Abstract:
A-X 202 X 203 X 204 X 205 X 206 X 207 X 208 X 209 X 210 X 211 X 212 X 213 -B, wherein A represents amino acid residues 38-201 of SEQ ID NO: 2, B represents a sequence starting from amino acid 214 of SEQ ID NO: 2 and terminating at an amino acid between residues 1131 and 1164, inclusive, of SEQ ID NO: 2, and X 202  through X 213  are each selected independently from Ala, Val, Leu, Ile, Pro, Met, Phe, Trp, a bond, or a wild-type amino acid as found at a corresponding position of residues 202-213 of SEQ ID NO: 2, with the proviso that at least one of X 202  through X 213 , inclusive, is other than the wild type amino acid found at the corresponding position of SEQ ID NO: 2. The LPXTG motif, as found in the native protein at amino acid residues corresponding to residues 1132-1136 of SEQ ID NO: 2, may be deleted in the sequence of the mutant Cβ protein. The mutant Cβ protein is conjugated to a streptococcal capsular polysacharide in a vaccine composition, also having an acceptable pharmaceutical carrier, for use in a method of including an immune response in an animal. Nucleic acid molecules encoding the mutant protein, vectors containing these molecules, and host cells transformed therewith are also disclosed.

Description:
This application claims benefit to Provisional Application No. 60/024,707 filed Sep.. 6, 1996. 
    
    
     BACKGROUND OF THE INVENTION 
     1. Field of the Invention 
     The present invention concerns the construction of a protein having a reduced or eliminated ability to bind human IgA, but that retains the immunological properties useful for formulating a conjugate vaccine against Group B streptococci. 
     2. Related Art 
     Streptococci are a large and varied set of gram-positive bacteria which have been ordered into several groups based on the antigenicity and structure of their cell wall polysaccharide (Lancefield, R. C.,  J. Exp. Med.  57:571-595 (1933); Lancefield, R. C.,  Proc. Soc. Exp. Biol. and Med.  38:473-478 (1938)). Two of these groups have been associated with serious human infections. Those that have been classified into Group A streptococci are the bacteria that people are most familiar and are the organisms which cause “strep throat.” Organisms of Group A streptococci also are associated with the more serious infections of rheumatic fever, streptococcal impetigo, and sepsis. 
     Group B streptococci were not known as a human pathogen in standard medical textbooks until the early 1970&#39;s. Since that time, studies have shown that Group B streptococci are an important perinatal pathogen in both the United States as well as the developing countries (Smith, A. L. and J. Haas,  Infections of the Central Nervous System,  Raven Press, Ltd., New York. (1991) p. 313-333). Systemic Group B streptococcal infections during the first two months of life affect approximately three out of every 1000 births (Dillon, H. C., Jr., et al.,  J Pediat.  110:31-36 (1987)), resulting in 11,000 cases annually in the United States. These infections cause symptoms of congenital pneumonia, sepsis, and meningitis. A substantial number of these infants die or have permanent neurological sequelae. Furthermore, these Group B streptococcal infections may be implicated in the high pregnancy-related morbidity which occurs in nearly 50,000 women annually. Others who are at risk from Group B streptococcal infections include those who either congenitally, chemotherapeutically, or by other means, have an altered immune response. 
     Group B streptococci can be further classified into several different types based on the bacteria&#39;s capsular polysaccharide. The most pathogenically important of these different types are streptococci having types Ia, Ib, II, or III capsular polysaccharides. Group B streptococci of these four types represent over 90% of all reported cases. The structure of each of these various polysaccharide types has been elucidated and characterized (Jennings, H. J., et al.,  Biochemistry  22:1258-1263 (1983); Jennings, H. J., et al.,  Can. J. Biochem.  58:112-120(1980); Jennings, H. J., et al.,  Proc. Nat. Acad. Sci. USA.  77:2931-2935 (1980); Jennings, H. J., et al.,  J. Biol. Chem.  258:1793-1798 (1983); Wessels, M. R., et al.,  J. Biol. Chem.  262:8262-8267 (1987)). As is found with many other human bacterial pathogens, it has been ascertained that the capsular polysaccharides of Group B streptococci, when used as vaccines, provide very effective, efficacious protection against infections with these bacteria. This was first noted by Lancefield (Lancefield, R. C., et al.,  J. Exp. Med.  142:165-179 (1975)) and more recently in the numerous studies of Kasper and coworkers (Baker, C. J., et al.,  N. Engl. J. Med.  319:1180-1185 (1988); Baltimore, R. S., et al.,  J. Infect. Dis.  140:81-86 (1979); Kasper, D. L., et al.,  J. Exp. Med.  149:327-339 (1979); Madoff, L. C., et al.,  J. Clin. Invest.  94:286-292 (1994); Marques, M. B., et al.,  Infect. Immun.  62:1593-1599 (1994); Wessels, M. R., et al.,  J. Clin. Invest.  86:1428-1433 (1990); Wessels, M. R., et al.,  Infect. Immun.  61:4760-4766 (1993); Wyle, S. A., et al.,  J. Infect. Dis.  126:514-522 (1972)). However, much like many other capsular polysaccharide vaccines (Anderson, P., et al.,  J. Clin. Invest.  51:39-44 (1972); Gold, R., et al.,  J. Clin. Invest.  56:1536-1547 (1975); Gold, R., et al.,  J. Infect. Dis.  136S:S31-S35 (1977); Gold, R. M., et al.,  J. Infect. Dis.  138:731-735 (1978); Mäkelä, P. R. H., et al.,  J. Infect. Dis.  136:S43-50 (1977); Peltola, A., et al.,  Pediatrics  60:730-737 (1977); Peltola, H., et al.  N. Engl. J. Med.  297:686-691 (1977)), vaccines formulated from pure type Ia, Ib, II, and III capsular carbohydrates are relatively poor immunogens and have very little efficacy in children under the age of 18 months (Baker, C. J. and D. L. Kasper.  Rev. Inf. Dis.  7:458-467 (1985); Baker, C. J., et al.,  N. Engl. J. Med.  319:1180-1185 (1988); Baker, C. J., et al.,  New Engl. J. Med.  322:1857-1860 (1990)). These pure polysaccharides are classified as T cell independent antigens because they induce a similar immunological response in animals devoid of T lymphocytes (Howard, J. G., et al.,  Cell. Immunol.  2:614-626 (1971)). It is thought that these polysaccharides do not evoke a secondary booster response because they do not interact with T cells, and therefore fail to provoke a subsequent “helper response” via the secretion of various cytokines. For this reason, each consecutive administration of the polysaccharide as a vaccine results in the release of a constant amount of antibodies, while a T cell dependent antigen would elicit an ever increasing concentration of antibodies each time it was administered. 
     Goebel and Avery found in 1931 that by covalently linking a pure polysaccharide to a protein that they could evoke an immune response to the polysaccharide which could not be accomplished using the polysaccharide alone (Avery, O. T. and W. F. Goebel,  J. Exp. Med.  54:437-447 (1931); Goebel, W. F. and O. T. Avery,  J. Exp. Med.  54:431-436 (1931)). These observations initiated and formed the basis of the current conjugate vaccine technology. Numerous studies have followed and show that when polysaccharides are coupled to proteins prior to their administration as vaccines, the immune response to the polysaccharides changes from a T independent response to a T dependent response (see Dick, W. E., Jr. and M. Beurret, Glycoconjugates of bacterial carbohydrate antigens In:  Contributions to Microbiology and Immunology.  Cruse et al., eds., (1989) p. 48-114; Jennings, H. J. and R. K. Sood,  Neoglycoconjugates: Preparation and Applications.  Y. C. Lee and R. T. Lee, eds., Academic Press, New York. (1994) p. 325-371; Robbins, J. B. and R. Schneerson,  J. Infect. Dis.  161:821-832 (1990)for reviews). Currently, most of these polysaccharide-protein conjugate vaccines are formulated with well known proteins such as tetanus toxoid and diphtheria toxoid or mutants thereof. These proteins were originally used because they were already licensed for human use and were well characterized. However, as more and more polysaccharides were coupled to these proteins and used as vaccines, interference between the various vaccines which used the same protein became apparent. For example, if several different polysaccharides were linked to tetanus toxoid and given sequentially, the immune response to the first administered polysaccharide conjugate would be much larger than the last. If, however, each of the polysaccharides were coupled to a different protein and administered sequentially, the immune response to each of the polysaccharides would be the same. Carrier suppression is the term used to describe this observed phenomenon. One approach to overcome this problem is to match the protein and polysaccharide so that they are derived from the same organism. 
     Among the various antigens used to classify and subgroup Group B streptococci, one was a protein known as the Ibc antigen. This protein antigen was first described by Wilkinson and Eagon in 1971 (Wilkinson, H. W. and R. G. Eagon,  Infect. Immun.  4:596-604 (1971)) and was known to be made up of two distinct proteins designated as alpha and beta. Later, the Ibc antigen was shown to be effective when used as a vaccine antigen in a mouse model of infection by Lancefield and co-workers (Lancefield, R. C., et al.,  J. Exp. Med.  142:165-179 (1975)). The isolation, purification and functional characterization of the beta antigen (Cβ) protein of Group B streptococci was accomplished by Russell-Jones, et al. (Russell-Jones, G. J. and E. C. Gotschlich,  J. Exp. Med.  160:1476-1484 (1984); Russell-Jones, G. J., et al.,  J. Exp. Med.  160:1467-1475 (1984))(see U.S. Pat. No. 4,757,134)). They could demonstrate that one of the properties of the Cβ protein was to bind specifically to human IgA immunoglobulin. The binding site on the IgA molecule was localized to the Fc portion of the heavy chain of this immunoglobulin. They further showed that the Cβ protein consisted of a single polypeptide having an estimated molecular weight of 130,000 daltons. The gene responsible for the expression of the Cβ protein was cloned (Cleat, P. H. and K. N. Timmis,  Infect. Immun.  55:1151-1155 (1987)) and sequenced (Jerlström, P. G., et al.,  Molec. Microbiol.  5:843-849 (1991)) by a group led by Timmis. His later study demonstrated that the IgA binding activity could be assigned to a 746 bp DNA fragment of the gene defined by a leading BglII restriction endonuclease cleavage site and ending with a HpaI restriction endonuclease cleavage site. 
     As stated previously, the 1975 Lancefield study showed that the Ibc antigen was an effective vaccine antigen in a mouse model of Group B streptococcal infection (Lancefield, R. C., et al.,  J. Exp. Med.  142:165-179 (1975)). It was not clear at the time whether the alpha or beta protein component of the Ibc antigen was responsible for this protection. Madoff et al., began to shed light on this question and demonstrated that the purified Cβ protein used as a vaccine could protect infant mice from experimental infection with Group B streptococci expressing this protein (Madoff, L. C., et al.,  Infect. Immun.  60:4989-4994 (1992)). Madoff et al., then went on to show that when they coupled a Type III streptococcal capsular polysaccharide to the Cβ protein, producing a conjugate vaccine, this vaccine would protect infant mice against infection with either a Type III Group B streptococci (expressing no Cβ) or a Type Ib Group B streptococci (expressing Cβ but lacking a Type III capsular polysaccharide) (Madoff, L. C., et al.,  J. Clin. Invest.  94:286-292 (1994)). Thus, such a Cβ protein conjugate vaccine served several functions: the polysaccharide elicited protective antibodies to the polysaccharide capsule and the Cβ protein evoked protective antibodies to the protein as well as modified the immune response to the polysaccharide from a T independent response to a T dependent response. 
     This polysaccharide-Cβ protein conjugate strategy works well in mice. But clearly, the goal is to protect humans against Group B streptococcal infections. The only caveat with using the same strategy in humans is that the Cβ protein binds human IgA immunoglobulins non-specifically (Cβ does not bind mouse IgA). This human IgA binding activity of Cβ could diminish the efficacy of a polysaccharide-Cβ protein conjugate vaccine for humans, as antigens bound to IgA can be cleared from the system so rapidly that an antigen-specific antibody response is not produced. Furthermore, potentially protective epitopes on the Cβ protein could be hidden when the human IgA binds to the Cβ molecule. Thus, it would be advantageous to obtain a mutant Cβ protein which lacks the IgA binding capacity but retains as much of the native structure as possible. 
     With this goal in mind, several groups have attempted to determine the IgA binding region of the Cβ protein. Jerlström et al. ( Molec. Microbiol.  5:843-849 (1991)) used experiments wherein subfragments of the Cβ protein were expressed as fusion proteins to identify two regions of the Cβ protein capable of binding IgA. These experiments localized the IgA binding domains to a 747 bp BglII-HpaI fragment and a 1461 bp HpaI-HindIII fragment of the Cβ protein. Furthermore, International Patent Application No. PCT/US/06111 describes the isolation of a Cβ protein bearing a deletion of a region that binds IgA. 
     SUMMARY OF THE INVENTION 
     The invention relates to a mutant Cβ protein, wherein the IgA binding by the Cβ protein is reduced or eliminated, while the antigenicity of the protein when administered either alone or as part of a polysaccharide-protein conjugate is substantially retained. 
     In particular, the invention relates to a mutant Cβ protein comprising the amino acid sequence A-X 1 X 2 X 3 X 4 X 5 X 6 X 7 X 8 X 9 X 10 X 11 X 12 -B, wherein A comprises amino acids 1-164 of the sequence shown in FIG. 1 (SEQ ID NO: 2), B represents a sequence starting from amino acid 177 and terminating at an amino acid between residue 1094 and 1127, inclusive, of the sequence shown in FIG. 1 (SEQ ID NO: 2), and X 1 -X 12  are each selected independently from the group consisting of Ala, Val, Leu, Ile, Pro, Met, Phe, Trp, a bond, and the wild type amino acid found at the corresponding position of the sequence shown in FIG. 1 (SEQ ID NO: 2), wherein said amino acid positions are numbered from the first amino acid of the native amino acid sequence encoding said protein, with the proviso that at least one of X 1  through X 12 , inclusive, is other than the wild type amino acid. 
     The invention also relates to a polynucleotide molecule encoding a mutant Cβ protein, as well as vectors comprising such polynucleotide molecules, and host cells transformed therewith. 
     The invention also relates to a conjugate comprising the mutant Cβ protein covalently conjugated to a capsular polysaccharide. 
     The invention also relates to a vaccine comprising the mutant Cβ protein of the invention and a pharmaceutically acceptable carrier. 
     The invention also relates to a method of inducing an immune response in an animal, comprising administering the vaccine of the invention to an animal in an effective amount. 
    
