lys Lys Phe Ser Ala Ser  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Arg Phe Trp Asp Asp Cys Ile Lys Tyr Asn Cys Thr Val Val Gln Tyr  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ile Gly Glu Ile Cys Arg Tyr Leu Leu Lys Gln Pro Val Arg Glu Ala  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Glu Arg Arg His Arg Val Arg Leu Ala Val Gly Asn Gly Leu Arg Pro  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ala Ile Trp Glu Glu Phe Thr Glu Arg Phe Gly Val Arg Gln Ile Gly  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Ile Ala Asn Met Asp  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Lys Val Gly Ser Cys Gly Phe Asn Ser Arg Ile Leu Pro His Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Tyr Pro Ile Arg Leu Val Lys Val Asn Glu Asp Thr Met Glu Leu Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Arg Asp Ala Gln Gly Leu Cys Ile Pro Cys Gln Ala Gly Glu Pro Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Leu Val Gly Gln Ile Asn Gln Gln Asp Pro Leu Arg Arg Phe Asp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gly Tyr Val Ser Glu Ser Ala Thr Ser Lys Lys Ile Ala His Ser Val  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Phe Ser Lys Gly Asp Ser Ala Tyr Leu Ser Gly Asp Val Leu Val Met  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Asp Glu Leu Gly Tyr Met Tyr Phe Arg Asp Arg Ser Gly Asp Thr Phe  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Arg Trp Arg Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Val Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ser Arg Leu Leu Gly Gln Thr Asp Val Ala Val Tyr Gly Val Ala Val  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Gly Val Glu Gly Lys Ala Gly Met Ala Ala Val Ala Asp Pro His  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ser Leu Leu Asp Pro Asn Ala Ile Tyr Gln Glu Leu Gln Lys Val Leu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ala Pro Tyr Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Gln Val Asp  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Thr Thr Gly Thr Phe Lys Ile Gln Lys Thr Arg Leu Gln Arg Glu Gly  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Phe Asp Pro Arg Gln Thr Ser Asp Arg Leu Phe Phe Leu Asp Leu Lys  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Gln Gly His Tyr Leu Pro Leu Asn Glu Ala Val Tyr Thr Arg Ile Cys  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Ser Gly Ala Phe Ala Leu  
               
               
                                 645  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 39  
               
               
                 &lt;211&gt; LENGTH: 632  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 39  
               
               
                   
               
               
                 Leu Phe Ser Lys Leu Val Leu Lys Leu Pro Trp Thr Gln Val Gly Phe  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ser Leu Leu Phe Leu Tyr Leu Gly Ser Gly Gly Trp Arg Phe Ile Arg  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Val Phe Ile Lys Thr Ile Arg Arg Asp Ile Phe Gly Gly Leu Val Leu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Leu Lys Val Lys Ala Lys Val Arg Gln Cys Leu Gln Glu Arg Arg Thr  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Val Pro Ile Leu Phe Ala Ser Thr Val Arg Arg His Pro Asp Lys Thr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Leu Ile Phe Glu Gly Thr Asp Thr His Trp Thr Phe Arg Gln Leu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Glu Tyr Ser Ser Ser Val Ala Asn Phe Leu Gln Ala Arg Gly Leu  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ala Ser Gly Asp Val Ala Ala Ile Phe Met Glu Asn Arg Asn Glu Phe  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Val Gly Leu Trp Leu Gly Met Ala Lys Leu Gly Val Glu Ala Ala Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ile Asn Thr Asn Leu Arg Arg Asp Ala Leu Leu His Cys Leu Thr Thr  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Ser Arg Ala Arg Ala Leu Val Phe Gly Ser Glu Met Ala Ser Ala Ile  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Cys Glu Val His Ala Ser Leu Asp Pro Ser Leu Ser Leu Phe Cys Ser  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Gly Ser Trp Glu Pro Gly Ala Val Pro Pro Ser Thr Glu His Leu Asp  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Pro Leu Leu Lys Asp Ala Pro Lys His Leu Pro Ser Cys Pro Asp Lys  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Gly Phe Thr Asp Lys Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Leu Pro Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Ala Leu Val Tyr Tyr Gly Phe Arg Met Arg Pro Asn Asp Ile Val Tyr  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Asp Cys Leu Pro Leu Tyr His Ser Ala Gly Asn Ile Val Gly Ile Gly  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Gln Cys Leu Leu His Gly Met Thr Val Val Ile Arg Lys Lys Phe Ser  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ala Ser Arg Phe Trp Asp Asp Cys Ile Lys Tyr Asn Cys Thr Ile Val  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Gln Tyr Ile Gly Glu Leu Cys Arg Tyr Leu Leu Asn Gln Pro Pro Arg  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Glu Ala Glu Asn Gln His Gln Val Arg Met Ala Leu Gly Asn Gly Leu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Arg Gln Ser Ile Trp Thr Asn Phe Ser Ser Arg Phe His Ile Pro Gln  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Val Ala Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Leu Gly Asn  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Phe Asp Ser Gln Val Gly Ala Cys Gly Phe Asn Ser Arg Ile Leu Ser  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Phe Val Tyr Pro Ile Arg Leu Val Arg Val Asn Glu Asp Thr Met Glu  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Leu Ile Arg Gly Pro Asp Gly Val Cys Ile Pro Cys Gln Pro Gly Glu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Pro Gly Gln Leu Val Gly Arg Ile Ile Gln Lys Asp Pro Leu Arg Arg  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Phe Asp Gly Tyr Leu Asn Gln Gly Ala Asn Asn Lys Lys Ile Ala Lys  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Asp Val Phe Lys Lys Gly Asp Gln Ala Tyr Leu Thr Gly Asp Val Leu  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Val Met Asp Glu Leu Gly Tyr Leu Tyr Phe Arg Asp Arg Thr Gly Asp  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Thr Phe Arg Trp Lys Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Thr Leu Ser Arg Leu Leu Asp Met Ala Asp Val Ala Val Tyr Gly Val  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Glu Val Pro Gly Thr Glu Gly Arg Ala Gly Met Ala Ala Val Ala Ser  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Thr Gly Asn Cys Asp Leu Glu Arg Phe Ala Gln Val Leu Glu Lys  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Glu Leu Pro Leu Tyr Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Glu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu His Lys Thr Gly Thr Tyr Lys Phe Gln Lys Thr Glu Leu Arg Lys  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Glu Gly Phe Asp Pro Ala Ile Val Lys Asp Pro Leu Phe Tyr Leu Asp  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ala Gln Lys Gly Arg Tyr Val Pro Leu Asp Gln Glu Ala Tyr Ser Arg  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Ile Gln Ala Gly Glu Glu Lys Leu  
               
               
                 625                 630  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 40  
               
               
                 &lt;211&gt; LENGTH: 619  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 40  
               
               
                   
               
               
                 Met Leu Leu Ser Trp Leu Thr Val Leu Gly Ala Gly Met Val Val Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 His Phe Leu Gln Lys Leu Leu Phe Pro Tyr Phe Trp Asp Asp Phe Trp  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Val Leu Lys Val Val Leu Ile Ile Ile Arg Leu Lys Lys Tyr Glu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Arg Gly Glu Leu Val Thr Val Leu Asp Lys Phe Leu Ser His Ala  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Lys Arg Gln Pro Arg Lys Pro Phe Ile Ile Tyr Glu Gly Asp Ile Tyr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Thr Tyr Gln Asp Val Asp Lys Arg Ser Ser Arg Val Ala His Val Phe  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Leu Asn His Ser Ser Leu Lys Lys Gly Asp Thr Val Ala Leu Leu Met  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Asn Glu Pro Asp Phe Val His Val Trp Phe Gly Leu Ala Lys Leu  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Gly Cys Val Val Ala Phe Leu Asn Thr Asn Ile Arg Ser Asn Ser Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Leu Asn Cys Ile Arg Ala Cys Gly Pro Arg Ala Leu Val Val Gly Ala  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asp Leu Leu Gly Thr Val Glu Glu Ile Leu Pro Ser Leu Ser Glu Asn  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Ile Ser Val Trp Gly Met Lys Asp Ser Val Pro Gln Gly Val Ile Ser  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Leu Lys Glu Lys Leu Ser Thr Ser Pro Asp Glu Pro Val Pro Arg Ser  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 His His Val Val Ser Leu Leu Lys Ser Thr Cys Leu Tyr Ile Phe Thr  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala Val Ile Ser Gln Leu Gln  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Val Leu Arg Gly Ser Ala Val Leu Trp Ala Phe Gly Cys Thr Ala His  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Asp Ile Val Tyr Ile Thr Leu Pro Leu Tyr His Ser Ser Ala Ala Ile  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Leu Gly Ile Ser Gly Cys Val Glu Leu Gly Ala Thr Cys Val Leu Lys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Lys Lys Phe Ser Ala Ser Gln Phe Trp Ser Asp Cys Lys Lys Tyr Asp  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Val Thr Val Phe Gln Tyr Ile Gly Glu Leu Cys Arg Tyr Leu Cys Lys  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Gln Ser Lys Arg Glu Gly Glu Lys Asp His Lys Val Arg Leu Ala Ile  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Gly Asn Gly Ile Arg Ser Asp Val Trp Arg Glu Phe Leu Asp Arg Phe  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Gly Asn Ile Lys Val Cys Glu Leu Tyr Ala Ala Thr Glu Ser Ser Ile  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ser Phe Met Asn Tyr Thr Gly Arg Ile Gly Ala Ile Gly Arg Thr Asn  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Leu Phe Tyr Lys Leu Leu Ser Thr Phe Asp Leu Ile Lys Tyr Asp Phe  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gln Lys Asp Glu Pro Met Arg Asn Glu Gln Gly Trp Cys Ile His Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Lys Lys Gly Glu Pro Gly Leu Leu Ile Ser Arg Val Asn Ala Lys Asn  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Pro Phe Phe Gly Tyr Ala Gly Pro Tyr Lys His Thr Lys Asp Lys Leu  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Cys Asp Val Phe Lys Lys Gly Asp Val Tyr Leu Asn Thr Gly Asp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Leu Ile Val Gln Asp Gln Asp Asn Phe Leu Tyr Phe Trp Asp Arg Thr  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala Thr Thr Glu Val  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Ala Asp Val Ile Gly Met Leu Asp Phe Ile Gln Glu Ala Asn Val Tyr  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Gly Val Ala Ile Ser Gly Tyr Glu Gly Arg Ala Gly Met Ala Ser Ile  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ile Leu Lys Pro Asn Thr Ser Leu Asp Leu Glu Lys Val Tyr Glu Gln  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Val Val Thr Phe Leu Pro Ala Tyr Ala Cys Pro Arg Phe Leu Arg Ile  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Gln Glu Lys Met Glu Ala Thr Gly Thr Phe Lys Leu Leu Lys His Gln  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu Val Glu Asp Gly Phe Asn Pro Leu Lys Ile Ser Glu Pro Leu Tyr  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Phe Met Asp Asn Leu Lys Lys Ser Tyr Val Leu Leu Thr Arg Glu Leu  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Tyr Asp Gln Ile Met Leu Gly Glu Ile Lys Leu  
               
               
                     610                 615  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 41  
               
               
                 &lt;211&gt; LENGTH: 643  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 41  
               
               
                   
               
               
                 Met Leu Leu Gly Ala Ser Leu Val Gly Val Leu Leu Phe Ser Lys Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val Leu Lys Leu Pro Trp Thr Gln Val Gly Phe Ser Leu Leu Phe Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Tyr Leu Gly Ser Gly Gly Trp Arg Phe Ile Arg Val Phe Ile Lys Thr  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ile Arg Arg Asp Ile Phe Gly Gly Leu Val Leu Leu Lys Val Lys Ala  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Lys Val Arg Gln Cys Leu Gln Glu Arg Arg Thr Val Pro Ile Leu Phe  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Ser Thr Val Arg Arg His Pro Asp Lys Thr Ala Leu Ile Phe Glu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Thr Asp Thr His Trp Thr Phe Arg Gln Leu Asp Glu Tyr Ser Ser  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Val Ala Asn Phe Leu Gln Ala Arg Gly Leu Ala Ser Gly Asp Val  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Ala Ala Ile Phe Met Glu Asn Arg Asn Glu Phe Val Gly Leu Trp Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Gly Met Ala Lys Leu Gly Val Glu Ala Ala Leu Ile Asn Thr Asn Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Arg Arg Asp Ala Leu Leu His Cys Leu Thr Thr Ser Arg Ala Arg Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Leu Val Phe Gly Ser Glu Met Ala Ser Ala Ile Cys Glu Val His Ala  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Leu Asp Pro Ser Leu Ser Leu Phe Cys Ser Gly Ser Trp Glu Pro  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Ala Val Pro Pro Ser Thr Glu His Leu Asp Pro Leu Leu Lys Asp  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Pro Lys His Leu Pro Ser Cys Pro Asp Lys Gly Phe Thr Asp Lys  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ala Leu Val Tyr Tyr  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly Phe Arg Met Arg Pro Asn Asp Ile Val Tyr Asp Cys Leu Pro Leu  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Tyr His Ser Ala Gly Asn Ile Val Gly Ile Gly Gln Cys Leu Leu His  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Gly Met Thr Val Val Ile Arg Lys Lys Phe Ser Ala Ser Arg Phe Trp  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Asp Asp Cys Ile Lys Tyr Asn Cys Thr Ile Val Gln Tyr Ile Gly Glu  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Leu Cys Arg Tyr Leu Leu Asn Gln Pro Pro Arg Glu Ala Glu Asn Gln  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 His Gln Val Arg Met Ala Leu Gly Asn Gly Leu Arg Gln Ser Ile Trp  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Thr Asn Phe Ser Ser Arg Phe His Ile Pro Gln Val Ala Glu Phe Tyr  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gly Ala Thr Glu Cys Asn Cys Ser Leu Gly Asn Phe Asp Ser Gln Val  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Ala Cys Gly Phe Asn Ser Arg Ile Leu Ser Phe Val Tyr Pro Ile  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Arg Leu Val Arg Val Asn Glu Asp Thr Met Glu Leu Ile Arg Gly Pro  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Asp Gly Val Cys Ile Pro Cys Gln Pro Gly Glu Pro Gly Gln Leu Val  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Gly Arg Ile Ile Gln Lys Asp Pro Leu Arg Arg Phe Asp Gly Tyr Leu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Asn Gln Gly Ala Asn Asn Lys Lys Ile Ala Lys Asp Val Phe Lys Lys  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Gly Asp Gln Ala Tyr Leu Thr Gly Asp Val Leu Val Met Asp Glu Leu  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Gly Tyr Leu Tyr Phe Arg Asp Arg Thr Gly Asp Thr Phe Arg Trp Lys  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Thr Leu Ser Arg Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Leu Asp Met Ala Asp Val Ala Val Tyr Gly Val Glu Val Pro Gly Thr  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Glu Gly Arg Ala Gly Met Ala Ala Val Ala Ser Pro Thr Gly Asn Cys  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Asp Leu Glu Arg Phe Ala Gln Val Leu Glu Lys Glu Leu Pro Leu Tyr  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Glu Leu His Lys Thr Gly  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Thr Tyr Lys Phe Gln Lys Thr Glu Leu Arg Lys Glu Gly Phe Asp Pro  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ala Ile Val Lys Asp Pro Leu Phe Tyr Leu Asp Ala Gln Lys Gly Arg  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Tyr Val Pro Leu Asp Gln Glu Ala Tyr Ser Arg Ile Gln Ala Gly Glu  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Glu Lys Leu  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 42  
               
               
                 &lt;211&gt; LENGTH: 643  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: (1)...(643)  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 31, 144  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 42  
               
               
                   
               
               
                 Met Leu Leu Gly Ala Ser Leu Val Gly Val Leu Leu Phe Ser Lys Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val Leu Lys Leu Pro Trp Thr Gln Val Gly Phe Ser Leu Leu Xaa Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Tyr Leu Gly Ser Gly Gly Trp Arg Phe Ile Arg Val Phe Ile Lys Thr  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Val Arg Arg Asp Ile Phe Gly Gly Met Val Leu Leu Lys Val Lys Thr  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Lys Val Arg Arg Tyr Leu Gln Glu Arg Lys Thr Val Pro Leu Leu Phe  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Ser Met Val Gln Arg His Pro Asp Lys Thr Ala Leu Ile Phe Glu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Thr Asp Thr His Trp Thr Phe Arg Gln Leu Asp Glu Tyr Ser Ser  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Val Ala Asn Phe Leu Gln Ala Arg Gly Leu Ala Ser Gly Asn Val  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Val Ala Leu Phe Met Glu Asn Arg Asn Glu Phe Val Gly Leu Trp Xaa  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Gly Met Ala Lys Leu Gly Val Glu Ala Ala Leu Ile Asn Thr Asn Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Arg Arg Asp Ala Leu Arg His Cys Leu Asp Thr Ser Lys Ala Arg Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Leu Ile Phe Gly Ser Glu Met Ala Ser Ala Ile Cys Glu Ile His Ala  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Leu Gly Pro Thr Leu Ser Leu Phe Cys Ser Gly Ser Trp Glu Pro  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Ser Thr Val Pro Val Ser Thr Glu His Leu Asp Pro Leu Leu Glu Asp  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Pro Lys His Leu Pro Ser His Pro Asp Lys Gly Phe Thr Asp Lys  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ser Leu Val Tyr Tyr  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly Phe Arg Met Arg Pro Asp Asp Ile Val Tyr Asp Cys Leu Pro Leu  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Tyr His Ser Ser Arg Lys His Arg Gly Asp Trp Gln Cys Leu Leu His  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Gly Met Thr Val Val Ile Arg Lys Lys Phe Ser Ala Ser Arg Phe Trp  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Asp Asp Cys Ile Lys Tyr Asn Cys Thr Ile Val Gln Tyr Ile Gly Glu  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Leu Cys Arg Tyr Leu Leu Asn Gln Pro Pro Arg Glu Ala Glu Ser Arg  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 His Lys Val Arg Met Ala Leu Gly Asn Gly Leu Arg Gln Ser Ile Trp  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Thr Asp Phe Ser Ser Arg Phe His Ile Pro Gln Val Ala Glu Phe Tyr  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gly Ala Thr Glu Cys Asn Cys Ser Leu Gly Asn Phe Asp Ser Arg Val  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Ala Cys Gly Phe Asn Ser Arg Ile Leu Ser Phe Val Tyr Pro Ile  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Arg Leu Val Arg Val Asn Glu Asp Thr Met Glu Leu Ile Arg Gly Pro  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Asp Gly Val Cys Ile Pro Cys Gln Pro Gly Gln Pro Gly Gln Leu Val  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Gly Arg Ile Ile Gln Lys Asp Pro Leu Arg Arg Phe Asp Gly Tyr Leu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Asn Gln Gly Ala Asn Asn Lys Lys Ile Ala Asn Asp Val Phe Lys Lys  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Gly Asp Gln Ala Tyr Leu Thr Gly Asp Val Leu Val Met Asp Glu Leu  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Gly Tyr Leu Tyr Phe Arg Asp Arg Thr Gly Asp Thr Phe Arg Trp Lys  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Thr Leu Ser Arg Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Leu His Met Ala Asp Val Ala Val Tyr Gly Val Glu Val Pro Gly Thr  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Glu Gly Arg Ala Gly Met Ala Ala Val Ala Ser Pro Ile Ser Asn Cys  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Asp Leu Glu Ser Phe Ala Gln Thr Leu Lys Lys Glu Leu Pro Leu Tyr  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ala Arg Pro Ile Phe Leu Arg Phe Leu Pro Glu Leu His Lys Thr Gly  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Thr Phe Lys Phe Gln Lys Thr Glu Leu Arg Lys Glu Gly Phe Asp Pro  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ser Val Val Lys Asp Pro Leu Phe Tyr Leu Asp Ala Arg Lys Gly Cys  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Tyr Val Ala Leu Asp Gln Glu Ala Tyr Thr Arg Ile Gln Ala Gly Glu  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Glu Lys Leu  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 43  
               
               
                 &lt;211&gt; LENGTH: 630  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 43  
               
               
                   
               
               
                 Met Arg Ala Pro Gly Ala Gly Ala Ala Ser Val Val Ser Leu Ala Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Trp Leu Leu Gly Leu Pro Trp Thr Trp Ser Ala Ala Ala Ala Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Val Tyr Val Gly Ser Gly Gly Trp Arg Phe Leu Arg Ile Val Cys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Thr Ala Arg Arg Asp Leu Phe Gly Leu Ser Val Leu Ile Arg Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Arg Leu Glu Leu Arg Arg His Gln Arg Ala Gly His Thr Ile Pro Arg  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ile Phe Gln Ala Val Val Gln Arg Gln Pro Glu Arg Leu Ala Leu Val  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Ala Gly Thr Gly Glu Cys Trp Thr Phe Ala Gln Leu Asp Ala Tyr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Asn Ala Val Ala Asn Leu Phe Arg Gln Leu Gly Phe Ala Pro Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asp Val Val Ala Ile Phe Leu Glu Gly Arg Pro Glu Phe Val Gly Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Trp Leu Gly Leu Ala Lys Ala Gly Met Glu Ala Ala Leu Leu Asn Val  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asn Leu Arg Arg Glu Pro Leu Ala Phe Cys Leu Gly Thr Ser Gly Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Ser Gly His Leu Gly Lys Ser Leu Ile Lys Phe Cys Ser Gly Asp Leu  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Gly Pro Glu Gly Ile Leu Pro Asp Thr His Leu Leu Asp Pro Leu Leu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Lys Glu Ala Ser Thr Ala Pro Leu Ala Gln Ile Pro Ser Lys Gly Met  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Asp Asp Arg Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ala Phe  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Gly His His Ala Tyr Arg Met Gln Ala Ala Asp Val Leu Tyr Asp Cys  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Leu Pro Leu Tyr His Ser Ala Gly Asn Ile Ile Gly Val Gly Gln Cys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Leu Ile Tyr Gly Leu Thr Val Val Leu Arg Lys Lys Phe Ser Ala Ser  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Arg Phe Trp Asp Asp Cys Ile Lys Tyr Asn Cys Thr Val Val Gln Tyr  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Ile Gly Glu Ile Cys Arg Tyr Leu Leu Lys Gln Pro Val Arg Glu Ala  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Glu Arg Arg His Arg Val Arg Leu Ala Val Gly Asn Gly Leu Arg Pro  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Ala Ile Trp Glu Glu Phe Thr Glu Arg Phe Gly Val Arg Gln Ile Gly  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Ile Ala Asn Met Asp  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gly Lys Val Gly Ser Cys Gly Phe Asn Ser Arg Ile Leu Pro His Val  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Tyr Pro Ile Arg Leu Val Lys Val Asn Glu Asp Thr Met Glu Leu Leu  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Arg Asp Ala Gln Gly Leu Cys Ile Pro Cys Gln Ala Gly Glu Pro Gly  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Leu Leu Val Gly Gln Ile Asn Gln Gln Asp Pro Leu Arg Arg Phe Asp  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Gly Tyr Val Ser Glu Ser Ala Thr Ser Lys Lys Ile Ala His Ser Val  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Phe Ser Lys Gly Asp Ser Ala Tyr Leu Ser Gly Asp Val Leu Val Met  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Asp Glu Leu Gly Tyr Met Tyr Phe Arg Asp Arg Ser Gly Asp Thr Phe  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Arg Trp Arg Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Val Leu  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Ser Arg Leu Leu Gly Gln Thr Asp Val Ala Val Tyr Gly Val Ala Val  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Pro Gly Val Glu Gly Lys Ala Gly Met Ala Ala Val Ala Asp Pro His  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Ser Leu Leu Asp Pro Asn Ala Ile Tyr Gln Glu Leu Gln Lys Val Leu  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ala Pro Tyr Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Gln Val Asp  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Thr Thr Gly Thr Phe Lys Ile Gln Lys Thr Arg Leu Gln Arg Glu Gly  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Phe Asp Pro Arg Gln Thr Ser Asp Arg Leu Phe Phe Leu Asp Leu Lys  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Gln Gly His Tyr Leu Pro Leu Asn Glu Ala Val Tyr Thr Arg Ile Cys  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Ser Gly Ala Phe Ala Leu  
               
               
                 625                 630  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 44  
               
               
                 &lt;211&gt; LENGTH: 2710  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 44  
               
               
                   
               
               
                 atgctgcttg gagcctctct ggtgggggcg ctacttgggt ccaagctagt gctgaagctg     60  
               
               
                   
               
               
                 ccctggaccc aggtgggatt ctccctgttg ctcctgtact tggggtctgg tggctggcgt    120  
               
               
                   
               
               
                 ttcatccggg tcttcatcaa gacggtcagg agagatatct ttggtggcat ggtgctcctg    180  
               
               
                   
               
               
                 aaggtgaaga ccaaggtgcg acggtacctt caggagcgga agacggtgcc cctgctgttt    240  
               
               
                   
               
               
                 gcttcaatgg tacagcgcca cccggacaag acagccctga ttttcgaggg cacagacact    300  
               
               
                   
               
               
                 cactggacct tccgccagct ggatgagtac tccagtagtg tggccaactt cctgcaggcc    360  
               
               
                   
               
               
                 cggggcctgg cctcaggcaa tgtagttgcc ctctttatgg aaaaccgcaa tgagtttgtg    420  
               
               
                   
               
               
                 ggtctgtggc taggcatggc caagctgggc gtggaggcgg ctctcatcaa caccaacctt    480  
               
               
                   
               
               
                 aggcgggatg ccctgcgcca ctgtcttgac acctcaaagg cacgagctct catctttggc    540  
               
               
                   
               
               
                 agtgagatgg cctcagctat ctgtgagatc catgctagcc tggagcccac actcagcctc    600  
               
               
                   
               
               
                 ttctgctctg gatcctggga gcccagcaca gtgcccgtca gcacagagca tctggaccct    660  
               
               
                   
               
               
                 cttctggaag atgccccgaa gcacctgccc agtcacccag acaagggttt tacagataag    720  
               
               
                   
               
               
                 ctcttctaca tctacacatc gggcaccacg gggctaccca aagctgccat tgtggtgcac    780  
               
               
                   
               
               
                 agcaggtatt atcgtatggc ttccctggtg tactatggat tccgcatgcg gcctgatgac    840  
               
               
                   
               
               
                 attgtctatg actgcctccc cctctaccac tcaagcagga aacatcgtgg ggattggcag    900  
               
               
                   
               
               
                 tgcttactcc acggcatgac tgtggtgatc cggaagaagt tctcagcctc ccggttctgg    960  
               
               
                   
               
               
                 gatgattgta tcaagtacaa ctgcacagtg gtacagtaca ttggcgagct ctgccgctac   1020  
               
               
                   
               
               
                 ctcctgaacc agccaccccg tgaggctgag tctcggcaca aggtgcgcat ggcactgggc   1080  
               
               
                   
               
               
                 aacggtctcc ggcagtccat ctggaccgac ttctccagcc gtttccacat cccccaggtg   1140  
               
               
                   
               
               
                 gctgagttct atggggccac tgaatgcaac tgtagcctgg gcaactttga cagccgggtg   1200  
               
               
                   
               
               
                 ggggcctgtg gcttcaatag ccgcatcctg tcctttgtgt accctatccg tttggtacgt   1260  
               
               
                   
               
               
                 gtcaatgagg ataccatgga actgatccgg ggacccgatg gagtctgcat tccctgtcaa   1320  
               
               
                   
               
               
                 ccaggtcagc caggccagct ggtgggtcgc atcatccagc aggaccctct gcgccgtttc   1380  
               
               
                   
               
               
                 gacgggtacc tcaaccaggg tgccaacaac aagaagattg ctaatgatgt cttcaagaag   1440  
               
               
                   
               
               
                 ggggaccaag cctacctcac tggtgacgtc ctggtgatgg atgagctggg ttacctgtac   1500  
               
               
                   
               
               
                 ttccgagatc gcactgggga cacgttccgc tggaaagggg agaatgtatc taccactgag   1560  
               
               
                   
               
               
                 gtggagggca cactcagccg cctgcttcat atggcagatg tggcagttta tggtgttgag   1620  
               
               
                   
               
               
                 gtgccaggaa ctgaaggccg agcaggaatg gctgccgttg caagtcccat cagcaactgt   1680  
               
               
                   
               
               
                 gacctggaga gctttgcaca gaccttgaaa aaggagctgc ctctgtatgc ccgccccatc   1740  
               
               
                   
               
               
                 ttcctgcgct tcttgcctga gctgcacaag acagggacct tcaagttcca gaagacagag   1800  
               
               
                   
               
               
                 ttgcggaagg agggctttga cccatctgtt gtgaaagacc cgctgttcta tctggatgct   1860  
               
               
                   
               
               
                 cggaagggct gctacgttgc actggaccag gaggcctata cccgcatcca ggcaggcgag   1920  
               
               
                   
               
               
                 gagaagctgt gatttccccc tacatccctc tgagggccag aagatgctgg attcagagcc   1980  
               
               
                   
               
               
                 ctagcgtcca ccccagaggg tcctgggcaa tgccagacca aagctagcag ggcccgcacc   2040  
               
               
                   
               
               
                 tccgccccta ggtgctgatc tcccctctcc caaactgcca agtgactcac tgccgcttcc   2100  
               
               
                   
               
               
                 ccgaccctcc agaggctttc tgtgaaagtc tcatccaagc tgtgtcttct ggtccaggcg   2160  
               
               
                   
               
               
                 tggcccctgg ccccagggtt tctgataggc tcctttagga tggtatcttg ggtccagcgg   2220  
               
               
                   
               
               
                 gccagggtgt gggagaggag tcactaagat ccctccaatc agaagggagc ttacaaagga   2280  
               
               
                   
               
               
                 accaaggcaa agcctgtaga ctcaggaagc taagtggcca gagactatag tggccagtca   2340  
               
               
                   
               
               
                 tcccatgtcc acagaggatc ttggtccaga gctgccaaag tgtcacctct ccctgcctgc   2400  
               
               
                   
               
               
                 acctctgggg aaaagaggac agcatgtggc cactgggcac ctgtctcaag aagtcaggat   2460  
               
               
                   
               
               
                 cacacactca gtccttgttt ctccaggttc ccttgttctt gtctcgggga gggagggacg   2520  
               
               
                   
               
               
                 agtgtcctgt ctgtccttcc tgcctgtctg tgagtctgtg ttgcttctcc atctgtccta   2580  
               
               
                   
               
               
                 gcctgagtgt gggtggaaca ggcatgagga gagtgtggct caggggccaa taaactctgc   2640  
               
               
                   
               
               
                 cttgactcct cttaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa   2700  
               
               
                   
               
               
                 aaaaaaaaaa                                                          2710  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 45  
               
               
                 &lt;211&gt; LENGTH: 627  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 45  
               
               
                   
               
               
                 Met Leu Leu Gly Ala Ser Leu Val Gly Ala Leu Leu Phe Ser Lys Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val Leu Lys Leu Pro Trp Thr Gln Val Gly Phe Ser Leu Leu Leu Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Tyr Leu Gly Ser Gly Gly Trp Arg Phe Ile Arg Val Phe Ile Lys Thr  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Val Arg Arg Asp Ile Phe Gly Gly Met Val Leu Leu Lys Val Lys Thr  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Lys Val Arg Arg Tyr Leu Gln Glu Arg Lys Thr Val Pro Leu Leu Phe  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Ser Met Val Gln Arg His Pro Asp Lys Thr Ala Leu Ile Phe Glu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Thr Asp Thr His Trp Thr Phe Arg Gln Leu Asp Glu Tyr Ser Ser  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Val Ala Asn Phe Leu Gln Ala Arg Gly Leu Ala Ser Gly Asn Val  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Val Ala Leu Phe Met Glu Asn Arg Asn Glu Phe Val Gly Leu Trp Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Gly Met Ala Lys Leu Gly Val Glu Ala Ala Leu Ile Asn Thr Asn Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Arg Arg Asp Ala Leu Arg His Cys Leu Asp Thr Ser Lys Ala Arg Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Leu Ile Phe Gly Ser Glu Met Ala Ser Ala Ile Cys Glu Ile His Ala  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Leu Glu Pro Thr Leu Ser Leu Phe Cys Ser Gly Ser Trp Glu Pro  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Ser Thr Val Pro Val Ser Thr Glu His Leu Asp Pro Leu Leu Glu Asp  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ser Leu Val Tyr Tyr  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Gly Phe Arg Met Arg Pro Asp Asp Ile Val Tyr Asp Cys Leu Pro Leu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Tyr His Ser Ser Arg Lys His Arg Gly Asp Trp Gln Cys Leu Leu His  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Gly Met Thr Val Val Ile Arg Lys Lys Phe Ser Ala Ser Arg Phe Trp  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Asp Asp Cys Ile Lys Tyr Asn Cys Thr Val Val Gln Tyr Ile Gly Glu  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Leu Cys Arg Tyr Leu Leu Asn Gln Pro Pro Arg Glu Ala Glu Ser Arg  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 His Lys Val Arg Met Ala Leu Gly Asn Gly Leu Arg Gln Ser Ile Trp  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Thr Asp Phe Ser Ser Arg Phe His Ile Pro Gln Val Ala Glu Phe Tyr  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Gly Ala Thr Glu Cys Asn Cys Ser Leu Gly Asn Phe Asp Ser Arg Val  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gly Ala Cys Gly Phe Asn Ser Arg Ile Leu Ser Phe Val Tyr Pro Ile  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Arg Leu Val Arg Val Asn Glu Asp Thr Met Glu Leu Ile Arg Gly Pro  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Asp Gly Val Cys Ile Pro Cys Gln Pro Gly Gln Pro Gly Gln Leu Val  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Gly Arg Ile Ile Gln Gln Asp Pro Leu Arg Arg Phe Asp Gly Tyr Leu  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Asn Gln Gly Ala Asn Asn Lys Lys Ile Ala Asn Asp Val Phe Lys Lys  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gly Asp Gln Ala Tyr Leu Thr Gly Asp Val Leu Val Met Asp Glu Leu  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Gly Tyr Leu Tyr Phe Arg Asp Arg Thr Gly Asp Thr Phe Arg Trp Lys  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Thr Leu Ser Arg Leu  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Leu His Met Ala Asp Val Ala Val Tyr Gly Val Glu Val Pro Gly Thr  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Glu Gly Arg Ala Gly Met Ala Ala Val Ala Ser Pro Ile Ser Asn Cys  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Asp Leu Glu Ser Phe Ala Gln Thr Leu Lys Lys Glu Leu Pro Leu Tyr  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ala Arg Pro Ile Phe Leu Arg Phe Leu Pro Glu Leu His Lys Thr Gly  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Thr Phe Lys Phe Gln Lys Thr Glu Leu Arg Lys Glu Gly Phe Asp Pro  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Ser Val Val Lys Asp Pro Leu Phe Tyr Leu Asp Ala Arg Lys Gly Cys  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Tyr Val Ala Leu Asp Gln Glu Ala Tyr Thr Arg Ile Gln Ala Gly Glu  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Glu Lys Leu  
               
               
                 625  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 46  
               
               
                 &lt;211&gt; LENGTH: 3694  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 46  
               
               
                   
               
               
                 tcgacccacg gcgtccggga ccccaaagca gaagcccgca cagtaggcac agcgcaccca     60  
               
               
                   
               
               
                 agaagggtcc aggagtctgc agaaacagaa aggtccccgg cctcagcctc ctagtccctg    120  
               
               
                   
               
               
                 cctgcctcct gcctgagctt ctgggagact gaaggcacgg cttgcagctt caggatgcgg    180  
               
               
                   
               
               
                 gctccgggtg cgggcgcggc ctcggtggtc tcgctggcgc tgttgtggct gctggggctg    240  
               
               
                   
               
               
                 ccgtggacct ggagcgcggc agcggcgctc ggcgtgtacg tgggcagcgg cggctggcgc    300  
               
               
                   
               
               
                 ttcctgcgca tcgtctgcaa gaccgcgagg cgagacctct tcggtctctc tgtgctgatc    360  
               
               
                   
               
               
                 cgcgtgcgcc tggagctgcg gcggcaccag cgtgccggcc acaccatccc gcgcatcttt    420  
               
               
                   
               
               
                 caggcggtag tgcagcgaca gcccgagcgc ctggcgctgg tggatgccgg gaccggcgag    480  
               
               
                   
               
               
                 tgctggacct ttgcgcagct ggacgcctac tccaatgcgg tagccaacct cttccgccag    540  
               
               
                   
               
               
                 ctgggcttcg cgccgggcga cgtggtggcc atcttcctgg agggccggcc ggagttcgtg    600  
               
               
                   
               
               
                 gggctgtggc tgggcctggc caaggcgggc atggaggccg cgctgctcaa cgtgaacctg    660  
               
               
                   
               
               
                 cggcgcgagc ccctggcctt ctgcctgggc acctcgggcg ctaaggccct gatctttgga    720  
               
               
                   
               
               
                 ggagaaatgg tggcggcggt ggccgaagtg agcgggcatc tggggaaaag tttgatcaag    780  
               
               
                   
               
               
                 ttctgctctg gagacttggg gcccgagggc atcttgccgg acacccacct cctggacccg    840  
               
               
                   
               
               
                 ctgctgaagg aggcctctac tgcccccttg gcacagatcc ccagcaaggg catggacgat    900  
               
               
                   
               
               
                 cgtcttttct acatctacac gtcggggacc accgggctgc ccaaggctgc cattgtcgtg    960  
               
               
                   
               
               
                 cacagcaggt actaccgcat ggcagccttc ggccaccacg cctaccgcat gcaggcggct   1020  
               
               
                   
               
               
                 gacgtgctct atgactgcct gcccctgtac cactcggcag gaaacatcat cggcgtgggg   1080  
               
               
                   
               
               
                 cagtgtctca tctatgggct gacagtcgtc ctccgcaaga aattctcggc cagccgcttc   1140  
               
               
                   
               
               
                 tgggacgact gcatcaagta caactgcacg gtggttcagt acatcgggga gatctgccgc   1200  
               
               
                   
               
               
                 tacctgctga agcagccggt gcgcgaggcg gagaggcgac accgcgtgcg cctggcggtg   1260  
               
               
                   
               
               
                 gggaacgggc tgcgtcctgc catctgggag gagttcacgg agcgcttcgg cgtacgccaa   1320  
               
               
                   
               
               
                 atcggggagt tctacggcgc caccgagtgc aactgcagca ttgccaacat ggacggcaag   1380  
               
               
                   
               
               
                 gtcggctcct gtggtttcaa cagccgcatc ctgccccacg tgtaccccat ccggctggtg   1440  
               
               
                   
               
               
                 aaggtcaatg aggacacaat ggagctgctg cgggatgccc agggcctctg catcccctgc   1500  
               
               
                   
               
               
                 caggccgggg agcctggcct ccttgtgggt cagatcaacc aacaggaccc gctgcgccgc   1560  
               
               
                   
               
               
                 ttcgatggct atgtcagcga gagcgccacc agcaagaaga tcgcccacag cgtcttcagc   1620  
               
               
                   
               
               
                 aagggcgaca gcgcctacct ctcaggtgac gtgctagtga tggatgagct gggctacatg   1680  
               
               
                   
               
               
                 tacttccggg accgtagcgg ggacaccttc cgctggcgag gggagaacgt ctccaccacc   1740  
               
               
                   
               
               
                 gaggtggagg gcgtgctgag ccgcctgctg ggccagacag acgtggccgt ctatggggtg   1800  
               
               
                   
               
               
                 gctgttccag gagtggaggg taaggcaggg atggcggccg tcgcagaccc ccacagcctg   1860  
               
               
                   
               
               
                 ctggacccca acgcgatata ccaggagctg cagaaggtgc tggcacccta tgcccggccc   1920  
               
               
                   
               
               
                 atcttcctgc gcctcctgcc ccaggtggac accacaggca ccttcaagat ccagaagacg   1980  
               
               
                   
               
               
                 aggctgcagc gagagggctt tgacccacgc cagacctcag accggctctt cttcctggac   2040  
               
               
                   
               
               
                 ctgaagcagg gccactacct gcccttaaat gaggcagtct acactcgcat ctgctcgggc   2100  
               
               
                   
               
               
                 gccttcgccc tctgaagctg ttcctctact ggccacaaac tctgggcctg gtgggagagg   2160  
               
               
                   
               
               
                 ccagcttgag ccagacagcg ctgcccaggg gtggccgcct agtacacacc cacctggccg   2220  
               
               
                   
               
               
                 agctgtacct ggcacggccc atcctggact gagaaactgg aacctcagag gaacccgtgc   2280  
               
               
                   
               
               
                 ctctctgctg ccttggtgcc cctgtgtctg cctcctctcc ctgcttttca gcctctgtct   2340  
               
               
                   
               
               
                 ccttccatcc ctgtccctgt ctggccttaa ctcttccctc tctttctttt ctttctttct   2400  
               
               
                   
               
               
                 ttcttttttt ttaagataga gtctcactct gctgcccggg ctagagtgca gtggtgggat   2460  
               
               
                   
               
               
                 ctcggctcac tgcaacctct gcctcctggg gttcaagtga tcctcccacc tcagcctcct   2520  
               
               
                   
               
               
                 gagtagctgg gattacaggc acccgccacc acgtccagct aatttttata tttttagtag   2580  
               
               
                   
               
               
                 agacggggtt tcaccatgtt ggtcaggctg gtcttgaact cctgacctca ggtgatccgc   2640  
               
               
                   
               
               
                 tggcctcggc ctcccagagt gctgggatta taggcgtgag cctctggccc ggcctttcct   2700  
               
               
                   
               
               
                 ttttcctctc ctctcctgcc gagagtggaa cacacgtgtc ctgggagctg catcttgtgt   2760  
               
               
                   
               
               
                 agggtccagc tgcttttggg gactgcagga atcatctccc ctgggccctg gactcggact   2820  
               
               
                   
               
               
                 ggggcctccc cacctccctc tcggctgtgc cttacggagc cccaatccag gcctcctgtg   2880  
               
               
                   
               
               
                 gctgttgggt tccagatgct gcagctccat gtgacttcca agcaggccct ccgccctccc   2940  
               
               
                   
               
               
                 tgctgaatgg aggagccggg ggtcccccag gccaactgga aaatctccca ggctaggcca   3000  
               
               
                   
               
               
                 attgcctttt gcacttcccc gttcctgtca catttcccca gccccacctt cccctcctga   3060  
               
               
                   
               
               
                 tgccctgaaa gcttccggaa ttgactgtga ccacttggat gtcaccactg tcagcccctg   3120  
               
               
                   
               
               
                 ccttgatgtc cccatttagc catctccatg gagctcctgc tggagggccc tgaaccctgc   3180  
               
               
                   
               
               
                 actgcgtggc tgcccagcca gctgcctcct gtcctgggag gaggcctcct gggtgtcctc   3240  
               
               
                   
               
               
                 atctggtgtg tctactggag ggtcccacag gagaggcagc agaggggtca ggggaggtct   3300  
               
               
                   
               
               
                 cctgccgggg gttggcctct caagcctcag gggttctagc ctgttgaata taccccacct   3360  
               
               
                   
               
               
                 ggtgggtggc ccctccgatg tccccactga tggctctgac accgtgttgg tggcgatgtc   3420  
               
               
                   
               
               
                 ccagacaatc ccaccaggac ggcccagaca tccctactgg cttcgctggt ggctcatctc   3480  
               
               
                   
               
               
                 gaacatccac gccagccttt ctggggccgg ccacccaggc cgcctgtccg tctgtcctcc   3540  
               
               
                   
               
               
                 ctccagcagc accccctggc ccctggagtg gtggggccat ggcaagagac accgtggcgt   3600  
               
               
                   
               
               
                 ctcatgtgaa ctttcctggg cactgtggtt ttatttccta attgatttaa gaaataaacc   3660  
               
               
                   
               
               
                 tgaagaccgt ctggtgaaaa aaaaaaaaaa aaaa                               3694  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 47  
               
               
                 &lt;211&gt; LENGTH: 646  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 47  
               
               
                   
               
               
                 Met Arg Ala Pro Gly Ala Gly Ala Ala Ser Val Val Ser Leu Ala Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Trp Leu Leu Gly Leu Pro Trp Thr Trp Ser Ala Ala Ala Ala Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Val Tyr Val Gly Ser Gly Gly Trp Arg Phe Leu Arg Ile Val Cys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Thr Ala Arg Arg Asp Leu Phe Gly Leu Ser Val Leu Ile Arg Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Arg Leu Glu Leu Arg Arg His Gln Arg Ala Gly His Thr Ile Pro Arg  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ile Phe Gln Ala Val Val Gln Arg Gln Pro Glu Arg Leu Ala Leu Val  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Ala Gly Thr Gly Glu Cys Trp Thr Phe Ala Gln Leu Asp Ala Tyr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Asn Ala Val Ala Asn Leu Phe Arg Gln Leu Gly Phe Ala Pro Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asp Val Val Ala Ile Phe Leu Glu Gly Arg Pro Glu Phe Val Gly Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Trp Leu Gly Leu Ala Lys Ala Gly Met Glu Ala Ala Leu Leu Asn Val  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asn Leu Arg Arg Glu Pro Leu Ala Phe Cys Leu Gly Thr Ser Gly Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Lys Ala Leu Ile Phe Gly Gly Glu Met Val Ala Ala Val Ala Glu Val  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Gly His Leu Gly Lys Ser Leu Ile Lys Phe Cys Ser Gly Asp Leu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Pro Glu Gly Ile Leu Pro Asp Thr His Leu Leu Asp Pro Leu Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Lys Glu Ala Ser Thr Ala Pro Leu Ala Gln Ile Pro Ser Lys Gly Met  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asp Asp Arg Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ala Phe  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly His His Ala Tyr Arg Met Gln Ala Ala Asp Val Leu Tyr Asp Cys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Leu Pro Leu Tyr His Ser Ala Gly Asn Ile Ile Gly Val Gly Gln Cys  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Leu Ile Tyr Gly Leu Thr Val Val Leu Arg Lys Lys Phe Ser Ala Ser  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Arg Phe Trp Asp Asp Cys Ile Lys Tyr Asn Cys Thr Val Val Gln Tyr  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ile Gly Glu Ile Cys Arg Tyr Leu Leu Lys Gln Pro Val Arg Glu Ala  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Glu Arg Arg His Arg Val Arg Leu Ala Val Gly Asn Gly Leu Arg Pro  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ala Ile Trp Glu Glu Phe Thr Glu Arg Phe Gly Val Arg Gln Ile Gly  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Ile Ala Asn Met Asp  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Lys Val Gly Ser Cys Gly Phe Asn Ser Arg Ile Leu Pro His Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Tyr Pro Ile Arg Leu Val Lys Val Asn Glu Asp Thr Met Glu Leu Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Arg Asp Ala Gln Gly Leu Cys Ile Pro Cys Gln Ala Gly Glu Pro Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Leu Val Gly Gln Ile Asn Gln Gln Asp Pro Leu Arg Arg Phe Asp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gly Tyr Val Ser Glu Ser Ala Thr Ser Lys Lys Ile Ala His Ser Val  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Phe Ser Lys Gly Asp Ser Ala Tyr Leu Ser Gly Asp Val Leu Val Met  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Asp Glu Leu Gly Tyr Met Tyr Phe Arg Asp Arg Ser Gly Asp Thr Phe  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Arg Trp Arg Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Val Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ser Arg Leu Leu Gly Gln Thr Asp Val Ala Val Tyr Gly Val Ala Val  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Gly Val Glu Gly Lys Ala Gly Met Ala Ala Val Ala Asp Pro His  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ser Leu Leu Asp Pro Asn Ala Ile Tyr Gln Glu Leu Gln Lys Val Leu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ala Pro Tyr Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Gln Val Asp  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Thr Thr Gly Thr Phe Lys Ile Gln Lys Thr Arg Leu Gln Arg Glu Gly  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Phe Asp Pro Arg Gln Thr Ser Asp Arg Leu Phe Phe Leu Asp Leu Lys  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Gln Gly His Tyr Leu Pro Leu Asn Glu Ala Val Tyr Thr Arg Ile Cys  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Ser Gly Ala Phe Ala Leu  
               
               
                                 645  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 48  
               
               
                 &lt;211&gt; LENGTH: 2362  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 48  
               
               
                   
               
               
                 ggaattccaa aaaaaaaaaa tacgactaca cctgctccgg agcccgcggc ggtacctgca     60  
               
               
                   
               
               
                 gcggaggagc tctgtcttcc ccttcatctc acgcgagccc ggcgtcccgc cgcgtgcgcc    120  
               
               
                   
               
               
                 ccggcgcagc ccgccagtcc gcccggagcc cgcccagtcg ccgcgctgca cgcccggggt    180  
               
               
                   
               
               
                 gaaccctctg ccctcgctgg gacagagggc cccgcagccg tcatgctttc cgccatctac    240  
               
               
                   
               
               
                 acagtcctgg cgggactgct gttcctgccg ctcctggtga acctctgctg cccatacttc    300  
               
               
                   
               
               
                 ttccaggaca taggctactt cttgaaggtg gccgccgtgg gccggagggt gcgcagctac    360  
               
               
                   
               
               
                 gggcagcggc ggccggcgcg caccatcctg cgggcgttcc tggagaaagc gcgccagacg    420  
               
               
                   
               
               
                 ccacacaagc cttttctgct cttccgcgac gagactctca cctacgcgca ggtggaccgg    480  
               
               
                   
               
               
                 cgcagcaatc aagtggcccg ggcgctgcac gaccacctcg gcctgcgcca gggagactgc    540  
               
               
                   
               
               
                 gtggcgctcc ttatgggtaa cgagccggcc tacgtgtggc tgtggctggg gctggtgaag    600  
               
               
                   
               
               
                 ctgggctgtg ccatggcgtg cctcaattac aacatccgcg cgaagtccct gctgcactgc    660  
               
               
                   
               
               
                 ttccagtgct gcggggcgaa ggtgctgctg gtgtcgccag aactacaagc agctgtcgaa    720  
               
               
                   
               
               
                 gagatactgc caagccttaa aaaagatgat gtgtccatct attatgtgag cagaacttct    780  
               
               
                   
               
               
                 aacacagatg ggattgactc tttcctggac aaagtggatg aagtatcaac tgaacctatc    840  
               
               
                   
               
               
                 ccagagtcat ggaggtctga agtcactttt tccactcctg ccttatacat ttatacttct    900  
               
               
                   
               
               
                 ggaaccacag gtcttccaaa agcagccatg atcactcatc agcgcatatg gtatggaact    960  
               
               
                   
               
               
                 ggcctcactt ttgtaagcgg attgaaggca gatgatgtca tctatatcac tctgcccttt   1020  
               
               
                   
               
               
                 taccacagtg ctgcactact gattggcatt cacggatgta ttgtggctgg tgctactctt   1080  
               
               
                   
               
               
                 gccttgcgga ctaaattttc agccagccag ttttgggatg actgcagaaa atacaacgtc   1140  
               
               
                   
               
               
                 actgtcattc agtatatcgg tgaactgctt cggtatttat gcaactcacc acagaaacca   1200  
               
               
                   
               
               
                 aatgaccgtg atcataaagt gagactggca ctgggaaatg gcttacgagg agatgtgtgg   1260  
               
               
                   
               
               
                 agacaatttg tcaagagatt tggggacata tgcatctatg agttctatgc tgccactgaa   1320  
               
               
                   
               
               
                 ggcaatattg gatttatgaa ttatgcgaga aaagttggtg ctgttggaag agtaaactac   1380  
               
               
                   
               
               
                 ctacagaaaa aaatcataac ttatgacctg attaaatatg atgtggagaa agatgaacct   1440  
               
               
                   
               
               
                 gtccgagatg aaaatggata ttgcgtcaga gttcccaaag gtgaagttgg acttctggtt   1500  
               
               
                   
               
               
                 tgcaaaatca cacaacttac accatttaat ggctatgctg gagcaaaggc tcagacagag   1560  
               
               
                   
               
               
                 aagaaaaaac tgagagatgt ctttaagaaa ggagacctct atttcaacag tggagatctc   1620  
               
               
                   
               
               
                 ttaatggttg accatgaaaa tttcatctat ttccacgaca gagttggaga tacattccgg   1680  
               
               
                   
               
               
                 tggaaagggg aaaatgtggc caccactgaa gttgctgata cagttggact ggttgatttt   1740  
               
               
                   
               
               
                 gtccaagaag taaatgttta tggagtgcat gtgccagatc atgagggtcg cattggcatg   1800  
               
               
                   
               
               
                 gcctccatca aaatgaaaga aaaccatgaa tttgatggaa agaaactctt tcagcacatt   1860  
               
               
                   
               
               
                 gctgattacc tacctagtta tgcaaggccc cggtttctaa gaatacagga caccattgag   1920  
               
               
                   
               
               
                 atcactggaa cttttaaaca ccgcaaaatg accctggtgg aggagggctt taaccctgct   1980  
               
               
                   
               
               
                 gtcatcaaag atgccttgta tttcttggat gacacagcaa aaatgtatgt gcctatgact   2040  
               
               
                   
               
               
                 gaggacatct ataatgccat aagtgctaaa accctgaaac tctgaatatt cccaggagga   2100  
               
               
                   
               
               
                 taactcaaca tttccagaaa gaaactgaat ggacagccac ttgatataat ccaactttaa   2160  
               
               
                   
               
               
                 tttgattgaa gattgtgagg aaattttgta ggaaatttgc atacccgtaa agggagactt   2220  
               
               
                   
               
               
                 ttttaaataa cagttgagtc tttgcaagta aaaagattta gagattatta tttttcagtg   2280  
               
               
                   
               
               
                 tgcacctact gtttgtattt gcaaactgag cttgttggag ggaaggcatt attttttaaa   2340  
               
               
                   
               
               
                 atacttagta aattaaatga ac                                            2362  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 49  
               
               
                 &lt;211&gt; LENGTH: 620  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 49  
               
               
                   
               
               
                 Met Leu Ser Ala Ile Tyr Thr Val Leu Ala Gly Leu Leu Phe Leu Pro  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Leu Val Asn Leu Cys Cys Pro Tyr Phe Phe Gln Asp Ile Gly Tyr  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Leu Lys Val Ala Ala Val Gly Arg Arg Val Arg Ser Tyr Gly Gln  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Arg Arg Pro Ala Arg Thr Ile Leu Arg Ala Phe Leu Glu Lys Ala Arg  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Gln Thr Pro His Lys Pro Phe Leu Leu Phe Arg Asp Glu Thr Leu Thr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Tyr Ala Gln Val Asp Arg Arg Ser Asn Gln Val Ala Arg Ala Leu His  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp His Leu Gly Leu Arg Gln Gly Asp Cys Val Ala Leu Leu Met Gly  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Asn Glu Pro Ala Tyr Val Trp Leu Trp Leu Gly Leu Val Lys Leu Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Cys Ala Met Ala Cys Leu Asn Tyr Asn Ile Arg Ala Lys Ser Leu Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 His Cys Phe Gln Cys Cys Gly Ala Lys Val Leu Leu Val Ser Pro Glu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Leu Gln Ala Ala Val Glu Glu Ile Leu Pro Ser Leu Lys Lys Asp Asp  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Val Ser Ile Tyr Tyr Val Ser Arg Thr Ser Asn Thr Asp Gly Ile Asp  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Phe Leu Asp Lys Val Asp Glu Val Ser Thr Glu Pro Ile Pro Glu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Ser Trp Arg Ser Glu Val Thr Phe Ser Thr Pro Ala Leu Tyr Ile Tyr  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala Met Ile Thr His Gln  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Arg Ile Trp Tyr Gly Thr Gly Leu Thr Phe Val Ser Gly Leu Lys Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Asp Asp Val Ile Tyr Ile Thr Leu Pro Phe Tyr His Ser Ala Ala Leu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Leu Ile Gly Ile His Gly Cys Ile Val Ala Gly Ala Thr Leu Ala Leu  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Arg Thr Lys Phe Ser Ala Ser Gln Phe Trp Asp Asp Cys Arg Lys Tyr  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Asn Val Thr Val Ile Gln Tyr Ile Gly Glu Leu Leu Arg Tyr Leu Cys  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Asn Ser Pro Gln Lys Pro Asn Asp Arg Asp His Lys Val Arg Leu Ala  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Leu Gly Asn Gly Leu Arg Gly Asp Val Trp Arg Gln Phe Val Lys Arg  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Phe Gly Asp Ile Cys Ile Tyr Glu Phe Tyr Ala Ala Thr Glu Gly Asn  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ile Gly Phe Met Asn Tyr Ala Arg Lys Val Gly Ala Val Gly Arg Val  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Asn Tyr Leu Gln Lys Lys Ile Ile Thr Tyr Asp Leu Ile Lys Tyr Asp  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Val Glu Lys Asp Glu Pro Val Arg Asp Glu Asn Gly Tyr Cys Val Arg  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Val Pro Lys Gly Glu Val Gly Leu Leu Val Cys Lys Ile Thr Gln Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Thr Pro Phe Asn Gly Tyr Ala Gly Ala Lys Ala Gln Thr Glu Lys Lys  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Lys Leu Arg Asp Val Phe Lys Lys Gly Asp Leu Tyr Phe Asn Ser Gly  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Asp Leu Leu Met Val Asp His Glu Asn Phe Ile Tyr Phe His Asp Arg  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Val Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala Thr Thr Glu  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Val Ala Asp Thr Val Gly Leu Val Asp Phe Val Gln Glu Val Asn Val  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Tyr Gly Val His Val Pro Asp His Glu Gly Arg Ile Gly Met Ala Ser  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ile Lys Met Lys Glu Asn His Glu Phe Asp Gly Lys Lys Leu Phe Gln  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 His Ile Ala Asp Tyr Leu Pro Ser Tyr Ala Arg Pro Arg Phe Leu Arg  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ile Gln Asp Thr Ile Glu Ile Thr Gly Thr Phe Lys His Arg Lys Met  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Thr Leu Val Glu Glu Gly Phe Asn Pro Ala Val Ile Lys Asp Ala Leu  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Tyr Phe Leu Asp Asp Thr Ala Lys Met Tyr Val Pro Met Thr Glu Asp  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ile Tyr Asn Ala Ile Ser Ala Lys Thr Leu Lys Leu  
               
               
                     610                 615                 620  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 50  
               
               
                 &lt;211&gt; LENGTH: 1173  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 50  
               
               
                   
               
               
                 aagttctcgg ctggtcagtt ctgggaagat tgccagcagc acagggtgac ggtgttccag     60  
               
               
                   
               
               
                 tacattgggg agctgtgccg ataccttgtc aaccagcccc cgagcaaggc agaacgtggc    120  
               
               
                   
               
               
                 cataaggtcc ggctggcagt gggcagcggg ctgcgcccag atacctggga gcgttttgtg    180  
               
               
                   
               
               
                 cggcgcttcg ggcccctgca ggtgctggag acatatggac tgacagaggg caacgtggcc    240  
               
               
                   
               
               
                 accatcaact acacaggaca gcggggcgct gtggggcgtg cttcctggct ttacaagcat    300  
               
               
                   
               
               
                 atcttcccct tctccttgat tcgctatgat gtcaccacag gagagccaat tcgggacccc    360  
               
               
                   
               
               
                 caggggcact gtatggccac atctccaggt gagccagggc tgctggtggc cccggtaagc    420  
               
               
                   
               
               
                 cagcagtccc cattcctggg ctatgctggc gggccagagc tggcccaggg gaagttgcta    480  
               
               
                   
               
               
                 aaggatgtct tccggcctgg ggatgttttc ttcaacactg gggacctgct ggtctgcgat    540  
               
               
                   
               
               
                 gaccaaggtt ttctccgctt ccatgatcgt actggagaca ccttcaggtg gaagggggag    600  
               
               
                   
               
               
                 aatgtggcca caaccgaggt ggcagaggtc ttcgaggccc tagattttct tcaggaggtg    660  
               
               
                   
               
               
                 aacgtctatg gagtcactgt gccagggcat gaaggcaggg ctggaatggc agccctagtt    720  
               
               
                   
               
               
                 ctgcgtcccc cccacgcttt ggaccttatg cagctctaca cccacgtgtc tgagaacttg    780  
               
               
                   
               
               
                 ccaccttatg cccggccccg attcctcagg ctccaggagt ctttggccac cacagagacc    840  
               
               
                   
               
               
                 ttcaaacagc agaaagttcg gatggcaaat gagggcttcg accccagcac cctgtctgac    900  
               
               
                   
               
               
                 ccactgtacg ttctggacca ggctgtaggt gcctacctgc ccctcacaac tgcccggtac    960  
               
               
                   
               
               
                 agcgccctcc tggcaggaaa ccttcgaatc tgagaacttc cacacctgag gcacctgaga   1020  
               
               
                   
               
               
                 gaggaactct gtggggtggg ggccgttgca ggtgtactgg gctgtcaggg atcttttcta   1080  
               
               
                   
               
               
                 taccagaact gcggtcacta ttttgtaata aatgtggctg gagctgatcc agctgtctct   1140  
               
               
                   
               
               
                 gacaaaaaaa aaaaaaaaaa aaagggcggc cgc                                1173  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 51  
               
               
                 &lt;211&gt; LENGTH: 330  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 51  
               
               
                   
               
               
                 Lys Phe Ser Ala Gly Gln Phe Trp Glu Asp Cys Gln Gln His Arg Val  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Thr Val Phe Gln Tyr Ile Gly Glu Leu Cys Arg Tyr Leu Val Asn Gln  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Pro Pro Ser Lys Ala Glu Arg Gly His Lys Val Arg Leu Ala Val Gly  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ser Gly Leu Arg Pro Asp Thr Trp Glu Arg Phe Val Arg Arg Phe Gly  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Pro Leu Gln Val Leu Glu Thr Tyr Gly Leu Thr Glu Gly Asn Val Ala  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Thr Ile Asn Tyr Thr Gly Gln Arg Gly Ala Val Gly Arg Ala Ser Trp  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Leu Tyr Lys His Ile Phe Pro Phe Ser Leu Ile Arg Tyr Asp Val Thr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Thr Gly Glu Pro Ile Arg Asp Pro Gln Gly His Cys Met Ala Thr Ser  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Pro Gly Glu Pro Gly Leu Leu Val Ala Pro Val Ser Gln Gln Ser Pro  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Phe Leu Gly Tyr Ala Gly Gly Pro Glu Leu Ala Gln Gly Lys Leu Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Lys Asp Val Phe Arg Pro Gly Asp Val Phe Phe Asn Thr Gly Asp Leu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Leu Val Cys Asp Asp Gln Gly Phe Leu Arg Phe His Asp Arg Thr Gly  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala Thr Thr Glu Val Ala  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Glu Val Phe Glu Ala Leu Asp Phe Leu Gln Glu Val Asn Val Tyr Gly  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Val Thr Val Pro Gly His Glu Gly Arg Ala Gly Met Ala Ala Leu Val  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Leu Arg Pro Pro His Ala Leu Asp Leu Met Gln Leu Tyr Thr His Val  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Ser Glu Asn Leu Pro Pro Tyr Ala Arg Pro Arg Phe Leu Arg Leu Gln  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Glu Ser Leu Ala Thr Thr Glu Thr Phe Lys Gln Gln Lys Val Arg Met  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Ala Asn Glu Gly Phe Asp Pro Ser Thr Leu Ser Asp Pro Leu Tyr Val  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Leu Asp Gln Ala Val Gly Ala Tyr Leu Pro Leu Thr Thr Ala Arg Tyr  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Ser Ala Leu Leu Ala Gly Asn Leu Arg Ile  
               
               
                                 325                 330  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 52  
               
               
                 &lt;211&gt; LENGTH: 2907  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 52  
               
               
                   
               
               
                 cgacccacgc gtccgggcgg gcggggccgg gcggcgggcg gggctggcgg ggcggccggg     60  
               
               
                   
               
               
                 ccatgcaggg cgcagagccg gctaaaccct gctgagaccc ggctccgtgc gtccaggggc    120  
               
               
                   
               
               
                 ggctaatgcc cctcacgctg tctacgctgc tgcaaccggg ccgcatctgg acggggcgcc    180  
               
               
                   
               
               
                 gcgcggcgga gccgacgccg ggccacaatg ctgcttggag cctctctggt gggggtgctg    240  
               
               
                   
               
               
                 ctgttctcca agctggtgct gaaactgccc tggacccagg tgggattctc cctgttgttc    300  
               
               
                   
               
               
                 ctctacttgg gatctggcgg ctggcgcttc atccgggtct tcatcaagac catcaggcgc    360  
               
               
                   
               
               
                 gatatctttg gcggcctggt cctcctgaag gtgaaggcaa aggtgcgaca gtgcctgcag    420  
               
               
                   
               
               
                 gagcggcgga cagtgcccat tttgtttgcc tctaccgttc ggcgccaccc cgacaagacg    480  
               
               
                   
               
               
                 gccctgatct tcgagggcac agatacccac tggaccttcc gccagctgga tgagtactca    540  
               
               
                   
               
               
                 agcagtgtag ccaacttcct gcaggcccgg ggcctggcct cgggcgatgt ggctgccatc    600  
               
               
                   
               
               
                 ttcatggaga accgcaatga gttcgtgggc ctatggctgg gcatggccaa gctcggtgtg    660  
               
               
                   
               
               
                 gaggcagccc tcatcaacac caacctgcgg cgggatgctc tgctccactg cctcaccacc    720  
               
               
                   
               
               
                 tcgcgcgcac gggcccttgt ctttggcagc gaaatggcct cagccatctg tgaggtccat    780  
               
               
                   
               
               
                 gccagcctgg acccctcgct cagcctcttc tgctctggct cctgggagcc cggtgcggtg    840  
               
               
                   
               
               
                 cctccaagca cagaacacct ggaccctctg ctgaaagatg ctcccaagca ccttcccagt    900  
               
               
                   
               
               
                 tgccctgaca agggcttcac agataaactg ttctacatct acacatccgg caccacaggg    960  
               
               
                   
               
               
                 ctgcccaagg ccgccatcgt ggtgcacagc aggtattacc gcatggctgc cctggtgtac   1020  
               
               
                   
               
               
                 tatggattcc gcatgcggcc caacgacatc gtctatgact gcctccccct ctaccactca   1080  
               
               
                   
               
               
                 gcaggaaaca tcgtgggaat cggccagtgc ctgctgcatg gcatgacggt ggtgattcgg   1140  
               
               
                   
               
               
                 aagaagttct cagcctcccg gttctgggac gattgtatca agtacaactg cacgattgtg   1200  
               
               
                   
               
               
                 cagtacattg gtgaactgtg ccgctacctc ctgaaccagc caccgcggga ggcagaaaac   1260  
               
               
                   
               
               
                 cagcaccagg ttcgcatggc actaggcaat ggcctccggc agtccatctg gaccaacttt   1320  
               
               
                   
               
               
                 tccagccgct tccacatacc ccaggtggct gagttctacg gggccacaga gtgcaactgt   1380  
               
               
                   
               
               
                 agcctgggca acttcgacag ccaggtgggg gcctgtggtt tcaatagccg catcctgtcc   1440  
               
               
                   
               
               
                 ttcgtgtacc ccatccggtt ggtacgtgtc aacgaggaca ccatggagct gatccggggg   1500  
               
               
                   
               
               
                 cccgacggcg tctgcattcc ctgccagcca ggtgagccgg gccagctggt gggccgcatc   1560  
               
               
                   
               
               
                 atccagaaag accccctgcg ccgcttcgat ggctacctca accagggcgc caacaacaag   1620  
               
               
                   
               
               
                 aagattgcca aggatgtctt caagaagggg gaccaggcct accttactgg tgatgtgctg   1680  
               
               
                   
               
               
                 gtgatggacg agctgggcta cctgtacttc cgagaccgca ctggggacac gttccgctgg   1740  
               
               
                   
               
               
                 aaaggtgaga acgtgtccac caccgaggtg gaaggcacac tcagccgcct gctggacatg   1800  
               
               
                   
               
               
                 gctgacgtgg ccgtgtatgg tgtcgaggtg ccaggaaccg agggccgggc cggaatggct   1860  
               
               
                   
               
               
                 gctgtggcca gccccactgg caactgtgac ctggagcgct ttgctcaggt cttggagaag   1920  
               
               
                   
               
               
                 gaactgcccc tgtatgcgcg ccccatcttc ctgcgcctcc tgcctgagct gcacaaaaca   1980  
               
               
                   
               
               
                 ggaacctaca agttccagaa gacagagcta cggaaggagg gctttgaccc ggctattgtg   2040  
               
               
                   
               
               
                 aaagacccgc tgttctatct agatgcccag aagggccgct acgtcccgct ggaccaagag   2100  
               
               
                   
               
               
                 gcctacagcc gcatccaggc aggcgaggag aagctgtgat tccccccatc cctctgaggg   2160  
               
               
                   
               
               
                 ccggcggatg ctggatccgg agccccaggt tccgccccag agcggtcctg gacaaggcca   2220  
               
               
                   
               
               
                 gaccaaagca agcagggcct ggcacctcca tcctgaggtg ctgcccctcc atccaaaact   2280  
               
               
                   
               
               
                 gccaagtgac tcattgcctt cccaaccctt ccagaggctt tctgtgaaag tctcatgtcc   2340  
               
               
                   
               
               
                 aagttccgtc ttctgggctg ggcaggccct ctggttccca ggctgagact gacgggtttt   2400  
               
               
                   
               
               
                 ctcaggatga tgtcttgggt gagggtaggg agaggacaag gggtcaccga gcccttccca   2460  
               
               
                   
               
               
                 gagagcaggg agcttataaa tggaaccaga gcagaagtcc ccagactcag gaagtcaaca   2520  
               
               
                   
               
               
                 gagtgggcag ggacagtggt agcatccatc tggtggccaa agagaatcgt agccccagag   2580  
               
               
                   
               
               
                 ctgcccaagt tcactgggct ccacccccac ctccaggagg ggaggagagg acctgacatc   2640  
               
               
                   
               
               
                 tgtaggtggc ccctgatgcc ccatctacag caggaggtca ggaccacgcc cctggcctct   2700  
               
               
                   
               
               
                 ccccactccc ccatcctcct ccctgggtgg ctgcctgatt atccctcagg cagggcctct   2760  
               
               
                   
               
               
                 cagtccttgt gggtctgtgt cacctccatc tcagtcttgg cctggctatg aggggaggag   2820  
               
               
                   
               
               
                 gaatgggaga gggggctcag gggccaataa actctgcctt gagtcctcct aaaaaaaaaa   2880  
               
               
                   
               
               
                 aaaaaaaaaa aaaaaaaaaa aaaaaaa                                       2907  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 53  
               
               
                 &lt;211&gt; LENGTH: 643  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 53  
               
               
                   
               
               
                 Met Leu Leu Gly Ala Ser Leu Val Gly Val Leu Leu Phe Ser Lys Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val Leu Lys Leu Pro Trp Thr Gln Val Gly Phe Ser Leu Leu Phe Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Tyr Leu Gly Ser Gly Gly Trp Arg Phe Ile Arg Val Phe Ile Lys Thr  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ile Arg Arg Asp Ile Phe Gly Gly Leu Val Leu Leu Lys Val Lys Ala  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Lys Val Arg Gln Cys Leu Gln Glu Arg Arg Thr Val Pro Ile Leu Phe  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Ser Thr Val Arg Arg His Pro Asp Lys Thr Ala Leu Ile Phe Glu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Thr Asp Thr His Trp Thr Phe Arg Gln Leu Asp Glu Tyr Ser Ser  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Val Ala Asn Phe Leu Gln Ala Arg Gly Leu Ala Ser Gly Asp Val  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Ala Ala Ile Phe Met Glu Asn Arg Asn Glu Phe Val Gly Leu Trp Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Gly Met Ala Lys Leu Gly Val Glu Ala Ala Leu Ile Asn Thr Asn Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Arg Arg Asp Ala Leu Leu His Cys Leu Thr Thr Ser Arg Ala Arg Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Leu Val Phe Gly Ser Glu Met Ala Ser Ala Ile Cys Glu Val His Ala  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Leu Asp Pro Ser Leu Ser Leu Phe Cys Ser Gly Ser Trp Glu Pro  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Ala Val Pro Pro Ser Thr Glu His Leu Asp Pro Leu Leu Lys Asp  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Pro Lys His Leu Pro Ser Cys Pro Asp Lys Gly Phe Thr Asp Lys  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ala Leu Val Tyr Tyr  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly Phe Arg Met Arg Pro Asn Asp Ile Val Tyr Asp Cys Leu Pro Leu  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Tyr His Ser Ala Gly Asn Ile Val Gly Ile Gly Gln Cys Leu Leu His  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Gly Met Thr Val Val Ile Arg Lys Lys Phe Ser Ala Ser Arg Phe Trp  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Asp Asp Cys Ile Lys Tyr Asn Cys Thr Ile Val Gln Tyr Ile Gly Glu  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Leu Cys Arg Tyr Leu Leu Asn Gln Pro Pro Arg Glu Ala Glu Asn Gln  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 His Gln Val Arg Met Ala Leu Gly Asn Gly Leu Arg Gln Ser Ile Trp  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Thr Asn Phe Ser Ser Arg Phe His Ile Pro Gln Val Ala Glu Phe Tyr  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gly Ala Thr Glu Cys Asn Cys Ser Leu Gly Asn Phe Asp Ser Gln Val  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Ala Cys Gly Phe Asn Ser Arg Ile Leu Ser Phe Val Tyr Pro Ile  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Arg Leu Val Arg Val Asn Glu Asp Thr Met Glu Leu Ile Arg Gly Pro  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Asp Gly Val Cys Ile Pro Cys Gln Pro Gly Glu Pro Gly Gln Leu Val  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Gly Arg Ile Ile Gln Lys Asp Pro Leu Arg Arg Phe Asp Gly Tyr Leu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Asn Gln Gly Ala Asn Asn Lys Lys Ile Ala Lys Asp Val Phe Lys Lys  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Gly Asp Gln Ala Tyr Leu Thr Gly Asp Val Leu Val Met Asp Glu Leu  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Gly Tyr Leu Tyr Phe Arg Asp Arg Thr Gly Asp Thr Phe Arg Trp Lys  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Thr Leu Ser Arg Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Leu Asp Met Ala Asp Val Ala Val Tyr Gly Val Glu Val Pro Gly Thr  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Glu Gly Arg Ala Gly Met Ala Ala Val Ala Ser Pro Thr Gly Asn Cys  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Asp Leu Glu Arg Phe Ala Gln Val Leu Glu Lys Glu Leu Pro Leu Tyr  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Glu Leu His Lys Thr Gly  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Thr Tyr Lys Phe Gln Lys Thr Glu Leu Arg Lys Glu Gly Phe Asp Pro  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ala Ile Val Lys Asp Pro Leu Phe Tyr Leu Asp Ala Gln Lys Gly Arg  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Tyr Val Pro Leu Asp Gln Glu Ala Tyr Ser Arg Ile Gln Ala Gly Glu  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Glu Lys Leu  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 54  
               
               
                 &lt;211&gt; LENGTH: 1248  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: (1)...(1248)  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 262  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 54  
               
               
                   
               
               
                 gtcgttggga tcctcggctg cttagatctc ggagccacct gtgttctggc ccccaagttc     60  
               
               
                   
               
               
                 tctacttcct gcttctggga tgactgtcgg cagcatggcg tgacagtgat cctgtatgtg    120  
               
               
                   
               
               
                 ggcgagctcc tgcgatactt gtgtaacatt ccccagcaac cagaggaccg gacacataca    180  
               
               
                   
               
               
                 gtccgcctgg caatgggcaa tggactacgg gctgatgtgt ggggagacct tccagcagcg    240  
               
               
                   
               
               
                 tttcggtcct atttcggatc tngggaagtc ttacgggctt ccacagaagg gcaacatggg    300  
               
               
                   
               
               
                 gctttagttc aaatattgtt gggggcgctg cggggccctg ggggcaaaga tggagcttgc    360  
               
               
                   
               
               
                 ctcctccgaa tgctgtcccc ctttgagctg gtgcagttcg acatggaggc ggcggagcct    420  
               
               
                   
               
               
                 gtgagggaca atcagggctt ctgcatccct gtagggctag gggagccggg gctgctgttg    480  
               
               
                   
               
               
                 accaaggtgg taagccagca acccttcgtg ggctaccgcg gcccccgaga gctgtcggaa    540  
               
               
                   
               
               
                 cggaagctgg tgcgcaacgt gcggcaatcg ggcgacgttt actacaacac cggggacgta    600  
               
               
                   
               
               
                 ctggccatgg accgcgaagg cttcctctac ttccgcgacc gactcgggga caccttccga    660  
               
               
                   
               
               
                 tggaagggcg agaacgtgtc cacgcacgag gtggagggcg tgttgtcgca ggtggacttc    720  
               
               
                   
               
               
                 ttgcaacagg ttaacgtgta tggcgtgtgc gtgccaggtt gtgagggtaa ggtgggcatg    780  
               
               
                   
               
               
                 gctgctgtgg cattagcccc cggccagact ttcgacgggg agaagttgta ccagcacgtt    840  
               
               
                   
               
               
                 cgcgcttggc tccctgccta cgctaccccc catttcatcc gcatccagga cgccatggag    900  
               
               
                   
               
               
                 gtcaccagca cgttcaaact gatgaagacc cggttggtgc gtgagggctt caatgtgggg    960  
               
               
                   
               
               
                 atcgtggttg accctctgtt tgtactggac aaccgggccc agtccttccg gcccctgacg   1020  
               
               
                   
               
               
                 cagaaatgt accaggctgt gtgtgaggga acctggaggc tctgatcacc tggccaaccc    1080  
               
               
                   
               
               
                 ctggggtag ggatcaaagc cagccacccc caccccaaca cactcggtgt ccctttcatc    1140  
               
               
                   
               
               
                 tgggcctgt gtgaatccca gcctggccat accctcaacc tcagtgggct ggaaatgaca    1200  
               
               
                   
               
               
                 tgggccctg tagcagtggc agaataaact cagmtgygtt cacagaaa                 1248  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 55  
               
               
                 &lt;211&gt; LENGTH: 354  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: (1)...(354)  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 88  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 55  
               
               
                   
               
               
                 Val Val Gly Ile Leu Gly Cys Leu Asp Leu Gly Ala Thr Cys Val Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ala Pro Lys Phe Ser Thr Ser Cys Phe Trp Asp Asp Cys Arg Gln His  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Val Thr Val Ile Leu Tyr Val Gly Glu Leu Leu Arg Tyr Leu Cys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Asn Ile Pro Gln Gln Pro Glu Asp Arg Thr His Thr Val Arg Leu Ala  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Met Gly Asn Gly Leu Arg Ala Asp Val Trp Gly Asp Leu Pro Ala Ala  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Phe Arg Ser Tyr Phe Gly Ser Xaa Glu Val Leu Arg Ala Ser Thr Glu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Gln His Gly Ala Leu Val Gln Ile Leu Leu Gly Ala Leu Arg Gly  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Pro Gly Gly Lys Asp Gly Ala Cys Leu Leu Arg Met Leu Ser Pro Phe  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Glu Leu Val Gln Phe Asp Met Glu Ala Ala Glu Pro Val Arg Asp Asn  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Gln Gly Phe Cys Ile Pro Val Gly Leu Gly Glu Pro Gly Leu Leu Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Thr Lys Val Val Ser Gln Gln Pro Phe Val Gly Tyr Arg Gly Pro Arg  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Glu Leu Ser Glu Arg Lys Leu Val Arg Asn Val Arg Gln Ser Gly Asp  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Val Tyr Tyr Asn Thr Gly Asp Val Leu Ala Met Asp Arg Glu Gly Phe  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Leu Tyr Phe Arg Asp Arg Leu Gly Asp Thr Phe Arg Trp Lys Gly Glu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Asn Val Ser Thr His Glu Val Glu Gly Val Leu Ser Gln Val Asp Phe  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Leu Gln Gln Val Asn Val Tyr Gly Val Cys Val Pro Gly Cys Glu Gly  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Val Gly Met Ala Ala Val Ala Leu Ala Pro Gly Gln Thr Phe Asp  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly Glu Lys Leu Tyr Gln His Val Arg Ala Trp Leu Pro Ala Tyr Ala  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Thr Pro His Phe Ile Arg Ile Gln Asp Ala Met Glu Val Thr Ser Thr  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Phe Lys Leu Met Lys Thr Arg Leu Val Arg Glu Gly Phe Asn Val Gly  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Ile Val Val Asp Pro Leu Phe Val Leu Asp Asn Arg Ala Gln Ser Phe  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Arg Pro Leu Thr Ala Glu Met Tyr Gln Ala Val Cys Glu Gly Thr Trp  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Arg Leu  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 56  
               
               
                 &lt;211&gt; LENGTH: 2885  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 56  
               
               
                   
               
               
                 aacggcaagt aagcgcaacg caattaatgt gagtagctca ctcattaggc accccaggct     60  
               
               
                   
               
               
                 ttacacttta tgcttccggg ctcgtatgtt gtgtggaatt gtgagcggat accaatttca    120  
               
               
                   
               
               
                 cacaggaacc agctatgaca tgattacgaa tttaatacga ctcactatag ggaatttggc    180  
               
               
                   
               
               
                 cctcgaggcc aagaattcgg cacgaggggt gctgagcccc tgcgcggttt ctggtgcgta    240  
               
               
                   
               
               
                 gagactgtaa atcgctgcgc ttctcagtca tcatcatccc agcttttccc ggctcgaatt    300  
               
               
                   
               
               
                 cagcctccaa ctcaagctcg cgggaaagac tacctgagag gagaaaagct tctgtccctg    360  
               
               
                   
               
               
                 gaccttcttc tgagggtgga gtcggaggct ccctgctttc cagccgccca gtgacccaag    420  
               
               
                   
               
               
                 cttaatcttc agcaccactt ggggcgacct tttcggtgca aacctacgat tctgtttctc    480  
               
               
                   
               
               
                 aggattcctc cccatcccgc ttcgccccgg aaaagctgac aagaacttca ggtgtaagcc    540  
               
               
                   
               
               
                 ctgagtagtg aggatctgcg gtctccgtgg agagctgtgc ctggaagaga aggacgctgg    600  
               
               
                   
               
               
                 tgggggctga gatcagagct gtcttctggc ccagttgccc ccatgcttct gtcatggcta    660  
               
               
                   
               
               
                 acagttctag gggctggaat ggtcgtcctg cacttcttgc agaaactcct gttcccttac    720  
               
               
                   
               
               
                 ttttgggatg acttctggtt cgtgttgaag gtggtgctca ttataattcg gctgaagaag    780  
               
               
                   
               
               
                 tatgaaaaga gaggggagct ggtgactgtg ctggataaat tcttgagtca tgccaaaaga    840  
               
               
                   
               
               
                 caacctcgga aacctttcat catctatgag ggagacatct acacctatca ggatgtagac    900  
               
               
                   
               
               
                 aaaaggagca gcagagtggc ccatgtcttc ctgaaccatt cctctctgaa aaagggggac    960  
               
               
                   
               
               
                 cggtggctc tgctgatgag caatgagccg gacttcgttc acgtgtggtt cggcctcgcc    1020  
               
               
                   
               
               
                 agctgggct gcgtggtggc ctttctcaac accaacattc gctccaactc cctcctgaat    1080  
               
               
                   
               
               
                 gcatccgcg cctgtgggcc cagagcccta gtggtgggcg cagatttgct tggaacggta    1140  
               
               
                   
               
               
                 aagaaatcc ttccaagcct ctcagaaaat atcagtgttt gggggatgaa agattctgtt    1200  
               
               
                   
               
               
                 cacaaggtg taatttcact caaagaaaaa ctgagcacct cacctgatga gcccgtgcca    1260  
               
               
                   
               
               
                 gcagccacc atgttgtctc actcctcaag tctacttgtc tttacatttt tacctctgga    1320  
               
               
                   