    
     BRIEF DESCRIPTION OF THE FIGURES 
     FIG. 1 (SEQ ID NOS: 1 and 2) shows the DNA sequence and deduced amino acid sequence of wild type Cβ1 (Jerlström, P. G., et al.,  Molec. Microbiol.  5:843-849 (1991)). The BglII and PstI sites shown in FIGS. 2,  3  and  4  are identified. 
     FIG. 2 is a map of the region of the Cβ gene which encodes the IgA binding site of the Cβ protein; 2 amino acid substitutions are indicated, generating mutant dgb2 (SEQ ID NO: 22)(see Table 1). 
     FIG. 3 is a map of the region of the Cβ gene which encodes the IgA binding site of the Cβ protein; 2 amino acid substitutions are indicated, generating mutant nv34qp (SEQ ID NO: 21)(see Table 1). 
     FIG. 4 is a map of the region of the Cβ gene which encodes the IgA binding site of the Cβ protein; 6 amino acids have been deleted from this region in the mutant protein, generating mutant dgb1 (SEQ ID NO: 23)(see Table 1). 
     FIG. 5 is a graph showing the competitive inhibition of ELISA reactivity by Cβ proteins. 
     FIGS. 6A,  6 B- 6 G (SEQ ID NOS: 3 and 4) show the complete DNA sequence of the gene encoding Cβ mutant dgb2 (see Table 1), as well as the deduced amino acid sequence of this mutant. The mutations are underlined. 
     FIGS. 7A,  7 B- 7 F (SEQ ID NOS: 5 and 6) show the complete DNA sequence of the gene encoding Cβ mutant nv34qp (see Table 1), as well as the deduced amino acid sequence of this mutant. The mutations are underlined. 
     FIGS. 8A,  8 B- 8 G (SEQ ID NOS: 7 and 8) show the complete DNA sequence of the gene encoding Cβ mutant dgb1 (see Table 1), as well as the deduced amino acid sequence of this mutant. 
     FIGS. 9A,  9 B- 9 G (SEQ ID NOS: 9 and 10) show the complete DNA sequence of the gene encoding Cβ mutant pnv231 (see Table 1), as well as the deduced amino acid sequence of this mutant. The mutations are underlined. 
    
    
     DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS 
     The invention relates to a mutant Cβ protein of the group B streptococcal (GBS) beta antigen, wherein IgA binding by the Cβ protein is reduced or eliminated and wherein at least a majority of the antigenicity of the protein is retained. 
     It has been discovered that mutation of a region of the Cβ protein located between about amino acid residues 163 and 176 of the wildtype Cβ sequence shown in FIG. 1 (SEQ ID NO:2) results in a Cβ protein which has reduced or eliminated IgA binding properties, but which retains enough of its tertiary structure to maintain the majority of its antigenicity (see Examples 4 and 5). 
     As the region of the Cβ polypeptide has been found which is responsible for IgA binding, and as it has been demonstrated in the Examples below that amino acid substitutions or deletions in this region reduce or eliminate IgA binding while maintaining antigenicity of the protein, those of ordinary skill in the art will understand how to alter the amino acid sequence of the Cβ polypeptide so as to achieve the objects of the invention. Appropriate amino acid substitutions which eliminate IgA binding will include replacement of one or more residues with an amino acid having different properties. For example, a strongly hydrophilic amino acid can be replaced with a strongly hydrophobic amino acid. Amino acids which can be grouped together include the aliphatic amino acids Ala, Val, Leu and Ile, the hydroxyl residues Ser and Thr, the acidic residues Asp and Glu, the amide residues Asn and Gln, the basic residues Lys and Arg and the aromatic residues Phe and Tyr. Thus, those of ordinary skill in the art will understand how to determine suitable amino acid substitutions or deletions in the region between about residues 163 and 176 in the Cβ protein in order to reduce or eliminate IgA binding. 
     Further guidance concerning which amino acid changes are likely to have a significant deleterious effect on a function can be found in Bowie, J. U., et al., “Deciphering the Message in Protein Sequences: Tolerance to Amino Acid Substitutions,”  Science  247:1306-1310 (1990). 
     Thus, in particular, the invention relates to a mutant group B streptococcal (GBS) beta antigen, Cβ, comprising the amino acid sequence A-X 1 X 2 X 3 X 4 X 5 X 6 X 7 X 8 X 9 X 10 X 11 X 12 -B, wherein A comprises amino acids 1-164 of the sequence shown in FIG. 1 (SEQ ID NO: 2), B represents a sequence starting from amino acid 177 and terminating at an amino acid between residue 1094 and 1127, inclusive, of the sequence shown in FIG. 1 (SEQ ID NO: 2), and X 1 -X 12  are each selected independently from the group consisting of Ala, Arg, Asp, Val, Leu, Ile, Pro, Met, Phe, Trp, a bond, and the wild type amino acid found at the corresponding position of the sequence shown in FIG. 1 (SEQ ID NO: 2), wherein said amino acid positions are numbered from the first amino acid of the native amino acid sequence encoding said protein, with the proviso that at least one of X 1  through X 12 , inclusive, is other than the wild type amino acid. In a particularly preferred mutant Cβ protein, amino acids X 7  and X 12  are Ala. In another preferred mutant, amino acids X 4  and X 11  are Pro. In another preferred mutant, amino acid X 7  is Thr and amino acid X 12  is Leu. In a more preferred mutant, amino acids X 5 , X 7 , X 8 , X 10 , X 11  and X 12  are each replaced with a bond. 
     As the Cβ protein is, in its wild type state, membrane bound, it is possible to improve purification of the above-mentioned Cβ mutants by eliminating the hydrophobic residues of the transmembrane domain of the Cβ protein (the transmembrane domain corresponds to residues 1095-1127 of the sequence shown in FIG. 1 (SEQ ID NO: 2)). This can be accomplished by substitution of non-hydrophobic residues for the hydrophobic residues (residues 1108-1116 of the sequence shown in FIG. 1 (SEQ ID NO: 2)) or by deletion of the hydrophobic residues. While purification of membrane-bound Cβ requires the use of detergent, a mutant Cβ which lacks the hydrophobic membrane spanning region can be purified without using detergent. Thus, the invention also relates to a mutant Cβ wherein the nine hydrophobic residues making up the transmembrane domain are deleted or replaced by non-hydrophobic amino acids. 
     It has been discovered that the IgA-binding ability of Cβ may require dimerization of Cβ. Thus, even where the IgA-binding region of Cβ is not mutated as described above, mutation of the region of Cβ which is believed to be required for dimerization can result in a form of Cβ that cannot bind IgA. Deletion of a portion of Cβ from residue 729 to the C-terminus of the sequence shown in FIG. 1 (SEQ ID NO: 2) eliminates dimerization Cβ. The results of experiments supporting this finding may be found in Table 1. (IgAbs+(SEQ ID NO: 11); dgb6 (SEQ ID NO: 12); dgb6p (SEQ ID NO: 13); dgb7 (SEQ ID NO: 14); dgb7p (SEQ ID NO: 15); dgb8 (SEQ ID NO: 16); dgb8p (SEQ ID NO: 17); dgb10 (SEQ ID NO: 18); dgb12 (SEQ ID NO: 19); dgb11 (SEQ ID NO: 20); nv34qp (SEQ ID NO: 21); dgb2 (SEQ ID NO: 22); dgb1 (SEQ ID NO: 23); and pnv231 (SEQ ID NO: 24)). Several fragments of Cβ were inserted into each of two different vectors. Where sequences shown in the table are preceded or followed by an outward facing bracket, this indicates that the Cβ sequence does not extend further on that end of the fragment, i.e. that the nucleotide sequence inserted into the vector encodes only those amino acids shown, and no more of the Cβ sequence. Where sequences shown in the table are preceded or followed by ellipses, this indicates that the remainder of the Cβ sequence at that end of the fragment is also included in the vector. Nucleotide sequences encoding the peptides shown in the upper part of the table were inserted into either the vector pTOPE or the vector pET17b. Both of these vectors allow expression of inserted fragments from the T7 promoter, and both produce fusion proteins containing a fragment of the φ10 capsid protein N terminal to the amino acid sequence encoded by the insert. However, while pET17b encodes only 8 amino acids of the φ10 protein, pTOPE encodes a 288 amino acid fragment of the φ10 protein. 
     As shown in Table 1 (SEQ ID NOS: 11-24), certain fragments of Cβ produced from pET17b exhibit reduced IgA-binding, while the same fragment produced by pTOPE is capable of binding IgA. The fragments tested lack the region of Cβ predicted to be involved in dimerization, but do not contain any mutations in the putative IgA binding domain (note that the Cβ fragments inserted into vector pET24b, shown at the bottom of Table 1, contain the putative dimerization region but nonetheless exhibit reduced IgA binding due to mutations in the IgA binding domain, as described above). It is postulated that these Cβ fragments bind DNA when produced from pTOPE because the 288 amino acid fragment of the φ10 protein allows dimerization of the Cβ fragment. This may be due to the fact that the φ10 capsid protein normally forms oligomers; the region responsible for oligomerization may thus allow dimerization of the inserted Cβ fragments, and thus IgA-binding. Thus, the invention also relates to a mutant Cβ protein having a mutation in the dimerization domain of Cβ, wherein the mutant Cβ protein is incapable of binding IgA. Of course, in the interest of producing a non-IgA binding Cβ protein retaining as much of the antigenicity of the wild type Cβ protein as possible, dimerization of Cβ should not be interrupted. 
     It has also been discovered that production of Cβ protein from  E. coli  can be problematic because the protein is cleaved at a specific region, presumably by an  E. coli  signal peptidase. This cleavage results in a truncated protein, which obviously is not ideal for a vaccine, as it lacks many antigenic epitopes of the wildtype Cβ protein. The cleavage site has been predicted by sequence analysis and by matrix assisted laser desorption initiated time of flight (MALDI-TOF) mass spectrometry (von Heijne,  Nucleic Acids Res.  14: 4683-4690 (1986)). The cleavage site is between amino acid residues 538 and 539 (after alanine and before glutamine) of the amino acid sequence shown in FIG. 1 (SEQ ID NO:2). The signal peptidase recognition site is located within a 20 amino acid stretch located between residues 521 and 541 of the amino acid sequence shown in FIG. 1 (SEQ ID NO:2). Therefore, by deleting this region, the Cβ protein or a non-IgA binding mutant thereof can successfully be produced in  E coli.  Furthermore, as signal peptidases have very strict sequence specificity, alteration of the signal peptidase recognition sequence, including even a single, conservative amino acid substitution in this region, may eliminate cleavage of Cβ by  E. coli.  The recognition sequence required for cleavage by this signal peptidase is believed to be GluLeuIleLysSerAlaGlnGlnGlu (SEQ ID NO:25), corresponding to amino acid residues 533-541 of the sequence shown in FIG. 1 (SEQ ID NO:2). Alteration of either the serine or the alanine residue of this sequence by either deletion or non-conservative substitution is expected to eliminate cleavage by the signal peptidase. Of course, ideally, the mutagenesis of Cβ will be kept to a minimum so as to retain the tertiary structure of the wildtype antigen for the purposes of eliciting an immunogenic response. 
     Thus, the invention also relates to a mutant Cβ protein of the group B streptococcal (GBS) beta antigen, wherein IgA binding by the Cβ protein is reduced or eliminated by any of the mutations described above, and wherein at least one of amino acid residues 521-541 of the amino acid sequence shown in FIG. 1 (SEQ ID NO:2) is either (a) deleted or (b) altered, so that the protein is not cleaved in this region when Cβ is produced in  E. coli.  In a preferred embodiment, at least one of amino acid residues 533-541 of the sequence shown in FIG. 1 (SEQ ID NO:2) is either (a) deleted or (b) altered. In a more preferred embodiment, at least one of amino acid residues 537 and 538 is either (a) deleted or (b) altered. Of course, one of ordinary skill will be able to determine other suitable amino acid substitutions by routine experimentation, and by reference to the article by von Heijne ( Nucleic Acids Res.  14: 4683-4690 (1986)). 
     The invention also relates to polynucleotide molecules encoding the mutant proteins of the invention, vectors comprising those polynucleotide molecules, and host cells transformed therewith. 
     The invention also relates to the expression of novel mutant Cβ polypeptides, wherein IgA binding by the Cβ protein is reduced or eliminated, in a cellular host. 
     Prokaryotic hosts that may be used for cloning and expressing the polypeptides of the invention are well known in the art. Vectors which replicate in such host cells are also well known. 
     Preferred prokaryotic hosts include, but are not limited to, bacteria of the genus Escherichia, Bacillus, Streptomyces, Pseudomonas, Salmonella, Serratia, Xanthomonas, etc. Two such prokaryotic hosts are  E. coli  DH10B and DH5αF′IQ (available from LTI, Gaithersburg, Md.). The most preferred host for cloning and expressing the polypeptides of the invention is  E. coli  BL21 (Novagen, Wis.), which is lysogenic for DE3 phage. 
     The present invention also relates to vectors which include the isolated DNA molecules of the present invention, host cells which are genetically engineered with the recombinant vectors, and the production of the polypeptides of the invention by recombinant techniques. 
     Host cells can be genetically engineered to incorporate nucleic acid molecules and express polypeptides of the present invention. For instance, recombinant constructs may be introduced into host cells using well known techniques of infection, transduction, transfection, and transformation. The polynucleotides may be introduced alone or with other polynucleotides. Such other polynucleotides may be introduced independently, co-introduced or introduced joined to the polynucleotides of the invention. 
     Thus, for instance, the polynucleotides may be joined to a vector containing a selectable marker for propagation in a host. The vector construct may be introduced into host cells by the aforementioned techniques. Generally, a plasmid vector is introduced as DNA in a precipitate, such as a calcium phosphate precipitate, or in a complex with a charged lipid. Electroporation also may be used to introduce polynucleotides into a host. If the vector is a virus, it may be packaged in vitro or introduced into a packaging cell and the packaged virus may be transduced into cells. A wide variety of techniques suitable for making polynucleotides and for introducing polynucleotides into cells in accordance with this aspect of the invention are well known and routine to those of skill in the art. Such techniques are reviewed at length in Sambrook et al. cited above, which is illustrative of the many laboratory manuals that detail these techniques. 
     In accordance with this aspect of the invention the vector may be, for example, a plasmid vector, a single or double-stranded phage vector, a single or double-stranded RNA or DNA viral vector. Such vectors may be introduced into cells as polynucleotides, preferably DNA, by well known techniques for introducing DNA and RNA into cells. The vectors, in the case of phage and viral vectors also may be and preferably are introduced into cells as packaged or encapsulated virus by well known techniques for infection and transduction. Viral vectors may be replication competent or replication defective. In the latter case viral propagation generally will occur only in complementing host cells. 
     Preferred among vectors, in certain respects, are those for expression of polynucleotides and polypeptides of the present invention. Generally, such vectors comprise cis-acting control regions effective for expression in a host operatively linked to the polynucleotide to be expressed. Appropriate transacting factors either are supplied by the host, supplied by a complementing vector or supplied by the vector itself upon introduction into the host. 
     In certain preferred embodiments in this regard, the vectors provide for specific expression. Such specific expression may be inducible expression or expression only in certain types of cells or both inducible and cell-specific. Particularly preferred among inducible vectors are vectors that can be induced for expression by environmental factors that are easy to manipulate, such as temperature and nutrient additives. A variety of vectors suitable to this aspect of the invention, including constitutive and inducible expression vectors for use in prokaryotic and eukaryotic hosts, are well known and employed routinely by those of skill in the art (see U.S. Pat. No. 5,464,758). 
     The engineered host cells can be cultured in conventional nutrient media, which may be modified as appropriate for, inter alia, activating promoters, selecting transformants or amplifying genes. Culture conditions, such as temperature, pH and the like, previously used with the host cell selected for expression generally will be suitable for expression of polypeptides of the present invention as will be apparent to those of skill in the art. 
     A great variety of expression vectors can be used to express a polypeptide of the invention. Such vectors include chromosomal, episomal and virus-derived vectors e.g., vectors derived from bacterial plasmids, from bacteriophage, from yeast episomes, from yeast chromosomal elements, from viruses such as baculoviruses, papova viruses, such as SV40, vaccinia viruses, adenoviruses, fowl pox viruses, pseudorabies viruses and retroviruses, and vectors derived from combinations thereof, such as those derived from plasmid and bacteriophage genetic elements, such as cosmids and phagemids, all may be used for expression in accordance with this aspect of the present invention. Generally, any vector suitable to maintain or propagate, polynucleotides, or to express a polypeptide, in a host may be used for expression in this regard. 
     The appropriate DNA molecule may be inserted into the vector by any of a variety of well-known and routine techniques. In general, a DNA molecule for expression is joined to an expression vector by cleaving the DNA sequence and the expression vector with one or more restriction endonucleases and then joining the restriction fragments together using T4 DNA ligase. Procedures for restriction and ligation that can be used to this end are well known and routine to those of skill in the art. Suitable procedures in this regard, and for constructing expression vectors using alternative techniques, which also are well known and routine to those skill, are set forth in great detail in Sambrook et al. cited above. 
     The DNA molecule inserted in the expression vector is operatively linked to appropriate expression control sequence(s), including, for instance, a promoter to direct mRNA transcription. Representatives of such promoters include the phage lambda PL promoter, the  E. coli  lac, trp and tac promoters, the SV40 early and late promoters and promoters of retroviral LTRs, to name just a few of the well-known promoters. It will be understood that numerous promoters not mentioned are suitable for use in this aspect of the invention are well known and readily may be employed by those of skill in the art in the manner illustrated by the discussion and the examples herein. 
     In general, expression constructs will contain sites for transcription initiation and termination, and, in the transcribed region, a ribosome binding site for translation. The coding portion of the mature transcripts expressed by the constructs will include a translation initiating AUG at the beginning and a termination codon appropriately positioned at the end of the polypeptide to be translated. 
     In addition, the constructs may contain control regions that regulate as well as engender expression. Generally, in accordance with many commonly practiced procedures, such regions will operate by controlling transcription, such as repressor binding sites and enhancers, among others. 
     Vectors for propagation and expression generally will include selectable markers. Such markers also may be suitable for amplification or the vectors may contain additional markers for this purpose. In this regard, the expression vectors preferably contain one or more selectable marker genes to provide a phenotypic trait for selection of transformed host cells. Preferred markers include dihydrofolate reductase or neomycin resistance for eukaryotic cell culture, and tetracycline or ampicillin resistance genes for culturing  E. coli  and other bacteria. 
     The vector containing the appropriate DNA sequence as described elsewhere herein, as well as an appropriate promoter, and other appropriate control sequences, may be introduced into an appropriate host using a variety of well known techniques suitable to expression therein of a desired polypeptide. Representative examples of appropriate hosts include bacterial cells, such as  E. coli,  Streptomyces and  Salmonella typhimurium  cells. Hosts for a great variety of expression constructs are well known, and those of skill will be enabled by the present disclosure readily to select a host for expressing a polypeptides in accordance with this aspect of the present invention. 
     More particularly, the present invention also includes recombinant constructs, such as expression constructs, comprising one or more of the sequences described above. The constructs comprise a vector, such as a plasmid or viral vector, into which such a sequence of the invention has been inserted. The sequence may be inserted in a forward or reverse orientation. In certain preferred embodiments in this regard, the construct further comprises regulatory sequences, including, for example, a promoter, operably linked to the sequence. Large numbers of suitable vectors and promoters are known to those of skill in the art, and there are many commercially available vectors suitable for use in the present invention. 
     As the invention concerns the construction of a protein having a reduced or eliminated ability to bind human IgA, the invention thus relates to using in vitro mutagenesis methods to generate the mutant Cβ proteins of the invention. A number of in vitro mutagenesis methods are well known to those of skill in the art; several are provided here as examples. 
     One such method introduces deletions or insertions into a polynucleotide molecule inserted into a plasmid by either partially or completely digesting the plasmid with an appropriate restriction enzyme, and then ligating the ends to again generate a plasmid. Very short deletions can be made by first cutting a plasmid at a restriction site, and then subjecting the linear DNA to controlled nuclease digestion to remove small groups of bases at each end. Precise insertions may also be made by ligating double stranded oligonucleotide linkers to a plasmid cut at a single restriction site. 
     Chemical methods can also be used to introduce mutations to a single stranded polynucleotide molecule. For example, single base pair changes at cytosine residues can be created using chemicals such as bisulfite, which deaminates cytosine to uracil, thus converting GC base pairs to AT base pairs. 
     Preferably, oligonucleotide directed mutagenesis will be used so that all possible classes of base pair changes at any determined site along a DNA molecule can be made. In general, this technique involves annealing a oligonucleotide complementary (except for one or more mismatches) to a single stranded nucleotide sequence of interest. The mismatched oligonucleotide is then extended by DNA polymerase, generating a double stranded DNA molecule which contains the desired change in sequence on one strand. The changes in sequence can of course result in the deletion, substitution, or insertion of an amino acid if the change is made in the coding region of a gene. The double stranded polynucleotide can then be inserted into an appropriate expression vector, and a mutant polypeptide can thus be produced. The above-described oligonucleotide directed mutagenesis can of course be carried out via PCR. An example of such a system is the Ex-Site™ PCR site-directed mutagenesis technique (Stratagene, Calif.) used in Example 4. 
     Using the Ex-Site™ PCR site-directed mutagenesis technique, several different oligonucleotides were made to induce different changes in the DNA sequence in the region of interest. In one particular example, overlapping primers were obtained, wherein both primers contained the sequence required to change lysine to alanine at amino acids 170 and 175 in the sequence shown in FIG. 1 (SEQ ID NO: 2) (see FIG.  2  and Table 1). The forward primer, designated Cβ 613, had the sequence (SEQ ID NO:.26) 5′-GTT GAA GCA ATG GCA GAG CAA GCG GGA ATC ACA AAT GAA G-3′ and the reverse primer, designated Cβ 642R had the sequence (SEQ ID NO:27) 5′-GAT TCC CGC TTG CTC TGC CAT TGC TTC AAC TTG ACT TTT TTG-3′ (the substitutions are noted in BOLD). These oligonucleotides were combined with pNV222 template, which consists of the Cβ gene inserted into the pSP76 vector. PCR was performed, and the products were ligated and introduced into  E. coli  strain DH5α, thus generating clones containing the mutant Cβ gene. 
     The following vectors, which are commercially available, may be used in the practice of the invention. Among vectors preferred for use in bacteria are pQE70, pQE60 and pQE-9, available from Qiagen; pBS vectors, Phagescript vectors, Bluescript® vectors, pNH8A, pNH16a, pNH18A, and pNH46A, available from Stratagene; ptrc99a, pKK223-3, pKK233-3, pDR540, and pRIT5 available from Pharmacia; pUC18, pUC19 and pPROEX-1, available from LTI, and pTOPE, pET17b, and pET24a (Novagen Inc., Madison, Wis.). These vectors are listed solely by way of illustration of the many commercially available and well known vectors that are available to those of skill in the art for use in accordance with this aspect of the present invention. It will be appreciated that any other plasmid or vector suitable for, for example, introduction, maintenance, propagation or expression of a polynucleotide or polypeptide of the invention in a host may be used in this aspect of the invention. 
     Promoter regions can be selected from any desired gene using vectors that contain a reporter transcription unit lacking a promoter region, such as a chloramphenicol acetyl transferase (“CAT”) transcription unit, downstream of restriction site or sites for introducing a candidate promoter fragment; i.e., a fragment that may contain a promoter. As is well known, introduction into the vector of a promoter-containing fragment at the restriction site upstream of the CAT gene engenders production of CAT activity, which can be detected by standard CAT assays. Vectors suitable to this end are well known and readily available. Two such vectors are pKK232-8 and pCM7. Thus, promoters for expression of polynucleotides of the present invention include not only well known and readily available promoters, but also promoters that readily may be obtained by the foregoing technique, using a reporter gene. 