               
               
                 caacaggtc taccaaaagc agctgtgatt agtcagctgc aggttttaag gggttctgct    1380  
               
               
                   
               
               
                 tcctgtggg cttttggttg tactgctcat gacattgttt atataaccct tcctctgtat    1440  
               
               
                   
               
               
                 atagttcag cagctatcct gggaatttct ggatgtgttg agttgggtgc cacttgtgtg    1500  
               
               
                   
               
               
                 taaagaaga aattttcagc aagccagttt tggagtgact gcaagaagta tgatgtgact    1560  
               
               
                   
               
               
                 tgtttcagt atattggaga actttgtcgc tacctttgca aacaatctaa gagagaagga    1620  
               
               
                   
               
               
                 aaaaggatc ataaggtgcg tttggcaatt ggaaatggca tacggagtga tgtatggaga    1680  
               
               
                   
               
               
                 aatttttag acagatttgg aaatataaag gtgtgtgaac tttatgcagc taccgaatca    1740  
               
               
                   
               
               
                 gcatatctt tcatgaacta cactgggaga attggagcaa ttgggagaac aaatttgttt    1800  
               
               
                   
               
               
                 acaaacttc tttccacttt tgacttaata aagtatgact ttcagaaaga tgaacccatg    1860  
               
               
                   
               
               
                 gaaatgagc agggttggtg tattcatgtg aaaaaaggag aacctggact tctcatttct    1920  
               
               
                   
               
               
                 gagtgaatg caaaaaatcc cttctttggc tatgctgggc cttataagca cacaaaagac    1980  
               
               
                   
               
               
                 aattgcttt gtgatgtttt taagaaggga gatgtttacc ttaatactgg agacttaata    2040  
               
               
                   
               
               
                 tccaggatc aggacaattt cctttatttt tgggaccgta ctggagacac tttcagatgg    2100  
               
               
                   
               
               
                 aaggagaaa atgtcgcaac cactgaggtt gctgatgtta ttggaatgtt ggatttcata    2160  
               
               
                   
               
               
                 aggaagcaa acgtctatgg tgtggctata tcaggttatg aaggaagagc aggaatggct    2220  
               
               
                   
               
               
                 ctattattt taaaaccaaa tacatcttta gatttggaaa aagtttatga acaagttgta    2280  
               
               
                   
               
               
                 catttctac cagcttatgc ttgtccacga tttttaagaa ttcaggaaaa aatggaagca    2340  
               
               
                   
               
               
                 caggaacat tcaaactatt gaagcatcag ttggtggaag atggatttaa tccactgaaa    2400  
               
               
                   
               
               
                 tttctgaac cactttactt catggataac ttgaaaaagt cttatgttct actgaccagg    2460  
               
               
                   
               
               
                 aactttatg atcaaataat gttaggggaa ataaaacttt aagattttta tatctagaac    2520  
               
               
                   
               
               
                 ttcatatgc tttcttagga agagtgagag gggggtatat gattctttat gaaatgggga    2580  
               
               
                   
               
               
                 agggagcta acattaatta tgcatgtact atatttcctt aatatgagag ataatttttt    2640  
               
               
                   
               
               
                 attgcataa gaattttaat ttcttttaat tgatataaac attagttgat tattcttttt    2700  
               
               
                   
               
               
                 tctatttgg agattcagtg cataactaag tattttcctt aatactaaag attttaaata    2760  
               
               
                   
               
               
                 taaatagtg gctagcggtt tggacaatca ctaaaaatgt actttctaat aagtaaaatt    2820  
               
               
                   
               
               
                 ctaattttg aataaaagat taaattttac tgaaaaaaaa aaaaaaaaaa aaaattggcg    2880  
               
               
                   
               
               
                 ccgc                                                                2885  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 57  
               
               
                 &lt;211&gt; LENGTH: 619  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 57  
               
               
                   
               
               
                 Met Leu Leu Ser Trp Leu Thr Val Leu Gly Ala Gly Met Val Val Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 His Phe Leu Gln Lys Leu Leu Phe Pro Tyr Phe Trp Asp Asp Phe Trp  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Val Leu Lys Val Val Leu Ile Ile Ile Arg Leu Lys Lys Tyr Glu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Arg Gly Glu Leu Val Thr Val Leu Asp Lys Phe Leu Ser His Ala  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Lys Arg Gln Pro Arg Lys Pro Phe Ile Ile Tyr Glu Gly Asp Ile Tyr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Thr Tyr Gln Asp Val Asp Lys Arg Ser Ser Arg Val Ala His Val Phe  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Leu Asn His Ser Ser Leu Lys Lys Gly Asp Thr Val Ala Leu Leu Met  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Asn Glu Pro Asp Phe Val His Val Trp Phe Gly Leu Ala Lys Leu  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Gly Cys Val Val Ala Phe Leu Asn Thr Asn Ile Arg Ser Asn Ser Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Leu Asn Cys Ile Arg Ala Cys Gly Pro Arg Ala Leu Val Val Gly Ala  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asp Leu Leu Gly Thr Val Glu Glu Ile Leu Pro Ser Leu Ser Glu Asn  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Ile Ser Val Trp Gly Met Lys Asp Ser Val Pro Gln Gly Val Ile Ser  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Leu Lys Glu Lys Leu Ser Thr Ser Pro Asp Glu Pro Val Pro Arg Ser  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 His His Val Val Ser Leu Leu Lys Ser Thr Cys Leu Tyr Ile Phe Thr  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala Val Ile Ser Gln Leu Gln  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Val Leu Arg Gly Ser Ala Val Leu Trp Ala Phe Gly Cys Thr Ala His  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Asp Ile Val Tyr Ile Thr Leu Pro Leu Tyr His Ser Ser Ala Ala Ile  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Leu Gly Ile Ser Gly Cys Val Glu Leu Gly Ala Thr Cys Val Leu Lys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Lys Lys Phe Ser Ala Ser Gln Phe Trp Ser Asp Cys Lys Lys Tyr Asp  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Val Thr Val Phe Gln Tyr Ile Gly Glu Leu Cys Arg Tyr Leu Cys Lys  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Gln Ser Lys Arg Glu Gly Glu Lys Asp His Lys Val Arg Leu Ala Ile  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Gly Asn Gly Ile Arg Ser Asp Val Trp Arg Glu Phe Leu Asp Arg Phe  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Gly Asn Ile Lys Val Cys Glu Leu Tyr Ala Ala Thr Glu Ser Ser Ile  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ser Phe Met Asn Tyr Thr Gly Arg Ile Gly Ala Ile Gly Arg Thr Asn  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Leu Phe Tyr Lys Leu Leu Ser Thr Phe Asp Leu Ile Lys Tyr Asp Phe  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gln Lys Asp Glu Pro Met Arg Asn Glu Gln Gly Trp Cys Ile His Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Lys Lys Gly Glu Pro Gly Leu Leu Ile Ser Arg Val Asn Ala Lys Asn  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Pro Phe Phe Gly Tyr Ala Gly Pro Tyr Lys His Thr Lys Asp Lys Leu  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Cys Asp Val Phe Lys Lys Gly Asp Val Tyr Leu Asn Thr Gly Asp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Leu Ile Val Gln Asp Gln Asp Asn Phe Leu Tyr Phe Trp Asp Arg Thr  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala Thr Thr Glu Val  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Ala Asp Val Ile Gly Met Leu Asp Phe Ile Gln Glu Ala Asn Val Tyr  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Gly Val Ala Ile Ser Gly Tyr Glu Gly Arg Ala Gly Met Ala Ser Ile  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ile Leu Lys Pro Asn Thr Ser Leu Asp Leu Glu Lys Val Tyr Glu Gln  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Val Val Thr Phe Leu Pro Ala Tyr Ala Cys Pro Arg Phe Leu Arg Ile  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Gln Glu Lys Met Glu Ala Thr Gly Thr Phe Lys Leu Leu Lys His Gln  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu Val Glu Asp Gly Phe Asn Pro Leu Lys Ile Ser Glu Pro Leu Tyr  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Phe Met Asp Asn Leu Lys Lys Ser Tyr Val Leu Leu Thr Arg Glu Leu  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Tyr Asp Gln Ile Met Leu Gly Glu Ile Lys Leu  
               
               
                     610                 615  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 58  
               
               
                 &lt;211&gt; LENGTH: 3098  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Rattus norvegicus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 58  
               
               
                   
               
               
                 aagttcccac tccagacttc tgcgagaacc cgtgaggaag cagcgagaac cgggggtttg     60  
               
               
                   
               
               
                 caagccagag aaggatgcgg actccgggag caggaacagc ctctgtggcc tcattggggc    120  
               
               
                   
               
               
                 tgctttggct tctgggactt ccgtggacct ggagcgcggc ggcggcgttc ggtgtgtacg    180  
               
               
                   
               
               
                 tgggtagcgg tggctggcga tttctgcgta tcgtctgcaa gacggcgagg cgagacctct    240  
               
               
                   
               
               
                 ttggcctctc tgttctgatc cgcgtgcggc tagagctacg acgacaccgg cgagcaggag    300  
               
               
                   
               
               
                 acacgatccc acgcatcttc caggccgtgg cccagcgaca gccggagcgc ctggcgctgg    360  
               
               
                   
               
               
                 tagatgcgag tagcggtatc tgctggacct tcgcacagct agacacctac tccaatgctg    420  
               
               
                   
               
               
                 tggccaatct gttcctccag ctgggctttg cgccaggcga tgtggtggct gtgttcctgg    480  
               
               
                   
               
               
                 aaggccggcc cgagttcgtg ggactgtggc tgggcctggc caaggccggt gtagtggctg    540  
               
               
                   
               
               
                 cgcttctcaa tgtcaacctg aggcgggagc cccttgcctt ctgcttgggc acatcagctg    600  
               
               
                   
               
               
                 ccaaggccct catttatggc ggggagatgg cagcggcggt ggcggaggtg agtgagcagc    660  
               
               
                   
               
               
                 tggggaagag cctgctcaag ttctgctctg gagatctggg gcctgagagc gtcctgcctg    720  
               
               
                   
               
               
                 acacgcagct tctggacccc atgcttgctg aggcgcccac cacacccctg gcacaggccc    780  
               
               
                   
               
               
                 caggcaaggg catggatgat cggctatttt acatctatac ttctgggacc accggacttc    840  
               
               
                   
               
               
                 ctaaggcggc cattgtggtg cacagcaggt actaccgcat cgcagccttc ggccaccatt    900  
               
               
                   
               
               
                 cctacagcat gcgggccaac gatgtgctct atgactgcct acctctctac cactcagcag    960  
               
               
                   
               
               
                 ggaacatcat gggcgtggga cagtgtatca tctacgggtt aacggtggta ctgcgcaaga   1020  
               
               
                   
               
               
                 agttctccgc cagccgcttc tgggacgact gtgtcaaata taattgcacg gtagtgcagt   1080  
               
               
                   
               
               
                 acatcggtga aatatgccgc tacctgctaa ggcagccggt tcgcgatgta gagcggcggc   1140  
               
               
                   
               
               
                 accgcgtgcg cctggccgtg ggtaacggac tgcggccagc catctgggag gagttcacgc   1200  
               
               
                   
               
               
                 agggtttcgg tgtgcgacag attggcgagt tctacggcgc caccgaatgc aactgcagca   1260  
               
               
                   
               
               
                 ttgccaacat ggacggcaag gtcggctcct gcggcttcaa cagccgtatc ctcacgcatg   1320  
               
               
                   
               
               
                 tgtaccccat ccgtctggtc aaggtcaacg aggacacgat ggagccactg agggactccc   1380  
               
               
                   
               
               
                 aaggcctctg catcccgtgc cagcccgggg aacctgggct tctcgtgggc cagatcaacc   1440  
               
               
                   
               
               
                 agcaagaccc tctgcggcgc ttcgatggct atgttagtga cagcgccacc aacaagaaga   1500  
               
               
                   
               
               
                 ttgcccacag cgtgttccga aagggggaca gcgcctacct ttcaggtgac gtgctagtga   1560  
               
               
                   
               
               
                 tggacgagct ggggtacatg tacttccgtg accgcagcgg ggataccttc cgatggcgcg   1620  
               
               
                   
               
               
                 gcgagaacgt atccaccacg gaggtggaag ccgtgctgag ccgcctgttg ggccagacgg   1680  
               
               
                   
               
               
                 acgtggctgt gtatggagtg gctgtgccag gagtggaggg gaaaagcggc atggcggcca   1740  
               
               
                   
               
               
                 ttgcagaccc ccacaaccag ctggacccta actcaatgta ccaggaattg cagaaggttc   1800  
               
               
                   
               
               
                 ttgcatccta tgcccagccc atcttcctgc gtcttctgcc ccaagtggat acaacaggca   1860  
               
               
                   
               
               
                 ccttcaagat ccagaagacc cgactacagc gtgaaggctt tgacccccgc cagacctcag   1920  
               
               
                   
               
               
                 accggctctt ctttctagac ctgaaacagg gacgctacct acccctggat gagagagtcc   1980  
               
               
                   
               
               
                 atgcccgcat ctgcgcaggc gacttctcac tctgagcctg gtgagtggga tggccctgga   2040  
               
               
                   
               
               
                 cttgtgagac cagggagccg gacacccctg ttcaggtgtt tctcctgcct ggccacgtgg   2100  
               
               
                   
               
               
                 ccagcagcac ctgtgggtgc aggaaactgg aacctgagtg gccgggtgtc cctttcctac   2160  
               
               
                   
               
               
                 aacccaccat gcacacatct agcctctgcc ttggtctttt tctccatctc tttcctccgt   2220  
               
               
                   
               
               
                 gcccagcagg agccccacag acacattggc tgctgtgtcc tgcagtggga ccggtgtcta   2280  
               
               
                   
               
               
                 ggggtccatg ctgcaggctg tgacccgcac tggtgcccac ctcccttccc cattgtgcct   2340  
               
               
                   
               
               
                 taggttcctc cactgtgcgc cggtgaagca agtggggacc cacatagctg ttgtccctgc   2400  
               
               
                   
               
               
                 tgagggttgg tagcaaatgc accctcatgt cagctgggag acacatgcag tctcccactg   2460  
               
               
                   
               
               
                 acccccaatc aactgaagat actgttttgt attattgttt tgagataggg tctcactgtg   2520  
               
               
                   
               
               
                 gaggccaagc tggcctcagg ctcaccactc tactgcctcc gggcaccagc ctgcagtttg   2580  
               
               
                   
               
               
                 atgacatgta tgcactattg ttctaagggt cttctgagtc cctgctttcc cctcatgtcc   2640  
               
               
                   
               
               
                 taaaaccttc cagaactgac tctgatcact tggatgtagc tagtgttggc cctgcccacg   2700  
               
               
                   
               
               
                 tgtgtcaatt caggggtccc caggcatcat ctctggaggc cctaaccttg gcaaagcttg   2760  
               
               
                   
               
               
                 gatgtcctca catcacagca ggagacccag gaaggttgct gtggtgtctc ttgggcaccc   2820  
               
               
                   
               
               
                 ctggcggcag ccgtggacat gcttccctgc tgtgatagcc caaactgttg cctatgacat   2880  
               
               
                   
               
               
                 ttgaggtcta cccttctggc tgccatggtc cccattgaga tctttggtga ctcacctcag   2940  
               
               
                   
               
               
                 ccaccaagcc aggcctctgc cttccttcag ctctaagggc atgaagggtg tggacagagc   3000  
               
               
                   
               
               
                 agccacaggc tgcccacagt cacccacatg caagtgttat ttccttgttt gttttaaaaa   3060  
               
               
                   
               
               
                 aataaacatg ctgagccttg aaaaaaaaaa aaaaaaaa                           3098  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 59  
               
               
                 &lt;211&gt; LENGTH: 630  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Rattus norvegicus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 59  
               
               
                   
               
               
                 Met Arg Thr Pro Gly Ala Gly Thr Ala Ser Val Ala Ser Leu Gly Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Trp Leu Leu Gly Leu Pro Trp Thr Trp Ser Ala Ala Ala Ala Phe  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Val Tyr Val Gly Ser Gly Gly Trp Arg Phe Leu Arg Ile Val Cys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Thr Ala Arg Arg Asp Leu Phe Gly Leu Ser Val Leu Ile Arg Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Arg Leu Glu Leu Arg Arg His Arg Arg Ala Gly Asp Thr Ile Pro Arg  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ile Phe Gln Ala Val Ala Gln Arg Gln Pro Glu Arg Leu Ala Leu Val  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Ala Ser Ser Gly Ile Cys Trp Thr Phe Ala Gln Leu Asp Thr Tyr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Asn Ala Val Ala Asn Leu Phe Leu Gln Leu Gly Phe Ala Pro Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asp Val Val Ala Val Phe Leu Glu Gly Arg Pro Glu Phe Val Gly Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Trp Leu Gly Leu Ala Lys Ala Gly Val Val Ala Ala Leu Leu Asn Val  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asn Leu Arg Arg Glu Pro Leu Ala Phe Cys Leu Gly Thr Ser Ala Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Lys Ala Leu Ile Tyr Gly Gly Glu Met Ala Ala Ala Val Ala Glu Val  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Glu Gln Leu Gly Lys Ser Leu Leu Lys Phe Cys Ser Gly Asp Leu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Pro Glu Ser Val Leu Pro Asp Thr Gln Leu Leu Asp Pro Met Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Glu Ala Pro Thr Thr Pro Leu Ala Gln Ala Pro Gly Lys Gly Met  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asp Asp Arg Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Ile Ala Ala Phe  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly His His Ser Tyr Ser Met Arg Ala Asn Asp Val Leu Tyr Asp Cys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Leu Pro Leu Tyr His Ser Ala Gly Asn Ile Met Gly Val Gly Gln Cys  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ile Ile Tyr Gly Leu Thr Val Val Leu Arg Lys Lys Phe Ser Ala Ser  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Arg Phe Trp Asp Asp Cys Val Lys Tyr Asn Cys Thr Val Val Gln Tyr  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ile Gly Glu Ile Cys Arg Tyr Leu Leu Arg Gln Pro Val Arg Asp Val  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Glu Arg Arg His Arg Val Arg Leu Ala Val Gly Asn Gly Leu Arg Pro  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ala Ile Trp Glu Glu Phe Thr Gln Gly Phe Gly Val Arg Gln Ile Gly  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Ile Ala Asn Met Asp  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Lys Val Gly Ser Cys Gly Phe Asn Ser Arg Ile Leu Thr His Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Tyr Pro Ile Arg Leu Val Lys Val Asn Glu Asp Thr Met Glu Pro Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Arg Asp Ser Gln Gly Leu Cys Ile Pro Cys Gln Pro Gly Glu Pro Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Leu Val Gly Gln Ile Asn Gln Gln Asp Pro Leu Arg Arg Phe Asp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gly Tyr Val Ser Asp Ser Ala Thr Asn Lys Lys Ile Ala His Ser Val  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Asp Glu Leu Gly Tyr Met Tyr Phe Arg Asp Arg Ser Gly Asp Thr Phe  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Arg Trp Arg Gly Glu Asn Val Ser Thr Thr Glu Val Glu Ala Val Leu  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Ser Arg Leu Leu Gly Gln Thr Asp Val Ala Val Tyr Gly Val Ala Val  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Pro Gly Val Glu Gly Lys Ser Gly Met Ala Ala Ile Ala Asp Pro His  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Asn Gln Leu Asp Pro Asn Ser Met Tyr Gln Glu Leu Gln Lys Val Leu  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ala Ser Tyr Ala Gln Pro Ile Phe Leu Arg Leu Leu Pro Gln Val Asp  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Thr Thr Gly Thr Phe Lys Ile Gln Lys Thr Arg Leu Gln Arg Glu Gly  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Phe Asp Pro Arg Gln Thr Ser Asp Arg Leu Phe Phe Leu Asp Leu Lys  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Gln Gly Arg Tyr Leu Pro Leu Asp Glu Arg Val His Ala Arg Ile Cys  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Ala Gly Asp Phe Ser Leu  
               
               
                 625                 630  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 60  
               
               
                 &lt;211&gt; LENGTH: 2963  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Rattus norvegicus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 60  
               
               
                   
               
               
                 gacacagtac tgccgatgtt ggacagagga tcgcttaaca gaacgaaatc tcaaaacaaa     60  
               
               
                   
               
               
                 ttaacaggac ccggttgctt gatttcccaa atcagaaaag gctcgaaatg tctagagggg    120  
               
               
                   
               
               
                 ctgactgatg cagcggtgac ccggactgga gacagttgga cgcgatcatc tctggtgctt    180  
               
               
                   
               
               
                 ttgttcaacc ttgaaacctt cgccacagga gacttgcctg agcagagaag caaacgtgga    240  
               
               
                   
               
               
                 gaaacaaaga gagatctagc gaaaagcctc tgggaccaag gaggggaggt gggactctgg    300  
               
               
                   
               
               
                 gttggcggtg gcacctgctg ccggctatta ataatagggt cgcgatgcgt ttataaggtg    360  
               
               
                   
               
               
                 tttgattaaa caaagactct atgagagaag aataactagc aacagcccca cgtctgagtc    420  
               
               
                   
               
               
                 gtcgcctccg acctttttca acgtgggttc tttgggccga gcgtcgtttg ccgagaacta    480  
               
               
                   
               
               
                 gatctcacct gaccccagac gctgaaaaca agcgctgtgg catcctgggc cacccaagct    540  
               
               
                   
               
               
                 gacaagggcg cgccccctga gcacacgagg tgccccacga gggggaggga cccacagccg    600  
               
               
                   
               
               
                 tcccgcccgc accgcggtgt ccgctgcggg cacctgcagc cgagccgcca cccgcagtcg    660  
               
               
                   
               
               
                 cagcgcgtcc ggcggccgaa cccggtcgtc agctcgtcag cacctgctct gcttctctcc    720  
               
               
                   
               
               
                 cgcccgccgc cgcgctgcac gcctcgagcg ctccctcggc cccggcgggg accggggacc    780  
               
               
                   
               
               
                 ccgcagccac cgccatgctg cctgtgctct acaccggcct ggcggggctg ctgctgctgc    840  
               
               
                   
               
               
                 ctctgctgct cacctgctgc tgcccctacc tcctccagga cgtgcggttc ttcctgcaac    900  
               
               
                   
               
               
                 tggccaacat ggcccggcag gtgcgcagct accggcagcg gcgacccgtg cgcaccatcc    960  
               
               
                   
               
               
                 tgcatgtctt cttggagcaa gcgcgcaaga ccccgcacaa gcccttcctg ctgtttcgcg   1020  
               
               
                   
               
               
                 acgagacgct tacctacgcc caggtagacc ggcgcagcaa ccaagtagcg cgagcgctgc   1080  
               
               
                   
               
               
                 atgatcacct gggcctgcgg cagggggatt gcgtggccct cttcatgggc aatgagccgg   1140  
               
               
                   
               
               
                 cctacgtgtg gctctggctg ggactgctca aactgggctg tcccatggcg tgcctcaact   1200  
               
               
                   
               
               
                 acaacatccg tgccaagtct ctgctacact gctttcagtg ctgcggggcg aaggtgctgc   1260  
               
               
                   
               
               
                 tggcctcccc agagctacac gaagctgtcg aggaggttct tccaaccctg aaaaaggagg   1320  
               
               
                   
               
               
                 gcgtgtccgt cttctacgta agcagaactt ctaacactaa tggcgtggac acagtactgg   1380  
               
               
                   
               
               
                 acaaagtaga cggggtgtcg gcggacccca tcccggagtc gtggaggtct gaagtcacgt   1440  
               
               
                   
               
               
                 tcaccacacc cgcagtctac atatatactt cgggcaccac aggtcttcca aaggctgcaa   1500  
               
               
                   
               
               
                 ccattaatca ccatcgcctc tggtatggga ccagccttgc cctgaggtcc ggaattaagg   1560  
               
               
                   
               
               
                 ctcatgacgt catctacacc accatgcccc tgtaccacag cgcggcgctc atgattggcc   1620  
               
               
                   
               
               
                 tccacggatg cattgtggtt ggggctacat ttgctttgcg gagcaaattt tcagccagcc   1680  
               
               
                   
               
               
                 agttttggga cgactgcagg aaatacaacg ccactgtcat tcagtacatc ggtgaactgc   1740  
               
               
                   
               
               
                 ttcggtacct ctgcaacacg ccccagaaac caaatgaccg ggaccacaaa gtgaaaatag   1800  
               
               
                   
               
               
                 cactaggaaa tggcttacga ggagatgtgt ggagagagtt catcaagaga tttggggaca   1860  
               
               
                   
               
               
                 ttcacattta tgagttctac gcttccactg aaggcaacat tggatttatg aactatccaa   1920  
               
               
                   
               
               
                 gaaaaatcgg agctgttgga agagaaaatt acctacaaaa aaaagttgta aggcacgagc   1980  
               
               
                   
               
               
                 tgatcaagta tgacgtggag aaggatgagc ctgtccgtga tgcaaatgga tattgcatca   2040  
               
               
                   
               
               
                 aagtccccaa aggagaggtt ggactcttga tttgcaaaat cacagagctc acaccatttt   2100  
               
               
                   
               
               
                 ttggctatgc tggaggaaag acccagacag agaagaaaaa gctcagagat gtttttaaga   2160  
               
               
                   
               
               
                 aaggagacgt ctacttcaac agtggcgatc tcctgatgat cgaccgtgaa aatttcatct   2220  
               
               
                   
               
               
                 attttcacga cagagttgga gacaccttcc ggtggaaagg agagaatgta gctaccacgg   2280  
               
               
                   
               
               
                 aagtcgctga cattgtggga ctggtagatt ttgttgaaga agtgaatgtt tacggtgtgc   2340  
               
               
                   
               
               
                 ccgtgccagg tcatgaaggt cgcatcggga tggcctcgat caagatgaaa gaaaactacg   2400  
               
               
                   
               
               
                 agttcaatgg aaagaaactc tttcagcaca tctcggagta cctgcccagt tactcgaggc   2460  
               
               
                   
               
               
                 ctcggttcct gagaatacaa gataccattg agatcaccgg gacttttaaa caccgcaaag   2520  
               
               
                   
               
               
                 tgaccctgat ggaagagggc tttaacccct cagtcatcaa agataccttg tatttcatgg   2580  
               
               
                   
               
               
                 atgacacaga aaaaacatac gtgcccatga ctgaggacat ttataatgcc ataattgata   2640  
               
               
                   
               
               
                 agactctgaa gctctgaatg ttgcctggct cctaacactt ccagaaagaa acacaatagg   2700  
               
               
                   
               
               
                 cctagcatag ccccttcaca tgtgtaatcc aactttaact tgattaaagg ttataggtgt   2760  
               
               
                   
               
               
                 gatttttcct aggaaattat tcatttaaag gacaattgtt tgtttgtttg tttgtttttt   2820  
               
               
                   
               
               
                 attaattaca ccagaacgtt tgcaagtaaa aagatttaaa gtcacttatt tttcaatgtg   2880  
               
               
                   
               
               
                 cacctgccat ttgtccttgc aaacttagct tcttggagag agggccttat ttttttaaag   2940  
               
               
                   
               
               
                 acataataaa ctatgtaaac act                                           2963  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 61  
               
               
                 &lt;211&gt; LENGTH: 620  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Rattus norvegicus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 61  
               
               
                   
               
               
                 Met Leu Pro Val Leu Tyr Thr Gly Leu Ala Gly Leu Leu Leu Leu Pro  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Leu Leu Thr Cys Cys Cys Pro Tyr Leu Leu Gln Asp Val Arg Phe  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Leu Gln Leu Ala Asn Met Ala Arg Gln Val Arg Ser Tyr Arg Gln  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Arg Arg Pro Val Arg Thr Ile Leu His Val Phe Leu Glu Gln Ala Arg  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Lys Thr Pro His Lys Pro Phe Leu Leu Phe Arg Asp Glu Thr Leu Thr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Tyr Ala Gln Val Asp Arg Arg Ser Asn Gln Val Ala Arg Ala Leu His  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp His Leu Gly Leu Arg Gln Gly Asp Cys Val Ala Leu Phe Met Gly  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Asn Glu Pro Ala Tyr Val Trp Leu Trp Leu Gly Leu Leu Lys Leu Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Cys Pro Met Ala Cys Leu Asn Tyr Asn Ile Arg Ala Lys Ser Leu Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 His Cys Phe Gln Cys Cys Gly Ala Lys Val Leu Leu Ala Ser Pro Glu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Leu His Glu Ala Val Glu Glu Val Leu Pro Thr Leu Lys Lys Glu Gly  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Val Ser Val Phe Tyr Val Ser Arg Thr Ser Asn Thr Asn Gly Val Asp  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Thr Val Leu Asp Lys Val Asp Gly Val Ser Ala Asp Pro Ile Pro Glu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Ser Trp Arg Ser Glu Val Thr Phe Thr Thr Pro Ala Val Tyr Ile Tyr  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala Thr Ile Asn His His  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Arg Leu Trp Tyr Gly Thr Ser Leu Ala Leu Arg Ser Gly Ile Lys Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 His Asp Val Ile Tyr Thr Thr Met Pro Leu Tyr His Ser Ala Ala Leu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Met Ile Gly Leu His Gly Cys Ile Val Val Gly Ala Thr Phe Ala Leu  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Arg Ser Lys Phe Ser Ala Ser Gln Phe Trp Asp Asp Cys Arg Lys Tyr  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Asn Ala Thr Val Ile Gln Tyr Ile Gly Glu Leu Leu Arg Tyr Leu Cys  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Asn Thr Pro Gln Lys Pro Asn Asp Arg Asp His Lys Val Lys Ile Ala  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Leu Gly Asn Gly Leu Arg Gly Asp Val Trp Arg Glu Phe Ile Lys Arg  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Phe Gly Asp Ile His Ile Tyr Glu Phe Tyr Ala Ser Thr Glu Gly Asn  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ile Gly Phe Met Asn Tyr Pro Arg Lys Ile Gly Ala Val Gly Arg Glu  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Asn Tyr Leu Gln Lys Lys Val Val Arg His Glu Leu Ile Lys Tyr Asp  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Val Glu Lys Asp Glu Pro Val Arg Asp Ala Asn Gly Tyr Cys Ile Lys  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Val Pro Lys Gly Glu Val Gly Leu Leu Ile Cys Lys Ile Thr Glu Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Thr Pro Phe Phe Gly Tyr Ala Gly Gly Lys Thr Gln Thr Glu Lys Lys  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Lys Leu Arg Asp Val Phe Lys Lys Gly Asp Val Tyr Phe Asn Ser Gly  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Asp Leu Leu Met Ile Asp Arg Glu Asn Phe Ile Tyr Phe His Asp Arg  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Val Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala Thr Thr Glu  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Val Ala Asp Ile Val Gly Leu Val Asp Phe Val Glu Glu Val Asn Val  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Tyr Gly Val Pro Val Pro Gly His Glu Gly Arg Ile Gly Met Ala Ser  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ile Lys Met Lys Glu Asn Tyr Glu Phe Asn Gly Lys Lys Leu Phe Gln  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 His Ile Ser Glu Tyr Leu Pro Ser Tyr Ser Arg Pro Arg Phe Leu Arg  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ile Gln Asp Thr Ile Glu Ile Thr Gly Thr Phe Lys His Arg Lys Val  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Thr Leu Met Glu Glu Gly Phe Asn Pro Ser Val Ile Lys Asp Thr Leu  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Tyr Phe Met Asp Asp Thr Glu Lys Thr Tyr Val Pro Met Thr Glu Asp  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ile Tyr Asn Ala Ile Ile Asp Lys Thr Leu Lys Leu  
               
               
                     610                 615                 620  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 62  
               
               
                 &lt;211&gt; LENGTH: 1350  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Rattus norvegicus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 62  
               
               
                   
               
               
                 gatcagctct tctatatcta cacgtcgggc accacggggc tacccaaagc tgccattgtg     60  
               
               
                   
               
               
                 gtgcacagca ggtattaccg aatggctgcc ctggtgtact atggattccg catgcggcct    120  
               
               
                   
               
               
                 gatgacattg tctatgactg cctccccctc taccactcag caggaaacat tgtggggatt    180  
               
               
                   
               
               
                 ggccagtgcg tactccacgg catgactgtg gtgatccgga agaagttttc agcctcccgg    240  
               
               
                   
               
               
                 ttctgggatg actgtatcaa gtacaactgc acaattgtac agtacattgg tgagctttgc    300  
               
               
                   
               
               
                 cgctacctcc tgaaccagcc accccgtgag gctgagtctc ggcacaaggt gcgcatggca    360  
               
               
                   
               
               
                 ctgggcaacg gtctccggca gtccatctgg accgacttct ccagccgttt ccacattccc    420  
               
               
                   
               
               
                 aaggtggccg agttctacgg ggccaccgag tgcaactgta gcttgggcaa ctttgacagc    480  
               
               
                   
               
               
                 caggtggggg cctgtggctt caatagccgc atcctgtcct ttgtgtaccc catccgcttg    540  
               
               
                   
               
               
                 gtacgagtca atgaggatac catggaactg atccggggac ccgatggcgt ctgcattccc    600  
               
               
                   
               
               
                 tgtcaaccag gccagccagg ccagctggtg ggtcgcatca tccagcagga ccccctacgc    660  
               
               
                   
               
               
                 cgttttgatg gctacctcaa ccagggtgcc aacaacaaga agattgctag tgatgtcttc    720  
               
               
                   
               
               
                 aagaaagggg accaagccta cctcactggt gacgtgctgg tgatggatga gctgggctac    780  
               
               
                   
               
               
                 ctgtacttcc gagaccgcac aggggacacg ttccgctgga aaggggagaa tgtgtctacc    840  
               
               
                   
               
               
                 actgaagtgg agggcacact cagccgcctg cttcagatgg cagatgtggc tgtttatggt    900  
               
               
                   
               
               
                 gttgaggtgc caggagctga gggccgagca ggaatggctg ctgtggcaag ccccactagc    960  
               
               
                   
               
               
                 aactgtgacc tggagagctt tgcacagacc ttgaaaaagg agctgcccct gtacgcccgc   1020  
               
               
                   
               
               
                 cccatcttcc tccgcttctt gcctgagctg cacaaaacag gaaccttcaa gttccagaag   1080  
               
               
                   
               
               
                 acagagttgc ggaaggaggg ctttgacccg tctgttgtga aagacccact cttctatttg   1140  
               
               
                   
               
               
                 gatgcccgga caggctgcta tgttgcactg gaccaagagg cctatacccg catccaggca   1200  
               
               
                   
               
               
                 ggcgaggaga agctgtgatt tcccccacat ccctctgagg gccagaggat gctggattca   1260  
               
               
                   
               
               
                 gagccccagc ttccactcca gaaggggtct gggcaaggcc agaccaaagc tagcagggcc   1320  
               
               
                   
               
               
                 cgcaccttca ccctaggtgc tgatccccct                                    1350  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 63  
               
               
                 &lt;211&gt; LENGTH: 405  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Rattus norvegicus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 63  
               
               
                   
               
               
                 Asp Gln Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ala Leu Val  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Tyr Tyr Gly Phe Arg Met Arg Pro Asp Asp Ile Val Tyr Asp Cys Leu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Pro Leu Tyr His Ser Ala Gly Asn Ile Val Gly Ile Gly Gln Cys Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Leu His Gly Met Thr Val Val Ile Arg Lys Lys Phe Ser Ala Ser Arg  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Phe Trp Asp Asp Cys Ile Lys Tyr Asn Cys Thr Ile Val Gln Tyr Ile  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Glu Leu Cys Arg Tyr Leu Leu Asn Gln Pro Pro Arg Glu Ala Glu  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Arg His Lys Val Arg Met Ala Leu Gly Asn Gly Leu Arg Gln Ser  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Ile Trp Thr Asp Phe Ser Ser Arg Phe His Ile Pro Lys Val Ala Glu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Leu Gly Asn Phe Asp Ser  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Gln Val Gly Ala Cys Gly Phe Asn Ser Arg Ile Leu Ser Phe Val Tyr  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Pro Ile Arg Leu Val Arg Val Asn Glu Asp Thr Met Glu Leu Ile Arg  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Gly Pro Asp Gly Val Cys Ile Pro Cys Gln Pro Gly Gln Pro Gly Gln  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Leu Val Gly Arg Ile Ile Gln Gln Asp Pro Leu Arg Arg Phe Asp Gly  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Tyr Leu Asn Gln Gly Ala Asn Asn Lys Lys Ile Ala Ser Asp Val Phe  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Lys Lys Gly Asp Gln Ala Tyr Leu Thr Gly Asp Val Leu Val Met Asp  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Glu Leu Gly Tyr Leu Tyr Phe Arg Asp Arg Thr Gly Asp Thr Phe Arg  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Trp Lys Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Thr Leu Ser  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Arg Leu Leu Gln Met Ala Asp Val Ala Val Tyr Gly Val Glu Val Pro  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Gly Ala Glu Gly Arg Ala Gly Met Ala Ala Val Ala Ser Pro Thr Ser  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Asn Cys Asp Leu Glu Ser Phe Ala Gln Thr Leu Lys Lys Glu Leu Pro  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Leu Tyr Ala Arg Pro Ile Phe Leu Arg Phe Leu Pro Glu Leu His Lys  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Thr Gly Thr Phe Lys Phe Gln Lys Thr Glu Leu Arg Lys Glu Gly Phe  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Asp Pro Ser Val Val Lys Asp Pro Leu Phe Tyr Leu Asp Ala Arg Thr  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gly Cys Tyr Val Ala Leu Asp Gln Glu Ala Tyr Thr Arg Ile Gln Ala  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Glu Glu Lys Leu  
               
               
                                 405  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 64  
               
               
                 &lt;211&gt; LENGTH: 3217  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 64  
               
               
                   
               
               
                 atgcgggctc ctggagcagg aacagcctct gtggcctcac tggcgctgct ttggtttctg     60  
               
               
                   
               
               
                 ggacttccgt ggacctggag cgcggcggcg gcgttctgtg tgtacgtggg tggcggcggc    120  
               
               
                   
               
               
                 tggcgctttc tgcgtatcgt ctgcaagacg gcgaggcgag acctctttgg cctctctgtt    180  
               
               
                   
               
               
                 ctgattcgtg ttcggctaga gctgcgacga caccggcgag caggagacac gatcccgtgc    240  
               
               
                   
               
               
                 atcttccagg ctgtggcccg gcgacaacca gagcgcctgg cactggtgga cgccagtagt    300  
               
               
                   
               
               
                 ggtatatgct ggaccttcgc acagctggac acctactcca atgctgtagc caacctgttc    360  
               
               
                   
               
               
                 cgccagctgg gctttgcacc aggcgatgtg gtggctgtgt tcctggaggg ccggccggag    420  
               
               
                   
               
               
                 ttcgtgggac tgtggctggg cctggccaag gccggtgtgg tggctgctct tctcaatgtc    480  
               
               
                   
               
               
                 aacctgaggc gggagcccct ggccttctgc ctgggcacat cagctgccaa ggccctcatt    540  
               
               
                   
               
               
                 tatggcgggg agatggcagc ggcggtggcg gaggtgagcg agcagctggg gaagagcctc    600  
               
               
                   
               
               
                 ctcaagttct gctctggaga tctggggcct gagagcatcc tgcctgacac gcagctcctg    660  
               
               
                   
               
               
                 gaccccatgc ttgctgaggc gcccaccaca cccctggcac aagccccagg caagggcatg    720  
               
               
                   
               
               
                 gatgatcggc tgttttacat ctatacttct gggaccaccg ggcttcctaa ggctgccatt    780  
               
               
                   
               
               
                 gtggtgcaca gcaggtacta ccgcattgct gcctttggcc accattccta cagcatgcgt    840  
               
               
                   
               
               
                 gccgccgatg tgctctatga ctgcctgcca ctctaccact ctgcagggaa catcatgggt    900  
               
               
                   
               
               
                 gtggggcagt gcgtcatcta cgggttgacg gtggtactgc gcaagaagtt ctccgccagc    960  
               
               
                   
               
               
                 cgcttctggg atgactgtgt caagtacaat tgcacggtag tggatgacat aggtgaaatc   1020  
               
               
                   
               
               
                 tgccgctacc tgctgaggca gccggttcgc gacgtggagc agcgacaccg cgtgcgcctg   1080  
               
               
                   
               
               
                 gccgtgggta atgggctgcg gccagccatc tgggaggagt tcacgcagcg cttcggtgtg   1140  
               
               
                   
               
               
                 ccacagatcg gcgagttcta cggcgctacc gagtgcaact gcagcattgc caacatggac   1200  
               
               
                   
               
               
                 ggcaaggtcg gctcctgcgg cttcaacagc cgtatcctca cgcatgtgta ccccatccgt   1260  
               
               
                   
               
               
                 ctggtcaagg tcaatgagga cacgatggag ccactgcggg actccgaggg cctctgcatc   1320  
               
               
                   
               
               
                 ccgtgccagc ccggggaacc cggccttctc gtgggccaga tcaaccagca ggaccctctg   1380  
               
               
                   
               
               
                 cggcgtttcg atggttatgt tagtgacagt gccaccaaca agaagattgc ccacagcgtt   1440  
               
               
                   
               
               
                 ttccgaaagg gcgatagcgc ctacctctca ggtgacgtgc tagtgatgga cgagctgggc   1500  
               
               
                   
               
               
                 tacatgtatt tccgtgaccg cagcggggac accttccgct ggcgcgggga gaacgtgtcc   1560  
               
               
                   
               
               
                 accacggagg tggaagccgt gctgagccgc ctactgggcc agacggacgt ggctgtgtat   1620  
               
               
                   
               
               
                 ggggtggctg tgccaggagt ggaggggaaa gctggcatgg cagccatcgc agatccccac   1680  
               
               
                   
               
               
                 agccagttgg accctaactc aatgtaccag gaattacaga aggttcttgc atcctatgct   1740  
               
               
                   
               
               
                 cggcccatct tcctgcgtct tctgccccag gtggatacca caggcacctt caagatccag   1800  
               
               
                   