     Among known bacterial promoters suitable for expression of polynucleotides and polypeptides in accordance with the present invention are the  E. coli  lacI and lacZ and promoters, the T3 and T7 promoters, the gpt promoter, the lambda PR, PL promoters and the trp promoter. 
     Selection of appropriate vectors and promoters for expression in a host cell is a well known procedure and the requisite techniques for expression vector construction, introduction of the vector into the host and expression in the host are routine skills in the art. 
     The present invention also relates to host cells containing the constructs discussed above. The host cell can be a prokaryotic cell, such as a bacterial cell. 
     Constructs in host cells can be used in a conventional manner to produce the gene product encoded by the recombinant sequence. Alternatively, the polypeptides of the invention can be synthetically produced by conventional peptide synthesizers. 
     Following transformation of a suitable host strain and growth of the host strain to an appropriate cell density, where the selected promoter is inducible, it is induced by appropriate means (e.g., temperature shift or exposure to chemical inducer) and cells are cultured for an additional period. 
     Cells typically are then harvested by centrifugation, disrupted by physical or chemical means, and the resulting crude extract retained for further purification. 
     Microbial cells employed in expression of proteins can be disrupted by any convenient method, including freeze-thaw cycling, sonication, mechanical disruption, or use of cell lysing agents; such methods are well know to those skilled in the art. 
     The invention also relates to a vaccine comprising a mutant Cβ protein, wherein IgA binding by the Cβ protein is reduced or eliminated as described herein, together with a pharmaceutically acceptable carrier. In a preferred embodiment, the protein is conjugated to a polysaccharide. 
     The conjugates of the invention may be formed by reacting the reducing end groups of the polysaccharide to primary amino groups (that is, lysine residues) of the Cβ protein by reductive amination. The polysaccharide may be conjugated to any or all of the primary amino groups of the protein. The reducing groups may be formed by selective hydrolysis or specific oxidative cleavage, or a combination of both. Preferably, the Cβ protein is conjugated to the polysaccharide by the method of Jennings et al., U.S. Pat. No. 4,356,170, which involves controlled oxidation of the polysaccharide with periodate followed by reductive amination with the Cβ protein of the invention. 
     In a preferred embodiment, the polysaccharide is one of the Group B streptococcal capsular polysaccharides selected from types Ia, II, III and V. See Baker, C. J. and D. L. Kasper,  Rev. Inf. Dis.  7:458-467 (1985); Baker, C. J., et al.,  N. Engl. J. Med.  319:1180-1185 (1988); Baker, C. J., et al.,  New Engl. J. Med.  322:1857-1860 (1990). The vaccine may also be a combination vaccine comprising one or more of the Cβ protein-polysaccharide conjugates selected from the group consisting of Cβ conjugated to Group B capsular polysaccharide type Ia (Cβ-Ia); Cβ conjugated to Group B capsular polysaccharide type II (Cβ-II); Cβ conjugated to Group B capsular polysaccharide type III (Cβ-III); and Cβ conjugated to Group B capsular polysaccharide type V (Cβ-V). Most preferably, the vaccine is a combination vaccine comprising Cβ-Ia, Cβ-II, Cβ-III and Cβ-V. Such a combination vaccine will elicit antibodies to Group B streptoccoci of Types Ia, II, III, V, and Ib (as Type Ib Group B streptococci also express Cβ). Furthermore, the immune response to the polysaccharides of the combination vaccine will be a T dependent response. 
     The vaccine of the present invention comprises one or more of the Cβ protein vaccines or conjugate vaccines in amounts effective depending on the route of administration. Although subcutaneous or intramuscular routes of administration are preferred, the vaccine of the present invention can also be administered by an intraperitoneal or intravenous route. One skilled in the art will appreciate that the amounts to be administered for any particular treatment protocol can be readily determined without undue experimentation. With respect to each conjugate, suitable amounts are expected to fall within the range of 2 micrograms of the protein per kg body weight to 100 micrograms per kg body weight. In a preferred embodiment, the vaccine comprises about 2 μg of the Cβ protein or an equivalent amount of the protein-polysaccharide conjugate. In another preferred embodiment, the vaccine comprises about 5 μg of the Cβ protein or an equivalent amount of the protein-polysaccharide conjugate. 
     The vaccine of the present invention may be employed in such forms as capsules, liquid solutions, suspensions or elixirs for oral administration, or sterile liquid forms such as solutions or suspensions. Any inert carrier is preferably used, such as saline, phosphate-buffered saline, or any such carrier in which the non-IgA Fc binding group B streptococcal Cβ protein or conjugate vaccine have suitable solubility properties. The vaccines may be in the form of single dose preparations or in multi-dose flasks which can be used for mass vaccination programs. Reference is made to Remington&#39;s  Pharmaceutical Sciences,  Mack Publishing Co., Easton, Pa., Osol (ed.) (1980); and  New Trends and Developments in Vaccines,  Voller et al. (eds.), University Park Press, Baltimore, Md. (1978), for methods of preparing and using vaccines. 
     The vaccines of the present invention may further comprise adjuvants which enhance production of Cβ-specific antibodies. Such adjuvants include, but are not limited to, various oil formulations such as Freund&#39;s complete adjuvant (CFA), stearyl tyrosine (ST, see U.S. Pat. No. 4,258,029), the dipeptide known as MDP, saponin (see U.S. Pat. No. 5,057,540), aluminum hydroxide, and lymphatic cytokine. 
     Freund&#39;s adjuvant is an emulsion of mineral oil and water which is mixed with the immunogenic substance. Although Freund&#39;s adjuvant is powerful, it is usually not administered to humans. Instead, the adjuvant alum (aluminum hydroxide) or ST may be used for administration to a human. The Cβ protein vaccine or a conjugate vaccine thereof may be absorbed onto the aluminum hydroxide from which it is slowly released after injection. The vaccine may also be encapsulated within liposomes according to Fullerton, U.S. Pat. No. 4,235,877. 
     In another preferred embodiment, the present invention relates to a method of inducing an immune response in an animal comprising administering to the animal the vaccine of the invention, produced according to methods described, in an amount effective to induce an immune response. 
     Having now generally described the invention, the same will be more readily understood through reference to the following Examples which are provided by way of illustration, and are not intended to be limiting of the present invention, unless specified. 
     EXAMPLES 
     Example 1 
     Cloning and Expression of the Gene Encoding Cβ 
     To locate the IgA binding site on the Cβ protein, two oligonucleotides were synthesized. The first oligonucleotide, oligo 1, corresponds to the 5′ end of the mature protein, and has the sequence (SEQ ID NO: 28) 5′-AAGGATCCAAGTGAGCTTGTAAAGGACGAT-3′, which includes a BamHI site. The second oligonucleotide falls just short of the 3′ end of the gene, and has the sequence (SEQ ID NO:29) 5′-AAAACTCGAGTTTCTTTTCCGTTGTTGATGTA-3′, and includes a XhoI site. The oligonucleotide for the 3′ end of the gene was chosen to eliminate the LPXTG motif found in most gram positive cell wall proteins. This sequence motif has been shown to be involved in the processing of these cell wall proteins and is the part of these proteins which eventually becomes covalently bound to peptidoglycan (Navarre, W. W. and O. Schneewind,  Molec. Microbiol.  14:115-121 (1994); Schneewind, O., et al.,  Science  268:103-106 (1995)). Using chromosomal DNA from Strain A909 Group B streptococci containing the gene for the Cβ protein as a template, and standard PCR procedures, a product of approximately 3.2 kb was produced as observed when electrophoresed on a 1% agarose gel. The PCR product containing the Cβ protein gene was cleaved with the endonuclease restriction enzymes BamHI and XhoI. This BamHI-XhoI DNA fragment contained the sequence for the entire Cβ protein except for the last 33 amino acids at the carboxyl terminus, including the putative IgA binding site. The DNA fragment was then ligated into the appropriately restricted T7 expression plasmid pET17b (Novagen Inc., Madison, Wis.) using a standard T4 ligase procedure. The plasmid was then transformed into the  E. coli  strain BL21(DE3) using the manufacturer&#39;s suggested protocols (Novagen Inc.).  E. coli  cells containing the plasmid were selected on LB plates containing 50 μg/ml carbenicillin. These plates were incubated overnight at 37° C. The transformant colonies were carefully lifted onto nitrocellulose filters saturated with IPTG. After 30 min, the bacteria were lysed by placing the filters into a chloroform vapor chamber for 15 min at room temperature. 
     After the filters were removed from the chamber, they were placed, colony-side up, onto a Whatman® 3 MM filter which had been previously saturated with 20 mM Tris®-HCl, pH 7.9, 6 M urea, and 0.5 M NaCl. After 15 min, the filters were washed three times in PBS and incubated for 1 hr with purified human IgA in PBS-Tween®. The filters were then rewashed in the PBS-Tween® and developed by standard procedures (Blake, M. S., et al.,  Analyt. Biochem.  136:175-17 (1984)) using a goat antihuman IgA-alkaline phosphatase conjugate (Cappel Research Products, West Chester, Pa.). Several colonies demonstrating high IgA binding activity were selected and grown overnight in 1 ml LB broth containing carbenicillin at 30° C. These cultures were then diluted 1 to 100 with fresh LB-carbenicillin broth and incubated at 30° C. for an addition 6 hr. Expression was then induced by the addition of IPTG and the culture continued for an addition 2 hr at 30° C. The cells were collected by centrifugation, resuspended in water and subjected to several freeze-thaw cycles. The cells were once again collected by centrifugation and the supernatants saved for examination of their IgA binding activity. 
     Example 2 
     Identification of the IgA Binding Domain of Cβ 
     Once certain a stable plasmid producing a recombinant Cβ protein had been achieved and that the expressed protein bound human IgA, a strategy similar to that of the Novatope® System (Novagen, Inc.) was utilized to locate the IgA binding region of Cβ. This procedure was performed according to the manufacturer&#39;s instructions. Briefly, the purified plasmid containing the Cβ gene was randomly digested with DNase I and electrophoresed in a 2% low melting point agarose gel. Fragments of the DNA corresponding to sizes between 100 to 300 base pairs were excised from the gel, purified, and resuspended in TE buffer. A single dA was added to the fragments using the recommended reaction mixture and the fragments ligated into the pETOPET vector which contained single dT ends. After the standard ligation procedure, the plasmids were transformed into competent NovaBlue (DE3) cells (Novagen, Inc.) and plated on LB plates containing 50 μg/ml carbenicillin. These plates were incubated overnight at 37° C. The transformant colonies were tested for IgA binding activity as described in Example 1. Several clones were selected on the bases of their binding to the IgA. The bacteria from each of these clones were inoculated separately onto fresh LB plates and retested for their IgA binding ability as before. Plasmid preparations were made from each by standard means and sequenced. 
     The nucleotide sequences of the cloned Cβ protein gene fragments were determined by the dideoxy method using denatured double-stranded plasmid DNA template as described (Current Protocols in Molecular Biology, John Wiley &amp; Sons, New York, N.Y. (1993)). Sequenase® II kits (United States Biochemical Corp., Cleveland, Ohio) were used in accordance with the manufacturer&#39;s instructions. The smallest fragment of DNA obtained that included part of the Cβ gene is shown in FIG.  1 . The translation of this sequence corresponds to amino acid 101 to 230 of the mature Cβ protein shown in FIG. 1 (SEQ ID NO: 2). Attempts to further shorten this DNA fragment failed to give any IgA binding activity. 
     Example 3 
     ELISA Inhibition Assays: Peptide Binding Studies 
     Several synthetic peptides were made corresponding to the amino acid sequence contained within this region of the Cβ protein. Peptides were synthesized using NMP t-butoxycarbonyl chemistry on an ABI 430A peptide synthesizer (Applied Biosystems, Foster City, Calif.) and were deprotected. Peptides from a sample of the resin were removed from the resin by treatment with HF in the presence of anisole (0° C./1 h). Preparative purification of these peptides were performed using a C18 column (2.14 ID×30 cm)(Dynamax-Rainin, Woburn, Mass.). The peptides were quantitated by PTC amino acid analysis using Waters Picotag system (Waters, Milford, Mass.). The synthesized peptides eluted from the C18 column as a major peak consisting of usually 75-85% of the total elution profile. The amino acid composition of the purified peptides were in good agreement with the sequence which was used to synthesize the peptides. These peptides were used in ELISA inhibition assays to block the binding of human IgA to the purified Cβ protein as follows. Microtiter plates (Nunc-Immuno Plate IIF, Vangard International, Neptune, N.J.) were sensitized by adding 0.1 ml per well of purified Cβ at a concentration of 2.0 μg/ml in 0.1 M carbonate buffer, pH 9.6 with 0.02% azide. The plates were incubated overnight at room temperature. The plates were washed five times with 0.9% NaCl, 0.05% Brij® 35, 10 mM sodium acetate pH 7.0, 0.02% azide. A purified human IgA myeloma protein was purchased from Cappel Laboratories, was diluted in PBS with 0.5% Brij® 35 and added to the plate and incubated for 1 hr at room temperature. The plates were again washed as before and the secondary antibody, alkaline phosphatase conjugated goat anti-human IgA (Tago Inc., Burlingame, Calif.), was diluted in PBS-Brij®, added to the plates and incubated for 1 h at room temperature. The plates were washed as before and p-nitrophenyl phosphate (Sigma 104® phosphatase substrate) (1 mg/ml) in 0.1 M diethanolamine, 1 mM MgCl 2 , 0.1 mM ZnCl 2 , 0.02% azide, pH 9.8 added. The plates were incubated at 37° C. for 1 h and the absorbance at 405 nm determined using an Elida-5 microtiter plate reader (Physica, New York, N.Y.). Control wells lacked either the primary and/or secondary antibody. This was done to obtain a titer of the human IgA myeloma protein which would give a half-maximal reading in the ELISA assay. This titer would be used in the inhibition ELISA. The microtiter plate were sensitize and washed as before. Purified synthetic peptides were added and diluted in PBS-Brij®. The dilution of the human IgA myeloma protein which gave the half maximal reading was then added. The mixture was then incubated for 1 hr at room temperature. The plates were rewashed and the conjugated second antibody added as stated. The plates were then processed and read as described. The percentage of inhibition would be calculated as follows: 
     1-(ELISA value with the peptide added)/(ELISA value without the peptide added). 
     The peptide which inhibited in this ELISA assay contained the sequence Asn-His-Gln-Lys-Ser-Gln-Val-Glu-Lys-Met-Ala-Glu-Gln-Lys-Gly (SEQ ID NO:30). This suggested that at least part of the IgA binding domain of the Cβ was comprised within the region of the protein containing this sequence. 
     Example 4 
     Oligonucleotide Directed Mutagenesis of the Gene Encoding Cβ 
     In order to confirm the importance of this region in the Cβ protein for IgA binding activity and to begin to generate the mutant proteins that in the end would be used in the vaccine formulation, a modification of the Ex-Site™ PCR site-directed mutagenesis protocol was employed as developed by Stratagene (Stratagene, Calif.). The template used was a plasmid called pNV222 which consisted of the Cβ gene inserted into the pSP76 vector (Promega,Madison). DNA oligonucleotides were synthesized on an Applied Biosystems model 292 DNA Synthesizer (Foster City, Calif.). The oligonucleotides were manually cleaved from the column by treatment with 1.5 ml of ammonium hydroxide for 2 hours with gentle mixing every 15 minutes. They were deprotected at 55° C. for 16-18 hours. After deprotection they were dried down and used directly or purified using oligonucleotide purification columns (Applied Biosystems, Foster City Calif.). Several different oligonucleotides were made to induce different changes in the DNA sequence in the region of interest. An example of which is the following. The primers, in this particular example, were overlapping primers, both containing the sequence required to change lysine to alanine at amino acids 170 and 175 in the sequence shown in FIG. 1 (SEQ ID NO: 2) The forward primer, designated Cβ 613, had the sequence (SEQ ID NO: 26) 5′-GTT GAA GCA ATG GCA GAG CAA GCG GGA ATC ACA AAT GAA G-3′ and the reverse primer, designated Cβ 642R had the sequence (SEQ ID NO: 27) 5′-GAT TCC CGC TTG CTC TGC CAT TGC TTC AAC TTG ACT TTT TTG-3′ (the substitutions are noted in BOLD). The reaction conditions were as follows: 10 ng pNV222 template, 15 pmol. of each primer, 1 mM of each dNTP, 1X Vent® Polymerase Buffer (20 mM Tris®-HCl, pH 7.5; 10 mM KCl; 10 mM (NH 4 ) 2  SO 4 ; 2 mM MgSO 4  0.1% (v/v) Triton® X-100; 0.1 mg/ml bovine serum albumin (BSA)), 10 units of Vent® Polymerase, and H 2 O to 100 μl. The reactions were prepared with PCR Gem 10 wax beads as per the Hot Start Protocol (Perkin Elmer, Foster City, Calif.). The reactions were run in a Perkin Elmer® Thermocycler (Perkin Elmer, Foster City, Calif.) under the following conditions: 1 cycle of 94° C. for 5 minutes; 10 cycles of 94° C. for 30 seconds, 37° C. for 2 minutes, 72° C. for 10 minutes; 30 cycles of 94° C. for 30 seconds, 55° C. for 2 minutes, 72° C. for 10 minutes; and 1 cycle of 72° C. for 12 minutes. The reaction was treated with 10 units of DpnI at 37° C. for 30 minutes to destroy the template DNA, followed by a 60 minute treatment at 72° C. with PfuI polymerase to fill in any remaining overhangs. The reaction was diluted 1:4.6 in 1 X Vent® Buffer plus 0.38 mM dATP. The diluted reaction was ligated for 24 hours at 25° C. and transformed into competent DH5α cells (Gibco/BRL, Gaithersburg, Md.). Selected colonies were grown in 3 ml of LB plus kanamycin (50 mg/ml) at 37° C. for 16-18 hours. DNA was prepared using QIAspin™ columns (Qiagen, Chatsworth, Calif.). The clones were analyzed for insert size on 0.8% agarose gels and then sequenced. Selected clones were then grown in 100 ml LB plus kanamycin (50 mg/ml) at 37° C. for 16-18 hours. DNA was prepared using the Qiagen®-tip 100 (Qiagen, Chatsworth, Calif.). They were then digested with NdeI and PstI and run on 0.8% agarose gels to separate the mutated region. The 2300 bp fragment was isolated and purified from the gel using the Gene-Clean Spin Kit™ (Bio 101, Vista, Calif.). A clone named pNV34 which consisted of the expression vector pET 24a (Novagen Inc.) and the native Cβ gene, was also digested with NdeI and PstI and run on a 0.8% agarose gel. The large band (6300 bp) containing the pET vector and the remainder of the Cβ gene was isolated and purified from the gel using the Gene-Clean Spin Kit™ (Bio 101). These two fragments were ligated at 4° C. for 24 hours and transformed into competant BL21(DE3) cells. Selected colonies were grown in 3 ml of LB plus kanamycin (50 mg/ml) at 37° C. for 16-18 hours. DNA was prepared using QIAspin™ columns (Qiagen) and the clones were analyzed for insert size on 0.8% agarose gels. 
     Also constructed were clones encoding mutant Cβ proteins wherein two glutaminyl residues are replaced by prolinyl residues (FIG.  3  and SEQ ID NO:6), and wherein a deletion in the Cβ gene had occurred resulting in a 6 amino acid deletion in the region of interest (FIG.  4  and SEQ ID NO:8). 
     Clones expressing a Cβ protein which lacked or had reduced IgA binding activity but still reacted with the anti-βag antiserum were selected (see Example 5) and grown in 100 ml LB plus kanamycin (50 mg/ml) at 37° C. for 16-18 hours. Plasmid DNA from these clones was prepared using Qiagen® tip 100 (Qiagen) and the mutated Cβ gene entirely sequenced. 
     Example 5 
     Western Blot and ELISA Analysis of IgA Binding by Cβ Mutants 
     The proteins encoded by the mutated genes were expressed and subjected to SDS-PAGE and western blot analysis in order to determine if mutations in the gene encoding the Cβ protein reduced or eliminated IgA binding, while retaining Cβ antigenicity. Two western blots were made for each sample and reacted with either the purified human IgA myeloma protein or hyperimmune rabbit anti-βag protein antiserum. The clone expressing a Cβ protein wherein lysine is changed to alanine at amino acids 170 and 175 in the sequence shown in FIG. 1 (SEQ ID NO:2) demonstrated almost no IgA binding activity, but the ability of the protein to react with anti-Cβ antiserum remained high. IgA binding activity was also substantially eliminated in the clone expressing a Cβ protein wherein two glutaminyl residues are replaced by prolinyl residues (FIG.  3  and SEQ ID NO:6) and in the clone encoding a Cβ protein having a six amino acid deletion (FIG.  4  and SEQ ID NO:8), while reactivity with the anti-Cβ antiserum was maintained for both. The data for the clone having a six amino acid deletion suggested that the residues responsible for the IgA binding activity of the Cβ protein were located within this region of the protein, and that other possible mutations within this area would effect the IgA binding activity. 
     A competitive inhibition ELISA was used to more precisely determine the amount of antigenic and/or structure change the sequence modifications had on the Cβ protein. Microtiter plates (Nunc-Immuno Plate IIF, Vangard International, Neptune, N.J.) were sensitized by adding 0.1 ml per well of purified Cβ at a concentration of 2.0 μg/ml in 0.1M carbonate buffer, pH 9.6 with 0.02% azide. The plates were incubated overnight at room temperature. The plates were washed five times with 0.9% NaCl, 0.05% Brij® 35, 10 mM sodium acetate pH 7.0, 0.02% azide. Hyperimmune rabbit antiserum to the Cβ protein was diluted in PBS with 0.5% Brij® 35 and added to the plate and incubated for 1 hr at room temperature. The plates were again washed as before and the secondary antibody, alkaline phosphatase conjugated goat anti-rabbit IgG (Tago Inc., Burlingame, Calif.), was diluted in PBS-Brij®, added to the plates and incubated for 1 h at room temperature. The plates were washed as before and p-nitrophenyl phosphate (Sigma 104® Phosphatase Substrate 104) (1 mg/ml) in 0.1M diethanolamine, 1 mM MgCl 2 , 0.1 mM ZnCl 2 , 0.02% azide, pH 9.8, was added. The plates were incubated at 37° C. for 1 h and the absorbance at 405 nm determined using an Elida-5 microtiter plate reader (Physica, New York, N.Y.). Control wells lacked either the primary and/or secondary antibody. This was done to obtain a titer of the rabbit anti-Cβ protein which would give a half-maximal reading in the ELISA assay. This titer would be used in the inhibition ELISA. The microtiter plate were sensitized and washed as before. Purified Cβ protein or mutations of the Cβ protein were added and diluted in PBS-Brij®. The dilution of the rabbit anti-Cβ protein which gave the half maximal reading was then added. The mixture was then incubated for 1 hr at room temperature. The plates were rewashed and the conjugated second antibody added as stated. The plates were then processed and read as described. The percentage of inhibition would be calculated as follows: 
     1-(ELISA value with the protein added)/(ELISA value without the proteins added). 
     FIG. 5, shows the results of one of these inhibition ELISA assays. In this assay the inhibition of the wildtype Cβ protein from streptococci is compared with the recombinant Cβ protein and the glutaminyl to prolinyl mutants, both expressed in  E. coli.  As can be seen from the figure, this assay is sensitive enough to detect the absence of the membrane spanning region in the recombinants of the Cβ proteins. However, when the recombinant Cβ protein containing the wildtype sequence is compared to the substitution mutant lacking IgA binding activity, the antigenic differences are minimal. This would suggest that such substitution mutants maintain most of the antigenic character of the Cβ protein but lack the unwanted IgA binding activity. 
     Although the foregoing refers to particular preferred embodiments, it will be understood that the present invention is not so limited. It will occur to those of ordinary skill in the art that various modifications may be made to the disclosed embodiments and that such modifications are intended to be within the scope of the present invention, which is defined by the following Claims. All patents and publications cited herein are incorporated by reference herein in their entirety. 
     
       
         
               
               
               
               
             
               
               
               
               
             
           
               
                   
               
               
                   
                   
                   
                 % 
               
               
                   
                   
                   
                 wild- 
               
               
                 Name 
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                 Vector 
                 type 
               
               
                   
               
             
             
               
                   
               
             
          
           
               
                 IgAbs+ 
                                  ]LLHIKQHEEVEKDKKAKQQKTLKQSDTKVDLSNIDKELNHQKSQVEKMAEQKGITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKVREELGKLFS- 
                 pTOPE 
                 100 
               
               
                   
                 STKAGLDQEIQ[ 
               
               
                   
               
               
                 dgb6 
                 ]DSDALLELENQFNETNRLLHIKQHEEVEKDKKAKQQKTLKQSDTKVDLSNIDKELNHQKSQVEKMAEQKGITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKVREELGKLFS- 
                 17b 
                 20 
               
               
                   
                 STKAGLDQEIQEHVKKETSSEENTQKVDEHYANSL[ 
               
               
                   
               
               
                 dgb6p 
                 ]DSDALLELENQFNETNRLLHIKQHEEVEKDKKAKQQKTLKQSDTKVDLSNIDKELNHQKSQVEKMAEQKGITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKVREELGKLFS- 
                 pTOPE 
                 100 
               
               
                   
                 STKAGLDQEIQEHVKKETSSEENTQKVDEHYANSL[ 
               
               
                   
               
               
                 dgb7 
                                                              ]VDLSNIDKELNHQKSQVEKMAEQKGITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKVREELGKLFS- 
                 17b 
                 0 
               
               
                   
                 STKAGLDQEIQEHVKKETSSEENTQKVDEHYANSLQNLAQKSLE[ 
               
               
                   
               
               
                 dgb7p 
                                                              ]VDLSNIDKELNHQKSQVEKMAEQKGITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKVREELGKLFS- 
                 pTOPE 
                 100 
               
               
                   
                 STKAGLDQEIQEHVKKETSSEENTQKVDEHYANSLQNLAQKSLE[ 
               
               
                   
               
               
                 dgb8 
                                                              ]VDLSNIDKELNHQKSQVEKMAEQKGITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKVREELGKLFS- 
                 17b 
                 0 
               
               
                   
                 STKAGLDQEIQEHVKKETSSEENTQKVDEHYANSLQNLAQKSLEELDKATTNE[ 
               
               
                   
               
               
                 dgb8p 
                                                              ]VDLSNIDKELNHQKSQVEKMAEQKGITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKVREELGKLFS- 
                 pTOPE 
                 100 
               
               
                   
                 STKAGLDQEIQEHVKKETSSEENTQKVDEHYANSLQNLAQKSLEELDKATTNE[ 
               
               
                   
               
               
                 dgb10 
                                                              ]VDLSNIDKELNHQKSQVEKMAEQKGITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKV[ 
                 17b 
                 10 
               
               
                   
               
               
                 dgb12 
                                                           ....VDLSNIDKELNHQKSQVEKMAEQKGITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKV[ 
                 17b 
                 20 
               
               
                   
               
               
                 dgb11 
                                                           ....VDLSNIDKELNHQKSQVEKMAEQKGITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKVREELGKLFS- 
                 17b 
                 20 
               
               
                   
                 STKAGLDQEIQEHVKKETSSEENTQKVDEHYANSL[ 
               
               
                   
               
               
                 nv34qp 
                                                           ....VDLSNIDKELNHQKS P VEKMAE P KGITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKVREELGKLFS- 
                 24a 
                 10 
               
               
                   
                 STKAGLDQEIQ... 
               
               
                   
               
               
                 dgb2 
                                                           ....VDLSNIDKELNHQKSQVE A MAEQ A GITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKVREELGKLFS- 
                 24a 
                 60 
               
               
                   
                 STKAGLDQEIQ... 
               
               
                   
               
               
                 dgb1 
                                                           ....VDLSNIDKELNHQKSQE{—Δ—} A GITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKVREELGKLFS- 
                 24a 
                 0 
               
               
                   
                 STKAGLDQEIQ... 
               
               
                   
               
               
                 pnv231 
                                                           ....VDLSNIDKELNHQKSQVE T MAEQ L GITNEDKDSMLKKIEDIRKQAQQADKKEDAEVKVREELGKLFS- 
                 24a 
                 60 
               
               
                   
                 STKAGLDQEIQ... 
               
               
                   
               
             
          
         
       
     
     
       
         
           
             34 
           
           
             