               
               
                 aagacccggc tgcagcgtga aggctttgac ccccgtcaga cctcagacag gctcttcttt   1860  
               
               
                   
               
               
                 ctagacctga agtccggcac gaggtatcta cccctggatg agagagtcca tgcccgcatt   1920  
               
               
                   
               
               
                 tgcgcaggcg acttctcact ctgagcctgg agagtgggct gggcctggac tcctgagacc   1980  
               
               
                   
               
               
                 tgggagcctg acacccctct tcgggtgctt ctcctgcctg gccacatgga cagcagcacc   2040  
               
               
                   
               
               
                 tgtgagagta ggaaaatgga acctgagtgg ctgggacccc tctcctactt cccactatgc   2100  
               
               
                   
               
               
                 atccattttg cctctgcctt gatctttttc tccatctctt ttctccctac ccagcaggag   2160  
               
               
                   
               
               
                 ccccacaaac acatgttggc tgctgtgtcc tgcagttgga ccagtgtcca ggggtacagg   2220  
               
               
                   
               
               
                 cttcaggctg tgacccacac tggtacccac ctccctttcc tattttgcct taggttcatc   2280  
               
               
                   
               
               
                 cacggttccc ctgtggagca agtgggggcc cacatagctg ctgtccctgc tgagggttgg   2340  
               
               
                   
               
               
                 tagcaatcac accctcatgt cagctgggag acacgcgcag tctcccactg acccccaatc   2400  
               
               
                   
               
               
                 aactgaaaat attgttttga ctactttttg tttttttgtt tttttgtttt tttttttttt   2460  
               
               
                   
               
               
                 cgagacagag tttctctgta tagccctggc tgtcctggaa ctcactttgt agaccaggct   2520  
               
               
                   
               
               
                 ggcctcgaac tcaaaaatcc tcctgactct gcctctgctt cccaagtgct gggattaaag   2580  
               
               
                   
               
               
                 acgtgcgcca ccaccgcctg gctgttttgt atttttgttt tgttttgacg atagggtctc   2640  
               
               
                   
               
               
                 actgtggagg ccaagctggc ctcagactcc ccaccccatt gcctctgggc accattctat   2700  
               
               
                   
               
               
                 attctcagac tgatgacaat gcactagtgt ccctaggagt cttgagtctg cactttcccc   2760  
               
               
                   
               
               
                 tcatagcctc aagcttccag aactgactct gatcacttgg atgtggctag tgttggctct   2820  
               
               
                   
               
               
                 acccacatgt gtcaattcag gggtccccag gcatagtctc tggaagccct cacccggaaa   2880  
               
               
                   
               
               
                 aagcttggag agacccagga aggttgttgt gttctcttgg gcaccccctg gtggcagtcc   2940  
               
               
                   
               
               
                 tgggcatgct tccgcactgt actggtgcat atagcccaga cctatgacat ttgaggtcta   3000  
               
               
                   
               
               
                 cccttctggc tcctgtggtc cccattgaga tccttggtga ctcacctcag tcaccaagca   3060  
               
               
                   
               
               
                 gagcctctgc ctgccttcat cttcaaggtc atgaaggatg tggacagagc agctacaggc   3120  
               
               
                   
               
               
                 tgccagcagt caaccacatg agagtgttac ttccttgttg gtttttaaaa aataaatgtg   3180  
               
               
                   
               
               
                 ctgagcctcg aaaaaaaaaa aaaaaaaaaa aaaaaaa                            3217  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 65  
               
               
                 &lt;211&gt; LENGTH: 647  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 65  
               
               
                   
               
               
                 Met Arg Ala Pro Gly Ala Gly Thr Ala Ser Val Ala Ser Leu Ala Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Trp Phe Leu Gly Leu Pro Trp Thr Trp Ser Ala Ala Ala Ala Phe  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Cys Val Tyr Val Gly Gly Gly Gly Trp Arg Phe Leu Arg Ile Val Cys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Thr Ala Arg Arg Asp Leu Phe Gly Leu Ser Val Leu Ile Arg Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Arg Leu Glu Leu Arg Arg His Arg Arg Ala Gly Asp Thr Ile Pro Cys  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ile Phe Gln Ala Val Ala Arg Arg Gln Pro Glu Arg Leu Ala Leu Val  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Ala Ser Ser Gly Ile Cys Trp Thr Phe Ala Gln Leu Asp Thr Tyr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Asn Ala Val Ala Asn Leu Phe Arg Gln Leu Gly Phe Ala Pro Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asp Val Val Ala Val Phe Leu Glu Gly Arg Pro Glu Phe Val Gly Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Trp Leu Gly Leu Ala Lys Ala Gly Val Val Ala Ala Leu Leu Asn Val  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asn Leu Arg Arg Glu Pro Leu Ala Phe Cys Leu Gly Thr Ser Ala Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Lys Ala Leu Ile Tyr Gly Gly Glu Met Ala Ala Ala Val Ala Glu Val  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Glu Gln Leu Gly Lys Ser Leu Leu Lys Phe Cys Ser Gly Asp Leu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Pro Glu Ser Ile Leu Pro Asp Thr Gln Leu Leu Asp Pro Met Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Glu Ala Pro Thr Thr Pro Leu Ala Gln Ala Pro Gly Lys Gly Met  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asp Asp Arg Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Ile Ala Ala Phe  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly His His Ser Tyr Ser Met Arg Ala Ala Asp Val Leu Tyr Asp Cys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Leu Pro Leu Tyr His Ser Ala Gly Asn Ile Met Gly Val Gly Gln Cys  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Val Ile Tyr Gly Leu Thr Val Val Leu Arg Lys Lys Phe Ser Ala Ser  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Arg Phe Trp Asp Asp Cys Val Lys Tyr Asn Cys Thr Val Val Asp Asp  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ile Gly Glu Ile Cys Arg Tyr Leu Leu Arg Gln Pro Val Arg Asp Val  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Glu Gln Arg His Arg Val Arg Leu Ala Val Gly Asn Gly Leu Arg Pro  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ala Ile Trp Glu Glu Phe Thr Gln Arg Phe Gly Val Pro Gln Ile Gly  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Ile Ala Asn Met Asp  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Lys Val Gly Ser Cys Gly Phe Asn Ser Arg Ile Leu Thr His Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Tyr Pro Ile Arg Leu Val Lys Val Asn Glu Asp Thr Met Glu Pro Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Arg Asp Ser Glu Gly Leu Cys Ile Pro Cys Gln Pro Gly Glu Pro Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Leu Val Gly Gln Ile Asn Gln Gln Asp Pro Leu Arg Arg Phe Asp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gly Tyr Val Ser Asp Ser Ala Thr Asn Lys Lys Ile Ala His Ser Val  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Phe Arg Lys Gly Asp Ser Ala Tyr Leu Ser Gly Asp Val Leu Val Met  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Asp Glu Leu Gly Tyr Met Tyr Phe Arg Asp Arg Ser Gly Asp Thr Phe  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Arg Trp Arg Gly Glu Asn Val Ser Thr Thr Glu Val Glu Ala Val Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ser Arg Leu Leu Gly Gln Thr Asp Val Ala Val Tyr Gly Val Ala Val  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Gly Val Glu Gly Lys Ala Gly Met Ala Ala Ile Ala Asp Pro His  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ser Gln Leu Asp Pro Asn Ser Met Tyr Gln Glu Leu Gln Lys Val Leu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ala Ser Tyr Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Gln Val Asp  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Thr Thr Gly Thr Phe Lys Ile Gln Lys Thr Arg Leu Gln Arg Glu Gly  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Phe Asp Pro Arg Gln Thr Ser Asp Arg Leu Phe Phe Leu Asp Leu Lys  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Ser Gly Thr Arg Tyr Leu Pro Leu Asp Glu Arg Val His Ala Arg Ile  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Cys Ala Gly Asp Phe Ser Leu  
               
               
                                 645  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 66  
               
               
                 &lt;211&gt; LENGTH: 2338  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 66  
               
               
                   
               
               
                 gggcggaggc cgagcccagt cgccagctcc tgctctgctc ctctcccgcc tgccgccgcg     60  
               
               
                   
               
               
                 ctgcacgcct cgagcactcc ctcggccccg gcggggaccg gggaccccgc agctaccgcc    120  
               
               
                   
               
               
                 atgctgccag tgctctacac cggcctggcg gggctgctgc tgctgcctct gctgctcacc    180  
               
               
                   
               
               
                 tgctgctgcc cctacctcct ccaagatgtg cggtacttcc tgcggctggc caacatggcc    240  
               
               
                   
               
               
                 cggcgggtgc gcagctaccg gcagcggcga cccgtgcgta ccatcctgcg ggccttcctg    300  
               
               
                   
               
               
                 gaacaagcgc gcaagacccc acacaagccc ttcctgctgt tccgagacga gacgctcacc    360  
               
               
                   
               
               
                 tacgcccagg tggaccggcg cagcaaccaa gtggcgcggg cgctgcacga tcaactgggc    420  
               
               
                   
               
               
                 ctacgacagg gggattgcgt agccctcttc atgggcaatg agccggccta cgtgtggatc    480  
               
               
                   
               
               
                 tggctgggac tgctcaaact gggctgtccc atggcgtgcc tcaactacaa cattcgtgcc    540  
               
               
                   
               
               
                 aagtctctgc tgcactgctt tcaatgctgc ggggcgaagg tgctgctggc ctccccagat    600  
               
               
                   
               
               
                 ctacaagaag ctgtggagga ggttcttcca accctgaaaa aggatgccgt gtccgtcttt    660  
               
               
                   
               
               
                 tacgtaagca gaacttctaa cacaaatggt gtggacacaa tactggacaa agtagacgga    720  
               
               
                   
               
               
                 gtgtcggcgg aacccacccc ggagtcgtgg aggtctgaag tcacttttac cacgccagca    780  
               
               
                   
               
               
                 gtatacattt atacttcggg aaccacaggt cttccaaaaa gcggaaccat caatcatcat    840  
               
               
                   
               
               
                 cgcctaaggt atgggacaag ccttgctatg tcgagtggga atcacggcca aggatgtcat    900  
               
               
                   
               
               
                 ctataccaac aatgcccctg ttccaacagt gcaacgctca agatcggcct tcacggatgc    960  
               
               
                   
               
               
                 atcctgggtt ggggctactt taaccttggc ggggcaaatt ctcaagcaag ccaattttgg   1020  
               
               
                   
               
               
                 gaacgactgg caggaaatac aacgtcaacg gtcattcagt acattggtga actgcttcgg   1080  
               
               
                   
               
               
                 tacctgtgca acacaccgca gaaaccaaat gaccgggacc acaaagtgaa aaaagccctg   1140  
               
               
                   
               
               
                 ggaaatggct tacgaggaga tgtgtggaga gagttcatca agagatttgg ggacatccac   1200  
               
               
                   
               
               
                 gtgtatgagt tctacgcatc cactgaaggc aacattggat ttgtgaacta tccaaggaaa   1260  
               
               
                   
               
               
                 atcggtgctg tcgggagagc aaactaccta caaagaaaag ttgcaaggta tgagctgatc   1320  
               
               
                   
               
               
                 aagtatgacg tggagaagga cgagccggtc cgtgacgcaa atggatattg catcaaagtc   1380  
               
               
                   
               
               
                 cccaaaggtg aggttggact cttggtttgc aaaatcacac agctcacacc atttattggc   1440  
               
               
                   
               
               
                 tatgctggag gaaagaccca gacagagaag aaaaaactca gagatgtctt taagaaaggc   1500  
               
               
                   
               
               
                 gacatctact tcaacagcgg agacctcctg atgatcgacc gtgagaactt cgtctacttt   1560  
               
               
                   
               
               
                 cacgacaggg ttggagatac tttccggtgg aaaggagaga acgtagctac cacagaagtc   1620  
               
               
                   
               
               
                 gctgacatcg tgggactggt agattttgtt gaagaagtga atgtgtatgg cgtgcctgtg   1680  
               
               
                   
               
               
                 ccaggtcatg agggtcgaat tgggatggcc tccctcaaga tcaaagaaaa ctacgagttc   1740  
               
               
                   
               
               
                 aatggaaaga aactctttca acacatcgcg gagtacctgc ccagttacgc gaggcctcgg   1800  
               
               
                   
               
               
                 ttcctgagga tacaagatac cattgagatc actgggactt ttaaacaccg caaagtgacc   1860  
               
               
                   
               
               
                 ctgatggaag agggcttcaa tcccacagtc atcaaagata ccttgtattt catggatgat   1920  
               
               
                   
               
               
                 gcagagaaaa catttgtgcc catgactgag aacatttata atgccataat tgataaaact   1980  
               
               
                   
               
               
                 ctgaagctct gaatattccc tggtggttta gctcatgaca tttccagaaa gaaactcgat   2040  
               
               
                   
               
               
                 agacctcgca gagccacttc atacgtagaa tccaacttta acttgattga agactataag   2100  
               
               
                   
               
               
                 gtgcgatttt atttttagga aattattcat taaaaggata gttttttttt ttttttttaa   2160  
               
               
                   
               
               
                 ttacacctga acctttgcaa gtaaaaagat ttagagacaa ttatttttca atgtgcacct   2220  
               
               
                   
               
               
                 gccatttgtc cttgcaaact aagcttcttg gagagagggc cttatttttt taaagacata   2280  
               
               
                   
               
               
                 ataaactata ttaacactaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaa     2338  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 67  
               
               
                 &lt;211&gt; LENGTH: 623  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 67  
               
               
                   
               
               
                 Met Leu Pro Val Leu Tyr Thr Gly Leu Ala Gly Leu Leu Leu Leu Pro  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Leu Leu Thr Cys Cys Cys Pro Tyr Leu Leu Gln Asp Val Arg Tyr  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Leu Arg Leu Ala Asn Met Ala Arg Arg Val Arg Ser Tyr Arg Gln  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Arg Arg Pro Val Arg Thr Ile Leu Arg Ala Phe Leu Glu Gln Ala Arg  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Lys Thr Pro His Lys Pro Phe Leu Leu Phe Arg Asp Glu Thr Leu Thr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Tyr Ala Gln Val Asp Arg Arg Ser Asn Gln Val Ala Arg Ala Leu His  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Gln Leu Gly Leu Arg Gln Gly Asp Cys Val Ala Leu Phe Met Gly  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Asn Glu Pro Ala Tyr Val Trp Ile Trp Leu Gly Leu Leu Lys Leu Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Cys Pro Met Ala Cys Leu Asn Tyr Asn Ile Arg Ala Lys Ser Leu Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 His Cys Phe Gln Cys Cys Gly Ala Lys Val Leu Leu Ala Ser Pro Asp  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Leu Gln Glu Ala Val Glu Glu Val Leu Pro Thr Leu Lys Lys Asp Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Val Ser Val Phe Tyr Val Ser Arg Thr Ser Asn Thr Asn Gly Val Asp  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Thr Ile Leu Asp Lys Val Asp Gly Val Ser Ala Glu Pro Thr Pro Glu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Ser Trp Arg Ser Glu Val Thr Phe Thr Thr Pro Ala Val Tyr Ile Tyr  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Thr Ser Gly Thr Thr Gly Leu Pro Lys Ser Gly Thr Ile Asn His His  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Arg Leu Arg Tyr Gly Thr Ser Leu Ala Met Ser Ser Gly Asn His Gly  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Gln Gly Cys His Leu Tyr Gln Gln Cys Pro Cys Ser Asn Ser Ala Thr  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Leu Lys Ile Gly Leu His Gly Cys Ile Leu Gly Trp Gly Tyr Phe Asn  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Leu Gly Gly Ala Asn Ser Gln Ala Ser Gln Phe Trp Glu Arg Leu Ala  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Gly Asn Thr Thr Ser Thr Val Ile Gln Tyr Ile Gly Glu Leu Leu Arg  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Tyr Leu Cys Asn Thr Pro Gln Lys Pro Asn Asp Arg Asp His Lys Val  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Lys Lys Ala Leu Gly Asn Gly Leu Arg Gly Asp Val Trp Arg Glu Phe  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Ile Lys Arg Phe Gly Asp Ile His Val Tyr Glu Phe Tyr Ala Ser Thr  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Glu Gly Asn Ile Gly Phe Val Asn Tyr Pro Arg Lys Ile Gly Ala Val  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gly Arg Ala Asn Tyr Leu Gln Arg Lys Val Ala Arg Tyr Glu Leu Ile  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Lys Tyr Asp Val Glu Lys Asp Glu Pro Val Arg Asp Ala Asn Gly Tyr  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Cys Ile Lys Val Pro Lys Gly Glu Val Gly Leu Leu Val Cys Lys Ile  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Thr Gln Leu Thr Pro Phe Ile Gly Tyr Ala Gly Gly Lys Thr Gln Thr  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Glu Lys Lys Lys Leu Arg Asp Val Phe Lys Lys Gly Asp Ile Tyr Phe  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Asn Ser Gly Asp Leu Leu Met Ile Asp Arg Glu Asn Phe Val Tyr Phe  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 His Asp Arg Val Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Thr Thr Glu Val Ala Asp Ile Val Gly Leu Val Asp Phe Val Glu Glu  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Val Asn Val Tyr Gly Val Pro Val Pro Gly His Glu Gly Arg Ile Gly  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Met Ala Ser Leu Lys Ile Lys Glu Asn Tyr Glu Phe Asn Gly Lys Lys  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Leu Phe Gln His Ile Ala Glu Tyr Leu Pro Ser Tyr Ala Arg Pro Arg  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Phe Leu Arg Ile Gln Asp Thr Ile Glu Ile Thr Gly Thr Phe Lys His  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Arg Lys Val Thr Leu Met Glu Glu Gly Phe Asn Pro Thr Val Ile Lys  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Asp Thr Leu Tyr Phe Met Asp Asp Ala Glu Lys Thr Phe Val Pro Met  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Thr Glu Asn Ile Tyr Asn Ala Ile Ile Asp Lys Thr Leu Lys Leu  
               
               
                     610                 615                 620  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 68  
               
               
                 &lt;211&gt; LENGTH: 1998  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 68  
               
               
                   
               
               
                 gaaagctctg agagcgggtg cagtctggcc tggcgtctcg cgtacctggc ccgggagcag     60  
               
               
                   
               
               
                 ccgacacaca ccttcctcat ccacggcgcg cagcgcttta gctacgcgga ggctgagcgc    120  
               
               
                   
               
               
                 gagagcaacc ggattgctcg cgcctttctg cgcgcacggg gctggaccgg gggccgccga    180  
               
               
                   
               
               
                 ggctcgggca ggggcagcac tgaggaaggc gcacgcgtgg cgcctccggc tggagatgcg    240  
               
               
                   
               
               
                 gctgctagag ggacgaccgc gccccctctg gcacccgggg cgaccgtggc gctgctcctc    300  
               
               
                   
               
               
                 ccagcgggcc cggatttcct ttggatttgg ttcggactgg ccaaagctgg cctgcgcacg    360  
               
               
                   
               
               
                 gcctttgtgc ccaccgcttt acgccgagga cccctgctgc actgcctccg cagctgcggt    420  
               
               
                   
               
               
                 gcgagtgcgc tcgtgctggc cacagagttc ctggagtccc tggagccgga cctgccggcc    480  
               
               
                   
               
               
                 ttgagagcca tggggctcca cctatgggcg acgggccctg aaactaatgt agctggaatc    540  
               
               
                   
               
               
                 agcaatttgc tatcggaagc agcagaccaa gtggatgagc cagtgccggg gtacctctct    600  
               
               
                   
               
               
                 gccccccaga acataatgga cacctgcctg tacatcttca cctctggcac tactggcctg    660  
               
               
                   
               
               
                 cccaaggctg ctcgaatcag tcatctgaag gttctacagt gccagggatt ctaccatctg    720  
               
               
                   
               
               
                 tgtggagtcc accaggagga cgtgatctac ctcgcactcc cactgtacca catgtctggc    780  
               
               
                   
               
               
                 tcccttctgg gcattgtggg ctgcttgggc attggggcca ccgtggtgct gaaacccaag    840  
               
               
                   
               
               
                 ttctcagcta gccagttctg ggacgattgc cagaaacaca gggtgacagt gttccagtac    900  
               
               
                   
               
               
                 attggggagt tgtgccgata cctcgtcaac cagcccccga gcaaggcaga gtttgaccat    960  
               
               
                   
               
               
                 aaggtgcgct tggcagtggg cagtgggttg cgcccagaca cctgggagcg tttcctgcgg   1020  
               
               
                   
               
               
                 cgatttggac ctctgcagat actggagacg tatggcatga cagagggcaa cgtagctacg   1080  
               
               
                   
               
               
                 ttcaattaca caggacggca gggtgcagtg gggcgagctt cctggcttta caagcacatc   1140  
               
               
                   
               
               
                 ttccccttct ccttgattcg atacgatgtc atgacagggg agcctattcg gaatgcccag   1200  
               
               
                   
               
               
                 gggcactgca tgaccacatc tccaggtgag ccaggcctac tggtggcccc agtgagccag   1260  
               
               
                   
               
               
                 cagtccccct tcctgggcta tgctggggct ccggagctgg ccaaggacaa gctgctgaag   1320  
               
               
                   
               
               
                 gatgtcttct ggtctgggga cgttttcttc aatactgggg acctcttggt ctgtgatgag   1380  
               
               
                   
               
               
                 caaggctttc ttcacttcca cgatcgtact ggagacacca tcaggtggaa gggagagaat   1440  
               
               
                   
               
               
                 gtggccacaa ctgaagtggc tgaggtcttg gagaccctgg acttccttca ggaggtgaac   1500  
               
               
                   
               
               
                 atctatggag tcacggtgcc agggcacgaa ggcagggcag gcatggcggc cttggctctg   1560  
               
               
                   
               
               
                 cggcccccgc aggctctgaa cctggtgcag ctctacagcc atgtttctga gaacttgcca   1620  
               
               
                   
               
               
                 ccgtatgccc gacctcggtt tctcaggctc caggaatctt tggccactac tgagaccttc   1680  
               
               
                   
               
               
                 aaacagcaga aggttaggat ggccaatgag ggctttgacc ccagtgtact gtctgaccca   1740  
               
               
                   
               
               
                 ctctatgttc tggaccaaga tataggggcc tacctgcccc tcacacctgc ccggtacagt   1800  
               
               
                   
               
               
                 gccctcctgt ctggagacct tcgaatctga aaccttccac ttgagggagg ggctcggagg   1860  
               
               
                   
               
               
                 gtacaggcca ccatggctgc accagggagg gttttcgggt atcttttgta tatggagtca   1920  
               
               
                   
               
               
                 ttattttgta ataaacagct ggagcttaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa   1980  
               
               
                   
               
               
                 aaaaaaaaaa aaaaaaaa                                                 1998  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 69  
               
               
                 &lt;211&gt; LENGTH: 609  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 69  
               
               
                   
               
               
                 Glu Ser Ser Glu Ser Gly Cys Ser Leu Ala Trp Arg Leu Ala Tyr Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ala Arg Glu Gln Pro Thr His Thr Phe Leu Ile His Gly Ala Gln Arg  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Ser Tyr Ala Glu Ala Glu Arg Glu Ser Asn Arg Ile Ala Arg Ala  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Phe Leu Arg Ala Arg Gly Trp Thr Gly Gly Arg Arg Gly Ser Gly Arg  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Gly Ser Thr Glu Glu Gly Ala Arg Val Ala Pro Pro Ala Gly Asp Ala  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Ala Arg Gly Thr Thr Ala Pro Pro Leu Ala Pro Gly Ala Thr Val  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Ala Leu Leu Leu Pro Ala Gly Pro Asp Phe Leu Trp Ile Trp Phe Gly  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Leu Ala Lys Ala Gly Leu Arg Thr Ala Phe Val Pro Thr Ala Leu Arg  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Arg Gly Pro Leu Leu His Cys Leu Arg Ser Cys Gly Ala Ser Ala Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Val Leu Ala Thr Glu Phe Leu Glu Ser Leu Glu Pro Asp Leu Pro Ala  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Leu Arg Ala Met Gly Leu His Leu Trp Ala Thr Gly Pro Glu Thr Asn  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Val Ala Gly Ile Ser Asn Leu Leu Ser Glu Ala Ala Asp Gln Val Asp  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Glu Pro Val Pro Gly Tyr Leu Ser Ala Pro Gln Asn Ile Met Asp Thr  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Cys Leu Tyr Ile Phe Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Arg Ile Ser His Leu Lys Val Leu Gln Cys Gln Gly Phe Tyr His Leu  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Cys Gly Val His Gln Glu Asp Val Ile Tyr Leu Ala Leu Pro Leu Tyr  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 His Met Ser Gly Ser Leu Leu Gly Ile Val Gly Cys Leu Gly Ile Gly  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Ala Thr Val Val Leu Lys Pro Lys Phe Ser Ala Ser Gln Phe Trp Asp  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Asp Cys Gln Lys His Arg Val Thr Val Phe Gln Tyr Ile Gly Glu Leu  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Cys Arg Tyr Leu Val Asn Gln Pro Pro Ser Lys Ala Glu Phe Asp His  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Lys Val Arg Leu Ala Val Gly Ser Gly Leu Arg Pro Asp Thr Trp Glu  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Arg Phe Leu Arg Arg Phe Gly Pro Leu Gln Ile Leu Glu Thr Tyr Gly  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Met Thr Glu Gly Asn Val Ala Thr Phe Asn Tyr Thr Gly Arg Gln Gly  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ala Val Gly Arg Ala Ser Trp Leu Tyr Lys His Ile Phe Pro Phe Ser  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Leu Ile Arg Tyr Asp Val Met Thr Gly Glu Pro Ile Arg Asn Ala Gln  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly His Cys Met Thr Thr Ser Pro Gly Glu Pro Gly Leu Leu Val Ala  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Pro Val Ser Gln Gln Ser Pro Phe Leu Gly Tyr Ala Gly Ala Pro Glu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Leu Ala Lys Asp Lys Leu Leu Lys Asp Val Phe Trp Ser Gly Asp Val  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Phe Phe Asn Thr Gly Asp Leu Leu Val Cys Asp Glu Gln Gly Phe Leu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 His Phe His Asp Arg Thr Gly Asp Thr Ile Arg Trp Lys Gly Glu Asn  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Val Ala Thr Thr Glu Val Ala Glu Val Leu Glu Thr Leu Asp Phe Leu  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Gln Glu Val Asn Ile Tyr Gly Val Thr Val Pro Gly His Glu Gly Arg  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Ala Gly Met Ala Ala Leu Ala Leu Arg Pro Pro Gln Ala Leu Asn Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Val Gln Leu Tyr Ser His Val Ser Glu Asn Leu Pro Pro Tyr Ala Arg  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Arg Phe Leu Arg Leu Gln Glu Ser Leu Ala Thr Thr Glu Thr Phe  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Lys Gln Gln Lys Val Arg Met Ala Asn Glu Gly Phe Asp Pro Ser Val  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu Ser Asp Pro Leu Tyr Val Leu Asp Gln Asp Ile Gly Ala Tyr Leu  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Pro Leu Thr Pro Ala Arg Tyr Ser Ala Leu Leu Ser Gly Asp Leu Arg  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ile  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 70  
               
               
                 &lt;211&gt; LENGTH: 2710  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 70  
               
               
                   
               
               
                 atgctgcttg gagcctctct ggtgggggcg ctactgttct ccaagctagt gctgaagctg     60  
               
               
                   
               
               
                 ccctggaccc aggtgggatt ctccctgttg ctcctgtact tggggtctgg tggctggcgt    120  
               
               
                   
               
               
                 ttcatccggg tcttcatcaa gacggtcagg agagatatct ttggtggcat ggtgctcctg    180  
               
               
                   
               
               
                 aaggtgaaga ccaaggtgcg acggtacctt caggagcgga agacggtgcc cctgctgttt    240  
               
               
                   
               
               
                 gcttcaatgg tacagcgcca cccggacaag acagccctga ttttcgaggg cacagacact    300  
               
               
                   
               
               
                 cactggacct tccgccagct ggatgagtac tccagtagtg tggccaactt cctgcaggcc    360  
               
               
                   
               
               
                 cggggcctgg cctcaggcaa tgtagttgcc ctctttatgg aaaaccgcaa tgagtttgtg    420  
               
               
                   
               
               
                 ggtctgtggc taggcatggc caagctgggc gtggaggcgg ctctcatcaa caccaacctt    480  
               
               
                   
               
               
                 aggcgggatg ccctgcgcca ctgtcttgac acctcaaagg cacgagctct catctttggc    540  
               
               
                   
               
               
                 agtgagatgg cctcagctat ctgtgagatc catgctagcc tggagcccac actcagcctc    600  
               
               
                   
               
               
                 ttctgctctg gatcctggga gcccagcaca gtgcccgtca gcacagagca tctggaccct    660  
               
               
                   
               
               
                 cttctggaag atgccccgaa gcacctgccc agtcacccag acaagggttt tacagataag    720  
               
               
                   
               
               
                 ctcttctaca tctacacatc gggcaccacg gggctaccca aagctgccat tgtggtgcac    780  
               
               
                   
               
               
                 agcaggtatt atcgtatggc ttccctggtg tactatggat tccgcatgcg gcctgatgac    840  
               
               
                   
               
               
                 attgtctatg actgcctccc cctctaccac tcaagcagga aacatcgtgg ggattggcag    900  
               
               
                   
               
               
                 tgcttactcc acggcatgac tgtggtgatc cggaagaagt tctcagcctc ccggttctgg    960  
               
               
                   
               
               
                 gatgattgta tcaagtacaa ctgcacagtg gtacagtaca ttggcgagct ctgccgctac   1020  
               
               
                   
               
               
                 tcctgaacc agccaccccg tgaggctgag tctcggcaca aggtgcgcat ggcactgggc    1080  
               
               
                   
               
               
                 acggtctcc ggcagtccat ctggaccgac ttctccagcc gtttccacat cccccaggtg    1140  
               
               
                   
               
               
                 ctgagttct atggggccac tgaatgcaac tgtagcctgg gcaactttga cagccgggtg    1200  
               
               
                   
               
               
                 gggcctgtg gcttcaatag ccgcatcctg tcctttgtgt accctatccg tttggtacgt    1260  
               
               
                   
               
               
                 tcaatgagg ataccatgga actgatccgg ggacccgatg gagtctgcat tccctgtcaa    1320  
               
               
                   
               
               
                 caggtcagc caggccagct ggtgggtcgc atcatccagc aggaccctct gcgccgtttc    1380  
               
               
                   
               
               
                 acgggtacc tcaaccaggg tgccaacaac aagaagattg ctaatgatgt cttcaagaag    1440  
               
               
                   
               
               
                 gggaccaag cctacctcac tggtgacgtc ctggtgatgg atgagctggg ttacctgtac    1500  
               
               
                   
               
               
                 tccgagatc gcactgggga cacgttccgc tggaaagggg agaatgtatc taccactgag    1560  
               
               
                   
               
               
                 tggagggca cactcagccg cctgcttcat atggcagatg tggcagttta tggtgttgag    1620  
               
               
                   
               
               
                 tgccaggaa ctgaaggccg agcaggaatg gctgccgttg caagtcccat cagcaactgt    1680  
               
               
                   
               
               
                 acctggaga gctttgcaca gaccttgaaa aaggagctgc ctctgtatgc ccgccccatc    1740  
               
               
                   
               
               
                 tcctgcgct tcttgcctga gctgcacaag acagggacct tcaagttcca gaagacagag    1800  
               
               
                   
               
               
                 tgcggaagg agggctttga cccatctgtt gtgaaagacc cgctgttcta tctggatgct    1860  
               
               
                   
               
               
                 ggaagggct gctacgttgc actggaccag gaggcctata cccgcatcca ggcaggcgag    1920  
               
               
                   
               
               
                 agaagctgt gatttccccc tacatccctc tgagggccag aagatgctgg attcagagcc    1980  
               
               
                   
               
               
                 tagcgtcca ccccagaggg tcctgggcaa tgccagacca aagctagcag ggcccgcacc    2040  
               
               
                   
               
               
                 ccgccccta ggtgctgatc tcccctctcc caaactgcca agtgactcac tgccgcttcc    2100  
               
               
                   
               
               
                 cgaccctcc agaggctttc tgtgaaagtc tcatccaagc tgtgtcttct ggtccaggcg    2160  
               
               
                   
               
               
                 ggcccctgg ccccagggtt tctgataggc tcctttagga tggtatcttg ggtccagcgg    2220  
               
               
                   
               
               
                 ccagggtgt gggagaggag tcactaagat ccctccaatc agaagggagc ttacaaagga    2280  
               
               
                   
               
               
                 ccaaggcaa agcctgtaga ctcaggaagc taagtggcca gagactatag tggccagtca    2340  
               
               
                   
               
               
                 cccatgtcc acagaggatc ttggtccaga gctgccaaag tgtcacctct ccctgcctgc    2400  
               
               
                   
               
               
                 cctctgggg aaaagaggac agcatgtggc cactgggcac ctgtctcaag aagtcaggat    2460  
               
               
                   
               
               
                 acacactca gtccttgttt ctccaggttc ccttgttctt gtctcgggga gggagggacg    2520  
               
               
                   
               
               
                 gtgtcctgt ctgtccttcc tgcctgtctg tgagtctgtg ttgcttctcc atctgtccta    2580  
               
               
                   
               
               
                 cctgagtgt gggtggaaca ggcatgagga gagtgtggct caggggccaa taaactctgc    2640  
               
               
                   
               
               
                 ttgactcct cttaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa    2700  
               
               
                   
               
               
                 aaaaaaaaa                                                           2710  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 71  
               
               
                 &lt;211&gt; LENGTH: 643  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 71  
               
               
                   
               
               
                 Met Leu Leu Gly Ala Ser Leu Val Gly Ala Leu Leu Gly Ser Lys Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val Leu Lys Leu Pro Trp Thr Gln Val Gly Phe Ser Leu Leu Leu Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Tyr Leu Gly Ser Gly Gly Trp Arg Phe Ile Arg Val Phe Ile Lys Thr  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Val Arg Arg Asp Ile Phe Gly Gly Met Val Leu Leu Lys Val Lys Thr  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Lys Val Arg Arg Tyr Leu Gln Glu Arg Lys Thr Val Pro Leu Leu Phe  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Ser Met Val Gln Arg His Pro Asp Lys Thr Ala Leu Ile Phe Glu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Thr Asp Thr His Trp Thr Phe Arg Gln Leu Asp Glu Tyr Ser Ser  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Val Ala Asn Phe Leu Gln Ala Arg Gly Leu Ala Ser Gly Asn Val  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Val Ala Leu Phe Met Glu Asn Arg Asn Glu Phe Val Gly Leu Trp Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Gly Met Ala Lys Leu Gly Val Glu Ala Ala Leu Ile Asn Thr Asn Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Arg Arg Asp Ala Leu Arg His Cys Leu Asp Thr Ser Lys Ala Arg Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Leu Ile Phe Gly Ser Glu Met Ala Ser Ala Ile Cys Glu Ile His Ala  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Leu Glu Pro Thr Leu Ser Leu Phe Cys Ser Gly Ser Trp Glu Pro  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Ser Thr Val Pro Val Ser Thr Glu His Leu Asp Pro Leu Leu Glu Asp  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Pro Lys His Leu Pro Ser His Pro Asp Lys Gly Phe Thr Asp Lys  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ser Leu Val Tyr Tyr  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly Phe Arg Met Arg Pro Asp Asp Ile Val Tyr Asp Cys Leu Pro Leu  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Tyr His Ser Ser Arg Lys His Arg Gly Asp Trp Gln Cys Leu Leu His  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Gly Met Thr Val Val Ile Arg Lys Lys Phe Ser Ala Ser Arg Phe Trp  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Asp Asp Cys Ile Lys Tyr Asn Cys Thr Val Val Gln Tyr Ile Gly Glu  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Leu Cys Arg Tyr Leu Leu Asn Gln Pro Pro Arg Glu Ala Glu Ser Arg  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 His Lys Val Arg Met Ala Leu Gly Asn Gly Leu Arg Gln Ser Ile Trp  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Thr Asp Phe Ser Ser Arg Phe His Ile Pro Gln Val Ala Glu Phe Tyr  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gly Ala Thr Glu Cys Asn Cys Ser Leu Gly Asn Phe Asp Ser Arg Val  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Ala Cys Gly Phe Asn Ser Arg Ile Leu Ser Phe Val Tyr Pro Ile  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Arg Leu Val Arg Val Asn Glu Asp Thr Met Glu Leu Ile Arg Gly Pro  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Asp Gly Val Cys Ile Pro Cys Gln Pro Gly Gln Pro Gly Gln Leu Val  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Gly Arg Ile Ile Gln Gln Asp Pro Leu Arg Arg Phe Asp Gly Tyr Leu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Asn Gln Gly Ala Asn Asn Lys Lys Ile Ala Asn Asp Val Phe Lys Lys  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Gly Asp Gln Ala Tyr Leu Thr Gly Asp Val Leu Val Met Asp Glu Leu  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Gly Tyr Leu Tyr Phe Arg Asp Arg Thr Gly Asp Thr Phe Arg Trp Lys  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Thr Leu Ser Arg Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Leu His Met Ala Asp Val Ala Val Tyr Gly Val Glu Val Pro Gly Thr  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Glu Gly Arg Ala Gly Met Ala Ala Val Ala Ser Pro Ile Ser Asn Cys  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Asp Leu Glu Ser Phe Ala Gln Thr Leu Lys Lys Glu Leu Pro Leu Tyr  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ala Arg Pro Ile Phe Leu Arg Phe Leu Pro Glu Leu His Lys Thr Gly  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Thr Phe Lys Phe Gln Lys Thr Glu Leu Arg Lys Glu Gly Phe Asp Pro  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ser Val Val Lys Asp Pro Leu Phe Tyr Leu Asp Ala Arg Lys Gly Cys  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Tyr Val Ala Leu Asp Gln Glu Ala Tyr Thr Arg Ile Gln Ala Gly Glu  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Glu Lys Leu  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 72  
               
               
                 &lt;211&gt; LENGTH: 2277  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 72  
               
               
                   
               
               
                 cactcatcag agctaagaga gactacacgc tctcatctac ttcagaaaga gccaatgcca     60  
               
               
                   
               
               
                 tgggtatttg gaagaaacta accttactgc tgttgctgct tctgctggtt ggcctggggc    120  
               
               
                   
               
               
                 agcccccatg gccagcagct atggctctgg ccctgcgttg gttcctggga gaccccacat    180  
               
               
                   
               
               
                 gccttgtgct gcttggcttg gcattgctgg gcagaccctg gatcagctcc tggatgcccc    240  
               
               
                   
               
               
                 actggctgag cctggtagga gcagctctta ccttattcct attgcctcta cagccacccc    300  
               
               
                   
               
               
                 cagggctacg ctggctgcat aaagatgtgg ctttcacctt caagatgctt ttctatggcc    360  
               
               
                   
               
               
                 taaagttcag gcgacgcctt aacaaacatc ctccagagac ctttgtggat gctttagagc    420  
               
               
                   
               
               
                 ggcaagcact ggcatggcct gaccgggtgg ccttggtgtg tactgggtct gagggctcct    480  
               
               
                   
               
               
                 caatcacaaa tagccagctg gatgccaggt cctgtcaggc agcatgggtc ctgaaagcaa    540  
               
               
                   
               
               
                 agctgaagga tgccgtaatc cagaacacaa gagatgctgc tgctatctta gttctcccgt    600  
               
               
                   
               
               
                 ccaagaccat ttctgctttg agtgtgtttc tggggttggc caagttgggc tgccctgtgg    660  
               
               
                   
               
               
                 cctggatcaa tccacacagc cgagggatgc ccttgctaca ctctgtacgg agctctgggg    720  
               
               
                   
               
               
                 ccagtgtgct gattgtggat ccagacctcc aggagaacct ggaagaagtc cttcccaagc    780  
               
               
                   
               
               
                 tgctagctga gaacattcac tgcttctacc ttggccacag ctcacccacc ccgggagtag    840  
               
               
                   
               
               
                 aggctctggg agcttccctg gatgctgcac cttctgaccc agtacctgcc agccttcgag    900  
               
               
                   
               
               
                 ctacgattaa gtggaaatct cctgccatat tcatctttac ttcagggacc actggactcc    960  
               
               
                   
               
               
                 aaagccagc catcttatca catgagcggg tcatacaagt gagcaacgtg ctgtccttct    1020  
               
               
                   
               
               
                 tggatgcag agctgatgat gtggtctatg acgtcctacc tctgtaccat acgatagggc    1080  
               
               
                   
               
               
                 tgtccttgg attccttggc tgcttacaag ttggagccac ctgtgtcctg gcccccaagt    1140  
               
               
                   
               
               
                 ctctgcctc ccgattctgg gctgagtgcc ggcagcatgg cgtaacagtg atcttgtatg    1200  
               
               
                   
               
               
                 gggtgaaat cctgcggtac ttgtgtaacg tccctgagca accagaagac aagatacata    1260  
               
               
                   
               
               
                 agtgcgctt ggccatggga actggacttc gggcaaatgt gtggaaaaac ttccagcaac    1320  
               
               
                   
               
               
                 ctttggtcc cattcggatc tgggaattct acggatccac agagggcaat gtgggcttaa    1380  
               
               
                   
               
               
                 gaactatgt gggccactgc ggggctgtgg gaaggaccag ctgcatcctt cgaatgctga    1440  
               
               
                   
               
               
                 tccctttga gcttgtacag ttcgacatag agacagcaga gcctctgagg gacaaacagg    1500  
               
               
                   
               
               
                 tttttgcat tcctgtggag ccaggaaagc caggacttct tttgaccaag gttcgaaaga    1560  
               
               
                   
               
               
                 ccaaccctt cctgggctac cgtggttccc aggccgagtc caatcggaaa cttgttgcga    1620  
               
               
                   
               
               
                 tgtacgacg cgtaggagac ctgtacttca acactgggga cgtgctgacc ttggaccagg    1680  
               
               
                   