               4200 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA 
             
             
               not provided 
             
             
               CDS 
                320..3811 
             
              1
AAGCTTATGC TTGTCAATAA TCACAAATTT GTAGATCACT TCCTTTTTAG GACTGTAAAG     60
CATCCTAATT ACTTTTTAAA TATATTACCA GAACTAGTTG GTTTGGCCCT GGTGAGTCAT    120
GCTTATGTGA CATTCATCTT TATTTTTCCT GTCTATGCGG TTATTCTTTA TCAAAGAATA    180
GCAGAGGAAG AAAAATTATT GCAGGAAGTT ATTATTCCGA ATGGAAGAAT GAAAGGTTAA    240
AAATAATATA CCCAATTTAA TATGCAGTTC ATATTGGAAG GGTATACTGT AGATAAATAA    300
AATATTGGAG GATATCGAT ATG TTT AAA TCT AAT TAT GAA AGA AAA ATG CGT     352
                     Met Phe Lys Ser Asn Tyr Glu Arg Lys Met Arg
                       1               5                  10
TAT TCC ATT CGT AAA TTT AGT GTA GGA GTA GCT AGT GTA GCG GTA GCT      400
Tyr Ser Ile Arg Lys Phe Ser Val Gly Val Ala Ser Val Ala Val Ala
             15                  20                  25
AGT TTG TTC ATG GGA AGC GTT GCT CAT GCA AGT GAG CTT GTA AAG GAC      448
Ser Leu Phe Met Gly Ser Val Ala His Ala Ser Glu Leu Val Lys Asp
         30                  35                  40
GAT AGT GTG AAG ACT ACC GAG GTT GCA GCT AAG CCC TAT CCA AGT ATG      496
Asp Ser Val Lys Thr Thr Glu Val Ala Ala Lys Pro Tyr Pro Ser Met
     45                  50                  55
GCT CAA ACA GAT CAA GGA AAT AAT TCA TCA TCC TCG GAA CTT GAG ACA      544
Ala Gln Thr Asp Gln Gly Asn Asn Ser Ser Ser Ser Glu Leu Glu Thr
 60                  65                  70                  75
ACA AAG ATG GAA ATT CCT ACA ACA GAC ATA AAA AAA GCT GTT GAA CCG      592
Thr Lys Met Glu Ile Pro Thr Thr Asp Ile Lys Lys Ala Val Glu Pro
                 80                  85                  90
GTC GAG AAA ACA GCT GGG GAA ACA TCT GCC ACT GAT ACT GGA AAA CGA      640
Val Glu Lys Thr Ala Gly Glu Thr Ser Ala Thr Asp Thr Gly Lys Arg
             95                 100                 105
GAG AAA CAA TTA CAA CAA TGG AAA AAT AAT CTA AAA AAT GAT GTG GAT      688
Glu Lys Gln Leu Gln Gln Trp Lys Asn Asn Leu Lys Asn Asp Val Asp
        110                 115                 120
AAC ACA ATT CTA TCT CAT GAA CAG AAA AAT GAG TTT AAA ACA AAA ATT      736
Asn Thr Ile Leu Ser His Glu Gln Lys Asn Glu Phe Lys Thr Lys Ile
    125                 130                 135
GAT GAA ACA AAT GAT TCT GAT GCA TTA TTA GAA TTA GAA AAT CAA TTT      784
Asp Glu Thr Asn Asp Ser Asp Ala Leu Leu Glu Leu Glu Asn Gln Phe
140                 145                 150                 155
AAC GAA ACT AAT AGA CTG TTA CAC ATC AAA CAA CAT GAA GAA GTT GAG      832
Asn Glu Thr Asn Arg Leu Leu His Ile Lys Gln His Glu Glu Val Glu
                160                 165                 170
AAA GAT AAG AAA GCT AAG CAA CAG AAA ACT CTG AAA CAG TCA GAT ACG      880
Lys Asp Lys Lys Ala Lys Gln Gln Lys Thr Leu Lys Gln Ser Asp Thr
            175                 180                 185
AAA GTA GAT CTA AGC AAT ATT GAC AAA GAG CTT AAT CAT CAA AAA AGT      928
Lys Val Asp Leu Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser
        190                 195                 200
CAA GTT GAA AAA ATG GCA GAG CAA AAG GGA ATC ACA AAT GAA GAT AAA      976
Gln Val Glu Lys Met Ala Glu Gln Lys Gly Ile Thr Asn Glu Asp Lys
    205                 210                 215
GAT TCT ATG CTG AAA AAA ATC GAA GAT ATT CGT AAA CAA GCT CAA CAA     1024
Asp Ser Met Leu Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln
220                 225                 230                 235
GCA GAT AAA AAA GAA GAT GCC GAA GTA AAG GTT CGT GAA GAA CTA GGT     1072
Ala Asp Lys Lys Glu Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly
                240                 245                 250
AAA CTC TTT AGT TCA ACT AAA GCT GGT CTG GAT CAA GAA ATT CAA GAG     1120
Lys Leu Phe Ser Ser Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln Glu
            255                 260                 265
CAT GTG AAG AAA GAA ACG AGT AGT GAG GAA AAT ACT CAG AAA GTT GAT     1168
His Val Lys Lys Glu Thr Ser Ser Glu Glu Asn Thr Gln Lys Val Asp
        270                 275                 280
GAA CAC TAT GCT AAT AGC CTT CAG AAC CTT GCT CAA AAA TCT CTT GAA     1216
Glu His Tyr Ala Asn Ser Leu Gln Asn Leu Ala Gln Lys Ser Leu Glu
    285                 290                 295
GAA CTA GAT AAG GCA ACT ACC AAT GAA CAA GCT ACA CAA GTT AAA AAT     1264
Glu Leu Asp Lys Ala Thr Thr Asn Glu Gln Ala Thr Gln Val Lys Asn
300                 305                 310                 315
CAA TTC TTA GAA AAC GCT CAA AAG CTC AAA GAA ATA CAA CCT CTT ATC     1312
Gln Phe Leu Glu Asn Ala Gln Lys Leu Lys Glu Ile Gln Pro Leu Ile
                320                 325                 330
AAA GAA ACG AAT GTG AAA TTG TAT AAG GCT ATG AGT GAG AGC TTG GAG     1360
Lys Glu Thr Asn Val Lys Leu Tyr Lys Ala Met Ser Glu Ser Leu Glu
            335                 340                 345
CAG GTT GAG AAG GAA TTA AAA CAT AAT TCG GAA GCT AAT TTA GAA GAT     1408
Gln Val Glu Lys Glu Leu Lys His Asn Ser Glu Ala Asn Leu Glu Asp
        350                 355                 360
TTG GTT GCG AAA TCT AAA GAA ATC GTA AGA GAA TAC GAA GGA AAA CTT     1456
Leu Val Ala Lys Ser Lys Glu Ile Val Arg Glu Tyr Glu Gly Lys Leu
    365                 370                 375
AAT CAA TCT AAA AAT CTT CCA GAA TTA AAG CAA CTA GAA GAG GAA GCT     1504
Asn Gln Ser Lys Asn Leu Pro Glu Leu Lys Gln Leu Glu Glu Glu Ala
380                 385                 390                 395
CAT TCG AAG TTG AAA CAA GTT GTG GAG GAT TTT AGA AAA AAA TTT AAA     1552
His Ser Lys Leu Lys Gln Val Val Glu Asp Phe Arg Lys Lys Phe Lys
                400                 405                 410
ACG TCA GAG CAA GTG ACA CCA AAA AAA CGT GTC AAA CGA GAT TTA GCT     1600
Thr Ser Glu Gln Val Thr Pro Lys Lys Arg Val Lys Arg Asp Leu Ala
            415                 420                 425
GCT AAT GAA AAT AAT CAA CAA AAG ATT GAG TTA ACA GTT TCA CCA GAG     1648
Ala Asn Glu Asn Asn Gln Gln Lys Ile Glu Leu Thr Val Ser Pro Glu
        430                 435                 440
AAT ATC ACT GTA TAT GAA GGT GAA GAC GTG AAA TTT ACA GTC ACA GCT     1696
Asn Ile Thr Val Tyr Glu Gly Glu Asp Val Lys Phe Thr Val Thr Ala
    445                 450                 455
AAA AGT GAT TCG AAG ACG ACG TTG GAC TTC AGT GAT CTT TTA ACA AAA     1744
Lys Ser Asp Ser Lys Thr Thr Leu Asp Phe Ser Asp Leu Leu Thr Lys
460                 465                 470                 475
TAT AAT CCG TCT GTA TCA GAT AGA ATT AGT ACA AAT TAT AAG ACT AAC     1792
Tyr Asn Pro Ser Val Ser Asp Arg Ile Ser Thr Asn Tyr Lys Thr Asn
                480                 485                 490
ACG GAT AAT CAT AAG ATT GCC GAA ATC ACT ATC AAG AAT TTG AAG CTA     1840
Thr Asp Asn His Lys Ile Ala Glu Ile Thr Ile Lys Asn Leu Lys Leu
            495                 500                 505
AAT GAA AGT CAA ACA GTG ACT CTA AAA GCT AAA GAT GAT TCT GGC AAT     1888
Asn Glu Ser Gln Thr Val Thr Leu Lys Ala Lys Asp Asp Ser Gly Asn
        510                 515                 520
GTA GTT GAA AAA ACA TTC ACT ATT ACA GTG CAA AAG AAA GAG GAG AAA     1936
Val Val Glu Lys Thr Phe Thr Ile Thr Val Gln Lys Lys Glu Glu Lys
    525                 530                 535
CAA GTT CCT AAA ACA CCA GAG CAG AAA GAT TCT AAA ACG GAA GAA AAG     1984
Gln Val Pro Lys Thr Pro Glu Gln Lys Asp Ser Lys Thr Glu Glu Lys
540                 545                 550                 555
GTT CCT CAA GAA CCA AAA TCA AAT GAC AAG AAT CAA TTA CAA GAG TTG     2032
Val Pro Gln Glu Pro Lys Ser Asn Asp Lys Asn Gln Leu Gln Glu Leu
                560                 565                 570
ATT AAA TCA GCT CAA CAA GAA CTG GAA AAG TTA GAA AAA GCA ATA AAA     2080
Ile Lys Ser Ala Gln Gln Glu Leu Glu Lys Leu Glu Lys Ala Ile Lys
            575                 580                 585
GAA TTA ATG GAG CAA CCA GAG ATT CCA TCC AAT CCA GAG TAT GGT ATT     2128
Glu Leu Met Glu Gln Pro Glu Ile Pro Ser Asn Pro Glu Tyr Gly Ile
        590                 595                 600
CAA AAA TCT ATT TGG GAG TCA CAA AAA GAG CCT ATC CAG GAA GCC ATA     2176
Gln Lys Ser Ile Trp Glu Ser Gln Lys Glu Pro Ile Gln Glu Ala Ile
    605                 610                 615
ACA AGT TTT AAG AAG ATT ATT GGT GAT TCA TCT TCA AAA TAC TAC ACA     2224
Thr Ser Phe Lys Lys Ile Ile Gly Asp Ser Ser Ser Lys Tyr Tyr Thr
620                 625                 630                 635
GAG CAC TAT TTT AAC AAA TAT AAA TCT GAT TTT ATG AAT TAT CAA CTT     2272
Glu His Tyr Phe Asn Lys Tyr Lys Ser Asp Phe Met Asn Tyr Gln Leu
                640                 645                 650
CAT GCA CAA ATG GAG ATG CTG ACT AGA AAA GTG GTT CAG TAT ATG AAC     2320
His Ala Gln Met Glu Met Leu Thr Arg Lys Val Val Gln Tyr Met Asn
            655                 660                 665
AAA TAT CCT GAT AAT GCA GAA ATT AAA AAG ATA TTT GAG TCA GAT ATG     2368
Lys Tyr Pro Asp Asn Ala Glu Ile Lys Lys Ile Phe Glu Ser Asp Met
        670                 675                 680
AAG AGA ACG AAA GAA GAT AAT TAC GGA AGT TTA GAA AAT GAT GCT TTG     2416
Lys Arg Thr Lys Glu Asp Asn Tyr Gly Ser Leu Glu Asn Asp Ala Leu
    685                 690                 695
AAA GGC TAT TTT GAG AAA TAT TTC CTT ACA CCA TTT AAT AAA ATT AAG     2464
Lys Gly Tyr Phe Glu Lys Tyr Phe Leu Thr Pro Phe Asn Lys Ile Lys
700                 705                 710                 715
CAG ATT GTA GAT GAT TTG GAT AAA AAA GTA GAA CAA GAT CAG CCA GCA     2512
Gln Ile Val Asp Asp Leu Asp Lys Lys Val Glu Gln Asp Gln Pro Ala
                720                 725                 730
CCA ATT CCG GAA AAT TCA GAA ATG GAT CAG GCT AAG GAA AAG GCT AAG     2560
Pro Ile Pro Glu Asn Ser Glu Met Asp Gln Ala Lys Glu Lys Ala Lys
            735                 740                 745
ATT GCT GTA TCG AAG TAT ATG AGT AAG GTT TTA GAT GGA GTT CAT CAA     2608
Ile Ala Val Ser Lys Tyr Met Ser Lys Val Leu Asp Gly Val His Gln
        750                 755                 760
CAT CTG CAG AAG AAA AAT AAC AGT AAA ATT GTT GAT CTT TTT AAG GAA     2656
His Leu Gln Lys Lys Asn Asn Ser Lys Ile Val Asp Leu Phe Lys Glu
    765                 770                 775
CTT GAA GCG ATT AAA CAA CAA ACT ATT TTT GAT ATT GAC AAT GCA AAG     2704
Leu Glu Ala Ile Lys Gln Gln Thr Ile Phe Asp Ile Asp Asn Ala Lys
780                 785                 790                 795
ACT GAA GTA GAG ATT GAT AAC TTA GTA CAC GAT GCA TTC TCA AAA ATG     2752
Thr Glu Val Glu Ile Asp Asn Leu Val His Asp Ala Phe Ser Lys Met
                800                 805                 810
AAT GCT ACT GTT GCT AAA TTT CAA AAA GGT CTA GAG ACA AAT ACG CCA     2800
Asn Ala Thr Val Ala Lys Phe Gln Lys Gly Leu Glu Thr Asn Thr Pro
            815                 820                 825
GAA ACT CCA GAT ACA CCG AAG ATT CCA GAG CTA CCT CAA GCC CCA GAT     2848
Glu Thr Pro Asp Thr Pro Lys Ile Pro Glu Leu Pro Gln Ala Pro Asp
        830                 835                 840
ACA CCG CAG GCT CCA GAC ACA CCG CAT GTT CCG GAA TCA CCA AAG GCC     2896
Thr Pro Gln Ala Pro Asp Thr Pro His Val Pro Glu Ser Pro Lys Ala
    845                 850                 855
CCA GAA GCA CCG CGT GTT CCG GAA TCA CCA AAG ACT CCA GAA GCA CCG     2944
Pro Glu Ala Pro Arg Val Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro
860                 865                 870                 875
CAT GTT CCG GAA TCA CCA AAG GCC CCA GAA GCA CCG CGT GTT CCG GAA     2992
His Val Pro Glu Ser Pro Lys Ala Pro Glu Ala Pro Arg Val Pro Glu
                880                 885                 890
TCA CCA AAG ACT CCA GAA GCA CCG CAT GTT CCG GAA TCA CCA AAG ACT     3040
Ser Pro Lys Thr Pro Glu Ala Pro His Val Pro Glu Ser Pro Lys Thr
            895                 900                 905
CCA GAA GCA CCA AAG ATT CCG AAA CCC CCT AAG ACT CCA GAC GTC CCT     3088
Pro Glu Ala Pro Lys Ile Pro Lys Pro Pro Lys Thr Pro Asp Val Pro
        910                 915                 920
AAG CTT CCA GAC GTC CCT AAG CTT CCA GAC GTC CCT AAG CTT CCA GAT     3136
Lys Leu Pro Asp Val Pro Lys Leu Pro Asp Val Pro Lys Leu Pro Asp
    925                 930                 935
GCA CCG AAG TTA CCA GAT GGG TTA AAT AAA GTT GGA CAA GCA GTA TTT     3184
Ala Pro Lys Leu Pro Asp Gly Leu Asn Lys Val Gly Gln Ala Val Phe
940                 945                 950                 955
ACA TCA ACT GAT GGA AAT ACT AAG GTT ACG GTT GTA TTT GAT AAA CCT     3232
Thr Ser Thr Asp Gly Asn Thr Lys Val Thr Val Val Phe Asp Lys Pro
                960                 965                 970
ACA GAT GCT GAT AAG TTA CAT CTC AAG GAA GTA ACG ACG AAA GAG TTG     3280
Thr Asp Ala Asp Lys Leu His Leu Lys Glu Val Thr Thr Lys Glu Leu
            975                 980                 985
GCT GAT AAA ATT GCT CAT AAA ACA GGA GGA GGA ACA GTT CGT GTG TTT     3328
Ala Asp Lys Ile Ala His Lys Thr Gly Gly Gly Thr Val Arg Val Phe
        990                 995                 1000
GAC TTA TCT CTT TCT AAA GGA GGC AAG GAA ACA CAT GTC AAT GGA GAA     3376
Asp Leu Ser Leu Ser Lys Gly Gly Lys Glu Thr His Val Asn Gly Glu
    1005                1010                1015
CGA ACT GTT CGG CTC GCG CTT GGG CAG ACT GGC TCA GAT GTT CAC GTC     3424
Arg Thr Val Arg Leu Ala Leu Gly Gln Thr Gly Ser Asp Val His Val
1020                1025                1030                1035
TAT CAC GTA AAG GAA AAT GGC GAC CTT GAG CGT ATT CCT TCT AAA GTT     3472
Tyr His Val Lys Glu Asn Gly Asp Leu Glu Arg Ile Pro Ser Lys Val
                1040                1045                1050
GAA AAT GGG CAA GTT GTT TTT AAA ACG AAC CAC TTC AGT TTG TTT GCG     3520
Glu Asn Gly Gln Val Val Phe Lys Thr Asn His Phe Ser Leu Phe Ala
            1055                1060                1065
ATT AAG ACA CTT TCT AAG GAT CAA AAT GTT ACT CCA CCG AAG CAG ACT     3568
Ile Lys Thr Leu Ser Lys Asp Gln Asn Val Thr Pro Pro Lys Gln Thr
        1070                1075                1080
AAA CCT TCT ACC CAA GGC AGT CAA GTA GAG ATT GCA GAG AGT CAA ACT     3616
Lys Pro Ser Thr Gln Gly Ser Gln Val Glu Ile Ala Glu Ser Gln Thr
    1085                1090                1095
GGA AAA TTC CAG AGT AAA GCA GCT AAT CAT AAA GCA CTG GCT ACT GGA     3664
Gly Lys Phe Gln Ser Lys Ala Ala Asn His Lys Ala Leu Ala Thr Gly
1100                1105                1110                1115
AAT GAA ACA GTG GCA AAA GGA AAT CCT ACA TCA ACA ACG GAA AAG AAA     3712
Asn Glu Thr Val Ala Lys Gly Asn Pro Thr Ser Thr Thr Glu Lys Lys
                1120                1125                1130
TTG CCA TAT ACA GGA GTG GCA TCT AAT CTA GTT CTT GAA ATT ATG GGT     3760
Leu Pro Tyr Thr Gly Val Ala Ser Asn Leu Val Leu Glu Ile Met Gly
            1135                1140                1145
CTC CTT GGT TTG ATT GGA ACT TCA TTC ATC GCA ATG AAA AGA AGA AAA     3808
Leu Leu Gly Leu Ile Gly Thr Ser Phe Ile Ala Met Lys Arg Arg Lys
        1150                1155                1160
TCA TGATTCAGTT TTTTAAAAAT ATCCACTTTC GATATCTAGC ATTTGATTGG          3861
Ser
TTATCTGTGG ATGATTCTAA AGATGTTACC TATCGTTGGT ATGTAACAAT TATAAGTCAT   3921
TTCATATAAA AGAGGCTCTT TGTCAACTGT AGTTGGTTGA AACAAGGCTA CAAACTAGAA   3981
AGGACGCATT TTGTCCTTTC TTTTTGATGT TGAGGGCAAT GAAAATACGC TTTTTGAAGT   4041
TTTCAAAATT CCGAAAACTA AAGATATTGT ATTTGAAAAG TTTAATGAGA TGATTAGTTG   4101
CTTCCAATTT TGCGTTGGAG TAGGTTTACT GAAGGACGTT GACGATATTC TCTTTGCTTT   4161
TGAGAATGAT TTTAAAGATA GTCTGAAAAA GAGGATGAA                          4200 
           