               
               
                 aggcttctt ctactttcaa gaccgccttg gtgacacctt ccggtggaag ggcgaaaacg    1740  
               
               
                   
               
               
                 atctactgg agaggtggag tgtgttttgt ctagcctaga cttcctagag gaagtcaatg    1800  
               
               
                   
               
               
                 ctatggtgt gcctgtgcca gggtgtgagg gtaaggttgg catggctgct gtgaaactgg    1860  
               
               
                   
               
               
                 tcctgggaa gacttttgat gggcagaagc tataccagca tgtccgctcc tggctccctg    1920  
               
               
                   
               
               
                 ctatgccac acctcatttc atccgtatcc aggattccct ggagatcaca aacacctaca    1980  
               
               
                   
               
               
                 gctggtaaa gtcacggctg gtgcgtgagg gttttgatgt ggggatcatt gctgaccccc    2040  
               
               
                   
               
               
                 ctacatact ggacaacaag gcccagacct tccggagtct gatgccagat gtgtaccagg    2100  
               
               
                   
               
               
                 tgtgtgtga aggaacctgg aatctctgac cacctagcca actggaaggc aatccaaaag    2160  
               
               
                   
               
               
                 gtagagatt gacactagtc agcttcacaa agttgtccgg gttccagatg cccatggccc    2220  
               
               
                   
               
               
                 gtagtactt agagaataaa cttgaatgtg tatacaaaaa aaaaaaaaaa aaaaaaa       2277  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 73  
               
               
                 &lt;211&gt; LENGTH: 689  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 73  
               
               
                   
               
               
                 Met Gly Ile Trp Lys Lys Leu Thr Leu Leu Leu Leu Leu Leu Leu Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val Gly Leu Gly Gln Pro Pro Trp Pro Ala Ala Met Ala Leu Ala Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Arg Trp Phe Leu Gly Asp Pro Thr Cys Leu Val Leu Leu Gly Leu Ala  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Leu Leu Gly Arg Pro Trp Ile Ser Ser Trp Met Pro His Trp Leu Ser  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Leu Val Gly Ala Ala Leu Thr Leu Phe Leu Leu Pro Leu Gln Pro Pro  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Pro Gly Leu Arg Trp Leu His Lys Asp Val Ala Phe Thr Phe Lys Met  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Leu Phe Tyr Gly Leu Lys Phe Arg Arg Arg Leu Asn Lys His Pro Pro  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Glu Thr Phe Val Asp Ala Leu Glu Arg Gln Ala Leu Ala Trp Pro Asp  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Arg Val Ala Leu Val Cys Thr Gly Ser Glu Gly Ser Ser Ile Thr Asn  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ser Gln Leu Asp Ala Arg Ser Cys Gln Ala Ala Trp Val Leu Lys Ala  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Lys Leu Lys Asp Ala Val Ile Gln Asn Thr Arg Asp Ala Ala Ala Ile  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Leu Val Leu Pro Ser Lys Thr Ile Ser Ala Leu Ser Val Phe Leu Gly  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Leu Ala Lys Leu Gly Cys Pro Val Ala Trp Ile Asn Pro His Ser Arg  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Met Pro Leu Leu His Ser Val Arg Ser Ser Gly Ala Ser Val Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ile Val Asp Pro Asp Leu Gln Glu Asn Leu Glu Glu Val Leu Pro Lys  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Leu Leu Ala Glu Asn Ile His Cys Phe Tyr Leu Gly His Ser Ser Pro  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Thr Pro Gly Val Glu Ala Leu Gly Ala Ser Leu Asp Ala Ala Pro Ser  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Asp Pro Val Pro Ala Ser Leu Arg Ala Thr Ile Lys Trp Lys Ser Pro  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Ala Ile Phe Ile Phe Thr Ser Gly Thr Thr Gly Leu Pro Lys Pro Ala  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ile Leu Ser His Glu Arg Val Ile Gln Val Ser Asn Val Leu Ser Phe  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Cys Gly Cys Arg Ala Asp Asp Val Val Tyr Asp Val Leu Pro Leu Tyr  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 His Thr Ile Gly Leu Val Leu Gly Phe Leu Gly Cys Leu Gln Val Gly  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Ala Thr Cys Val Leu Ala Pro Lys Phe Ser Ala Ser Arg Phe Trp Ala  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Glu Cys Arg Gln His Gly Val Thr Val Ile Leu Tyr Val Gly Glu Ile  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Leu Arg Tyr Leu Cys Asn Val Pro Glu Gln Pro Glu Asp Lys Ile His  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Thr Val Arg Leu Ala Met Gly Thr Gly Leu Arg Ala Asn Val Trp Lys  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Asn Phe Gln Gln Arg Phe Gly Pro Ile Arg Ile Trp Glu Phe Tyr Gly  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Ser Thr Glu Gly Asn Val Gly Leu Met Asn Tyr Val Gly His Cys Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Ala Val Gly Arg Thr Ser Cys Ile Leu Arg Met Leu Thr Pro Phe Glu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Leu Val Gln Phe Asp Ile Glu Thr Ala Glu Pro Leu Arg Asp Lys Gln  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Gly Phe Cys Ile Pro Val Glu Pro Gly Lys Pro Gly Leu Leu Leu Thr  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Lys Val Arg Lys Asn Gln Pro Phe Leu Gly Tyr Arg Gly Ser Gln Ala  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Glu Ser Asn Arg Lys Leu Val Ala Asn Val Arg Arg Val Gly Asp Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Tyr Phe Asn Thr Gly Asp Val Leu Thr Leu Asp Gln Glu Gly Phe Phe  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Tyr Phe Gln Asp Arg Leu Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Val Ser Thr Gly Glu Val Glu Cys Val Leu Ser Ser Leu Asp Phe Leu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Glu Glu Val Asn Val Tyr Gly Val Pro Val Pro Gly Cys Glu Gly Lys  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Val Gly Met Ala Ala Val Lys Leu Ala Pro Gly Lys Thr Phe Asp Gly  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Gln Lys Leu Tyr Gln His Val Arg Ser Trp Leu Pro Ala Tyr Ala Thr  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Pro His Phe Ile Arg Ile Gln Asp Ser Leu Glu Ile Thr Asn Thr Tyr  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Lys Leu Val Lys Ser Arg Leu Val Arg Glu Gly Phe Asp Val Gly Ile  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Ile Ala Asp Pro Leu Tyr Ile Leu Asp Asn Lys Ala Gln Thr Phe Arg  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Ser Leu Met Pro Asp Val Tyr Gln Ala Val Cys Glu Gly Thr Trp Asn  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Leu  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 74  
               
               
                 &lt;211&gt; LENGTH: 2221  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Drosophila melanogaster  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 74  
               
               
                   
               
               
                 gctctctggg cctatatcaa gctgctgagg tacacgaagc gccatgagcg gctcaactac     60  
               
               
                   
               
               
                 acggtggcgg acgtcttcga acgaaatgtt caggcccatc cggacaaggt ggctgtggtc    120  
               
               
                   
               
               
                 agtgagacgc aacgctggac cttccgtcag gtgaacgagc atgcgaacaa ggtggccaat    180  
               
               
                   
               
               
                 gtgctgcagg ctcagggcta caaaaagggc gatgtggtgg ccctgttgct ggagaaccgc    240  
               
               
                   
               
               
                 gccgagtacg tggccacctg gctgggtctc tccaagatcg gtgtgatcac accgctgatc    300  
               
               
                   
               
               
                 aacacgaatc tgcgcggtcc ctccctgctg cacagcatca cggtggccca ttgctcggct    360  
               
               
                   
               
               
                 ctcatttacg gcgaggactt cctggaagct gtcaccgacg tggccaagga tctgccagcg    420  
               
               
                   
               
               
                 aacctcacac tcttccagtt caacaacgag aacaacaaca gcgagacgga aaagaacata    480  
               
               
                   
               
               
                 ccgcaggcca agaatctgaa cgcgctgctg accacggcca gctatgagaa gcctaacaag    540  
               
               
                   
               
               
                 acgcaggtta accaccacga caagctggtc tacatctaca cctccggcac cacaggattg    600  
               
               
                   
               
               
                 ccaaaggctg cggttatctc tcactcccgt tatctgttta tcgctgctgg catccactac    660  
               
               
                   
               
               
                 accatgggtt tccaggagga ggacatcttc tacacgccct tgcctttgta ccacaccgct    720  
               
               
                   
               
               
                 ggtggcatta tgtgcatggg tcagtcggtg ctctttggct ccacggtctc cattcgcaag    780  
               
               
                   
               
               
                 aagttctcgg catccaacta tttcgccgac tgcgccaagt ataatgcaac tattggtcag    840  
               
               
                   
               
               
                 tatatcggtg agatggctcg ctacattcta gctacgaaac cctcggaata cgaccagaaa    900  
               
               
                   
               
               
                 caccgagtgc gtctggtctt tggaaacgga ctgcgaccgc agatttggcc acagtttgtg    960  
               
               
                   
               
               
                 cagcgcttca acattgccaa ggttggcgag ttctacggcg ccaccgaggg taatgcgaac   1020  
               
               
                   
               
               
                 atcatgaatc atgacaacac ggtgggcgcc atcggctttg tgtcgcgcat cctgcccaag   1080  
               
               
                   
               
               
                 atctacccaa tctcgatcat tcgcgccgat ccggacaccg gagagcccat tagagatagg   1140  
               
               
                   
               
               
                 aatggcctat gccaactgtg cgctcccaac gagccaggcg tattcatcgg caagatcgtc   1200  
               
               
                   
               
               
                 aaaggaaatc cttctcgcga attcctcgga tacgtcgatg aaaaggcctc cgcgaagaag   1260  
               
               
                   
               
               
                 attgttaagg atgtgttcaa gcatggcgat atggctttca tctccggaga tctgctggtt   1320  
               
               
                   
               
               
                 gccgacgaga agggttatct gtacttcaag gatcgcaccg gtgacacctt ccgctggaag   1380  
               
               
                   
               
               
                 ggcgagaatg tttccaccag cgaggtggag gcgcaagtca gcaatgtggc cggttacaag   1440  
               
               
                   
               
               
                 gataccgtcg tttacggcgt aaccattccg cacaccgagg gaagggccgg catggccgcc   1500  
               
               
                   
               
               
                 atctatgatc cggagcgaga attggacctc gacgtcttcg ccgctagctt ggccaaggtg   1560  
               
               
                   
               
               
                 ctgcccgcgt acgctcgtcc ccagatcatt cgattgctca ccaaggtgga cctgactgga   1620  
               
               
                   
               
               
                 acctttaagc tgcgcaaggt agacctgcag aaggagggct acgatccgaa cgcgatcaag   1680  
               
               
                   
               
               
                 gacgcgctgt actaccagac ttccaagggt cggtacgagc tgctcacgcc ccaggtttac   1740  
               
               
                   
               
               
                 gaccaggtgc agcgcaacga aatccgcttc taagagctgc aatagagttg tgtctgaacc   1800  
               
               
                   
               
               
                 ttgccttttg cccaatatgc tgttaattag tttgtaaggc taagtgtagt agaggaaaat   1860  
               
               
                   
               
               
                 cgggggaaat cggcagcaaa gatcattcag cctaggagag atgcatccga agcacatttc   1920  
               
               
                   
               
               
                 catgtcaaca atgcactttt gtatatcgta agcatatata tatcgtatat cgtaaacgta   1980  
               
               
                   
               
               
                 gttgtatctg catttgtgta gatgatagcc tcctatacgc atttcaattg tttttagcgt   2040  
               
               
                   
               
               
                 gctaaagaac cttgttaaat gcaatttcag ctattgttta gtcagtttta gtggcattta   2100  
               
               
                   
               
               
                 cacttccatt ctcgttgcgt ttcgtttttg cctgtacata tgagaagctc tgatgttttt   2160  
               
               
                   
               
               
                 gtatcaaata aagttttttc cttcaccacg gaccacgtga aaaaaaaaaa aaaaaaaaaa   2220  
               
               
                   
               
               
                 a                                                                   2221  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 75  
               
               
                 &lt;211&gt; LENGTH: 590  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Drosophila melanogaster  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 75  
               
               
                   
               
               
                 Ala Leu Trp Ala Tyr Ile Lys Leu Leu Arg Tyr Thr Lys Arg His Glu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Arg Leu Asn Tyr Thr Val Ala Asp Val Phe Glu Arg Asn Val Gln Ala  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 His Pro Asp Lys Val Ala Val Val Ser Glu Thr Gln Arg Trp Thr Phe  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Arg Gln Val Asn Glu His Ala Asn Lys Val Ala Asn Val Leu Gln Ala  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Gln Gly Tyr Lys Lys Gly Asp Val Val Ala Leu Leu Leu Glu Asn Arg  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Glu Tyr Val Ala Thr Trp Leu Gly Leu Ser Lys Ile Gly Val Ile  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Thr Pro Leu Ile Asn Thr Asn Leu Arg Gly Pro Ser Leu Leu His Ser  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ile Thr Val Ala His Cys Ser Ala Leu Ile Tyr Gly Glu Asp Phe Leu  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Glu Ala Val Thr Asp Val Ala Lys Asp Leu Pro Ala Asn Leu Thr Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Phe Gln Phe Asn Asn Glu Asn Asn Asn Ser Glu Thr Glu Lys Asn Ile  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Pro Gln Ala Lys Asn Leu Asn Ala Leu Leu Thr Thr Ala Ser Tyr Glu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Lys Pro Asn Lys Thr Gln Val Asn His His Asp Lys Leu Val Tyr Ile  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala Val Ile Ser His  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Ser Arg Tyr Leu Phe Ile Ala Ala Gly Ile His Tyr Thr Met Gly Phe  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Gln Glu Glu Asp Ile Phe Tyr Thr Pro Leu Pro Leu Tyr His Thr Ala  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Gly Gly Ile Met Cys Met Gly Gln Ser Val Leu Phe Gly Ser Thr Val  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Ser Ile Arg Lys Lys Phe Ser Ala Ser Asn Tyr Phe Ala Asp Cys Ala  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Lys Tyr Asn Ala Thr Ile Gly Gln Tyr Ile Gly Glu Met Ala Arg Tyr  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Ile Leu Ala Thr Lys Pro Ser Glu Tyr Asp Gln Lys His Arg Val Arg  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Leu Val Phe Gly Asn Gly Leu Arg Pro Gln Ile Trp Pro Gln Phe Val  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Gln Arg Phe Asn Ile Ala Lys Val Gly Glu Phe Tyr Gly Ala Thr Glu  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Gly Asn Ala Asn Ile Met Asn His Asp Asn Thr Val Gly Ala Ile Gly  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Phe Val Ser Arg Ile Leu Pro Lys Ile Tyr Pro Ile Ser Ile Ile Arg  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ala Asp Pro Asp Thr Gly Glu Pro Ile Arg Asp Arg Asn Gly Leu Cys  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gln Leu Cys Ala Pro Asn Glu Pro Gly Val Phe Ile Gly Lys Ile Val  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Lys Gly Asn Pro Ser Arg Glu Phe Leu Gly Tyr Val Asp Glu Lys Ala  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Ser Ala Lys Lys Ile Val Lys Asp Val Phe Lys His Gly Asp Met Ala  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Phe Ile Ser Gly Asp Leu Leu Val Ala Asp Glu Lys Gly Tyr Leu Tyr  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Phe Lys Asp Arg Thr Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Ser Thr Ser Glu Val Glu Ala Gln Val Ser Asn Val Ala Gly Tyr Lys  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Asp Thr Val Val Tyr Gly Val Thr Ile Pro His Thr Glu Gly Arg Ala  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Gly Met Ala Ala Ile Tyr Asp Pro Glu Arg Glu Leu Asp Leu Asp Val  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Phe Ala Ala Ser Leu Ala Lys Val Leu Pro Ala Tyr Ala Arg Pro Gln  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ile Ile Arg Leu Leu Thr Lys Val Asp Leu Thr Gly Thr Phe Lys Leu  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Arg Lys Val Asp Leu Gln Lys Glu Gly Tyr Asp Pro Asn Ala Ile Lys  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Asp Ala Leu Tyr Tyr Gln Thr Ser Lys Gly Arg Tyr Glu Leu Leu Thr  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Pro Gln Val Tyr Asp Gln Val Gln Arg Asn Glu Ile Arg Phe  
               
               
                             580                 585                 590  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 76  
               
               
                 &lt;211&gt; LENGTH: 173  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Danio rerio  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 76  
               
               
                   
               
               
                 agtgtagata ccacaggaac gtttaaaatc cagaagacca gactgcaaag ggaaggatac     60  
               
               
                   
               
               
                 gatccacggc tcacaactga ccagatctac ttcctaaact ccagagcagg gcgttacgag    120  
               
               
                   
               
               
                 cttgtcaacg aggagctgta caatgcattt gaacaagggc aggatttccc ttt           173  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 77  
               
               
                 &lt;211&gt; LENGTH: 57  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Danio rerio  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 77  
               
               
                   
               
               
                 Ser Val Asp Thr Thr Gly Thr Phe Lys Ile Gln Lys Thr Arg Leu Gln  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Arg Glu Gly Tyr Asp Pro Arg Leu Thr Thr Asp Gln Ile Tyr Phe Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Asn Ser Arg Ala Gly Arg Tyr Glu Leu Val Asn Glu Glu Leu Tyr Asn  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ala Phe Glu Gln Gly Gln Asp Phe Pro  
               
               
                     50                  55  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 78  
               
               
                 &lt;211&gt; LENGTH: 1953  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Caenorhabditis elegans  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 78  
               
               
                   
               
               
                 atgaagctgg aggagcttgt gacagttatg cttctcacag tggctgtcat tgctcagaat     60  
               
               
                   
               
               
                 cttccgattg gagtaatatt ggctggagtt cttattttat acatcacagt ggttcatgga    120  
               
               
                   
               
               
                 gatttcattt atagaagtta tcttacgttg aatagggatt taacaggatt ggctctaatt    180  
               
               
                   
               
               
                   
               
               
                 attgaagtca aaatcgacct atggtggagg ttgcatcaga ataaaggaat ccatgaactg    240  
               
               
                   
               
               
                   
               
               
                 tttttggata ttgtgaaaaa gaatccaaat aagccggcga tgattgacat cgagacgaat    300  
               
               
                   
               
               
                   
               
               
                 acaacagaaa catacgcaga gttcaatgca cattgtaata gatatgccaa ttatttccag    360  
               
               
                   
               
               
                   
               
               
                 ggtcttggct atcgatccgg agacgttgtc gccttgtaca tggagaactc ggtcgagttt    420  
               
               
                   
               
               
                   
               
               
                 gtggccgcgt ggatgggact cgcaaaaatc ggagttgtaa cggcttggat caactcgaat    480  
               
               
                   
               
               
                   
               
               
                 ttgaaaagag agcaacttgt tcattgtatc actgcgagca agacaaaggc gattatcaca    540  
               
               
                   
               
               
                   
               
               
                 agtgtaacac ttcagaatat tatgcttgat gctatcgatc agaagctgtt tgatgttgag    600  
               
               
                   
               
               
                   
               
               
                 ggaattgagg tttactctgt cggagagccc aagaagaatt ctggattcaa gaatctcaag    660  
               
               
                   
               
               
                   
               
               
                 aagaagttgg atgctcaaat tactacggaa ccaaagaccc ttgacatagt agattttaaa    720  
               
               
                   
               
               
                   
               
               
                 agtattcttt gcttcatcta tacaagtggt actactggaa tgccaaaagc cgctgtcatg    780  
               
               
                   
               
               
                   
               
               
                 aagcacttca gatattactc gattgccgtt ggagccgcaa aatcattcgg aatccgccct    840  
               
               
                   
               
               
                   
               
               
                 tctgatcgta tgtacgtctc gatgccaatt tatcacactg cagctggaat tcttggagtt    900  
               
               
                   
               
               
                   
               
               
                 gggcaagctc tgttgggtgg atcatcgtgt gtcattagaa aaaaattctc ggctagcaac    960  
               
               
                   
               
               
                 ttttggaggg attgtgtaaa gtatgattgt acagtttcac aatacattgg agagatttgt   1020  
               
               
                   
               
               
                 cggtacttgt tggctcagcc agttgtggaa gaggaatcca ggcatagaat gagattgttg   1080  
               
               
                   
               
               
                 gttggaaacg gactccgtgc tgaaatctgg caaccatttg tagatcgatt ccgtgtcaga   1140  
               
               
                   
               
               
                 attggagaac tttatggttc aactgaagga acttcatctc tcgtgaacat tgacggacat   1200  
               
               
                   
               
               
                 gtcggagctt gcggattctt gccaatatcc ccattaacaa agaaaatgca tccggttcga   1260  
               
               
                   
               
               
                 ttaattaagg ttgatgatgt cactggagaa gcaatccgaa cttccgatgg actttgcatt   1320  
               
               
                   
               
               
                 gcatgtaatc caggagagtc tggagcaatg gtgtcgacga tcagaaaaaa taatccatta   1380  
               
               
                   
               
               
                 ttgcaattcg agggatatct gaataagaag gaaacgaata aaaagattat cagagatgtc   1440  
               
               
                   
               
               
                 ttcgcaaagg gagatagttg ctttttgact ggagatcttc ttcattggga tcgtcttggt   1500  
               
               
                   
               
               
                 tatgtatatt tcaaggatcg tactggagat actttccgtt ggaagggaga gaatgtgtcg   1560  
               
               
                   
               
               
                 actactgaag tcgaggcaat tcttcatcca attactggat tgtctgatgc aactgtttat   1620  
               
               
                   
               
               
                 ggtgtagagg ttcctcaaag agagggaaga gttggaatgg cgtcagttgt tcgagttgta   1680  
               
               
                   
               
               
                 tcgcatgagg aagatgaaac tcaatttgtt catagagttg gagcaagact tgcctcttcg   1740  
               
               
                   
               
               
                 cttaccagct acgcgattcc tcagtttatg cgaatttgtc aggatgttga gaaaacaggt   1800  
               
               
                   
               
               
                 acattcaaac ttgtgaagac gaatctacaa cgattaggta tcatggatgc tccttcagat   1860  
               
               
                   
               
               
                 tcaatttaca tctacaattc tgaaaatcgc aattttgtgc cgttcgacaa tgatttgagg   1920  
               
               
                   
               
               
                 tgcaaggtct cactgggaag ttatccattt taa                                1953  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 79  
               
               
                 &lt;211&gt; LENGTH: 650  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Caenorhabditis elegans  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 79  
               
               
                   
               
               
                 Met Lys Leu Glu Glu Leu Val Thr Val Met Leu Leu Thr Val Ala Val  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ile Ala Gln Asn Leu Pro Ile Gly Val Ile Leu Ala Gly Val Leu Ile  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Leu Tyr Ile Thr Val Val His Gly Asp Phe Ile Tyr Arg Ser Tyr Leu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Thr Leu Asn Arg Asp Leu Thr Gly Leu Ala Leu Ile Ile Glu Val Lys  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Ile Asp Leu Trp Trp Arg Leu His Gln Asn Lys Gly Ile His Glu Leu  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Phe Leu Asp Ile Val Lys Lys Asn Pro Asn Lys Pro Ala Met Ile Asp  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Ile Glu Thr Asn Thr Thr Glu Thr Tyr Ala Glu Phe Asn Ala His Cys  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Asn Arg Tyr Ala Asn Tyr Phe Gln Gly Leu Gly Tyr Arg Ser Gly Asp  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Val Val Ala Leu Tyr Met Glu Asn Ser Val Glu Phe Val Ala Ala Trp  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Met Gly Leu Ala Lys Ile Gly Val Val Thr Ala Trp Ile Asn Ser Asn  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Leu Lys Arg Glu Gln Leu Val His Cys Ile Thr Ala Ser Lys Thr Lys  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Ala Ile Ile Thr Ser Val Thr Leu Gln Asn Ile Met Leu Asp Ala Ile  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Asp Gln Lys Leu Phe Asp Val Glu Gly Ile Glu Val Tyr Ser Val Gly  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Glu Pro Lys Lys Asn Ser Gly Phe Lys Asn Leu Lys Lys Lys Leu Asp  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Gln Ile Thr Thr Glu Pro Lys Thr Leu Asp Ile Val Asp Phe Lys  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Ser Ile Leu Cys Phe Ile Tyr Thr Ser Gly Thr Thr Gly Met Pro Lys  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Ala Ala Val Met Lys His Phe Arg Tyr Tyr Ser Ile Ala Val Gly Ala  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Ala Lys Ser Phe Gly Ile Arg Pro Ser Asp Arg Met Tyr Val Ser Met  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Pro Ile Tyr His Thr Ala Ala Gly Ile Leu Gly Val Gly Gln Ala Leu  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Leu Gly Gly Ser Ser Cys Val Ile Arg Lys Lys Phe Ser Ala Ser Asn  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Phe Trp Arg Asp Cys Val Lys Tyr Asp Cys Thr Val Ser Gln Tyr Ile  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Gly Glu Ile Cys Arg Tyr Leu Leu Ala Gln Pro Val Val Glu Glu Glu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Ser Arg His Arg Met Arg Leu Leu Val Gly Asn Gly Leu Arg Ala Glu  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ile Trp Gln Pro Phe Val Asp Arg Phe Arg Val Arg Ile Gly Glu Leu  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Tyr Gly Ser Thr Glu Gly Thr Ser Ser Leu Val Asn Ile Asp Gly His  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Val Gly Ala Cys Gly Phe Leu Pro Ile Ser Pro Leu Thr Lys Lys Met  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 His Pro Val Arg Leu Ile Lys Val Asp Asp Val Thr Gly Glu Ala Ile  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Arg Thr Ser Asp Gly Leu Cys Ile Ala Cys Asn Pro Gly Glu Ser Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Ala Met Val Ser Thr Ile Arg Lys Asn Asn Pro Leu Leu Gln Phe Glu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gly Tyr Leu Asn Lys Lys Glu Thr Asn Lys Lys Ile Ile Arg Asp Val  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Phe Ala Lys Gly Asp Ser Cys Phe Leu Thr Gly Asp Leu Leu His Trp  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Asp Arg Leu Gly Tyr Val Tyr Phe Lys Asp Arg Thr Gly Asp Thr Phe  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Arg Trp Lys Gly Glu Asn Val Ser Thr Thr Glu Val Glu Ala Ile Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 His Pro Ile Thr Gly Leu Ser Asp Ala Thr Val Tyr Gly Val Glu Val  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Gln Arg Glu Gly Arg Val Gly Met Ala Ser Val Val Arg Val Val  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ser His Glu Glu Asp Glu Thr Gln Phe Val His Arg Val Gly Ala Arg  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu Ala Ser Ser Leu Thr Ser Tyr Ala Ile Pro Gln Phe Met Arg Ile  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Cys Gln Asp Val Glu Lys Thr Gly Thr Phe Lys Leu Val Lys Thr Asn  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Leu Gln Arg Leu Gly Ile Met Asp Ala Pro Ser Asp Ser Ile Tyr Ile  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Tyr Asn Ser Glu Asn Arg Asn Phe Val Pro Phe Asp Asn Asp Leu Arg  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Cys Lys Val Ser Leu Gly Ser Tyr Pro Phe  
               
               
                                 645                 650  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 80  
               
               
                 &lt;211&gt; LENGTH: 1968  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Caenorhabditis elegans  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 80  
               
               
                   
               
               
                 atgagggaaa tgccggacag tcccaagttt gcgttagtca cgtttgttgt gtatgcagtg     60  
               
               
                   
               
               
                 gttttgtaca atgtcaacag cgttttctgg aaatttgtat tcatcggata tgttgtattt    120  
               
               
                   
               
               
                 aggctgcttc gcactgattt tggaagaaga gcacttgcca cgttacctag agattttgcg    180  
               
               
                   
               
               
                 ggactgaagc tcttaatatc ggttaagtcg acaattcgtg gcttgttcaa gaaagatcgc    240  
               
               
                   
               
               
                 ccaattcatg aaatcttttt gaatcaggtg aaacagcatc caaacaaagt ggcgattatt    300  
               
               
                   
               
               
                 gaaattgaaa gtggtaggca gttgacgtat caagaattga atgcgttagc taatcagtat    360  
               
               
                   
               
               
                 gctaaccttt acgtgagtga aggttacaaa atgggcgacg ttgtcgcttt gtttatggaa    420  
               
               
                   
               
               
                 aatagcatcg acttctttgc aatttggctg ggactttcca agattggagt cgtgtcggcg    480  
               
               
                   
               
               
                 ttcatcaact caaacttgaa gttggagcca ttggcacatt cgattaatgt ttcgaagtgc    540  
               
               
                   
               
               
                 aaatcatgca ttaccaatat caatctgttg ccgatgttca aagccgctcg tgaaaagaat    600  
               
               
                   
               
               
                 ctgatcagtg acgagatcca cgtgtttctg gctggaactc aggttgatgg acgtcataga    660  
               
               
                   
               
               
                 agtcttcagc aagatctcca tcttttctct gaggatgaac ctccagttat agacggactc    720  
               
               
                   
               
               
                 aattttagaa gcgttctgtg ttatatttac acttccggta ctaccggaaa tccaaagcca    780  
               
               
                   
               
               
                 gccgtcatta aacacttccg ttacttctgg attgcgatgg gagcaggaaa agcatttgga    840  
               
               
                   
               
               
                 attaataagt cagacgttgt gtacattacg atgccaatgt atcactctgc cgccggtatc    900  
               
               
                   
               
               
                 atgggtattg gatcattaat tgcattcggg tcgaccgctg ttattaggaa aaagttttcg    960  
               
               
                   
               
               
                 gcaagcaact tctggaaaga ttgcgtcaag tacaacgtca cagcgacaca gtacattgga   1020  
               
               
                   
               
               
                 gaaatctgca ggtatcttct ggcagcgaat ccatgtcctg aagagaaaca acacaacgtg   1080  
               
               
                   
               
               
                 cgattgatgt ggggaaatgg tttgagagga caaatttgga aagagtttgt aggaagattt   1140  
               
               
                   
               
               
                 ggaattaaga aaattggaga gttgtacggc tcaacagaag gaaactccaa tattgttaac   1200  
               
               
                   
               
               
                 gtggataacc atgttggagc ttgtggattc atgccaattt atccccatat tggatccctc   1260  
               
               
                   
               
               
                 tacccagttc gacttattaa ggttgataga gccactggag agcttgaacg tgataagaac   1320  
               
               
                   
               
               
                 ggactctgtg tgccgtgtgt gcctggtgaa actggggaaa tggttggcgt tatcaaggag   1380  
               
               
                   
               
               
                 aaagatattc ttctaaagtt cgaaggatat gtcagcgaag gggatactgc aaagaaaatc   1440  
               
               
                   
               
               
                 tacagagatg tgttcaagca tggagataag gtgtttgcaa gtggagatat tcttcattgg   1500  
               
               
                   
               
               
                 gatgatcttg gatacttgta ctttgtggac cgttgtggag acactttccg ttggaaaggg   1560  
               
               
                   
               
               
                 gagaacgtgt caactactga agttgaggga attcttcagc ctgtgatgga tgtggaagat   1620  
               
               
                   
               
               
                 gcaactgttt atggagtcac tgtcggtaaa atggaggggc gtgccggaat ggctggtatt   1680  
               
               
                   
               
               
                 gtcgtcaagg atggaacgga tgttgagaaa ttcatcgccg atattacttc tcgactgacc   1740  
               
               
                   
               
               
                 gaaaatctgg cgtcttacgc aatccctgtt ttcattcggc tgtgcaagga agttgatcga   1800  
               
               
                   
               
               
                 accggaacct tcaaactcaa gaagactgat cttcaaaaac aaggttacga cctggttgct   1860  
               
               
                   
               
               
                 tgtaaaggag acccaattta ctactggtca gctgcagaaa aatcctacaa accactgact   1920  
               
               
                   
               
               
                 gacaaaatgc aacaggatat tgacactggt gtttatgatc gcatttaa                1968  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 81  
               
               
                 &lt;211&gt; LENGTH: 655  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Caenorhabditis elegans  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 81  
               
               
                   
               
               
                 Met Arg Glu Met Pro Asp Ser Pro Lys Phe Ala Leu Val Thr Phe Val  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val Tyr Ala Val Val Leu Tyr Asn Val Asn Ser Val Phe Trp Lys Phe  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Val Phe Ile Gly Tyr Val Val Phe Arg Leu Leu Arg Thr Asp Phe Gly  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Arg Arg Ala Leu Ala Thr Leu Pro Arg Asp Phe Ala Gly Leu Lys Leu  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Leu Ile Ser Val Lys Ser Thr Ile Arg Gly Leu Phe Lys Lys Asp Arg  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Pro Ile His Glu Ile Phe Leu Asn Gln Val Lys Gln His Pro Asn Lys  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Val Ala Ile Ile Glu Ile Glu Ser Gly Arg Gln Leu Thr Tyr Gln Glu  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Leu Asn Ala Leu Ala Asn Gln Tyr Ala Asn Leu Tyr Val Ser Glu Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Tyr Lys Met Gly Asp Val Val Ala Leu Phe Met Glu Asn Ser Ile Asp  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Phe Phe Ala Ile Trp Leu Gly Leu Ser Lys Ile Gly Val Val Ser Ala  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Phe Ile Asn Ser Asn Leu Lys Leu Glu Pro Leu Ala His Ser Ile Asn  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Val Ser Lys Cys Lys Ser Cys Ile Thr Asn Ile Asn Leu Leu Pro Met  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Phe Lys Ala Ala Arg Glu Lys Asn Leu Ile Ser Asp Glu Ile His Val  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Phe Leu Ala Gly Thr Gln Val Asp Gly Arg His Arg Ser Leu Gln Gln  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Asp Leu His Leu Phe Ser Glu Asp Glu Pro Pro Val Ile Asp Gly Leu  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asn Phe Arg Ser Val Leu Cys Tyr Ile Tyr Thr Ser Gly Thr Thr Gly  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Asn Pro Lys Pro Ala Val Ile Lys His Phe Arg Tyr Phe Trp Ile Ala  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Met Gly Ala Gly Lys Ala Phe Gly Ile Asn Lys Ser Asp Val Val Tyr  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Ile Thr Met Pro Met Tyr His Ser Ala Ala Gly Ile Met Gly Ile Gly  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ser Leu Ile Ala Phe Gly Ser Thr Ala Val Ile Arg Lys Lys Phe Ser  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Ala Ser Asn Phe Trp Lys Asp Cys Val Lys Tyr Asn Val Thr Ala Thr  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Gln Tyr Ile Gly Glu Ile Cys Arg Tyr Leu Leu Ala Ala Asn Pro Cys  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Pro Glu Glu Lys Gln His Asn Val Arg Leu Met Trp Gly Asn Gly Leu  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Arg Gly Gln Ile Trp Lys Glu Phe Val Gly Arg Phe Gly Ile Lys Lys  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Ile Gly Glu Leu Tyr Gly Ser Thr Glu Gly Asn Ser Asn Ile Val Asn  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Val Asp Asn His Val Gly Ala Cys Gly Phe Met Pro Ile Tyr Pro His  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Ile Gly Ser Leu Tyr Pro Val Arg Leu Ile Lys Val Asp Arg Ala Thr  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Gly Glu Leu Glu Arg Asp Lys Asn Gly Leu Cys Val Pro Cys Val Pro  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Gly Glu Thr Gly Glu Met Val Gly Val Ile Lys Glu Lys Asp Ile Leu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Leu Lys Phe Glu Gly Tyr Val Ser Glu Gly Asp Thr Ala Lys Lys Ile  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Tyr Arg Asp Val Phe Lys His Gly Asp Lys Val Phe Ala Ser Gly Asp  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Ile Leu His Trp Asp Asp Leu Gly Tyr Leu Tyr Phe Val Asp Arg Cys  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ser Thr Thr Glu Val  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Glu Gly Ile Leu Gln Pro Val Met Asp Val Glu Asp Ala Thr Val Tyr  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Gly Val Thr Val Gly Lys Met Glu Gly Arg Ala Gly Met Ala Gly Ile  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Val Val Lys Asp Gly Thr Asp Val Glu Lys Phe Ile Ala Asp Ile Thr  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ser Arg Leu Thr Glu Asn Leu Ala Ser Tyr Ala Ile Pro Val Phe Ile  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Arg Leu Cys Lys Glu Val Asp Arg Thr Gly Thr Phe Lys Leu Lys Lys  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Thr Asp Leu Gln Lys Gln Gly Tyr Asp Leu Val Ala Cys Lys Gly Asp  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Pro Ile Tyr Tyr Trp Ser Ala Ala Glu Lys Ser Tyr Lys Pro Leu Thr  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Asp Lys Met Gln Gln Asp Ile Asp Thr Gly Val Tyr Asp Arg Ile  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 82  
               
               
                 &lt;211&gt; LENGTH: 1932  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Cochliobolus heterostrophus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 82  
               
               
                   
               
               
                 atggcgtgta tgcatcaggc tcagctatac aatgatctag aggaattgct aactggtcca     60  
               
               
                   
               
               
                 tcagtaccca tcgttgctgg agctgctgga gctgcagctc tcactgccta cattaacgcc    120  
               
               
                   
               
               
                 aaataccaca tagcccatga tctcaagacc ctcggtggtg gattgacaca atcgtccgaa    180  
               
               
                   
               
               
                 gcgattgatt tcataaaccg ccgcgtcgca caaaagcgcg tcctcacgca ccacatcttc    240  
               
               
                   
               
               
                 caggagcagg tccaaaaaca atcaaatcat ccctttctta tctttgaggg caagacatgg    300  
               
               
                   
               
               
                 tcttacaagg agttctctga ggcatacacg agggtcgcga actggctgat tgatgagctg    360  
               
               
                   
               
               
                 gacgtacaag taggggagat ggtcgcaatt gatggcggaa atagtgcaga gcacctgatg    420  
               
               
                   
               
               
                 ctttggcttg cacttgatgc aatcggtgcg gctacgagtt ttttgaactg gaacctgaca    480  
               
               
                   
               
               
                 ggggcagggt taattcattg cataaagcta tgcgaatgtc gattcgttat cgcagacatc    540  
               
               
                   
               
               
                 gatattaaag cgaacattga accgtgccgt ggcgaactgg aggagacggg catcaacatt    600  
               
               
                   
               
               
                 cactactatg acccatcctt catctcatcg ctaccgaata acacgccaat tcccgacagc    660  
               
               
                   
               
               
                 cgcactgaga acattgaatt agattcagta cgaggactga tatacacatc tggaaccact    720  
               
               
                   
               
               
                 ggtctaccta aaggcgtgtt tataagcact ggccgcgagc ttaggactga ctggtcgatt    780  
               
               
                   
               
               
                 tcaaagtatc taaatctcaa gcccacggat cgaatgtata catgtatgcc gctctaccat    840  
               
               
                   
               
               
                 gccgctgcac acagcctctg tacagcatca gttattcatg gtggaggtac cgtggtattg    900  
               
               
                   
               
               
                 agcaggaaat tctcacacaa gaagttctgg cctgaagttg tggcttcgga agcaaatatc    960  
               
               
                   
               
               
                 attcagtacg ttggtgaatt aggtcgatat ctcctgaatg gtccaaagag tccttacgac   1020  
               
               
                   
               
               
                 agggcccata aagtccagat ggcgtggggc aatggcatgc gtccagacgt gtgggaagcg   1080  
               
               
                   
               
               
                 tttcgtgaac gcttcaacat accaattatt catgagctct atgccgcaac cgatgggctc   1140  
               
               
                   
               
               
                 gggtcaatga ccaatcgtaa cgcgggccct tttacagcaa actgtattgc gctgcgaggg   1200  
               
               
                   
               
               
                 ctgatctggc actggaaatt tcgaaatcag gaagtgctgg tcaagatgga tctcgatact   1260  
               
               
                   
               
               
                 gatgagatca tgagagatcg caatgggttt gcgatacgat gcgctgtcaa tgaacctgga   1320  
               
               
                   
               
               
                 cagatgcttt ttcggctgac acccgaaact ctggctggtg caccaagcta ctacaacaac   1380  
               
               
                   
               
               
                 gaaacggcca cacagagcag gcggattaca gatgtgtttc aaaagggtga cctgtggttc   1440  
               
               
                   
               
               
                 aagtccggtg acatgctacg gcaagacgcc gaaggccgcg tctactttgt cgatcgacta   1500  
               
               
                   
               
               
                 ggcgatacgt tccgctggaa atccgaaaac gtttctacca atgaagtcgc ggacgtgatg   1560  
               
               
                   
               
               
                 ggcacatttc ctcagattgc tgaaacgaat gtatacggtg tccttgtgcc gggtaacgat   1620  
               
               
                   
               
               
                 ggtcgagtgc gcagcctcaa ttgtcatggc agacggcgtg acagagtcga cattcgcttc   1680  
               
               
                   
               
               
                 gctgcccttg caaagcacgc ccgagatcgg ttaccgggtt atgctgtacc actgtttctg   1740  
               
               
                   
               
               
                 agggtaactc cagcacttga atatacgggc acattaaaga ttcagaaagg acgcctcaag   1800  
               
               
                   
               
               
                 caggaaggta tagacccaga taagatttcc ggcgaagata agttatactg gctgccgcct   1860  
               
               
                   
               
               
                 ggtagcgata tatatttacc atttggaaag atggagtggc agggaattgt agataagcgt   1920  
               
               
                   
               
               
                 atacggctgt ga                                                       1932  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 83  
               
               
                 &lt;211&gt; LENGTH: 643  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Cochliobolus heterostrophus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 83  
               
               
                   
               
               
                 Met Ala Cys Met His Gln Ala Gln Leu Tyr Asn Asp Leu Glu Glu Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Thr Gly Pro Ser Val Pro Ile Val Ala Gly Ala Ala Gly Ala Ala  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Ala Leu Thr Ala Tyr Ile Asn Ala Lys Tyr His Ile Ala His Asp Leu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Thr Leu Gly Gly Gly Leu Thr Gln Ser Ser Glu Ala Ile Asp Phe  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Ile Asn Arg Arg Val Ala Gln Lys Arg Val Leu Thr His His Ile Phe  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Gln Glu Gln Val Gln Lys Gln Ser Asn His Pro Phe Leu Ile Phe Glu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Lys Thr Trp Ser Tyr Lys Glu Phe Ser Glu Ala Tyr Thr Arg Val  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ala Asn Trp Leu Ile Asp Glu Leu Asp Val Gln Val Gly Glu Met Val  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Ala Ile Asp Gly Gly Asn Ser Ala Glu His Leu Met Leu Trp Leu Ala  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Leu Asp Ala Ile Gly Ala Ala Thr Ser Phe Leu Asn Trp Asn Leu Thr  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Gly Ala Gly Leu Ile His Cys Ile Lys Leu Cys Glu Cys Arg Phe Val  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Ile Ala Asp Ile Asp Ile Lys Ala Asn Ile Glu Pro Cys Arg Gly Glu  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Leu Glu Glu Thr Gly Ile Asn Ile His Tyr Tyr Asp Pro Ser Phe Ile  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Ser Ser Leu Pro Asn Asn Thr Pro Ile Pro Asp Ser Arg Thr Glu Asn  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ile Glu Leu Asp Ser Val Arg Gly Leu Ile Tyr Thr Ser Gly Thr Thr  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Gly Leu Pro Lys Gly Val Phe Ile Ser Thr Gly Arg Glu Leu Arg Thr  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Asp Trp Ser Ile Ser Lys Tyr Leu Asn Leu Lys Pro Thr Asp Arg Met  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Tyr Thr Cys Met Pro Leu Tyr His Ala Ala Ala His Ser Leu Cys Thr  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Ala Ser Val Ile His Gly Gly Gly Thr Val Val Leu Ser Arg Lys Phe  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ser His Lys Lys Phe Trp Pro Glu Val Val Ala Ser Glu Ala Asn Ile  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Ile Gln Tyr Val Gly Glu Leu Gly Arg Tyr Leu Leu Asn Gly Pro Lys  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ser Pro Tyr Asp Arg Ala His Lys Val Gln Met Ala Trp Gly Asn Gly  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Met Arg Pro Asp Val Trp Glu Ala Phe Arg Glu Arg Phe Asn Ile Pro  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ile Ile His Glu Leu Tyr Ala Ala Thr Asp Gly Leu Gly Ser Met Thr  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Asn Arg Asn Ala Gly Pro Phe Thr Ala Asn Cys Ile Ala Leu Arg Gly  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Leu Ile Trp His Trp Lys Phe Arg Asn Gln Glu Val Leu Val Lys Met  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Asp Leu Asp Thr Asp Glu Ile Met Arg Asp Arg Asn Gly Phe Ala Ile  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Arg Cys Ala Val Asn Glu Pro Gly Gln Met Leu Phe Arg Leu Thr Pro  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Glu Thr Leu Ala Gly Ala Pro Ser Tyr Tyr Asn Asn Glu Thr Ala Thr  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gln Ser Arg Arg Ile Thr Asp Val Phe Gln Lys Gly Asp Leu Trp Phe  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Lys Ser Gly Asp Met Leu Arg Gln Asp Ala Glu Gly Arg Val Tyr Phe  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Val Asp Arg Leu Gly Asp Thr Phe Arg Trp Lys Ser Glu Asn Val Ser  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Thr Asn Glu Val Ala Asp Val Met Gly Thr Phe Pro Gln Ile Ala Glu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Thr Asn Val Tyr Gly Val Leu Val Pro Gly Asn Asp Gly Arg Val Arg  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Ser Leu Asn Cys His Gly Arg Arg Arg Asp Arg Val Asp Ile Arg Phe  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ala Ala Leu Ala Lys His Ala Arg Asp Arg Leu Pro Gly Tyr Ala Val  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Pro Leu Phe Leu Arg Val Thr Pro Ala Leu Glu Tyr Thr Gly Thr Leu  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Lys Ile Gln Lys Gly Arg Leu Lys Gln Glu Gly Ile Asp Pro Asp Lys  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ile Ser Gly Glu Asp Lys Leu Tyr Trp Leu Pro Pro Gly Ser Asp Ile  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Tyr Leu Pro Phe Gly Lys Met Glu Trp Gln Gly Ile Val Asp Lys Arg  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Ile Arg Leu  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 84  
               
               
                 &lt;211&gt; LENGTH: 597  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Aspergillus nidulans  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 84  
               
               
                   
               
               
                 ctttaccatt catcagcttc attctgcatt tttagcttga cggcagccgg gtctacgctg     60  
               
               
                   
               
               
                 atcatcggcc gcaagttctc cgcgagaaac ttcataaagg aagcgcgcga gaacgacgcc    120  
               
               
                   
               
               
                 acggtcatcc agtacgtggg tgagaccttg cgatatctgc tcgccacccc cggtgaaacc    180  
               
               
                   
               
               
                 gatccagtta ctggcgaaga cctggacaaa aagcacaata ttcgagcagt atacggcaac    240  
               
               
                   
               
               
                 gggctacggc cggatatctg gaaccgcttc aaggagcgct tcaacgtgcc gacggttgcc    300  
               
               
                   
               
               
                 gaattttatg ctgcaaccga gagcccaggc ggaacatgga actattcaac aaatgacttc    360  
               
               
                   
               
               
                 actgccggag ccattgggca cactggcgtg cttagtggat ggcttcttgg acgcggcctt    420  
               
               
                   
               
               
                 actattgtcg aggtggacca ggaatcacag gaaccatggc gcgatcccca aaccgggttc    480  
               
               
                   
               
               
                 tgcaagccgg tcccgcgagg cgaagcaggc gagctcctgt atgccattga tccggccgac    540  
               
               
                   
               
               
                 ccgggcgaga ccttccaggg ctactaccgc aactccttta gagcacactg gcggccg       597  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 85  
               
               
                 &lt;211&gt; LENGTH: 199  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Aspergillus nidulans  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 85  
               
               
                   
               
               
                 Leu Tyr His Ser Ser Ala Ser Phe Cys Ile Phe Ser Leu Thr Ala Ala  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Gly Ser Thr Leu Ile Ile Gly Arg Lys Phe Ser Ala Arg Asn Phe Ile  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Lys Glu Ala Arg Glu Asn Asp Ala Thr Val Ile Gln Tyr Val Gly Glu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Thr Leu Arg Tyr Leu Leu Ala Thr Pro Gly Glu Thr Asp Pro Val Thr  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Gly Glu Asp Leu Asp Lys Lys His Asn Ile Arg Ala Val Tyr Gly Asn  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Gly Leu Arg Pro Asp Ile Trp Asn Arg Phe Lys Glu Arg Phe Asn Val  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Pro Thr Val Ala Glu Phe Tyr Ala Ala Thr Glu Ser Pro Gly Gly Thr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Trp Asn Tyr Ser Thr Asn Asp Phe Thr Ala Gly Ala Ile Gly His Thr  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Gly Val Leu Ser Gly Trp Leu Leu Gly Arg Gly Leu Thr Ile Val Glu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Val Asp Gln Glu Ser Gln Glu Pro Trp Arg Asp Pro Gln Thr Gly Phe  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Cys Lys Pro Val Pro Arg Gly Glu Ala Gly Glu Leu Leu Tyr Ala Ile  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asp Pro Ala Asp Pro Gly Glu Thr Phe Gln Gly Tyr Tyr Arg Asn Ser  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Phe Arg Ala His Trp Arg Pro  
               
               
                         195  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 86  
               
               
                 &lt;211&gt; LENGTH: 522  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Magnaporthe grisea  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: (1)...(522)  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 111  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 86  
               
               
                   
               
               
                 gcaaaggccg acgcgtggct gcggacgggt aacgtgatca gggcggacaa cgaagggcga     60  
               
               
                   
               
               
                 ctcttcttcc acgaccggat cggagacacg ttccgatgga agggagagac ngtcagcaca    120  
               
               
                   
               
               
                 caagaggtca gtttggtgct cggacgacac gactcaatca aggaggccaa cgtgtacggc    180  
               
               
                   
               
               
                 gtgacggtgc cgaaccacga cgggcgggcc ggctgcgctg cgctcacgct atcagacgct    240  
               
               
                   
               
               
                 ctggcgactg aaaagaagct gggcgatgag ctgctaaagg gattggctac tcactcgtcg    300  
               
               
                   
               
               
                 acttcgcttc ccaagtttgc ggtgccgcag ttcctacggg tggtgcgcgg cgagatgcag    360  
               
               
                   
               
               
                 tcaacgggca ccaacaagca acagaagcac gacctgaggg tgcagggtgt agagccgggc    420  
               
               
                   
               
               
                 aaggtgggcg tagacgaggt gtactggttg cggggaggga catatgtacc attcggaaca    480  
               
               
                   
               
               
                 gaggattggg atgggttgaa gaagggtctt gtgaagttgt ga                       522  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 87  
               
               
                 &lt;211&gt; LENGTH: 173  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Magnaporthe grisea  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 87  
               
               
                   
               
               
                 Ala Lys Ala Asp Ala Trp Leu Arg Thr Gly Asn Val Ile Arg Ala Asp  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Asn Glu Gly Arg Leu Phe Phe His Asp Arg Ile Gly Asp Thr Phe Arg  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Trp Lys Gly Glu Thr Val Ser Thr Gln Glu Val Ser Leu Val Leu Gly  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Arg His Asp Ser Ile Lys Glu Ala Asn Val Tyr Gly Val Thr Val Pro  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Asn His Asp Gly Arg Ala Gly Cys Ala Ala Leu Thr Leu Ser Asp Ala  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Leu Ala Thr Glu Lys Lys Leu Gly Asp Glu Leu Leu Lys Gly Leu Ala  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Thr His Ser Ser Thr Ser Leu Pro Lys Phe Ala Val Pro Gln Phe Leu  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Arg Val Val Arg Gly Glu Met Gln Ser Thr Gly Thr Asn Lys Gln Gln  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Lys His Asp Leu Arg Val Gln Gly Val Glu Pro Gly Lys Val Gly Val  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Asp Glu Val Tyr Trp Leu Arg Gly Gly Thr Tyr Val Pro Phe Gly Thr  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Glu Asp Trp Asp Gly Leu Lys Lys Gly Leu Val Lys Leu  
               
               
                                 165                 170  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 88  
               
               
                 &lt;211&gt; LENGTH: 1872  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Saccharomyces cerevisiae  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 88  
               
               
                   
               
               
                 atgtctccca tacaggttgt tgtctttgcc ttgtcaagga ttttcctgct attattcaga     60  
               
               
                   
               
               
                 cttatcaagc taattataac ccctatccag aaatcactgg gttatctatt tggtaattat    120  
               
               
                   
               
               
                 tttgatgaat tagaccgtaa atatagatac aaggaggatt ggtatattat tccttacttt    180  
               
               
                   
               
               
                 ttgaaaagcg tgttttgtta tatcattgat gtgagaagac ataggtttca aaactggtac    240  
               
               
                   
               
               
                 ttatttatta aacaggtcca acaaaatggt gaccatttag cgattagtta cacccgtccc    300  
               
               
                   
               
               
                 atggccgaaa agggagaatt tcaactcgaa acctttacgt atattgaaac ttataacata    360  
               
               
                   
               
               
                 gtgttgagat tgtctcatat tttgcatttt gattataacg ttcaggccgg tgactacgtg    420  
               
               
                   
               
               
                 gcaatcgatt gtactaataa acctcttttc gtatttttat ggctttcttt gtggaacatt    480  
               
               
                   
               
               
                 ggggctattc cagctttttt aaactataat actaaaggca ctccgctggt tcactcccta    540  
               
               
                   
               
               
                 aagatttcca atattacgca ggtatttatt gaccctgatg ccagtaatcc gatcagagaa    600  
               
               
                   
               
               
                 tcggaagaag aaatcaaaaa cgcacttcct gatgttaaat taaactatct tgaagaacaa    660  
               
               
                   
               
               
                 gacttaatgc atgaactttt aaattcgcaa tcaccggaat tcttacaaca agacaacgtt    720  
               
               
                   
               
               
                 aggacaccac taggcttgac cgattttaaa ccctctatgt taatttatac atctggaacc    780  
               
               
                   
               
               
                 actggtttgc ctaaatccgc tattatgtct tggagaaaat cctccgtagg ttgtcaagtt    840  
               
               
                   
               
               
                 tttggtcatg ttttacatat gactaatgaa agcactgtgt tcacagccat gccattgttc    900  
               
               
                   
               
               
                 cattcaactg ctgccttatt aggtgcgtgc gccattctat ctcacggtgg ttgccttgcg    960  
               
               
                   
               
               
                 ttatcgcata aattttctgc cagtacattt tggaagcaag tttatttaac aggagccacg   1020  
               
               
                   
               
               
                 cacatccaat atgtcggaga agtctgtaga tacctgttac atacgccaat ttctaagtat   1080  
               
               
                   
               
               
                 gaaaagatgc ataaggtgaa ggttgcttat ggtaacgggc tgagacctga catctggcag   1140  
               
               
                   
               
               
                 gacttcagga agaggttcaa catagaagtt attggtgaat tctatgccgc aactgaagct   1200  
               
               
                   
               
               
                 ccttttgcta caactacctt ccagaaaggt gactttggaa ttggcgcatg taggaactat   1260  
               
               
                   
               
               
                 ggtactataa ttcaatggtt tttgtcattc caacaaacat tggtaaggat ggacccaaat   1320  
               
               
                   
               
               
                 gacgattccg ttatatatag aaattccaag ggtttctgcg aagtggcccc tgttggcgaa   1380  
               
               
                   
               
               
                 ccaggagaaa tgttaatgag aatctttttc cctaaaaaac cagaaacatc ttttcaaggt   1440  
               
               
                   
               
               
                 tatcttggta atgccaagga aacaaagtcc aaagttgtga gggatgtctt cagacgtggc   1500  
               
               
                   
               
               
                 gatgcttggt atagatgtgg agatttatta aaagcggacg aatatggatt atggtatttc   1560  
               
               
                   
               
               
                 cttgatagaa tgggtgatac tttcagatgg aaatctgaaa atgtttccac tactgaagta   1620  
               
               
                   
               
               
                 gaagatcagt tgacggccag taacaaagaa caatatgcac aagttctagt tgttggtatt   1680  
               
               
                   
               
               
                 aaagtaccta aatatgaagg tagagctggt tttgcagtta ttaaactaac tgacaactct   1740  
               
               
                   
               
               
                 cttgacatca ctgcaaagac caaattatta aatgattcct tgagccggtt aaatctaccg   1800  
               
               
                   
               
               
                 tcttatgcta tgcccctatt tgttaaattt gttgatgaaa ttaaaatgac agataacctc   1860  
               
               
                   
               
               
                 ataaaatttt ga                                                       1872  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 89  
               
               
                 &lt;211&gt; LENGTH: 623  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Saccharomyces cerevisiae  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 89  
               
               
                   
               
               
                 Met Ser Pro Ile Gln Val Val Val Phe Ala Leu Ser Arg Ile Phe Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Leu Phe Arg Leu Ile Lys Leu Ile Ile Thr Pro Ile Gln Lys Ser  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Leu Gly Tyr Leu Phe Gly Asn Tyr Phe Asp Glu Leu Asp Arg Lys Tyr  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Arg Tyr Lys Glu Asp Trp Tyr Ile Ile Pro Tyr Phe Leu Lys Ser Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Phe Cys Tyr Ile Ile Asp Val Arg Arg His Arg Phe Gln Asn Trp Tyr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Leu Phe Ile Lys Gln Val Gln Gln Asn Gly Asp His Leu Ala Ile Ser  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Tyr Thr Arg Pro Met Ala Glu Lys Gly Glu Phe Gln Leu Glu Thr Phe  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Thr Tyr Ile Glu Thr Tyr Asn Ile Val Leu Arg Leu Ser His Ile Leu  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 His Phe Asp Tyr Asn Val Gln Ala Gly Asp Tyr Val Ala Ile Asp Cys  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Thr Asn Lys Pro Leu Phe Val Phe Leu Trp Leu Ser Leu Trp Asn Ile  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Gly Ala Ile Pro Ala Phe Leu Asn Tyr Asn Thr Lys Gly Thr Pro Leu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Val His Ser Leu Lys Ile Ser Asn Ile Thr Gln Val Phe Ile Asp Pro  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Asp Ala Ser Asn Pro Ile Arg Glu Ser Glu Glu Glu Ile Lys Asn Ala  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Leu Pro Asp Val Lys Leu Asn Tyr Leu Glu Glu Gln Asp Leu Met His  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Glu Leu Leu Asn Ser Gln Ser Pro Glu Phe Leu Gln Gln Asp Asn Val  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Arg Thr Pro Leu Gly Leu Thr Asp Phe Lys Pro Ser Met Leu Ile Tyr  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Thr Ser Gly Thr Thr Gly Leu Pro Lys Ser Ala Ile Met Ser Trp Arg  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Lys Ser Ser Val Gly Cys Gln Val Phe Gly His Val Leu His Met Thr  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Asn Glu Ser Thr Val Phe Thr Ala Met Pro Leu Phe His Ser Thr Ala  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ala Leu Leu Gly Ala Cys Ala Ile Leu Ser His Gly Gly Cys Leu Ala  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Leu Ser His Lys Phe Ser Ala Ser Thr Phe Trp Lys Gln Val Tyr Leu  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Thr Gly Ala Thr His Ile Gln Tyr Val Gly Glu Val Cys Arg Tyr Leu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Leu His Thr Pro Ile Ser Lys Tyr Glu Lys Met His Lys Val Lys Val  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ala Tyr Gly Asn Gly Leu Arg Pro Asp Ile Trp Gln Asp Phe Arg Lys  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Arg Phe Asn Ile Glu Val Ile Gly Glu Phe Tyr Ala Ala Thr Glu Ala  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Pro Phe Ala Thr Thr Thr Phe Gln Lys Gly Asp Phe Gly Ile Gly Ala  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Cys Arg Asn Tyr Gly Thr Ile Ile Gln Trp Phe Leu Ser Phe Gln Gln  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Thr Leu Val Arg Met Asp Pro Asn Asp Asp Ser Val Ile Tyr Arg Asn  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Ser Lys Gly Phe Cys Glu Val Ala Pro Val Gly Glu Pro Gly Glu Met  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Leu Met Arg Ile Phe Phe Pro Lys Lys Pro Glu Thr Ser Phe Gln Gly  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Tyr Leu Gly Asn Ala Lys Glu Thr Lys Ser Lys Val Val Arg Asp Val  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Phe Arg Arg Gly Asp Ala Trp Tyr Arg Cys Gly Asp Leu Leu Lys Ala  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Asp Glu Tyr Gly Leu Trp Tyr Phe Leu Asp Arg Met Gly Asp Thr Phe  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Arg Trp Lys Ser Glu Asn Val Ser Thr Thr Glu Val Glu Asp Gln Leu  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Thr Ala Ser Asn Lys Glu Gln Tyr Ala Gln Val Leu Val Val Gly Ile  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Lys Val Pro Lys Tyr Glu Gly Arg Ala Gly Phe Ala Val Ile Lys Leu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Thr Asp Asn Ser Leu Asp Ile Thr Ala Lys Thr Lys Leu Leu Asn Asp  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Ser Leu Ser Arg Leu Asn Leu Pro Ser Tyr Ala Met Pro Leu Phe Val  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Lys Phe Val Asp Glu Ile Lys Met Thr Asp Asn Leu Ile Lys Phe  
               
               
                     610                 615                 620  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 90  
               
               
                 &lt;211&gt; LENGTH: 1794  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mycobacterium tuberculosis  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 90  
               
               
                   
               
               
                 gtgtccgatt actacggcgg cgcacacaca acggtcaggc tgatcgacct ggcaactcgg     60  
               
               
                   
               
               
                 atgccgcgag tgttggcgga cacgccggtg attgtgcgtg gggcaatgac cgggctgctg    120  
               
               
                   
               
               
                 gcccggccga attccaaggc gtcgatcggc acggtgttcc aggaccgggc cgctcgctac    180  
               
               
                   
               
               
                 ggtgaccgag tcttcctgaa attcggcgat cagcagctga cctaccgcga cgctaacgcc    240  
               
               
                   
               
               
                 accgccaacc ggtacgccgc ggtgttggcc gcccgcggcg tcggccccgg cgacgtcgtt    300  
               
               
                   
               
               
                 ggcatcatgt tgcgtaactc acccagcaca gtcttggcga tgctggccac ggtcaagtgc    360  
               
               
                   
               
               
                 ggcgctatcg ccggcatgct caactaccac cagcgcggcg aggtgttggc gcacagcctg    420  
               
               
                   
               
               
                 ggtctgctgg acgcgaaggt actgatcgca gagtccgact tggtcagcgc cgtcgccgaa    480  
               
               
                   
               
               
                 tgcggcgcct cgcgcggccg ggtagcgggc gacgtgctga ccgtcgagga cgtggagcga    540  
               
               
                   
               
               
                 ttcgccacaa cggcgcccgc caccaacccg gcgtcggcgt cggcggtgca agccaaagac    600  
               
               
                   
               
               
                 accgcgttct acatcttcac ctcgggcacc accggatttc ccaaggccag tgtcatgacg    660  
               
               
                   
               
               
                 catcatcggt ggctgcgggc gctggccgtc ttcggaggga tggggctgcg gctgaagggt    720  
               
               
                   
               
               
                 tccgacacgc tctacagctg cctgccgctg taccacaaca acgcgttaac ggtcgcggtg    780  
               
               
                   
               
               
                 tcgtcggtga tcaattctgg ggcgaccctg gcgctgggta agtcgttttc ggcgtcgcgg    840  
               
               
                   
               
               
                 ttctgggatg aggtgattgc caaccgggcg acggcgttcg tctacatcgg cgaaatctgc    900  
               
               
                   
               
               
                 cgttatctgc tcaaccagcc ggccaagccg accgaccgtg cccaccaggt gcgggtgatc    960  
               
               
                   
               
               
                 tgcggtaacg ggctgcggcc ggagatctgg gatgagttca ccacccgctt cggggtcgcg   1020  
               
               
                   
               
               
                 cgggtgtgcg agttctacgc cgccagcgaa ggcaactcgg cctttatcaa catcttcaac   1080  
               
               
                   
               
               
                 gtgcccagga ccgccggggt atcgccgatg ccgcttgcct ttgtggaata cgacctggac   1140  
               
               
                   
               
               
                 accggcgatc cgctgcggga tgcgagcggg cgagtgcgtc gggtacccga cggtgaaccc   1200  
               
               
                   
               
               
                 ggcctgttgc ttagccgggt caaccggctg cagccgttcg acggctacac cgacccggtt   1260  
               
               
                   
               
               
                 gccagcgaaa agaagttggt gcgcaacgct tttcgagatg gcgactgttg gttcaacacc   1320  
               
               
                   
               
               
                 ggtgacgtga tgagcccgca gggcatgggc catgccgcct tcgtcgatcg gctgggcgac   1380  
               
               
                   
               
               
                 accttccgct ggaagggcga gaatgtcgcc accactcagg tcgaagcggc actggcctcc   1440  
               
               
                   
               
               
                 gaccagaccg tcgaggagtg cacggtctac ggcgtccaga ttccgcgcac cggcgggcgc   1500  
               
               
                   
               
               
                 gccggaatgg ccgcgatcac actgcgcgct ggcgccgaat tcgacggcca ggcgctggcc   1560  
               
               
                   
               
               
                 cgaacggttt acggtcactt gcccggctat gcacttccgc tctttgttcg ggtagtgggg   1620  
               
               
                   
               
               
                 tcgctggcgc acaccacgac gttcaagagt cgcaaggtgg agttgcgcaa ccaggcctat   1680  
               
               
                   
               
               
                 ggcgccgaca tcgaggatcc gctgtacgta ctggccggcc cggacgaagg atatgtgccg   1740  
               
               
                   
               
               
                 tactacgccg aataccctga ggaggtttcg ctcggaaggc gaccgcaggg ctag         1794  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 91  
               
               
                 &lt;211&gt; LENGTH: 597  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mycobacterium tuberculosis  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 91  
               
               
                   
               
               
                 Met Ser Asp Tyr Tyr Gly Gly Ala His Thr Thr Val Arg Leu Ile Asp  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Ala Thr Arg Met Pro Arg Val Leu Ala Asp Thr Pro Val Ile Val  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Arg Gly Ala Met Thr Gly Leu Leu Ala Arg Pro Asn Ser Lys Ala Ser  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ile Gly Thr Val Phe Gln Asp Arg Ala Ala Arg Tyr Gly Asp Arg Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Phe Leu Lys Phe Gly Asp Gln Gln Leu Thr Tyr Arg Asp Ala Asn Ala  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Thr Ala Asn Arg Tyr Ala Ala Val Leu Ala Ala Arg Gly Val Gly Pro  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Asp Val Val Gly Ile Met Leu Arg Asn Ser Pro Ser Thr Val Leu  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ala Met Leu Ala Thr Val Lys Cys Gly Ala Ile Ala Gly Met Leu Asn  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Tyr His Gln Arg Gly Glu Val Leu Ala His Ser Leu Gly Leu Leu Asp  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ala Lys Val Leu Ile Ala Glu Ser Asp Leu Val Ser Ala Val Ala Glu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Cys Gly Ala Ser Arg Gly Arg Val Ala Gly Asp Val Leu Thr Val Glu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asp Val Glu Arg Phe Ala Thr Thr Ala Pro Ala Thr Asn Pro Ala Ser  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ala Ser Ala Val Gln Ala Lys Asp Thr Ala Phe Tyr Ile Phe Thr Ser  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Thr Thr Gly Phe Pro Lys Ala Ser Val Met Thr His His Arg Trp  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Leu Arg Ala Leu Ala Val Phe Gly Gly Met Gly Leu Arg Leu Lys Gly  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Ser Asp Thr Leu Tyr Ser Cys Leu Pro Leu Tyr His Asn Asn Ala Leu  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Thr Val Ala Val Ser Ser Val Ile Asn Ser Gly Ala Thr Leu Ala Leu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly Lys Ser Phe Ser Ala Ser Arg Phe Trp Asp Glu Val Ile Ala Asn  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Arg Ala Thr Ala Phe Val Tyr Ile Gly Glu Ile Cys Arg Tyr Leu Leu  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Asn Gln Pro Ala Lys Pro Thr Asp Arg Ala His Gln Val Arg Val Ile  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Cys Gly Asn Gly Leu Arg Pro Glu Ile Trp Asp Glu Phe Thr Thr Arg  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Phe Gly Val Ala Arg Val Cys Glu Phe Tyr Ala Ala Ser Glu Gly Asn  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Ser Ala Phe Ile Asn Ile Phe Asn Val Pro Arg Thr Ala Gly Val Ser  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Pro Met Pro Leu Ala Phe Val Glu Tyr Asp Leu Asp Thr Gly Asp Pro  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Leu Arg Asp Ala Ser Gly Arg Val Arg Arg Val Pro Asp Gly Glu Pro  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Leu Leu Leu Ser Arg Val Asn Arg Leu Gln Pro Phe Asp Gly Tyr  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Thr Asp Pro Val Ala Ser Glu Lys Lys Leu Val Arg Asn Ala Phe Arg  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Asp Gly Asp Cys Trp Phe Asn Thr Gly Asp Val Met Ser Pro Gln Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Met Gly His Ala Ala Phe Val Asp Arg Leu Gly Asp Thr Phe Arg Trp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Lys Gly Glu Asn Val Ala Thr Thr Gln Val Glu Ala Ala Leu Ala Ser  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Asp Gln Thr Val Glu Glu Cys Thr Val Tyr Gly Val Gln Ile Pro Arg  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Thr Gly Gly Arg Ala Gly Met Ala Ala Ile Thr Leu Arg Ala Gly Ala  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Glu Phe Asp Gly Gln Ala Leu Ala Arg Thr Val Tyr Gly His Leu Pro  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Gly Tyr Ala Leu Pro Leu Phe Val Arg Val Val Gly Ser Leu Ala His  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Thr Thr Thr Phe Lys Ser Arg Lys Val Glu Leu Arg Asn Gln Ala Tyr  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Gly Ala Asp Ile Glu Asp Pro Leu Tyr Val Leu Ala Gly Pro Asp Glu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Gly Tyr Val Pro Tyr Tyr Ala Glu Tyr Pro Glu Glu Val Ser Leu Gly  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Arg Arg Pro Gln Gly  
               
               
                         595  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 92  
               
               
                 &lt;211&gt; LENGTH: 646  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 92  
               
               
                   
               
               
                 Met Arg Ala Pro Gly Ala Gly Thr Ala Ser Val Ala Ser Leu Ala Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Trp Phe Leu Gly Leu Pro Trp Thr Trp Ser Ala Ala Ala Ala Phe  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Cys Val Tyr Val Gly Gly Gly Gly Trp Arg Phe Leu Arg Ile Val Cys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Lys Thr Ala Arg Arg Asp Leu Phe Gly Leu Ser Val Leu Ile Arg Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Arg Leu Glu Leu Arg Arg His Arg Arg Ala Gly Asp Thr Ile Pro Cys  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ile Phe Gln Ala Val Ala Arg Arg Gln Pro Glu Arg Leu Ala Leu Val  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Ala Ser Ser Gly Ile Cys Trp Thr Phe Ala Gln Leu Asp Thr Tyr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Asn Ala Val Ala Asn Leu Phe Arg Gln Leu Gly Phe Ala Pro Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Asp Val Val Ala Val Phe Leu Glu Gly Arg Pro Glu Phe Val Gly Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Trp Leu Gly Leu Ala Lys Ala Gly Val Val Ala Ala Leu Leu Asn Val  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asn Leu Arg Arg Glu Pro Leu Ala Phe Cys Leu Gly Thr Ser Ala Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Lys Ala Leu Ile Tyr Gly Gly Glu Met Ala Ala Ala Val Ala Glu Val  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ser Glu Gln Leu Gly Lys Ser Leu Leu Lys Phe Cys Ser Gly Asp Leu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Pro Glu Ser Ile Leu Pro Asp Thr Gln Leu Leu Asp Pro Met Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Glu Ala Pro Thr Thr Pro Leu Ala Gln Ala Pro Gly Lys Gly Met  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asp Asp Arg Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Ile Ala Ala Phe  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly His His Ser Tyr Ser Met Arg Ala Ala Asp Val Leu Tyr Asp Cys  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Leu Pro Leu Tyr His Ser Ala Gly Asn Ile Met Gly Val Gly Gln Cys  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Val Ile Tyr Gly Leu Thr Val Val Leu Arg Lys Lys Phe Ser Ala Ser  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Arg Phe Trp Asp Asp Cys Val Lys Tyr Asn Cys Thr Val Val Gln Tyr  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ile Gly Glu Ile Cys Arg Tyr Leu Leu Arg Gln Pro Val Arg Asp Val  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Glu Gln Arg His Arg Val Arg Leu Ala Val Gly Asn Gly Leu Arg Pro  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ala Ile Trp Glu Glu Phe Thr Gln Arg Phe Gly Val Pro Gln Ile Gly  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Ile Ala Asn Met Asp  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Lys Val Gly Ser Cys Gly Phe Asn Ser Arg Ile Leu Thr His Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Tyr Pro Ile Arg Leu Val Lys Val Asn Glu Asp Thr Met Glu Pro Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Arg Asp Ser Glu Gly Leu Cys Ile Pro Cys Gln Pro Gly Glu Pro Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Leu Val Gly Gln Ile Asn Gln Gln Asp Pro Leu Arg Arg Phe Asp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gly Tyr Val Ser Asp Ser Ala Thr Asn Lys Lys Ile Ala His Ser Val  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Phe Arg Lys Gly Asp Ser Ala Tyr Leu Ser Gly Asp Val Leu Val Met  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Asp Glu Leu Gly Tyr Met Tyr Phe Arg Asp Arg Ser Gly Asp Thr Phe  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Arg Trp Arg Gly Glu Asn Val Ser Thr Thr Glu Val Glu Ala Val Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ser Arg Leu Leu Gly Gln Thr Asp Val Ala Val Tyr Gly Val Ala Val  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Gly Val Glu Gly Lys Ala Gly Met Ala Ala Ile Ala Asp Pro His  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ser Gln Leu Asp Pro Asn Ser Met Tyr Gln Glu Leu Gln Lys Val Leu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Ala Ser Tyr Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Gln Val Asp  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Thr Thr Gly Thr Phe Lys Ile Gln Lys Thr Arg Leu Gln Arg Glu Gly  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Phe Asp Pro Arg Gln Thr Ser Asp Arg Leu Phe Phe Leu Asp Leu Lys  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Gln Gly Arg Tyr Leu Pro Leu Asp Glu Arg Val His Ala Arg Ile Cys  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Ala Gly Asp Phe Ser Leu  
               
               
                                 645  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 93  
               
               
                 &lt;211&gt; LENGTH: 620  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: (1)...(620)  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 285, 286, 287  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 93  
               
               
                   
               
               
                 Met Leu Pro Val Leu Tyr Thr Gly Leu Ala Gly Leu Leu Leu Leu Pro  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Leu Leu Thr Cys Cys Cys Pro Tyr Leu Leu Gln Asp Val Arg Tyr  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Phe Leu Arg Leu Ala Asn Met Ala Arg Arg Val Arg Ser Tyr Arg Gln  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Arg Arg Pro Val Arg Thr Ile Leu Arg Ala Phe Leu Glu Gln Ala Arg  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Lys Thr Pro His Lys Pro Phe Leu Leu Phe Arg Asp Glu Thr Leu Thr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Tyr Ala Gln Val Asp Arg Arg Ser Asn Gln Val Ala Arg Ala Leu His  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Gln Leu Gly Leu Arg Gln Gly Asp Cys Val Ala Leu Phe Met Gly  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Asn Glu Pro Ala Tyr Val Trp Ile Trp Leu Gly Leu Leu Lys Leu Gly  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Cys Pro Met Ala Cys Leu Asn Tyr Asn Ile Arg Ala Lys Ser Leu Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 His Cys Phe Gln Cys Cys Gly Ala Lys Val Leu Leu Ala Ser Pro Asp  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Leu Gln Glu Ala Val Glu Glu Val Leu Pro Thr Leu Lys Lys Asp Ala  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Val Ser Val Phe Tyr Val Ser Arg Thr Ser Asn Thr Asn Gly Val Asp  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Thr Ile Leu Asp Lys Val Asp Gly Val Ser Ala Glu Pro Thr Pro Glu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Ser Trp Arg Ser Glu Val Thr Phe Thr Thr Pro Ala Val Tyr Ile Tyr  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala Thr Ile Asn His His  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Arg Leu Arg Tyr Gly Thr Gly Leu Ala Met Ser Ser Gly Ile Thr Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Gln Asp Val Ile Tyr Thr Thr Met Pro Leu Tyr His Ser Ala Ala Leu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Met Ile Gly Leu His Gly Cys Ile Val Val Gly Ala Xaa Xaa Xaa Leu  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Cys Asp Lys Phe Ser Ala Ser Gln Phe Trp Asp Asp Cys Arg Lys Tyr  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Asn Val Thr Val Ile Gln Tyr Ile Gly Glu Leu Leu Arg Tyr Leu Cys  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Asn Thr Pro Gln Lys Pro Asn Asp Arg Asp His Lys Val Lys Lys Ala  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Leu Gly Asn Gly Leu Arg Gly Asp Val Trp Arg Glu Phe Ile Lys Arg  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Phe Gly Asp Ile His Val Tyr Glu Phe Tyr Ala Ser Thr Glu Gly Asn  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ile Gly Phe Val Asn Tyr Pro Arg Lys Ile Gly Ala Val Gly Arg Ala  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Asn Tyr Leu Gln Arg Lys Val Ala Arg Tyr Glu Leu Ile Lys Tyr Asp  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Val Glu Lys Asp Glu Pro Val Arg Asp Ala Asn Gly Tyr Cys Ile Lys  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Val Pro Lys Gly Glu Val Gly Leu Leu Val Cys Lys Ile Thr Gln Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Thr Pro Phe Ile Gly Tyr Ala Gly Gly Lys Thr Gln Thr Glu Lys Lys  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Lys Leu Arg Asp Val Phe Lys Lys Gly Asp Ile Tyr Phe Asn Ser Gly  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Asp Leu Leu Met Ile Asp Arg Glu Asn Phe Val Tyr Phe His Asp Arg  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Val Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala Thr Thr Glu  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Val Ala Asp Ile Val Gly Leu Val Asp Phe Val Glu Glu Val Asn Val  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Tyr Gly Val Pro Val Pro Gly His Glu Gly Arg Ile Gly Met Ala Ser  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Leu Lys Ile Lys Glu Asn Tyr Glu Phe Asn Gly Lys Lys Leu Phe Gln  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 His Ile Ala Glu Tyr Leu Pro Ser Tyr Ala Arg Pro Arg Phe Leu Arg  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ile Gln Asp Thr Ile Glu Ile Thr Gly Thr Phe Lys His Arg Lys Val  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Thr Leu Met Glu Glu Gly Phe Asn Pro Thr Val Ile Lys Asp Thr Leu  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Tyr Phe Met Asp Asp Ala Glu Lys Thr Phe Val Pro Met Thr Glu Asn  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ile Tyr Asn Ala Ile Ile Asp Lys Thr Leu Lys Leu  
               
               
                     610                 615                 620  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 94  
               
               
                 &lt;211&gt; LENGTH: 613  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 94  
               
               
                   
               
               
                 Ala Ala Asp Pro Glu Ser Ser Glu Ser Gly Cys Ser Leu Ala Trp Arg  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Ala Tyr Leu Ala Arg Glu Gln Pro Thr His Thr Phe Leu Ile His  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Ala Gln Arg Phe Ser Tyr Ala Glu Ala Glu Arg Glu Ser Asn Arg  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ile Ala Arg Ala Phe Leu Arg Ala Arg Gly Trp Thr Gly Gly Arg Arg  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Gly Ser Gly Arg Gly Ser Thr Glu Glu Gly Ala Arg Val Ala Pro Pro  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Gly Asp Ala Ala Ala Arg Gly Thr Thr Ala Pro Pro Leu Ala Pro  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Ala Thr Val Ala Leu Leu Leu Pro Ala Gly Pro Asp Phe Leu Trp  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ile Trp Phe Gly Leu Ala Lys Ala Gly Leu Arg Thr Ala Phe Val Pro  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Thr Ala Leu Arg Arg Gly Pro Leu Leu His Cys Leu Arg Ser Cys Gly  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ala Ser Ala Leu Val Leu Ala Thr Glu Phe Leu Glu Ser Leu Glu Pro  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asp Leu Pro Ala Leu Arg Ala Met Gly Leu His Leu Trp Ala Thr Gly  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Pro Glu Thr Asn Val Ala Gly Ile Ser Asn Leu Leu Ser Glu Ala Ala  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Asp Gln Val Asp Glu Pro Val Pro Gly Tyr Leu Ser Ala Pro Gln Asn  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Ile Met Asp Thr Cys Leu Tyr Ile Phe Thr Ser Gly Thr Thr Gly Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Pro Lys Ala Ala Arg Ile Ser His Leu Lys Val Leu Gln Cys Gln Gly  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Phe Tyr His Leu Cys Gly Val His Gln Glu Asp Val Ile Tyr Leu Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Leu Pro Leu Tyr His Met Ser Gly Ser Leu Leu Gly Ile Val Gly Cys  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Leu Gly Ile Gly Ala Thr Val Val Leu Lys Pro Lys Phe Ser Ala Ser  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Gln Phe Trp Asp Asp Cys Gln Lys His Arg Val Thr Val Phe Gln Tyr  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ile Gly Glu Leu Cys Arg Tyr Leu Val Asn Gln Pro Pro Ser Lys Ala  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Glu Phe Asp His Lys Val Arg Leu Ala Val Gly Ser Gly Leu Arg Pro  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Asp Thr Trp Glu Arg Phe Leu Arg Arg Phe Gly Pro Leu Gln Ile Leu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Glu Thr Tyr Gly Met Thr Glu Gly Asn Val Ala Thr Phe Asn Tyr Thr  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Gly Arg Gln Gly Ala Val Gly Arg Ala Ser Trp Leu Tyr Lys His Ile  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Phe Pro Phe Ser Leu Ile Arg Tyr Asp Val Met Thr Gly Glu Pro Ile  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Arg Asn Ala Gln Gly His Cys Met Thr Thr Ser Pro Gly Glu Pro Gly  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Leu Leu Val Ala Pro Val Ser Gln Gln Ser Pro Phe Leu Gly Tyr Ala  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Gly Ala Pro Glu Leu Ala Lys Asp Lys Leu Leu Lys Asp Val Phe Trp  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Ser Gly Asp Val Phe Phe Asn Thr Gly Asp Leu Leu Val Cys Asp Glu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gln Gly Phe Leu His Phe His Asp Arg Thr Gly Asp Thr Ile Arg Trp  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Lys Gly Glu Asn Val Ala Thr Thr Glu Val Ala Glu Val Leu Glu Thr  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Leu Asp Phe Leu Gln Glu Val Asn Ile Tyr Gly Val Thr Val Pro Gly  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 His Glu Gly Arg Ala Gly Met Ala Ala Leu Ala Leu Arg Pro Pro Gln  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Ala Leu Asn Leu Val Gln Leu Tyr Ser His Val Ser Glu Asn Leu Pro  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Tyr Ala Arg Pro Arg Phe Leu Arg Leu Gln Glu Ser Leu Ala Thr  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Thr Glu Thr Phe Lys Gln Gln Lys Val Arg Met Ala Asn Glu Gly Phe  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Asp Pro Ser Val Leu Ser Asp Pro Leu Tyr Val Leu Asp Gln Asp Ile  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Gly Ala Tyr Leu Pro Leu Thr Pro Ala Arg Tyr Ser Ala Leu Leu Ser  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Gly Asp Leu Arg Ile  
               
               
                     610  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 95  
               
               
                 &lt;211&gt; LENGTH: 506  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 95  
               