           
             
               1164 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               not provided 
             
              2
Met Phe Lys Ser Asn Tyr Glu Arg Lys Met Arg Tyr Ser Ile Arg Lys
  1               5                  10                  15
Phe Ser Val Gly Val Ala Ser Val Ala Val Ala Ser Leu Phe Met Gly
             20                  25                  30
Ser Val Ala His Ala Ser Glu Leu Val Lys Asp Asp Ser Val Lys Thr
         35                  40                  45
Thr Glu Val Ala Ala Lys Pro Tyr Pro Ser Met Ala Gln Thr Asp Gln
     50                  55                  60
Gly Asn Asn Ser Ser Ser Ser Glu Leu Glu Thr Thr Lys Met Glu Ile
 65                  70                  75                  80
Pro Thr Thr Asp Ile Lys Lys Ala Val Glu Pro Val Glu Lys Thr Ala
                 85                  90                  95
Gly Glu Thr Ser Ala Thr Asp Thr Gly Lys Arg Glu Lys Gln Leu Gln
            100                 105                 110
Gln Trp Lys Asn Asn Leu Lys Asn Asp Val Asp Asn Thr Ile Leu Ser
        115                 120                 125
His Glu Gln Lys Asn Glu Phe Lys Thr Lys Ile Asp Glu Thr Asn Asp
    130                 135                 140
Ser Asp Ala Leu Leu Glu Leu Glu Asn Gln Phe Asn Glu Thr Asn Arg
145                 150                 155                 160
Leu Leu His Ile Lys Gln His Glu Glu Val Glu Lys Asp Lys Lys Ala
                165                 170                 175
Lys Gln Gln Lys Thr Leu Lys Gln Ser Asp Thr Lys Val Asp Leu Ser
            180                 185                 190
Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln Val Glu Lys Met
        195                 200                 205
Ala Glu Gln Lys Gly Ile Thr Asn Glu Asp Lys Asp Ser Met Leu Lys
    210                 215                 220
Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala Asp Lys Lys Glu
225                 230                 235                 240
Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys Leu Phe Ser Ser
                245                 250                 255
Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln Glu His Val Lys Lys Glu
            260                 265                 270
Thr Ser Ser Glu Glu Asn Thr Gln Lys Val Asp Glu His Tyr Ala Asn
        275                 280                 285
Ser Leu Gln Asn Leu Ala Gln Lys Ser Leu Glu Glu Leu Asp Lys Ala
    290                 295                 300
Thr Thr Asn Glu Gln Ala Thr Gln Val Lys Asn Gln Phe Leu Glu Asn
305                 310                 315                 320
Ala Gln Lys Leu Lys Glu Ile Gln Pro Leu Ile Lys Glu Thr Asn Val
                325                 330                 335
Lys Leu Tyr Lys Ala Met Ser Glu Ser Leu Glu Gln Val Glu Lys Glu
            340                 345                 350
Leu Lys His Asn Ser Glu Ala Asn Leu Glu Asp Leu Val Ala Lys Ser
        355                 360                 365
Lys Glu Ile Val Arg Glu Tyr Glu Gly Lys Leu Asn Gln Ser Lys Asn
    370                 375                 380
Leu Pro Glu Leu Lys Gln Leu Glu Glu Glu Ala His Ser Lys Leu Lys
385                 390                 395                 400
Gln Val Val Glu Asp Phe Arg Lys Lys Phe Lys Thr Ser Glu Gln Val
                405                 410                 415
Thr Pro Lys Lys Arg Val Lys Arg Asp Leu Ala Ala Asn Glu Asn Asn
            420                 425                 430
Gln Gln Lys Ile Glu Leu Thr Val Ser Pro Glu Asn Ile Thr Val Tyr
        435                 440                 445
Glu Gly Glu Asp Val Lys Phe Thr Val Thr Ala Lys Ser Asp Ser Lys
    450                 455                 460
Thr Thr Leu Asp Phe Ser Asp Leu Leu Thr Lys Tyr Asn Pro Ser Val
465                 470                 475                 480
Ser Asp Arg Ile Ser Thr Asn Tyr Lys Thr Asn Thr Asp Asn His Lys
                485                 490                 495
Ile Ala Glu Ile Thr Ile Lys Asn Leu Lys Leu Asn Glu Ser Gln Thr
            500                 505                 510
Val Thr Leu Lys Ala Lys Asp Asp Ser Gly Asn Val Val Glu Lys Thr
        515                 520                 525
Phe Thr Ile Thr Val Gln Lys Lys Glu Glu Lys Gln Val Pro Lys Thr
    530                 535                 540
Pro Glu Gln Lys Asp Ser Lys Thr Glu Glu Lys Val Pro Gln Glu Pro
545                 550                 555                 560
Lys Ser Asn Asp Lys Asn Gln Leu Gln Glu Leu Ile Lys Ser Ala Gln
                565                 570                 575
Gln Glu Leu Glu Lys Leu Glu Lys Ala Ile Lys Glu Leu Met Glu Gln
            580                 585                 590
Pro Glu Ile Pro Ser Asn Pro Glu Tyr Gly Ile Gln Lys Ser Ile Trp
        595                 600                 605
Glu Ser Gln Lys Glu Pro Ile Gln Glu Ala Ile Thr Ser Phe Lys Lys
    610                 615                 620
Ile Ile Gly Asp Ser Ser Ser Lys Tyr Tyr Thr Glu His Tyr Phe Asn
625                 630                 635                 640
Lys Tyr Lys Ser Asp Phe Met Asn Tyr Gln Leu His Ala Gln Met Glu
                645                 650                 655
Met Leu Thr Arg Lys Val Val Gln Tyr Met Asn Lys Tyr Pro Asp Asn
            660                 665                 670
Ala Glu Ile Lys Lys Ile Phe Glu Ser Asp Met Lys Arg Thr Lys Glu
        675                 680                 685
Asp Asn Tyr Gly Ser Leu Glu Asn Asp Ala Leu Lys Gly Tyr Phe Glu
    690                 695                 700
Lys Tyr Phe Leu Thr Pro Phe Asn Lys Ile Lys Gln Ile Val Asp Asp
705                 710                 715                 720
Leu Asp Lys Lys Val Glu Gln Asp Gln Pro Ala Pro Ile Pro Glu Asn
                725                 730                 735
Ser Glu Met Asp Gln Ala Lys Glu Lys Ala Lys Ile Ala Val Ser Lys
            740                 745                 750
Tyr Met Ser Lys Val Leu Asp Gly Val His Gln His Leu Gln Lys Lys
        755                 760                 765
Asn Asn Ser Lys Ile Val Asp Leu Phe Lys Glu Leu Glu Ala Ile Lys
    770                 775                 780
Gln Gln Thr Ile Phe Asp Ile Asp Asn Ala Lys Thr Glu Val Glu Ile
785                 790                 795                 800
Asp Asn Leu Val His Asp Ala Phe Ser Lys Met Asn Ala Thr Val Ala
                805                 810                 815
Lys Phe Gln Lys Gly Leu Glu Thr Asn Thr Pro Glu Thr Pro Asp Thr
            820                 825                 830
Pro Lys Ile Pro Glu Leu Pro Gln Ala Pro Asp Thr Pro Gln Ala Pro
        835                 840                 845
Asp Thr Pro His Val Pro Glu Ser Pro Lys Ala Pro Glu Ala Pro Arg
    850                 855                 860
Val Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro His Val Pro Glu Ser
865                 870                 875                 880
Pro Lys Ala Pro Glu Ala Pro Arg Val Pro Glu Ser Pro Lys Thr Pro
                885                 890                 895
Glu Ala Pro His Val Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro Lys
            900                 905                 910
Ile Pro Lys Pro Pro Lys Thr Pro Asp Val Pro Lys Leu Pro Asp Val
        915                 920                 925
Pro Lys Leu Pro Asp Val Pro Lys Leu Pro Asp Ala Pro Lys Leu Pro
    930                 935                 940
Asp Gly Leu Asn Lys Val Gly Gln Ala Val Phe Thr Ser Thr Asp Gly
945                 950                 955                 960
Asn Thr Lys Val Thr Val Val Phe Asp Lys Pro Thr Asp Ala Asp Lys
                965                 970                 975
Leu His Leu Lys Glu Val Thr Thr Lys Glu Leu Ala Asp Lys Ile Ala
            980                 985                 990
His Lys Thr Gly Gly Gly Thr Val Arg Val Phe Asp Leu Ser Leu Ser
        995                 1000                1005
Lys Gly Gly Lys Glu Thr His Val Asn Gly Glu Arg Thr Val Arg Leu
    1010                1015                1020
Ala Leu Gly Gln Thr Gly Ser Asp Val His Val Tyr His Val Lys Glu
1025                1030                1035                1040
Asn Gly Asp Leu Glu Arg Ile Pro Ser Lys Val Glu Asn Gly Gln Val
                1045                1050                1055
Val Phe Lys Thr Asn His Phe Ser Leu Phe Ala Ile Lys Thr Leu Ser
            1060                1065                1070
Lys Asp Gln Asn Val Thr Pro Pro Lys Gln Thr Lys Pro Ser Thr Gln
        1075                1080                1085
Gly Ser Gln Val Glu Ile Ala Glu Ser Gln Thr Gly Lys Phe Gln Ser
    1090                1095                1100
Lys Ala Ala Asn His Lys Ala Leu Ala Thr Gly Asn Glu Thr Val Ala
1105                1110                1115                1120
Lys Gly Asn Pro Thr Ser Thr Thr Glu Lys Lys Leu Pro Tyr Thr Gly
                1125                1130                1135
Val Ala Ser Asn Leu Val Leu Glu Ile Met Gly Leu Leu Gly Leu Ile
            1140                1145                1150
Gly Thr Ser Phe Ile Ala Met Lys Arg Arg Lys Ser
        1155                1160 
           
           
             
               3312 base pairs 
               nucleic acid 
               double 
               linear 
             