               
                   
               
               
                 His Ala Ser Ala His Ala Ser Gly Met Ala Lys Leu Gly Val Glu Ala  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ala Leu Ile Asn Thr Asn Leu Arg Arg Asp Ala Leu Arg His Cys Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Asp Thr Ser Lys Ala Arg Ala Leu Ile Phe Gly Ser Glu Met Ala Ser  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ala Ile Cys Glu Ile His Ala Ser Leu Glu Pro Thr Leu Ser Leu Phe  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Cys Ser Gly Ser Trp Glu Pro Ser Thr Val Pro Val Ser Thr Glu His  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Leu Asp Pro Leu Leu Glu Asp Ala Pro Lys His Leu Pro Ser His Pro  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Asp Lys Gly Phe Thr Asp Lys Leu Phe Tyr Ile Tyr Thr Ser Gly Thr  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Thr Gly Leu Pro Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Met Ala Ser Leu Val Tyr Tyr Gly Phe Arg Met Arg Pro Asp Asp Ile  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Val Tyr Asp Cys Leu Pro Leu Tyr His Ser Ser Arg Lys His Arg Gly  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asp Trp Gln Cys Leu Leu His Gly Met Thr Val Val Ile Arg Lys Lys  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Phe Ser Ala Ser Arg Phe Trp Asp Asp Cys Ile Lys Tyr Asn Cys Thr  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Val Val Gln Tyr Ile Gly Glu Leu Cys Arg Tyr Leu Leu Asn Gln Pro  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Pro Arg Glu Ala Glu Ser Arg His Lys Val Arg Met Ala Leu Gly Asn  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Gly Leu Arg Gln Ser Ile Trp Thr Asp Phe Ser Ser Arg Phe His Ile  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Pro Gln Val Ala Glu Phe Tyr Gly Ala Thr Glu Cys Asn Cys Ser Leu  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Gly Asn Phe Asp Ser Arg Val Gly Ala Cys Gly Phe Asn Ser Arg Ile  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Leu Ser Phe Val Tyr Pro Ile Arg Leu Val Arg Val Asn Glu Asp Thr  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Met Glu Leu Ile Arg Gly Pro Asp Gly Val Cys Ile Pro Cys Gln Pro  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Gly Gln Pro Gly Gln Leu Val Gly Arg Ile Ile Gln Gln Asp Pro Leu  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Arg Arg Phe Asp Gly Tyr Leu Asn Gln Gly Ala Asn Asn Lys Lys Ile  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ala Asn Asp Val Phe Lys Lys Gly Asp Gln Ala Tyr Leu Thr Gly Asp  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Val Leu Val Met Asp Glu Leu Gly Tyr Leu Tyr Phe Arg Asp Arg Thr  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ser Thr Thr Glu Val  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Glu Gly Thr Leu Ser Arg Leu Leu His Met Ala Asp Val Ala Val Tyr  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Val Glu Val Pro Gly Thr Glu Gly Arg Ala Gly Met Ala Ala Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Ala Ser Pro Ile Ser Asn Cys Asp Leu Glu Ser Phe Ala Gln Thr Leu  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Lys Lys Glu Leu Pro Leu Tyr Ala Arg Pro Ile Phe Leu Arg Phe Leu  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Pro Glu Leu His Lys Thr Gly Thr Phe Lys Phe Gln Lys Thr Glu Leu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Arg Lys Glu Gly Phe Asp Pro Ser Val Val Lys Asp Pro Leu Phe Tyr  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Leu Asp Ala Arg Lys Gly Cys Tyr Val Ala Leu Asp Gln Glu Ala Tyr  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Thr Arg Ile Gln Ala Gly Glu Glu Lys Leu  
               
               
                             500                 505  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 96  
               
               
                 &lt;211&gt; LENGTH: 662  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 96  
               
               
                   
               
               
                 Met Ala Leu Ala Leu Arg Trp Phe Leu Gly Asp Pro Thr Cys Leu Val  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Leu Gly Leu Ala Leu Leu Gly Arg Pro Trp Ile Ser Ser Trp Met  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Pro His Trp Leu Ser Leu Val Gly Ala Ala Leu Thr Leu Phe Leu Leu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Pro Leu Gln Pro Pro Pro Gly Leu Arg Trp Leu His Lys Asp Val Ala  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Phe Thr Phe Lys Met Leu Phe Tyr Gly Leu Lys Phe Arg Arg Arg Leu  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Asn Lys His Pro Pro Glu Thr Phe Val Asp Ala Leu Glu Arg Gln Ala  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Leu Ala Trp Pro Asp Arg Val Ala Leu Val Cys Thr Gly Ser Glu Gly  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Ser Ile Thr Asn Ser Gln Leu Asp Ala Arg Ser Cys Gln Ala Ala  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Trp Val Leu Lys Ala Lys Leu Lys Asp Ala Val Ile Gln Asn Thr Arg  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Asp Ala Ala Ala Ile Leu Val Leu Pro Ser Lys Thr Ile Ser Ala Leu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Ser Val Phe Leu Gly Leu Ala Lys Leu Gly Cys Pro Val Ala Trp Ile  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asn Pro His Ser Arg Gly Met Pro Leu Leu His Ser Val Arg Ser Ser  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Gly Ala Ser Val Leu Ile Val Asp Pro Asp Leu Gln Glu Asn Leu Glu  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Glu Val Leu Pro Lys Leu Leu Ala Glu Asn Ile His Cys Phe Tyr Leu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Gly His Ser Ser Pro Thr Pro Gly Val Glu Ala Leu Gly Ala Ser Leu  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asp Ala Ala Pro Ser Asp Pro Val Pro Ala Ser Leu Arg Ala Thr Ile  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Lys Trp Lys Ser Pro Ala Ile Phe Ile Phe Thr Ser Gly Thr Thr Gly  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Leu Pro Lys Pro Ala Ile Leu Ser His Glu Arg Val Ile Gln Val Ser  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Asn Val Leu Ser Phe Cys Gly Cys Arg Ala Asp Asp Val Val Tyr Asp  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Val Leu Pro Leu Tyr His Thr Ile Gly Leu Val Leu Gly Phe Leu Gly  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Cys Leu Gln Val Gly Ala Thr Cys Val Leu Ala Pro Lys Phe Ser Ala  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Ser Arg Phe Trp Ala Glu Cys Arg Gln His Gly Val Thr Val Ile Leu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Tyr Val Gly Glu Ile Leu Arg Tyr Leu Cys Asn Val Pro Glu Gln Pro  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Glu Asp Lys Ile His Thr Val Arg Leu Ala Met Gly Thr Gly Leu Arg  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Ala Asn Val Trp Lys Asn Phe Gln Gln Arg Phe Gly Pro Ile Arg Ile  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Trp Glu Phe Tyr Gly Ser Thr Glu Gly Asn Val Gly Leu Met Asn Tyr  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Val Gly His Cys Gly Ala Val Gly Arg Thr Ser Cys Ile Leu Arg Met  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Leu Thr Pro Phe Glu Leu Val Gln Phe Asp Ile Glu Thr Ala Glu Pro  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Leu Arg Asp Lys Gln Gly Phe Cys Ile Pro Val Glu Pro Gly Lys Pro  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gly Leu Leu Leu Thr Lys Val Arg Lys Asn Gln Pro Phe Leu Gly Tyr  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Arg Gly Ser Gln Ala Glu Ser Asn Arg Lys Leu Val Ala Asn Val Arg  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Arg Val Gly Asp Leu Tyr Phe Asn Thr Gly Asp Val Leu Thr Leu Asp  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Gln Glu Gly Phe Phe Tyr Phe Gln Asp Arg Leu Gly Asp Thr Phe Arg  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Trp Lys Gly Glu Asn Val Ser Thr Gly Glu Val Glu Cys Val Leu Ser  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Ser Leu Asp Phe Leu Glu Glu Val Asn Val Tyr Gly Val Pro Val Pro  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Gly Cys Glu Gly Lys Val Gly Met Ala Ala Val Lys Leu Ala Pro Gly  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Lys Thr Phe Asp Gly Gln Lys Leu Tyr Gln His Val Arg Ser Trp Leu  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Pro Ala Tyr Ala Thr Pro His Phe Ile Arg Ile Gln Asp Ser Leu Glu  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ile Thr Asn Thr Tyr Lys Leu Val Lys Ser Arg Leu Val Arg Glu Gly  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Phe Asp Val Gly Ile Ile Ala Asp Pro Leu Tyr Ile Leu Asp Asn Lys  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Ala Gln Thr Phe Arg Ser Leu Met Pro Asp Val Tyr Gln Ala Val Cys  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Glu Gly Thr Trp Asn Leu  
               
               
                             660  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 97  
               
               
                 &lt;211&gt; LENGTH: 650  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Caenorhabditis elegans  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 97  
               
               
                   
               
               
                 Met Lys Leu Glu Glu Leu Val Thr Val Met Leu Leu Thr Val Ala Val  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ile Ala Gln Asn Leu Pro Ile Gly Val Ile Leu Ala Gly Val Leu Ile  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Leu Tyr Ile Thr Val Val His Gly Asp Phe Ile Tyr Arg Ser Tyr Leu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Thr Leu Asn Arg Asp Leu Thr Gly Leu Ala Leu Ile Ile Glu Val Lys  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Ile Asp Leu Trp Trp Arg Leu His Gln Asn Lys Gly Ile His Glu Leu  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Phe Leu Asp Ile Val Lys Lys Asn Pro Asn Lys Pro Ala Met Ile Asp  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Ile Glu Thr Asn Thr Thr Glu Thr Tyr Ala Glu Phe Asn Ala His Cys  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Asn Arg Tyr Ala Asn Tyr Phe Gln Gly Leu Gly Tyr Arg Ser Gly Asp  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Val Val Ala Leu Tyr Met Glu Asn Ser Val Glu Phe Val Ala Ala Trp  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Met Gly Leu Ala Lys Ile Gly Val Val Thr Ala Trp Ile Asn Ser Asn  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Leu Lys Arg Glu Gln Leu Val His Cys Ile Thr Ala Ser Lys Thr Lys  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Ala Ile Ile Thr Ser Val Thr Leu Gln Asn Ile Met Leu Asp Ala Ile  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Asp Gln Lys Leu Phe Asp Val Glu Gly Ile Glu Val Tyr Ser Val Gly  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Glu Pro Lys Lys Asn Ser Gly Phe Lys Asn Leu Lys Lys Lys Leu Asp  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Gln Ile Thr Thr Glu Pro Lys Thr Leu Asp Ile Val Asp Phe Lys  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Ser Ile Leu Cys Phe Ile Tyr Thr Ser Gly Thr Thr Gly Met Pro Lys  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Ala Ala Val Met Lys His Phe Arg Tyr Tyr Ser Ile Ala Val Gly Ala  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Ala Lys Ser Phe Gly Ile Arg Pro Ser Asp Arg Met Tyr Val Ser Met  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Pro Ile Tyr His Thr Ala Ala Gly Ile Leu Gly Val Gly Gln Ala Leu  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Leu Gly Gly Ser Ser Cys Val Ile Arg Lys Lys Phe Ser Ala Ser Asn  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Phe Trp Arg Asp Cys Val Lys Tyr Asp Cys Thr Val Ser Gln Tyr Ile  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Gly Glu Ile Cys Arg Tyr Leu Leu Ala Gln Pro Val Val Glu Glu Glu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Ser Arg His Arg Met Arg Leu Leu Val Gly Asn Gly Leu Arg Ala Glu  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ile Trp Gln Pro Phe Val Asp Arg Phe Arg Val Arg Ile Gly Glu Leu  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Tyr Gly Ser Thr Glu Gly Thr Ser Ser Leu Val Asn Ile Asp Gly His  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Val Gly Ala Cys Gly Phe Leu Pro Ile Ser Pro Leu Thr Lys Lys Met  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 His Pro Val Arg Leu Ile Lys Val Asp Asp Val Thr Gly Glu Ala Ile  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Arg Thr Ser Asp Gly Leu Cys Ile Ala Cys Asn Pro Gly Glu Ser Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Ala Met Val Ser Thr Ile Arg Lys Asn Asn Pro Leu Leu Gln Phe Glu  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Gly Tyr Leu Asn Lys Lys Glu Thr Asn Lys Lys Ile Ile Arg Asp Val  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Phe Ala Lys Gly Asp Ser Cys Phe Leu Thr Gly Asp Leu Leu His Trp  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Asp Arg Leu Gly Tyr Val Tyr Phe Lys Asp Arg Thr Gly Asp Thr Phe  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Arg Trp Lys Gly Glu Asn Val Ser Thr Thr Glu Val Glu Ala Ile Leu  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 His Pro Ile Thr Gly Leu Ser Asp Ala Thr Val Tyr Gly Val Glu Val  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Pro Gln Arg Glu Gly Arg Val Gly Met Ala Ser Val Val Arg Val Val  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Ser His Glu Glu Asp Glu Thr Gln Phe Val His Arg Val Gly Ala Arg  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu Ala Ser Ser Leu Thr Ser Tyr Ala Ile Pro Gln Phe Met Arg Ile  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Cys Gln Asp Val Glu Lys Thr Gly Thr Phe Lys Leu Val Lys Thr Asn  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Leu Gln Arg Leu Gly Ile Met Asp Ala Pro Ser Asp Ser Ile Tyr Ile  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Tyr Asn Ser Glu Asn Arg Asn Phe Val Pro Phe Asp Asn Asp Leu Arg  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Cys Lys Val Ser Leu Gly Ser Tyr Pro Phe  
               
               
                                 645                 650  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 98  
               
               
                 &lt;211&gt; LENGTH: 623  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Saccharomyces cerevisiae  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 98  
               
               
                   
               
               
                 Met Ser Pro Ile Gln Val Val Val Phe Ala Leu Ser Arg Ile Phe Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Leu Phe Arg Leu Ile Lys Leu Ile Ile Thr Pro Ile Gln Lys Ser  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Leu Gly Tyr Leu Phe Gly Asn Tyr Phe Asp Glu Leu Asp Arg Lys Tyr  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Arg Tyr Lys Glu Asp Trp Tyr Ile Ile Pro Tyr Phe Leu Lys Ser Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Phe Cys Tyr Ile Ile Asp Val Arg Arg His Arg Phe Gln Asn Trp Tyr  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Leu Phe Ile Lys Gln Val Gln Gln Asn Gly Asp His Leu Ala Ile Ser  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Tyr Thr Arg Pro Met Ala Glu Lys Gly Glu Phe Gln Leu Glu Thr Phe  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Thr Tyr Ile Glu Thr Tyr Asn Ile Val Leu Arg Leu Ser His Ile Leu  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 His Phe Asp Tyr Asn Val Gln Ala Gly Asp Tyr Val Ala Ile Asp Cys  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Thr Asn Lys Pro Leu Phe Val Phe Leu Trp Leu Ser Leu Trp Asn Ile  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Gly Ala Ile Pro Ala Phe Leu Asn Tyr Asn Thr Lys Gly Thr Pro Leu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Val His Ser Leu Lys Ile Ser Asn Ile Thr Gln Val Phe Ile Asp Pro  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Asp Ala Ser Asn Pro Ile Arg Glu Ser Glu Glu Glu Ile Lys Asn Ala  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Leu Pro Asp Val Lys Leu Asn Tyr Leu Glu Glu Gln Asp Leu Met His  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Glu Leu Leu Asn Ser Gln Ser Pro Glu Phe Leu Gln Gln Asp Asn Val  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Arg Thr Pro Leu Gly Leu Thr Asp Phe Lys Pro Ser Met Leu Ile Tyr  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Thr Ser Gly Thr Thr Gly Leu Pro Lys Ser Ala Ile Met Ser Trp Arg  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Lys Ser Ser Val Gly Cys Gln Val Phe Gly His Val Leu His Met Thr  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Asn Glu Ser Thr Val Phe Thr Ala Met Pro Leu Phe His Ser Thr Ala  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ala Leu Leu Gly Ala Cys Ala Ile Leu Ser His Gly Gly Cys Leu Ala  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Leu Ser His Lys Phe Ser Ala Ser Thr Phe Trp Lys Gln Val Tyr Leu  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Thr Gly Ala Thr His Ile Gln Tyr Val Gly Glu Val Cys Arg Tyr Leu  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Leu His Thr Pro Ile Ser Lys Tyr Glu Lys Met His Lys Val Lys Val  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Ala Tyr Gly Asn Gly Leu Arg Pro Asp Ile Trp Gln Asp Phe Arg Lys  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Arg Phe Asn Ile Glu Val Ile Gly Glu Phe Tyr Ala Ala Thr Glu Ala  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Pro Phe Ala Thr Thr Thr Phe Gln Lys Gly Asp Phe Gly Ile Gly Ala  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Cys Arg Asn Tyr Gly Thr Ile Ile Gln Trp Phe Leu Ser Phe Gln Gln  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Thr Leu Val Arg Met Asp Pro Asn Asp Asp Ser Val Ile Tyr Arg Asn  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Ser Lys Gly Phe Cys Glu Val Ala Pro Val Gly Glu Pro Gly Glu Met  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Leu Met Arg Ile Phe Phe Pro Lys Lys Pro Glu Thr Ser Phe Gln Gly  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Tyr Leu Gly Asn Ala Lys Glu Thr Lys Ser Lys Val Val Arg Asp Val  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Phe Arg Arg Gly Asp Ala Trp Tyr Arg Cys Gly Asp Leu Leu Lys Ala  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Asp Glu Tyr Gly Leu Trp Tyr Phe Leu Asp Arg Met Gly Asp Thr Phe  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Arg Trp Lys Ser Glu Asn Val Ser Thr Thr Glu Val Glu Asp Gln Leu  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Thr Ala Ser Asn Lys Glu Gln Tyr Ala Gln Val Leu Val Val Gly Ile  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Lys Val Pro Lys Tyr Glu Gly Arg Ala Gly Phe Ala Val Ile Lys Leu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Thr Asp Asn Ser Leu Asp Ile Thr Ala Lys Thr Lys Leu Leu Asn Asp  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Ser Leu Ser Arg Leu Asn Leu Pro Ser Tyr Ala Met Pro Leu Phe Val  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Lys Phe Val Asp Glu Ile Lys Met Thr Asp Asn Leu Ile Lys Phe  
               
               
                     610                 615                 620  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 99  
               
               
                 &lt;211&gt; LENGTH: 597  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mycobacterium tuberculosis  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 99  
               
               
                   
               
               
                 Met Ser Asp Tyr Tyr Gly Gly Ala His Thr Thr Val Arg Leu Ile Asp  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Ala Thr Arg Met Pro Arg Val Leu Ala Asp Thr Pro Val Ile Val  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Arg Gly Ala Met Thr Gly Leu Leu Ala Arg Pro Asn Ser Lys Ala Ser  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ile Gly Thr Val Phe Gln Asp Arg Ala Ala Arg Tyr Gly Asp Arg Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Phe Leu Lys Phe Gly Asp Gln Gln Leu Thr Tyr Arg Asp Ala Asn Ala  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Thr Ala Asn Arg Tyr Ala Ala Val Leu Ala Ala Arg Gly Val Gly Pro  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Asp Val Val Gly Ile Met Leu Arg Asn Ser Pro Ser Thr Val Leu  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ala Met Leu Ala Thr Val Lys Cys Gly Ala Ile Ala Gly Met Leu Asn  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Tyr His Gln Arg Gly Glu Val Leu Ala His Ser Leu Gly Leu Leu Asp  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ala Lys Val Leu Ile Ala Glu Ser Asp Leu Val Ser Ala Val Ala Glu  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Cys Gly Ala Ser Arg Gly Arg Val Ala Gly Asp Val Leu Thr Val Glu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asp Val Glu Arg Phe Ala Thr Thr Ala Pro Ala Thr Asn Pro Ala Ser  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ala Ser Ala Val Gln Ala Lys Asp Thr Ala Phe Tyr Ile Phe Thr Ser  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Thr Thr Gly Phe Pro Lys Ala Ser Val Met Thr His His Arg Trp  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Leu Arg Ala Leu Ala Val Phe Gly Gly Met Gly Leu Arg Leu Lys Gly  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Ser Asp Thr Leu Tyr Ser Cys Leu Pro Leu Tyr His Asn Asn Ala Leu  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Thr Val Ala Val Ser Ser Val Ile Asn Ser Gly Ala Thr Leu Ala Leu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Gly Lys Ser Phe Ser Ala Ser Arg Phe Trp Asp Glu Val Ile Ala Asn  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Arg Ala Thr Ala Phe Val Tyr Ile Gly Glu Ile Cys Arg Tyr Leu Leu  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Asn Gln Pro Ala Lys Pro Thr Asp Arg Ala His Gln Val Arg Val Ile  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Cys Gly Asn Gly Leu Arg Pro Glu Ile Trp Asp Glu Phe Thr Thr Arg  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Phe Gly Val Ala Arg Val Cys Glu Phe Tyr Ala Ala Ser Glu Gly Asn  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Ser Ala Phe Ile Asn Ile Phe Asn Val Pro Arg Thr Ala Gly Val Ser  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Pro Met Pro Leu Ala Phe Val Glu Tyr Asp Leu Asp Thr Gly Asp Pro  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Leu Arg Asp Ala Ser Gly Arg Val Arg Arg Val Pro Asp Gly Glu Pro  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Gly Leu Leu Leu Ser Arg Val Asn Arg Leu Gln Pro Phe Asp Gly Tyr  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Thr Asp Pro Val Ala Ser Glu Lys Lys Leu Val Arg Asn Ala Phe Arg  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Asp Gly Asp Cys Trp Phe Asn Thr Gly Asp Val Met Ser Pro Gln Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Met Gly His Ala Ala Phe Val Asp Arg Leu Gly Asp Thr Phe Arg Trp  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Lys Gly Glu Asn Val Ala Thr Thr Gln Val Glu Ala Ala Leu Ala Ser  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Asp Gln Thr Val Glu Glu Cys Thr Val Tyr Gly Val Gln Ile Pro Arg  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Thr Gly Gly Arg Ala Gly Met Ala Ala Ile Thr Leu Arg Ala Gly Ala  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Glu Phe Asp Gly Gln Ala Leu Ala Arg Thr Val Tyr Gly His Leu Pro  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Gly Tyr Ala Leu Pro Leu Phe Val Arg Val Val Gly Ser Leu Ala His  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Thr Thr Thr Phe Lys Ser Arg Lys Val Glu Leu Arg Asn Gln Ala Tyr  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Gly Ala Asp Ile Glu Asp Pro Leu Tyr Val Leu Ala Gly Pro Asp Glu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Gly Tyr Val Pro Tyr Tyr Ala Glu Tyr Pro Glu Glu Val Ser Leu Gly  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Arg Arg Pro Gln Gly  
               
               
                         595  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 100  
               
               
                 &lt;211&gt; LENGTH: 304  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: concensus FATP signature sequence  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 100  
               
               
                   
               
               
                 Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala Ile Ile  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val His Ser Arg Tyr Tyr Arg Gly Ala Ala Leu His Ser Gly Arg Met  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Arg Pro Asp Val Val Tyr Asp Cys Leu Pro Leu Tyr His Ser Ala Ala  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Leu Ile Leu Gly Ile Gly Gln Cys Leu Leu His Gly Ala Thr Val Val  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Leu Arg Lys Lys Phe Ser Ala Ser Arg Phe Trp Asp Asp Cys Val Lys  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Tyr Asn Val Thr Val Ile Gln Tyr Ile Gly Glu Leu Cys Arg Tyr Leu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Leu Asn Gln Pro Pro Arg Pro Ala Glu Arg Arg His Lys Val Arg Leu  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ala Val Gly Asn Gly Leu Arg Pro Asp Ile Trp Glu Glu Phe Val Ser  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Arg Phe Gly Ile Pro Gln Ile Gly Glu Phe Tyr Gly Ala Thr Glu Gly  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Asn Cys Ser Leu Met Asn Tyr Asp Gly Lys Val Gly Ala Cys Gly Ser  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Arg Ile Leu Lys Lys Val Tyr Pro Ile Arg Leu Val Lys Val Asp Glu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asp Thr Gly Glu Pro Ile Arg Asp Ala Gln Gly Leu Cys Ile Pro Cys  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Gln Pro Gly Glu Pro Gly Leu Leu Val Gly Arg Ile Asn Gln Gln Asp  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Pro Phe Arg Gly Phe Gly Tyr Gly Ser Glu Gly Ala Thr Asn Lys Lys  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ile Ala Arg Asp Val Phe Lys Lys Gly Asp Val Ala Phe Asn Thr Gly  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Asp Val Leu Val Met Asp Glu Leu Gly Tyr Leu Tyr Phe Arg Asp Arg  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Thr Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ser Thr Thr Glu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Val Glu Gly Val Leu Ser Arg Leu Asp Phe Val Ala Glu Val Asn Val  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Tyr Gly Val Thr Val Pro Gly His Glu Gly Arg Ala Gly Met Ala Ala  
               
               
                     290                 295                 300  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 101  
               
               
                 &lt;211&gt; LENGTH: 2166  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: CDS  
               
               
                 &lt;222&gt; LOCATION: (19)...(2124)  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 101  
               
               
                   
               
               
                 cgacccacgc gtccgggg atg ttt gcg agc ggc tgg aac cag acg gtg ccg       51  
               
               
                                     Met Phe Ala Ser Gly Trp Asn Gln Thr Val Pro  
               
               
                                      1               5                   10  
               
               
                   
               
               
                 ata gag gaa gcg ggc tcc atg gct gcc ctc ctg ctg ctg ccc ctg ctg       99  
               
               
                 Ile Glu Glu Ala Gly Ser Met Ala Ala Leu Leu Leu Leu Pro Leu Leu  
               
               
                              15                  20                  25  
               
               
                   
               
               
                 ctg ttg cta ccg ctg ctg ctg ctg ctg aag cta cac ctc tgg ccg cag      147  
               
               
                 Leu Leu Leu Pro Leu Leu Leu Leu Leu Lys Leu His Leu Trp Pro Gln  
               
               
                          30                  35                  40  
               
               
                   
               
               
                 ttg cgc tgg ctt ccg gcg gac ttg gcc ttt gcg gtg cga gct ctg tgc      195  
               
               
                 Leu Arg Trp Leu Pro Ala Asp Leu Ala Phe Ala Val Arg Ala Leu Cys  
               
               
                      45                  50                  55  
               
               
                   
               
               
                 tgc aaa agg gct ctt cga gct cgc gcc ctg gcc gcg gct gcc gcc gac      243  
               
               
                 Cys Lys Arg Ala Leu Arg Ala Arg Ala Leu Ala Ala Ala Ala Ala Asp  
               
               
                  60                  65                  70                  75  
               
               
                   
               
               
                 ccg gaa ggt ccc gag ggg ggc tgc agc ctg gcc tgg cgc ctc gcg gaa      291  
               
               
                 Pro Glu Gly Pro Glu Gly Gly Cys Ser Leu Ala Trp Arg Leu Ala Glu  
               
               
                                  80                  85                  90  
               
               
                   
               
               
                 ctg gcc cag cag cgc gcc gcg cac acc ttt ctc att cac ggc tcg cgg      339  
               
               
                 Leu Ala Gln Gln Arg Ala Ala His Thr Phe Leu Ile His Gly Ser Arg  
               
               
                              95                 100                 105  
               
               
                   
               
               
                 cgc ttt agc tac tca gag gcg gag cgc gag agt aac agg gct gca cgc      387  
               
               
                 Arg Phe Ser Tyr Ser Glu Ala Glu Arg Glu Ser Asn Arg Ala Ala Arg  
               
               
                         110                 115                 120  
               
               
                   
               
               
                 gcc ttc cta cgt gcg cta ggc tgg gac tgg gga ccc gac ggc ggc gac      435  
               
               
                 Ala Phe Leu Arg Ala Leu Gly Trp Asp Trp Gly Pro Asp Gly Gly Asp  
               
               
                     125                 130                 135  
               
               
                   
               
               
                 agc ggc gag ggg agc gct gga gaa ggc gag cgg gca gcg ccg gga gcc      483  
               
               
                 Ser Gly Glu Gly Ser Ala Gly Glu Gly Glu Arg Ala Ala Pro Gly Ala  
               
               
                 140                 145                 150                 155  
               
               
                   
               
               
                 gga gat gca gcg gcc gga agc ggc gcg gag ttt gcc gga ggg gac ggt      531  
               
               
                 Gly Asp Ala Ala Ala Gly Ser Gly Ala Glu Phe Ala Gly Gly Asp Gly  
               
               
                                 160                 165                 170  
               
               
                   
               
               
                 gcc gcc aga ggt gga gga gag ccc gcc gcc cct ctg tca cct gga gca      579  
               
               
                 Ala Ala Arg Gly Gly Gly Glu Pro Ala Ala Pro Leu Ser Pro Gly Ala  
               
               
                             175                 180                 185  
               
               
                   
               
               
                 act gtg gcg ctg ctc ctc ccc gct ggc cca gag ttt ctg tgg ctc tgg      627  
               
               
                 Thr Val Ala Leu Leu Leu Pro Ala Gly Pro Glu Phe Leu Trp Leu Trp  
               
               
                         190                 195                 200  
               
               
                   
               
               
                 ttc ggg ctg gcc aag gcc ggc ctg cgc act gcc ttt gtg ccc acc gcc      675  
               
               
                 Phe Gly Leu Ala Lys Ala Gly Leu Arg Thr Ala Phe Val Pro Thr Ala  
               
               
                     205                 210                 215  
               
               
                   
               
               
                 ctg cgc cgg ggc ccc ctg ctg cac tgc ctc cgc agc tgc ggc gcg cgc      723  
               
               
                 Leu Arg Arg Gly Pro Leu Leu His Cys Leu Arg Ser Cys Gly Ala Arg  
               
               
                 220                 225                 230                 235  
               
               
                   
               
               
                 gcg ctg gtg ctg gcg cca gag ttt ctg gag tcc ctg gag ccg gac ctg      771  
               
               
                 Ala Leu Val Leu Ala Pro Glu Phe Leu Glu Ser Leu Glu Pro Asp Leu  
               
               
                                 240                 245                 250  
               
               
                   
               
               
                 ccc gcc ctg aga gcc atg ggg ctc cac ctg tgg gct gca ggc cca gga      819  
               
               
                 Pro Ala Leu Arg Ala Met Gly Leu His Leu Trp Ala Ala Gly Pro Gly  
               
               
                             255                 260                 265  
               
               
                   
               
               
                 acc cac cct gct gga att agc gat ttg ctg gct gaa gtg tcc gct gaa      867  
               
               
                 Thr His Pro Ala Gly Ile Ser Asp Leu Leu Ala Glu Val Ser Ala Glu  
               
               
                         270                 275                 280  
               
               
                   
               
               
                 gtg gat ggg cca gtg cca gga tac ctc tct tcc ccc cag agc ata aca      915  
               
               
                 Val Asp Gly Pro Val Pro Gly Tyr Leu Ser Ser Pro Gln Ser Ile Thr  
               
               
                     285                 290                 295  
               
               
                   
               
               
                 gac acg tgc ctg tac atc ttc acc tct ggc acc acg ggc ctc ccc aag      963  
               
               
                 Asp Thr Cys Leu Tyr Ile Phe Thr Ser Gly Thr Thr Gly Leu Pro Lys  
               
               
                 300                 305                 310                 315  
               
               
                   
               
               
                 gct gct cgg atc agt cat ctg aag atc ctg caa tgc cag ggc ttc tat     1011  
               
               
                 Ala Ala Arg Ile Ser His Leu Lys Ile Leu Gln Cys Gln Gly Phe Tyr  
               
               
                                 320                 325                 330  
               
               
                   
               
               
                 cag ctg tgt ggt gtc cac cag gaa gat gtg atc tac ctc gcc ctc cca     1059  
               
               
                 Gln Leu Cys Gly Val His Gln Glu Asp Val Ile Tyr Leu Ala Leu Pro  
               
               
                             335                 340                 345  
               
               
                   
               
               
                 ctc tac cac atg tcc ggt tcc ctg ctg ggc atc gtg ggc tgc atg ggc     1107  
               
               
                 Leu Tyr His Met Ser Gly Ser Leu Leu Gly Ile Val Gly Cys Met Gly  
               
               
                         350                 355                 360  
               
               
                   
               
               
                 att ggg gcc aca gtg gtg ctg aaa tcc aag ttc tcg gct ggt cag ttc     1155  
               
               
                 Ile Gly Ala Thr Val Val Leu Lys Ser Lys Phe Ser Ala Gly Gln Phe  
               
               
                     365                 370                 375  
               
               
                   
               
               
                 tgg gaa gat tgc cag cag cac agg gtg acg gtg ttc cag tac att ggg     1203  
               
               
                 Trp Glu Asp Cys Gln Gln His Arg Val Thr Val Phe Gln Tyr Ile Gly  
               
               
                 380                 385                 390                 395  
               
               
                   
               
               
                 gag ctg tgc cga tac ctt gtc aac cag ccc ccg agc aag gca gaa cgt     1251  
               
               
                 Glu Leu Cys Arg Tyr Leu Val Asn Gln Pro Pro Ser Lys Ala Glu Arg  
               
               
                                 400                 405                 410  
               
               
                   
               
               
                 ggc cat aag gtc cgg ctg gca gtg ggc agc ggg ctg cgc cca gat acc     1299  
               
               
                 Gly His Lys Val Arg Leu Ala Val Gly Ser Gly Leu Arg Pro Asp Thr  
               
               
                             415                 420                 425  
               
               
                   
               
               
                 tgg gag cgt ttt gtg cgg cgc ttc ggg ccc ctg cag gtg ctg gag aca     1347  
               
               
                 Trp Glu Arg Phe Val Arg Arg Phe Gly Pro Leu Gln Val Leu Glu Thr  
               
               
                         430                 435                 440  
               
               
                   
               
               
                 tat gga ctg aca gag ggc aac gtg gcc acc atc aac tac aca gga cag     1395  
               
               
                 Tyr Gly Leu Thr Glu Gly Asn Val Ala Thr Ile Asn Tyr Thr Gly Gln  
               
               
                     445                 450                 455  
               
               
                   
               
               
                 cgg ggc gct gtg ggg cgt gct tcc tgg ctt tac aag cat atc ttc ccc     1443  
               
               
                 Arg Gly Ala Val Gly Arg Ala Ser Trp Leu Tyr Lys His Ile Phe Pro  
               
               
                 460                 465                 470                 475  
               
               
                   
               
               
                 ttc tcc ttg att cgc tat gat gtc acc aca gga gag cca att cgg gac     1491  
               
               
                 Phe Ser Leu Ile Arg Tyr Asp Val Thr Thr Gly Glu Pro Ile Arg Asp  
               
               
                                 480                 485                 490  
               
               
                   
               
               
                 ccc cag ggg cac tgt atg gcc aca tct cca ggt gag cca ggg ctg ctg     1539  
               
               
                 Pro Gln Gly His Cys Met Ala Thr Ser Pro Gly Glu Pro Gly Leu Leu  
               
               
                             495                 500                 505  
               
               
                   
               
               
                 gtg gcc ccg gta agc cag cag tcc cca ttc ctg ggc tat gct ggc ggg     1587  
               
               
                 Val Ala Pro Val Ser Gln Gln Ser Pro Phe Leu Gly Tyr Ala Gly Gly  
               
               
                         510                 515                 520  
               
               
                   
               
               
                 cca gag ctg gcc cag ggg aag ttg cta aag gat gtc ttc cgg cct ggg     1635  
               
               
                 Pro Glu Leu Ala Gln Gly Lys Leu Leu Lys Asp Val Phe Arg Pro Gly  
               
               
                     525                 530                 535  
               
               
                   
               
               
                 gat gtt ttc ttc aac act ggg gac ctg ctg gtc tgc gat gac caa ggt     1683  
               
               
                 Asp Val Phe Phe Asn Thr Gly Asp Leu Leu Val Cys Asp Asp Gln Gly  
               
               
                 540                 545                 550                 555  
               
               
                   
               
               
                 ttt ctc cgc ttc cat gat cgt act gga gac acc ttc agg tgg aag ggg     1731  
               
               
                 Phe Leu Arg Phe His Asp Arg Thr Gly Asp Thr Phe Arg Trp Lys Gly  
               
               
                                 560                 565                 570  
               
               
                   
               
               
                 gag aat gtg gcc aca acc gag gtg gca gag gtc ttc gag gcc cta gat     1779  
               
               
                 Glu Asn Val Ala Thr Thr Glu Val Ala Glu Val Phe Glu Ala Leu Asp  
               
               
                             575                 580                 585  
               
               
                   
               
               
                 ttt ctt cag gag gtg aac gtc tat gga gtc act gtg cca ggg cat gaa     1827  
               
               
                 Phe Leu Gln Glu Val Asn Val Tyr Gly Val Thr Val Pro Gly His Glu  
               
               
                         590                 595                 600  
               
               
                   
               
               
                 ggc agg gct gga atg gca gcc cta gtt ctg cgt ccc ccc cac gct ttg     1875  
               
               
                 Gly Arg Ala Gly Met Ala Ala Leu Val Leu Arg Pro Pro His Ala Leu  
               
               
                     605                 610                 615  
               
               
                   
               
               
                 gac ctt atg cag ctc tac acc cac gtg tct gag aac ttg cca cct tat     1923  
               
               
                 Asp Leu Met Gln Leu Tyr Thr His Val Ser Glu Asn Leu Pro Pro Tyr  
               
               
                 620                 625                 630                 635  
               
               
                   
               
               
                 gcc cgg ccc cga ttc ctc agg ctc cag gag tct ttg gcc acc aca gag     1971  
               
               
                 Ala Arg Pro Arg Phe Leu Arg Leu Gln Glu Ser Leu Ala Thr Thr Glu  
               
               
                                 640                 645                 650  
               
               
                   
               
               
                 acc ttc aaa cag cag aaa gtt cgg atg gca aat gag ggc ttc gac ccc     2019  
               
               
                 Thr Phe Lys Gln Gln Lys Val Arg Met Ala Asn Glu Gly Phe Asp Pro  
               
               
                             655                 660                 665  
               
               
                   
               
               
                 agc acc ctg tct gac cca ctg tac gtt ctg gac cag gct gta ggt gcc     2067  
               
               
                 Ser Thr Leu Ser Asp Pro Leu Tyr Val Leu Asp Gln Ala Val Gly Ala  
               
               
                         670                 675                 680  
               
               
                   
               
               
                 tac ctg ccc ctc aca act gcc cgg tac agc gcc ctc ctg gca gga aac     2115  
               
               
                 Tyr Leu Pro Leu Thr Thr Ala Arg Tyr Ser Ala Leu Leu Ala Gly Asn  
               
               
                     685                 690                 695  
               
               
                   
               
               
                 ctt cga atc tgagaacttc cacacctgag gcacctgaga gaggaactct             2164  
               
               
                 Leu Arg Ile  
               
               
                 700  
               
               
                   
               
               
                 gt                                                                  2166  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 102  
               
               
                 &lt;211&gt; LENGTH: 702  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 102  
               
               
                   
               
               
                 Met Phe Ala Ser Gly Trp Asn Gln Thr Val Pro Ile Glu Glu Ala Gly  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ser Met Ala Ala Leu Leu Leu Leu Pro Leu Leu Leu Leu Leu Pro Leu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Leu Leu Leu Leu Lys Leu His Leu Trp Pro Gln Leu Arg Trp Leu Pro  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ala Asp Leu Ala Phe Ala Val Arg Ala Leu Cys Cys Lys Arg Ala Leu  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Arg Ala Arg Ala Leu Ala Ala Ala Ala Ala Asp Pro Glu Gly Pro Glu  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Gly Gly Cys Ser Leu Ala Trp Arg Leu Ala Glu Leu Ala Gln Gln Arg  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Ala Ala His Thr Phe Leu Ile His Gly Ser Arg Arg Phe Ser Tyr Ser  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Glu Ala Glu Arg Glu Ser Asn Arg Ala Ala Arg Ala Phe Leu Arg Ala  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Leu Gly Trp Asp Trp Gly Pro Asp Gly Gly Asp Ser Gly Glu Gly Ser  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ala Gly Glu Gly Glu Arg Ala Ala Pro Gly Ala Gly Asp Ala Ala Ala  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Gly Ser Gly Ala Glu Phe Ala Gly Gly Asp Gly Ala Ala Arg Gly Gly  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Gly Glu Pro Ala Ala Pro Leu Ser Pro Gly Ala Thr Val Ala Leu Leu  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Leu Pro Ala Gly Pro Glu Phe Leu Trp Leu Trp Phe Gly Leu Ala Lys  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Ala Gly Leu Arg Thr Ala Phe Val Pro Thr Ala Leu Arg Arg Gly Pro  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Leu Leu His Cys Leu Arg Ser Cys Gly Ala Arg Ala Leu Val Leu Ala  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Pro Glu Phe Leu Glu Ser Leu Glu Pro Asp Leu Pro Ala Leu Arg Ala  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Met Gly Leu His Leu Trp Ala Ala Gly Pro Gly Thr His Pro Ala Gly  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Ile Ser Asp Leu Leu Ala Glu Val Ser Ala Glu Val Asp Gly Pro Val  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Pro Gly Tyr Leu Ser Ser Pro Gln Ser Ile Thr Asp Thr Cys Leu Tyr  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Ile Phe Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala Arg Ile Ser  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 His Leu Lys Ile Leu Gln Cys Gln Gly Phe Tyr Gln Leu Cys Gly Val  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 His Gln Glu Asp Val Ile Tyr Leu Ala Leu Pro Leu Tyr His Met Ser  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Gly Ser Leu Leu Gly Ile Val Gly Cys Met Gly Ile Gly Ala Thr Val  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Val Leu Lys Ser Lys Phe Ser Ala Gly Gln Phe Trp Glu Asp Cys Gln  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gln His Arg Val Thr Val Phe Gln Tyr Ile Gly Glu Leu Cys Arg Tyr  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Leu Val Asn Gln Pro Pro Ser Lys Ala Glu Arg Gly His Lys Val Arg  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Leu Ala Val Gly Ser Gly Leu Arg Pro Asp Thr Trp Glu Arg Phe Val  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Arg Arg Phe Gly Pro Leu Gln Val Leu Glu Thr Tyr Gly Leu Thr Glu  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Gly Asn Val Ala Thr Ile Asn Tyr Thr Gly Gln Arg Gly Ala Val Gly  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Arg Ala Ser Trp Leu Tyr Lys His Ile Phe Pro Phe Ser Leu Ile Arg  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Tyr Asp Val Thr Thr Gly Glu Pro Ile Arg Asp Pro Gln Gly His Cys  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Met Ala Thr Ser Pro Gly Glu Pro Gly Leu Leu Val Ala Pro Val Ser  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Gln Gln Ser Pro Phe Leu Gly Tyr Ala Gly Gly Pro Glu Leu Ala Gln  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Gly Lys Leu Leu Lys Asp Val Phe Arg Pro Gly Asp Val Phe Phe Asn  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Thr Gly Asp Leu Leu Val Cys Asp Asp Gln Gly Phe Leu Arg Phe His  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Asp Arg Thr Gly Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala Thr  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Thr Glu Val Ala Glu Val Phe Glu Ala Leu Asp Phe Leu Gln Glu Val  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Asn Val Tyr Gly Val Thr Val Pro Gly His Glu Gly Arg Ala Gly Met  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Ala Ala Leu Val Leu Arg Pro Pro His Ala Leu Asp Leu Met Gln Leu  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Tyr Thr His Val Ser Glu Asn Leu Pro Pro Tyr Ala Arg Pro Arg Phe  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Leu Arg Leu Gln Glu Ser Leu Ala Thr Thr Glu Thr Phe Lys Gln Gln  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Lys Val Arg Met Ala Asn Glu Gly Phe Asp Pro Ser Thr Leu Ser Asp  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Pro Leu Tyr Val Leu Asp Gln Ala Val Gly Ala Tyr Leu Pro Leu Thr  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Thr Ala Arg Tyr Ser Ala Leu Leu Ala Gly Asn Leu Arg Ile  
               
               
                     690                 695                 700  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 103  
               
               
                 &lt;211&gt; LENGTH: 19  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Artificial Sequence  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;223&gt; OTHER INFORMATION: Oligonucleotide  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 103  
               
               
                   
               
               
                 cccccaccag agaggctcc                                                  19  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 104  
               
               
                 &lt;211&gt; LENGTH: 19  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Artificial Sequence  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;223&gt; OTHER INFORMATION: Oligonucleotide  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 104  
               
               
                   
               
               
                 ccacccccgg aaagcctgc                                                  19  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 105  
               
               
                 &lt;211&gt; LENGTH: 19  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Artificial Sequence  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;223&gt; OTHER INFORMATION: Oligonucleotide  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 105  
               
               
                   
               
               
                 ggagcctctc tggtggggg                                                  19  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 106  
               
               
                 &lt;211&gt; LENGTH: 60  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 106  
               
               
                   
               
               
                 gatggctggt ggtgtccaag ggggcggggc aggccgggtg atccggctgg gggctggaac     60  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 107  
               
               
                 &lt;211&gt; LENGTH: 59  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: (1)...(59)  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: misc_feature  
               
               
                 &lt;222&gt; LOCATION: 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33,  
               
               
                       34,35, 36, 37  
               
               
                 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 107  
               
               
                   
               
               
                 gatggctggt ggtgtccaan nnnnnnnnnn nnnnnnntga tccggctggg ggctggaac      59  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 108  
               
               
                 &lt;211&gt; LENGTH: 60  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 108  
               
               
                   
               
               
                 gatggctggt ggtgtccaag ggaacgaggc aggccgggtg atccggctgg gggctggaac     60  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 109  
               
               
                 &lt;211&gt; LENGTH: 61  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 109  
               
               
                   
               
               
                 atggctggtg gtgtccaagg gggcggggca ggccgggtga tccggctggg ggctggaact     60  
               
               
                   
               
               
                 g                                                                     61  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 110  
               
               
                 &lt;211&gt; LENGTH: 61  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 110  
               
               
                   
               
               
                 taccgaccac cacaggttcc cccgccccgt ccggcccact aggccgaccc ccgaccttga     60  
               
               
                   
               
               
                 c                                                                     61  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 111  
               
               
                 &lt;211&gt; LENGTH: 21  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 111  
               
               
                   
               
               
                 gtgtccaagg gggcggggca g                                               21  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 112  
               
               
                 &lt;211&gt; LENGTH: 21  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 112  
               
               
                   
               
               
                 cacaggttcc cccgccccgt c                                               21  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 113  
               
               
                 &lt;211&gt; LENGTH: 263  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 113  
               
               
                   
               
               
                 gaggatggct ggtggtgtcc aagggggcgg ggaggccggg tgatccggct gggggctgga     60  
               
               
                   
               
               
                 actgtagaat tcccagccag taagaactaa gtaacaaaag gacagagtcc atgggtcaca    120  
               
               
                   
               
               
                 ttcagttgct gatagtactt ggtcatattt gggaagtggg tagacagatt tccttaaagg    180  
               
               
                   
               
               
                 caggtagtta gggctttgga gcactcatca gagctaagag agattacacg ctctcatcta    240  
               
               
                   
               
               
                 cttcagaaag agccaatgcc atg                                            263  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 114  
               
               
                 &lt;211&gt; LENGTH: 9  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 114  
               
               
                   
               
               
                 ggggcgggg                                                              9  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 115  
               
               
                 &lt;211&gt; LENGTH: 10  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Artificial Sequence  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;223&gt; OTHER INFORMATION: primer  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 115  
               
               
                   
               
               
                 ctaacaggag                                                            10  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 116  
               
               
                 &lt;211&gt; LENGTH: 2402  
               
               
                 &lt;212&gt; TYPE: DNA  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: CDS  
               
               
                 &lt;222&gt; LOCATION: (51)...(2240)  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 116  
               
               
                   
               
               
                 cccgggtttc tgctctccgc ccgtgtggag tggtgggggc ctgggtggga atg ggc        56  
               
               
                                                                         Met Gly  
               
               
                                                                          1  
               
               
                   
               
               
                 gtg tgc cag cgc acg cgc gct ccc tgg aag gag aag tct cag cta gaa      104  
               
               
                 Val Cys Gln Arg Thr Arg Ala Pro Trp Lys Glu Lys Ser Gln Leu Glu  
               
               
                          5                   10                  15  
               
               
                   
               
               
                 cga gcg gcc cta ggt ttt cgg aag gga gga tca ggg atg ttt gcg agc      152  
               
               
                 Arg Ala Ala Leu Gly Phe Arg Lys Gly Gly Ser Gly Met Phe Ala Ser  
               
               
                      20                  25                  30  
               
               
                   
               
               
                 ggc tgg aac cag acg gtg ccg ata gag gaa gcg ggc tcc atg gct gcc      200  
               
               
                 Gly Trp Asn Gln Thr Val Pro Ile Glu Glu Ala Gly Ser Met Ala Ala  
               
               
                  35                  40                  45                  50  
               
               
                   
               
               
                 ctc ctg ctg ctg ccc ctg ctg ctg ttg cta ccg ctg ctg ctg ctg aag      248  
               
               
                 Leu Leu Leu Leu Pro Leu Leu Leu Leu Leu Pro Leu Leu Leu Leu Lys  
               
               
                                  55                  60                  65  
               
               
                   
               
               
                 cta cac ctc tgg ccg cag ttg cgc tgg ctt ccg gcg gac ttg gcc ttt      296  
               
               
                 Leu His Leu Trp Pro Gln Leu Arg Trp Leu Pro Ala Asp Leu Ala Phe  
               
               
                              70                  75                  80  
               
               
                   
               
               
                 gcg gtg cga gct ctg tgc tgc aaa agg gct ctt cga gct cgc gcc ctg      344  
               
               
                 Ala Val Arg Ala Leu Cys Cys Lys Arg Ala Leu Arg Ala Arg Ala Leu  
               
               
                          85                  90                  95  
               
               
                   
               
               
                 gcc gcg gct gcc gcc gac ccg gaa ggt ccc gag ggg ggc tgc agc ctg      392  
               
               
                 Ala Ala Ala Ala Ala Asp Pro Glu Gly Pro Glu Gly Gly Cys Ser Leu  
               
               
                     100                 105                 110  
               
               
                   
               
               
                 gcc tgg cgc ctc gcg gaa ctg gcc cag cag cgc gcc gcg cac acc ttt      440  
               
               
                 Ala Trp Arg Leu Ala Glu Leu Ala Gln Gln Arg Ala Ala His Thr Phe  
               
               
                 115                 120                 125                 130  
               
               
                   
               
               
                 ctc att cac ggc tcg cgg cgc ttt agc tac tca gag gcg gag cgc gag      488  
               
               
                 Leu Ile His Gly Ser Arg Arg Phe Ser Tyr Ser Glu Ala Glu Arg Glu  
               
               
                                 135                 140                 145  
               
               
                   
               
               
                 agt aac agg gct gca cgc gcc ttc cta cgt gcg cta ggc tgg gac tgg      536  
               
               
                 Ser Asn Arg Ala Ala Arg Ala Phe Leu Arg Ala Leu Gly Trp Asp Trp  
               
               
                             150                 155                 160  
               
               
                   
               
               
                 gga ccc gac ggc ggc gac agc ggc gag ggg agc gct gga gaa ggc gag      584  
               
               
                 Gly Pro Asp Gly Gly Asp Ser Gly Glu Gly Ser Ala Gly Glu Gly Glu  
               
               
                         165                 170                 175  
               
               
                   
               
               
                 cgg gca gcg ccg gga gcc gga gat gca gcg gcc gga agc ggc gcg gag      632  
               
               
                 Arg Ala Ala Pro Gly Ala Gly Asp Ala Ala Ala Gly Ser Gly Ala Glu  
               
               
                     180                 185                 190  
               
               
                   
               
               
                 ttt gcc gga ggg gac ggt gcc gcc aga ggt gga gga gcc gcc gcc cct      680  
               
               
                 Phe Ala Gly Gly Asp Gly Ala Ala Arg Gly Gly Gly Ala Ala Ala Pro  
               
               
                 195                 200                 205                 210  
               
               
                   
               
               
                 ctg tca cct gga gca act gtg gcg ctg ctc ctc ccc gct ggc cca gag      728  
               
               
                 Leu Ser Pro Gly Ala Thr Val Ala Leu Leu Leu Pro Ala Gly Pro Glu  
               
               
                                 215                 220                 225  
               
               
                   
               
               
                 ttt ctg tgg ctc tgg ttc ggg ctg gcc aag gcc ggc ctg cgc act gcc      776  
               
               
                 Phe Leu Trp Leu Trp Phe Gly Leu Ala Lys Ala Gly Leu Arg Thr Ala  
               
               
                             230                 235                 240  
               
               
                   
               
               
                 ttt gtg ccc acc gcc ctg cgc cgg ggc ccc ctg ctg cac tgc ctc cgc      824  
               
               
                 Phe Val Pro Thr Ala Leu Arg Arg Gly Pro Leu Leu His Cys Leu Arg  
               
               
                         245                 250                 255  
               
               
                   
               
               
                 agc tgc ggc gcg cgc gcg ctg gtg ctg gcg cca gag ttt ctg gag tcc      872  
               
               
                 Ser Cys Gly Ala Arg Ala Leu Val Leu Ala Pro Glu Phe Leu Glu Ser  
               
               
                     260                 265                 270  
               
               
                   
               
               
                 ctg gag ccg gac ctg ccc gcc ctg aga gcc atg ggg ctc cac ctg tgg      920  
               
               
                 Leu Glu Pro Asp Leu Pro Ala Leu Arg Ala Met Gly Leu His Leu Trp  
               
               
                 275                 280                 285                 290  
               
               
                   
               
               
                 gct gca ggc cca gga acc cac cct gct gga att agc gat ttg ctg gct      968  
               
               
                 Ala Ala Gly Pro Gly Thr His Pro Ala Gly Ile Ser Asp Leu Leu Ala  
               
               
                                 295                 300                 305  
               
               
                   
               
               
                 gaa gtg tcc gct gaa gtg gat ggg cca gtg cca gga tac ctc tct tcc     1016  
               
               
                 Glu Val Ser Ala Glu Val Asp Gly Pro Val Pro Gly Tyr Leu Ser Ser  
               
               
                             310                 315                 320  
               
               
                   
               
               
                 ccc cag agc ata aca gac acg tgc ctg tac atc ttc acc tct ggc acc     1064  
               
               
                 Pro Gln Ser Ile Thr Asp Thr Cys Leu Tyr Ile Phe Thr Ser Gly Thr  
               
               
                         325                 330                 335  
               
               
                   
               
               
                 acg ggc ctc ccc aag gct gct cgg atc agt cat ctg aag atc ctg caa     1112  
               
               
                 Thr Gly Leu Pro Lys Ala Ala Arg Ile Ser His Leu Lys Ile Leu Gln  
               
               
                     340                 345                 350  
               
               
                   
               
               
                 tgc cag ggc ttc tat cag ctg tgt ggt gtc cac cag gaa gat gtg atc     1160  
               
               
                 Cys Gln Gly Phe Tyr Gln Leu Cys Gly Val His Gln Glu Asp Val Ile  
               
               
                 355                 360                 365                 370  
               
               
                   
               
               
                 tac ctc gcc ctc cca ctc tac cac atg tcc ggt tcc ctg ctg ggc atc     1208  
               
               
                 Tyr Leu Ala Leu Pro Leu Tyr His Met Ser Gly Ser Leu Leu Gly Ile  
               
               
                                 375                 380                 385  
               
               
                   
               
               
                 gtg ggc tgc atg ggc att ggg gcc aca gtg gtg ctg aaa tcc aag ttc     1256  
               
               
                 Val Gly Cys Met Gly Ile Gly Ala Thr Val Val Leu Lys Ser Lys Phe  
               
               
                             390                 395                 400  
               
               
                   
               
               
                 tcg gct ggt cag ttc tgg gaa gat tgc cag cag cac agg gtg acg gtg     1304  
               
               
                 Ser Ala Gly Gln Phe Trp Glu Asp Cys Gln Gln His Arg Val Thr Val  
               
               
                         405                 410                 415  
               
               
                   
               
               
                 ttc cag tac att ggg gag ctg tgc cga tac ctt gtc aac cag ccc ccg     1352  
               
               
                 Phe Gln Tyr Ile Gly Glu Leu Cys Arg Tyr Leu Val Asn Gln Pro Pro  
               
               
                     420                 425                 430  
               
               
                   
               
               
                 agc aag gca gaa cgt ggc cat aag gtc cgg ctg gca gtg ggc agc ggg     1400  
               
               
                 Ser Lys Ala Glu Arg Gly His Lys Val Arg Leu Ala Val Gly Ser Gly  
               
               
                 435                 440                 445                 450  
               
               
                   
               
               
                 ctg cgc cca gat acc tgg gag cgt ttt gtg cgg cgc ttc ggg ccc ctg     1448  
               
               
                 Leu Arg Pro Asp Thr Trp Glu Arg Phe Val Arg Arg Phe Gly Pro Leu  
               
               
                                 455                 460                 465  
               
               
                   
               
               
                 cag gtg ctg gag aca tat gga ctg aca gag ggc aac gtg gcc acc atc     1496  
               
               
                 Gln Val Leu Glu Thr Tyr Gly Leu Thr Glu Gly Asn Val Ala Thr Ile  
               
               
                             470                 475                 480  
               
               
                   
               
               
                 aac tac aca gga cag cgg ggc gct gtg ggg cgt gct tcc tgg ctt tac     1544  
               
               
                 Asn Tyr Thr Gly Gln Arg Gly Ala Val Gly Arg Ala Ser Trp Leu Tyr  
               
               
                         485                 490                 495  
               
               
                   
               
               
                 aag cat atc ttc ccc ttc tcc ttg att cgc tat gat gtc acc aca gga     1592  
               
               
                 Lys His Ile Phe Pro Phe Ser Leu Ile Arg Tyr Asp Val Thr Thr Gly  
               
               
                     500                 505                 510  
               
               
                   
               
               
                 gag cca att cgg gac ccc cag ggg cac tgt atg gcc aca tct cca ggt     1640  
               
               
                 Glu Pro Ile Arg Asp Pro Gln Gly His Cys Met Ala Thr Ser Pro Gly  
               
               
                 515                 520                 525                 530  
               
               
                   
               
               
                 gag cca ggg ctg ctg gtg gcc ccg gta agc cag cag tcc cca ttc ctg     1688  
               
               
                 Glu Pro Gly Leu Leu Val Ala Pro Val Ser Gln Gln Ser Pro Phe Leu  
               
               
                                 535                 540                 545  
               
               
                   
               
               
                 ggc tat gct ggc ggg cca gag ctg gcc cag ggg aag ttg cta aag gat     1736  
               
               
                 Gly Tyr Ala Gly Gly Pro Glu Leu Ala Gln Gly Lys Leu Leu Lys Asp  
               
               
                             550                 555                 560  
               
               
                   
               
               
                 gtc ttc cgg cct ggg gat gtt ttc ttc aac act ggg gac ctg ctg gtc     1784  
               
               
                 Val Phe Arg Pro Gly Asp Val Phe Phe Asn Thr Gly Asp Leu Leu Val  
               
               
                         565                 570                 575  
               
               
                   
               
               
                 tgc gat gac caa ggt ttt ctc cgc ttc cat gat cgt act gga gac acc     1832  
               
               
                 Cys Asp Asp Gln Gly Phe Leu Arg Phe His Asp Arg Thr Gly Asp Thr  
               
               
                     580                 585                 590  
               
               
                   
               
               
                 ttc agg tgg aag ggg gag aat gtg gcc aca acc gag gtg gca gag gtc     1880  
               
               
                 Phe Arg Trp Lys Gly Glu Asn Val Ala Thr Thr Glu Val Ala Glu Val  
               
               
                 595                 600                 605                 610  
               
               
                   
               
               
                 ttc gag gcc cta gat ttt ctt cag gag gtg aac gtc tat gga gtc act     1928  
               
               
                 Phe Glu Ala Leu Asp Phe Leu Gln Glu Val Asn Val Tyr Gly Val Thr  
               
               
                                 615                 620                 625  
               
               
                   
               
               
                 gtg cca ggg cat gaa ggc agg gct gga atg gca gcc cta gtt ctg cgt     1976  
               
               
                 Val Pro Gly His Glu Gly Arg Ala Gly Met Ala Ala Leu Val Leu Arg  
               
               
                             630                 635                 640  
               
               
                   
               
               
                 ccc ccc cac gct ttg gac ctt atg cag ctc tac acc cac gtg tct gag     2024  
               
               
                 Pro Pro His Ala Leu Asp Leu Met Gln Leu Tyr Thr His Val Ser Glu  
               
               
                         645                 650                 655  
               
               
                   
               
               
                 aac ttg cca cct tat gcc cgg ccc cga ttc ctc agg ctc cag gag tct     2072  
               
               
                 Asn Leu Pro Pro Tyr Ala Arg Pro Arg Phe Leu Arg Leu Gln Glu Ser  
               
               
                     660                 665                 670  
               
               
                   
               
               
                 ttg gcc acc aca gag acc ttc aaa cag cag aaa gtt cgg atg gca aat     2120  
               
               
                 Leu Ala Thr Thr Glu Thr Phe Lys Gln Gln Lys Val Arg Met Ala Asn  
               
               
                 675                 680                 685                 690  
               
               
                   
               
               
                 gag ggc ttc gac ccc agc acc ctg tct gac cca ctg tac gtt ctg gac     2168  
               
               
                 Glu Gly Phe Asp Pro Ser Thr Leu Ser Asp Pro Leu Tyr Val Leu Asp  
               
               
                                 695                 700                 705  
               
               
                   
               
               
                 cag gct gta ggt gcc tac ctg ccc ctc aca act gcc cgg tac agc gcc     2216  
               
               
                 Gln Ala Val Gly Ala Tyr Leu Pro Leu Thr Thr Ala Arg Tyr Ser Ala  
               
               
                             710                 715                 720  
               
               
                   
               
               
                 ctc ctg gca gga aac ctt cga atc tgagaacttc cacacctgag gcacctgaga    2270  
               
               
                 Leu Leu Ala Gly Asn Leu Arg Ile  
               
               
                         725                 730  
               
               
                   
               
               
                 gaggaactct gtggggtggg ggccgttgca ggtgtactgg gctgtcaggg atcttttcta   2330  
               
               
                   
               
               
                 taccagaact gcggtcacta ttttgtaata aatgtggctg gagctgatcc agctgtctct   2390  
               
               
                   
               
               
                 gaaaaaaaaa aa                                                       2402  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 117  
               
               
                 &lt;211&gt; LENGTH: 730  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 117  
               
               
                   
               
               
                 Met Gly Val Cys Gln Arg Thr Arg Ala Pro Trp Lys Glu Lys Ser Gln  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Glu Arg Ala Ala Leu Gly Phe Arg Lys Gly Gly Ser Gly Met Phe  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Ala Ser Gly Trp Asn Gln Thr Val Pro Ile Glu Glu Ala Gly Ser Met  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ala Ala Leu Leu Leu Leu Pro Leu Leu Leu Leu Leu Pro Leu Leu Leu  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Leu Lys Leu His Leu Trp Pro Gln Leu Arg Trp Leu Pro Ala Asp Leu  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Phe Ala Val Arg Ala Leu Cys Cys Lys Arg Ala Leu Arg Ala Arg  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Ala Leu Ala Ala Ala Ala Ala Asp Pro Glu Gly Pro Glu Gly Gly Cys  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Ser Leu Ala Trp Arg Leu Ala Glu Leu Ala Gln Gln Arg Ala Ala His  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Thr Phe Leu Ile His Gly Ser Arg Arg Phe Ser Tyr Ser Glu Ala Glu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Arg Glu Ser Asn Arg Ala Ala Arg Ala Phe Leu Arg Ala Leu Gly Trp  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Asp Trp Gly Pro Asp Gly Gly Asp Ser Gly Glu Gly Ser Ala Gly Glu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Gly Glu Arg Ala Ala Pro Gly Ala Gly Asp Ala Ala Ala Gly Ser Gly  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ala Glu Phe Ala Gly Gly Asp Gly Ala Ala Arg Gly Gly Gly Ala Ala  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Ala Pro Leu Ser Pro Gly Ala Thr Val Ala Leu Leu Leu Pro Ala Gly  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Pro Glu Phe Leu Trp Leu Trp Phe Gly Leu Ala Lys Ala Gly Leu Arg  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Thr Ala Phe Val Pro Thr Ala Leu Arg Arg Gly Pro Leu Leu His Cys  
               
               
                                 245                 250                 255  
               
               
                   
               
               
                 Leu Arg Ser Cys Gly Ala Arg Ala Leu Val Leu Ala Pro Glu Phe Leu  
               
               
                             260                 265                 270  
               
               
                   
               
               
                 Glu Ser Leu Glu Pro Asp Leu Pro Ala Leu Arg Ala Met Gly Leu His  
               
               
                         275                 280                 285  
               
               
                   
               
               
                 Leu Trp Ala Ala Gly Pro Gly Thr His Pro Ala Gly Ile Ser Asp Leu  
               
               
                     290                 295                 300  
               
               
                   
               
               
                 Leu Ala Glu Val Ser Ala Glu Val Asp Gly Pro Val Pro Gly Tyr Leu  
               
               
                 305                 310                 315                 320  
               
               
                   
               
               
                 Ser Ser Pro Gln Ser Ile Thr Asp Thr Cys Leu Tyr Ile Phe Thr Ser  
               
               
                                 325                 330                 335  
               
               
                   
               
               
                 Gly Thr Thr Gly Leu Pro Lys Ala Ala Arg Ile Ser His Leu Lys Ile  
               
               
                             340                 345                 350  
               
               
                   
               
               
                 Leu Gln Cys Gln Gly Phe Tyr Gln Leu Cys Gly Val His Gln Glu Asp  
               
               
                         355                 360                 365  
               
               
                   
               
               
                 Val Ile Tyr Leu Ala Leu Pro Leu Tyr His Met Ser Gly Ser Leu Leu  
               
               
                     370                 375                 380  
               
               
                   
               
               
                 Gly Ile Val Gly Cys Met Gly Ile Gly Ala Thr Val Val Leu Lys Ser  
               
               
                 385                 390                 395                 400  
               
               
                   
               
               
                 Lys Phe Ser Ala Gly Gln Phe Trp Glu Asp Cys Gln Gln His Arg Val  
               
               
                                 405                 410                 415  
               
               
                   
               
               
                 Thr Val Phe Gln Tyr Ile Gly Glu Leu Cys Arg Tyr Leu Val Asn Gln  
               
               
                             420                 425                 430  
               
               
                   
               
               
                 Pro Pro Ser Lys Ala Glu Arg Gly His Lys Val Arg Leu Ala Val Gly  
               
               
                         435                 440                 445  
               
               
                   
               
               
                 Ser Gly Leu Arg Pro Asp Thr Trp Glu Arg Phe Val Arg Arg Phe Gly  
               
               
                     450                 455                 460  
               
               
                   
               
               
                 Pro Leu Gln Val Leu Glu Thr Tyr Gly Leu Thr Glu Gly Asn Val Ala  
               
               
                 465                 470                 475                 480  
               
               
                   
               
               
                 Thr Ile Asn Tyr Thr Gly Gln Arg Gly Ala Val Gly Arg Ala Ser Trp  
               
               
                                 485                 490                 495  
               
               
                   
               
               
                 Leu Tyr Lys His Ile Phe Pro Phe Ser Leu Ile Arg Tyr Asp Val Thr  
               
               
                             500                 505                 510  
               
               
                   
               
               
                 Thr Gly Glu Pro Ile Arg Asp Pro Gln Gly His Cys Met Ala Thr Ser  
               
               
                         515                 520                 525  
               
               
                   
               
               
                 Pro Gly Glu Pro Gly Leu Leu Val Ala Pro Val Ser Gln Gln Ser Pro  
               
               
                     530                 535                 540  
               
               
                   
               
               
                 Phe Leu Gly Tyr Ala Gly Gly Pro Glu Leu Ala Gln Gly Lys Leu Leu  
               
               
                 545                 550                 555                 560  
               
               
                   
               
               
                 Lys Asp Val Phe Arg Pro Gly Asp Val Phe Phe Asn Thr Gly Asp Leu  
               
               
                                 565                 570                 575  
               
               
                   
               
               
                 Leu Val Cys Asp Asp Gln Gly Phe Leu Arg Phe His Asp Arg Thr Gly  
               
               
                             580                 585                 590  
               
               
                   
               
               
                 Asp Thr Phe Arg Trp Lys Gly Glu Asn Val Ala Thr Thr Glu Val Ala  
               
               
                         595                 600                 605  
               
               
                   
               
               
                 Glu Val Phe Glu Ala Leu Asp Phe Leu Gln Glu Val Asn Val Tyr Gly  
               
               
                     610                 615                 620  
               
               
                   
               
               
                 Val Thr Val Pro Gly His Glu Gly Arg Ala Gly Met Ala Ala Leu Val  
               
               
                 625                 630                 635                 640  
               
               
                   
               
               
                 Leu Arg Pro Pro His Ala Leu Asp Leu Met Gln Leu Tyr Thr His Val  
               
               
                                 645                 650                 655  
               
               
                   
               
               
                 Ser Glu Asn Leu Pro Pro Tyr Ala Arg Pro Arg Phe Leu Arg Leu Gln  
               
               
                             660                 665                 670  
               
               
                   
               
               
                 Glu Ser Leu Ala Thr Thr Glu Thr Phe Lys Gln Gln Lys Val Arg Met  
               
               
                         675                 680                 685  
               
               
                   
               
               
                 Ala Asn Glu Gly Phe Asp Pro Ser Thr Leu Ser Asp Pro Leu Tyr Val  
               
               
                     690                 695                 700  
               
               
                   
               
               
                 Leu Asp Gln Ala Val Gly Ala Tyr Leu Pro Leu Thr Thr Ala Arg Tyr  
               
               
                 705                 710                 715                 720  
               
               
                   
               
               
                 Ser Ala Leu Leu Ala Gly Asn Leu Arg Ile  
               
               
                                 725                 730  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 118  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 118  
               
               
                   
               
               
                 000  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 119  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 119  
               
               
                   
               
               
                 000  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 120  
               
               
                 &lt;211&gt; LENGTH: 89  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Mus musculus  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 120  
               
               
                   
               
               
                 Arg Pro Pro Gln Ala Leu Asn Leu Val Gln Leu Tyr Ser His Val Ser  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Glu Asn Leu Pro Pro Tyr Ala Arg Pro Arg Phe Leu Arg Leu Gln Glu  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Ser Leu Ala Thr Thr Glu Thr Phe Lys Gln Gln Lys Val Arg Met Ala  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Asn Glu Gly Phe Asp Pro Ser Val Leu Ser Asp Pro Leu Tyr Val Leu  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Asp Gln Asp Ile Gly Ala Tyr Leu Pro Leu Thr Pro Ala Arg Tyr Ser  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Ala Leu Leu Ser Gly Asp Leu Arg Ile  
               
               
                                 85  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 121  
               
               
                 &lt;211&gt; LENGTH: 197  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 121  
               
               
                   
               
               
                 Arg Val Phe Ile Lys Thr Ile Arg Arg Asp Ile Phe Gly Gly Leu Val  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Leu Lys Val Lys Ala Lys Val Arg Gln Cys Leu Gln Glu Arg Arg  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Thr Val Pro Ile Leu Phe Ala Ser Thr Val Arg Arg His Pro Asp Lys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Thr Ala Leu Ile Phe Glu Gly Thr Asp Thr His Trp Thr Phe Arg Gln  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Leu Asp Glu Tyr Ser Ser Ser Val Ala Asn Phe Leu Gln Ala Arg Gly  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Leu Ala Ser Gly Asp Val Ala Ala Ile Phe Met Glu Asn Arg Asn Glu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Phe Val Gly Leu Trp Leu Gly Met Ala Lys Leu Gly Val Glu Ala Ala  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Leu Ile Asn Thr Asn Leu Arg Arg Asp Ala Leu Leu His Cys Leu Thr  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Thr Ser Arg Ala Arg Ala Leu Val Phe Gly Ser Glu Met Ala Ser Ala  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ile Cys Glu Val His Ala Ser Leu Asp Pro Ser Leu Ser Leu Phe Cys  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Ser Gly Ser Trp Glu Pro Gly Ala Val Pro Pro Ser Thr Glu His Leu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asp Pro Leu Leu Lys Asp Ala Pro Lys His Leu Pro Ser Cys Pro Asp  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Lys Gly Phe Thr Asp  
               
               
                         195  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 122  
               
               
                 &lt;211&gt; LENGTH: 248  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 122  
               
               
                   
               
               
                 Arg Val Phe Ile Lys Thr Ile Arg Arg Asp Ile Phe Gly Gly Leu Val  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Leu Lys Val Lys Ala Lys Val Arg Gln Cys Leu Gln Glu Arg Arg  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Thr Val Pro Ile Leu Phe Ala Ser Thr Val Arg Arg His Pro Asp Lys  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Thr Ala Leu Ile Phe Glu Gly Thr Asp Thr His Trp Thr Phe Arg Gln  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Leu Asp Glu Tyr Ser Ser Ser Val Ala Asn Phe Leu Gln Ala Arg Gly  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Leu Ala Ser Gly Asp Val Ala Ala Ile Phe Met Glu Asn Arg Asn Glu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Phe Val Gly Leu Trp Leu Gly Met Ala Lys Leu Gly Val Glu Ala Ala  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Leu Ile Asn Thr Asn Leu Arg Arg Asp Ala Leu Leu His Cys Leu Thr  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Thr Ser Arg Ala Arg Ala Leu Val Phe Gly Ser Glu Met Ala Ser Ala  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Ile Cys Glu Val His Ala Ser Leu Asp Pro Ser Leu Ser Leu Phe Cys  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Ser Gly Ser Trp Glu Pro Gly Ala Val Pro Pro Ser Thr Glu His Leu  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Asp Pro Leu Leu Lys Asp Ala Pro Lys His Leu Pro Ser Cys Pro Asp  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Lys Gly Phe Thr Asp Lys Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Gly Leu Pro Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Met  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Ala Ala Leu Val Tyr Tyr Gly Phe Arg Met Arg Pro Asn Asp Ile Val  
               
               
                 225                 230                 235                 240  
               
               
                   
               
               
                 Tyr Asp Cys Leu Pro Leu Tyr His  
               
               
                                 245  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 123  
               
               
                 &lt;211&gt; LENGTH: 165  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 123  
               
               
                   
               
               
                 Gly Asp Val Ala Ala Ile Phe Met Glu Asn Arg Asn Glu Phe Val Gly  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Leu Trp Leu Gly Met Ala Lys Leu Gly Val Glu Ala Ala Leu Ile Asn  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Thr Asn Leu Arg Arg Asp Ala Leu Leu His Cys Leu Thr Thr Ser Arg  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Ala Arg Ala Leu Val Phe Gly Ser Glu Met Ala Ser Ala Ile Cys Glu  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Val His Ala Ser Leu Asp Pro Ser Leu Ser Leu Phe Cys Ser Gly Ser  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Trp Glu Pro Gly Ala Val Pro Pro Ser Thr Glu His Leu Asp Pro Leu  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Leu Lys Asp Ala Pro Lys His Leu Pro Ser Cys Pro Asp Lys Gly Phe  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Thr Asp Lys Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Lys Ala Ala Ile Val Val His Ser Arg Tyr Tyr Arg Met Ala Ala Leu  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Val Tyr Tyr Gly Phe Arg Met Arg Pro Asn Asp Ile Val Tyr Asp Cys  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Leu Pro Leu Tyr His  
               
               
                                 165  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 124  
               
               
                 &lt;211&gt; LENGTH: 227  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 124  
               
               
                   
               
               
                 Arg Leu Val Arg Val Asn Glu Asp Thr Met Glu Leu Ile Arg Gly Pro  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Asp Gly Val Cys Ile Pro Cys Gln Pro Gly Glu Pro Gly Gln Leu Val  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Arg Ile Ile Gln Lys Asp Pro Leu Arg Arg Phe Asp Gly Tyr Leu  
               
               
                         35                  40                  45  
               
               
                   
               
               
                 Asn Gln Gly Ala Asn Asn Lys Lys Ile Ala Lys Asp Val Phe Lys Lys  
               
               
                     50                  55                  60  
               
               
                   
               
               
                 Gly Asp Gln Ala Tyr Leu Thr Gly Asp Val Leu Val Met Asp Glu Leu  
               
               
                 65                  70                  75                  80  
               
               
                   
               
               
                 Gly Tyr Leu Tyr Phe Arg Asp Arg Thr Gly Asp Thr Phe Arg Trp Lys  
               
               
                                 85                  90                  95  
               
               
                   
               
               
                 Gly Glu Asn Val Ser Thr Thr Glu Val Glu Gly Thr Leu Ser Arg Leu  
               
               
                             100                 105                 110  
               
               
                   
               
               
                 Leu Asp Met Ala Asp Val Ala Val Tyr Gly Val Glu Val Pro Gly Thr  
               
               
                         115                 120                 125  
               
               
                   
               
               
                 Glu Gly Arg Ala Gly Met Ala Ala Val Ala Ser Pro Thr Gly Asn Cys  
               
               
                     130                 135                 140  
               
               
                   
               
               
                 Asp Leu Glu Arg Phe Ala Gln Val Leu Glu Lys Glu Leu Pro Leu Tyr  
               
               
                 145                 150                 155                 160  
               
               
                   
               
               
                 Ala Arg Pro Ile Phe Leu Arg Leu Leu Pro Glu Leu His Lys Thr Gly  
               
               
                                 165                 170                 175  
               
               
                   
               
               
                 Thr Tyr Lys Phe Gln Lys Thr Glu Leu Arg Lys Glu Gly Phe Asp Pro  
               
               
                             180                 185                 190  
               
               
                   
               
               
                 Ala Ile Val Lys Asp Pro Leu Phe Tyr Leu Asp Ala Gln Lys Gly Arg  
               
               
                         195                 200                 205  
               
               
                   
               
               
                 Tyr Val Pro Leu Asp Gln Glu Ala Tyr Ser Arg Ile Gln Ala Gly Glu  
               
               
                     210                 215                 220  
               
               
                   
               
               
                 Glu Lys Leu  
               
               
                 225  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 125  
               
               
                 &lt;211&gt; LENGTH: 41  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Artificial Sequence  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;223&gt; OTHER INFORMATION: Lipocalin signature sequence  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: (1)...(41)  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;221&gt; NAME/KEY: VARIANT  
               
               
                 &lt;222&gt; LOCATION: 5, 16, 17, 41  
               
               
                 &lt;223&gt; OTHER INFORMATION: Xaa = Any Amino Acid  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 125  
               
               
                   
               
               
                 Asp Glu Asn Gly Xaa Asp Glu Asn Gln Gly Ser Thr Ala Arg Lys Xaa  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Xaa Asp Glu Asn Gln Ala Arg Lys Leu Ile Val Phe Tyr Cys Pro Gly  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Cys Trp Phe Tyr Trp Leu Arg His Xaa  
               
               
                         35                  40  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 126  
               
               
                 &lt;211&gt; LENGTH: 13  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 126  
               
               
                   
               
               
                 Ser Asn Glu Pro Asp Phe Val His Val Trp Phe Gly Leu  
               
               
                  1               5                  10  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 127  
               
               
                 &lt;211&gt; LENGTH: 13  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 127  
               
               
                   
               
               
                 Gly Asn Glu Pro Ala Tyr Val Trp Leu Trp Leu Gly Leu  
               
               
                  1               5                  10  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 128  
               
               
                 &lt;211&gt; LENGTH: 13  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 128  
               
               
                   
               
               
                 Pro Ala Gly Pro Glu Phe Leu Trp Leu Trp Phe Gly Leu  
               
               
                  1               5                  10  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 129  
               
               
                 &lt;211&gt; LENGTH: 15  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 129  
               
               
                   
               
               
                 Leu Ala Ser Gln Ala Val Pro Ala Leu Cys Met Trp Leu Gly Leu  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 130  
               
               
                 &lt;211&gt; LENGTH: 13  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 130  
               
               
                   
               
               
                 Glu Asn Arg Asn Glu Phe Val Gly Leu Trp Leu Gly Met  
               
               
                  1               5                  10  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 131  
               
               
                 &lt;211&gt; LENGTH: 13  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 131  
               
               
                   
               
               
                 Glu Gly Arg Pro Glu Phe Val Gly Leu Trp Leu Gly Leu  
               
               
                  1               5                  10  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 132  
               
               
                 &lt;211&gt; LENGTH: 20  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 132  
               
               
                   
               
               
                 Cys Leu Tyr Ile Phe Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Val Ile Ser Gln  
               
               
                             20  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 133  
               
               
                 &lt;211&gt; LENGTH: 20  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 133  
               
               
                   
               
               
                 Ala Leu Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Met Ile Thr His  
               
               
                             20  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 134  
               
               
                 &lt;211&gt; LENGTH: 20  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 134  
               
               
                   
               
               
                 Cys Leu Tyr Ile Phe Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Arg Ile Ser His  
               
               
                             20  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 135  
               
               
                 &lt;211&gt; LENGTH: 20  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 135  
               
               
                   
               
               
                 Ala Leu Phe Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Pro Ala  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ile Leu Thr His  
               
               
                             20  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 136  
               
               
                 &lt;211&gt; LENGTH: 20  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 136  
               
               
                   
               
               
                 Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ile Val Val His  
               
               
                             20  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 137  
               
               
                 &lt;211&gt; LENGTH: 20  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Homo sapiens  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 137  
               
               
                   
               
               
                 Leu Phe Tyr Ile Tyr Thr Ser Gly Thr Thr Gly Leu Pro Lys Ala Ala  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ile Val Val His  
               
               
                             20  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 138  
               
               
                 &lt;211&gt; LENGTH: 36  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Artificial Sequence  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;223&gt; OTHER INFORMATION: consensus sequence  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 138  
               
               
                   
               
               
                 Ala Ala Thr Gly Ala Gly Cys Cys Gly Gly Ala Cys Thr Thr Cys Gly  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Thr Thr Cys Ala Cys Gly Thr Gly Thr Gly Gly Thr Thr Cys Gly Gly  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Cys Cys Thr Cys  
               
               
                         35  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 139  
               
               
                 &lt;211&gt; LENGTH: 39  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Artificial Sequence  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;223&gt; OTHER INFORMATION: consensus sequence  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 139  
               
               
                   
               
               
                 Thr Cys Cys Cys Ala Gly Gly Cys Cys Gly Thr Thr Cys Cys Ala Gly  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Cys Cys Cys Thr Gly Thr Gly Thr Ala Thr Gly Thr Gly Gly Cys Thr  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Gly Gly Gly Cys Thr Gly  
               
               
                         35  
               
               
                   
               
               
                   
               
               
                 &lt;210&gt; SEQ ID NO 140  
               
               
                 &lt;211&gt; LENGTH: 42  
               
               
                 &lt;212&gt; TYPE: PRT  
               
               
                 &lt;213&gt; ORGANISM: Artificial Sequence  
               
               
                 &lt;220&gt; FEATURE:  
               
               
                 &lt;223&gt; OTHER INFORMATION: consensus sequence  
               
               
                   
               
               
                 &lt;400&gt; SEQUENCE: 140  
               
               
                   
               
               
                 Cys Thr Cys Cys Cys Cys Gly Cys Thr Gly Gly Cys Cys Cys Ala Gly  
               
               
                  1               5                  10                  15  
               
               
                   
               
               
                 Ala Gly Thr Thr Thr Cys Thr Gly Thr Gly Gly Cys Thr Cys Thr Gly  
               
               
                             20                  25                  30  
               
               
                   
               
               
                 Gly Thr Thr Cys Gly Gly Gly Cys Thr Gly  
               
               
                         35                  40