             
               cDNA 
             
             
               not provided 
             
             
               CDS 
                1..3312 
             
              3
GAA GGA GAT ATA CAT ATG AGT GAG CTT GTA AAG GAC GAT AGT GTG AAG       48
Glu Gly Asp Ile His Met Ser Glu Leu Val Lys Asp Asp Ser Val Lys
  1               5                  10                  15
ACT ACC GAG GTT GCA GCT AAG CCC TAT CCA AGT ATG GCT CAA ACA GAT       96
Thr Thr Glu Val Ala Ala Lys Pro Tyr Pro Ser Met Ala Gln Thr Asp
             20                  25                  30
CAA GGA AAT AAT TCA TCA TCC TCG GAA CTT GAG ACA ACA AGG ATG GAA      144
Gln Gly Asn Asn Ser Ser Ser Ser Glu Leu Glu Thr Thr Arg Met Glu
         35                  40                  45
ATT CCT ACA ACA CAC ATA AAA AAA GCT GTT GAA CCG GTC GAG AAA ACA      192
Ile Pro Thr Thr His Ile Lys Lys Ala Val Glu Pro Val Glu Lys Thr
     50                  55                  60
GCT GGG GAA ACA TCT GCC ACT GAT ACT GGA AAA CGA GAG AAA CAA TTA      240
Ala Gly Glu Thr Ser Ala Thr Asp Thr Gly Lys Arg Glu Lys Gln Leu
 65                  70                  75                  80
CAA CAA TGG AAA AAT AAT CTA AAA AAT GAT GTG GAT AAC ACA ATT CTA      288
Gln Gln Trp Lys Asn Asn Leu Lys Asn Asp Val Asp Asn Thr Ile Leu
                 85                  90                  95
TCT CAT GAA CAG AAA AAT GAG TTT AAA ACA AAA ATT GAT GAA ACA AAT      336
Ser His Glu Gln Lys Asn Glu Phe Lys Thr Lys Ile Asp Glu Thr Asn
            100                 105                 110
GAT TCT GAT GCA TTA TTA GAA TTA GAA AAT CAA TTT AAC GAA ACT AAT      384
Asp Ser Asp Ala Leu Leu Glu Leu Glu Asn Gln Phe Asn Glu Thr Asn
        115                 120                 125
AGA CTG TTA CAC ATC AAA CAA CAT GAA GAA GTT GAG AAA CAT AAC AAA      432
Arg Leu Leu His Ile Lys Gln His Glu Glu Val Glu Lys His Asn Lys
    130                 135                 140
CCT AAC CAA CAG AAA ACT CTG AAA CAG TCA GAT ACG AAA GTA GAT CTA      480
Pro Asn Gln Gln Lys Thr Leu Lys Gln Ser Asp Thr Lys Val Asp Leu
145                 150                 155                 160
AGC AAT ATT GAC AAA GAG CTT AAT CAT CAA AAA AGT CAA GTT GAA GCA      528
Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln Val Glu Ala
                165                 170                 175
ATG GCA GAG CAA GCG GGA ATC ACA AAT GAA GAT AAA GAT TCT ATG CTG      576
Met Ala Glu Gln Ala Gly Ile Thr Asn Glu Asp Lys Asp Ser Met Leu
            180                 185                 190
AAA AAA ATC GAA GAT ATT CGT AAA CAA GCT CAA CAA GCA GAT AAA AAA      624
Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala Asp Lys Lys
        195                 200                 205
GAA GAT GCC GAA GTA AAG GTT CGT GAA GAA CTA GGT AAA CTC TTT AGT      672
Glu Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys Leu Phe Ser
    210                 215                 220
TCA ACT AAA GCT GGT CTG GAT CAA CAA ATT CAA GAG CAT GTG AAG AAA      720
Ser Thr Lys Ala Gly Leu Asp Gln Gln Ile Gln Glu His Val Lys Lys
225                 230                 235                 240
GAA ACG AGT AGT GAG GAA AAT ACT CAG AAA GTT GAT GAA CAC TAT GCT      768
Glu Thr Ser Ser Glu Glu Asn Thr Gln Lys Val Asp Glu His Tyr Ala
                245                 250                 255
AAT AGC CTT CAG AAC CTT GCT CAA AAA TCT CTT GAA GAA CTA GAT AAG      816
Asn Ser Leu Gln Asn Leu Ala Gln Lys Ser Leu Glu Glu Leu Asp Lys
            260                 265                 270
GCA ACT ACC AAT GAA CAA GCT ACA CAA GTT AAA AAT CAA TTC TTA GAA      864
Ala Thr Thr Asn Glu Gln Ala Thr Gln Val Lys Asn Gln Phe Leu Glu
        275                 280                 285
AAC GCT CAA AAG CTC AAA GAA ATA CAA CCT CTT ATC AAA GAA ACG AAT      912
Asn Ala Gln Lys Leu Lys Glu Ile Gln Pro Leu Ile Lys Glu Thr Asn
    290                 295                 300
GTG AAA TTG TAT AAG GCT ATG AGT GAG AGC TTG GAG CAG GTT GAG AAG      960
Val Lys Leu Tyr Lys Ala Met Ser Glu Ser Leu Glu Gln Val Glu Lys
305                 310                 315                 320
GAA TTA AAA CAT AAT TCG GAA GCT AAT TTA CAA GAT TTG GTT GCG AAA     1008
Glu Leu Lys His Asn Ser Glu Ala Asn Leu Gln Asp Leu Val Ala Lys
                325                 330                 335
TCT AAA GAA ATC GTA AGA GAA TAC GAA GGA AAA CTT AAT CAA TCT AAA     1056
Ser Lys Glu Ile Val Arg Glu Tyr Glu Gly Lys Leu Asn Gln Ser Lys
            340                 345                 350
AAT CTT CCA GAA TTA AAG CAA CTA GAA GAG GAA GCT CAT TCG AAG TTG     1104
Asn Leu Pro Glu Leu Lys Gln Leu Glu Glu Glu Ala His Ser Lys Leu
        355                 360                 365
AAA CAA GTT GTG GAG CAT TTT AGA AAA AAA TTT AAA ACG TCA GAG CAA     1152
Lys Gln Val Val Glu His Phe Arg Lys Lys Phe Lys Thr Ser Glu Gln
    370                 375                 380
GTG ACA CCA AAA AAA CGT GTC AAA CGA GAT TTA GCT GCT AAT GAA AAT     1200
Val Thr Pro Lys Lys Arg Val Lys Arg Asp Leu Ala Ala Asn Glu Asn
385                 390                 395                 400
AAT CAA CAA AAG ATT GAG TTA ACA GTT TCA CCA GAG AAT ATC ACT GTA     1248
Asn Gln Gln Lys Ile Glu Leu Thr Val Ser Pro Glu Asn Ile Thr Val
                405                 410                 415
TAT GAA GGT GAA GAC GTG AAA TTT ACA GTC ACA GCT AAA AGT GAT TCG     1296
Tyr Glu Gly Glu Asp Val Lys Phe Thr Val Thr Ala Lys Ser Asp Ser
            420                 425                 430
AAG ACG ACG TTG GAC TTC AGT GAT CTT TTA ACA AAA TAT AAT CCG TCT     1344
Lys Thr Thr Leu Asp Phe Ser Asp Leu Leu Thr Lys Tyr Asn Pro Ser
        435                 440                 445
GTA TCA GAT AGA ATT AGT ACA AAT TAT AAG ACT AAC ACG GAT AAT CAT     1392
Val Ser Asp Arg Ile Ser Thr Asn Tyr Lys Thr Asn Thr Asp Asn His
    450                 455                 460
AAG ATT GCC GAA ATC ACT ATC AAG AAT TTG AAG CTA AAT CAA AGT CAA     1440
Lys Ile Ala Glu Ile Thr Ile Lys Asn Leu Lys Leu Asn Gln Ser Gln
465                 470                 475                 480
ACA GTG ACT CTA AAA GCT AAA GAT GAT TCT GGC AAT GTA GTT GAA AAA     1488
Thr Val Thr Leu Lys Ala Lys Asp Asp Ser Gly Asn Val Val Glu Lys
                485                 490                 495
ACA TTC ACT ATT ACA GTC CAA AAG AAA GAG GAG AAA CAA GTT CCT AAA     1536
Thr Phe Thr Ile Thr Val Gln Lys Lys Glu Glu Lys Gln Val Pro Lys
            500                 505                 510
ACA CCA GAG CAG AAA CAT TCT AAA ACG GAA CAA AAC GTT CCT CAA GAA     1584
Thr Pro Glu Gln Lys His Ser Lys Thr Glu Gln Asn Val Pro Gln Glu
        515                 520                 525
CCA AAA TCA AAT GAC AAG AAT CAA TTA CAA GAG TTG ATT AAA TCA GCT     1632
Pro Lys Ser Asn Asp Lys Asn Gln Leu Gln Glu Leu Ile Lys Ser Ala
    530                 535                 540
CAA CAA GAA CTC GAA AAG TTA GAA AAA GCA ATA AAA GAA TTA ATG GAG     1680
Gln Gln Glu Leu Glu Lys Leu Glu Lys Ala Ile Lys Glu Leu Met Glu
545                 550                 555                 560
CAA CCA GAG ATT CCA TCC AAT CCA GAG TAT GGT ATT CAA AAA TCT ATT     1728
Gln Pro Glu Ile Pro Ser Asn Pro Glu Tyr Gly Ile Gln Lys Ser Ile
                565                 570                 575
TGG GAG TCA CAA AAA GAG CCT ATC CAG GAA GCC ATA ACA AGT TTT AAC     1776
Trp Glu Ser Gln Lys Glu Pro Ile Gln Glu Ala Ile Thr Ser Phe Asn
            580                 585                 590
AAG ATT ATT GGT GAT TCA TCT TCA AAA TAC TAC ACA GAG CAC TAT TTT     1824
Lys Ile Ile Gly Asp Ser Ser Ser Lys Tyr Tyr Thr Glu His Tyr Phe
        595                 600                 605
AAC AAA TAT AAA TCT CAT TTT ATG AAT TAT CAA CTT CAT GCA CAA ATG     1872
Asn Lys Tyr Lys Ser His Phe Met Asn Tyr Gln Leu His Ala Gln Met
    610                 615                 620
GAG ATC CTG ACT AGA AAA GTG GTT CAG TAT ATG AAC AAA TAT CCT GAT     1920
Glu Ile Leu Thr Arg Lys Val Val Gln Tyr Met Asn Lys Tyr Pro Asp
625                 630                 635                 640
AAT GCA GAA ATT AAA AAG ATA TTT GAG TCA GAT ATG AAG AGA ACG AAA     1968
Asn Ala Glu Ile Lys Lys Ile Phe Glu Ser Asp Met Lys Arg Thr Lys
                645                 650                 655
GAA GAT AAT TAC GGA AGT TTA GAA AAT GAT GCT TTG AAA GGC TAT TTT     2016
Glu Asp Asn Tyr Gly Ser Leu Glu Asn Asp Ala Leu Lys Gly Tyr Phe
            660                 665                 670
GAG AAA TAT TTC CTT ACA CCA TTT AAT AAA ATT AAG CAG ATT GTA GAT     2064
Glu Lys Tyr Phe Leu Thr Pro Phe Asn Lys Ile Lys Gln Ile Val Asp
        675                 680                 685
GAT TTG GAT AAA AAA GTA GAA CAA GAT CAG CCA GCA CCA ATT CCG GAA     2112
Asp Leu Asp Lys Lys Val Glu Gln Asp Gln Pro Ala Pro Ile Pro Glu
    690                 695                 700
AAT TCA GAA ATG GAT CAG GCT AAG GAA AAG GCT AAG ATT GCT GTA TCG     2160
Asn Ser Glu Met Asp Gln Ala Lys Glu Lys Ala Lys Ile Ala Val Ser
705                 710                 715                 720
AAG TAT ATG AGT AAG GTT TTA GAT GGA GTT CAT CAA CAT CTG CAG AAG     2208
Lys Tyr Met Ser Lys Val Leu Asp Gly Val His Gln His Leu Gln Lys
                725                 730                 735
AAA AAT CAC AGT AAA ATT GTT GAT CTT TTT AAG GAA CTT GAA GCG ATT     2256
Lys Asn His Ser Lys Ile Val Asp Leu Phe Lys Glu Leu Glu Ala Ile
            740                 745                 750
AAA CAA CAA ACT ATT TTT GAT ATT GAC AAT GCA AAG ACT GAA GTA GAG     2304
Lys Gln Gln Thr Ile Phe Asp Ile Asp Asn Ala Lys Thr Glu Val Glu
        755                 760                 765
ATT GAT AAC TTA GTA CAC GAT GCA TTC TCA AAA ATG AAT GCT ACT GTT     2352
Ile Asp Asn Leu Val His Asp Ala Phe Ser Lys Met Asn Ala Thr Val
    770                 775                 780
GCT AAA TTT CAA AAA GGT CTA GAG ACA AAT ACG CCA GAA ACT CCA GAT     2400
Ala Lys Phe Gln Lys Gly Leu Glu Thr Asn Thr Pro Glu Thr Pro Asp
785                 790                 795                 800
ACA CCG AAG ATT CCA GAG CTA CCT CAA GCC CCA GAT ACA CCG CAG GCT     2448
Thr Pro Lys Ile Pro Glu Leu Pro Gln Ala Pro Asp Thr Pro Gln Ala
                805                 810                 815
CCA GAC ACA CCG CAT GTT CCG GAA TCA CCA AAG GCC CCA GAA GCA CCG     2496
Pro Asp Thr Pro His Val Pro Glu Ser Pro Lys Ala Pro Glu Ala Pro
            820                 825                 830
CGT GTT CCG GAA TCA CCA AAC ACT CCA GAA GCA CCG CAT GTT CCG GAA     2544
Arg Val Pro Glu Ser Pro Asn Thr Pro Glu Ala Pro His Val Pro Glu
        835                 840                 845
TCA CCA AAG GCC CCA GAA CCA CCG CGT GTT CCG GAA TCA CCA AAC ACT     2592
Ser Pro Lys Ala Pro Glu Pro Pro Arg Val Pro Glu Ser Pro Asn Thr
    850                 855                 860
CCA GAA GCA CCG CAT GTT CCG GAA TCA CCA AAG ACT CCA GAA GCA CCA     2640
Pro Glu Ala Pro His Val Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro
865                 870                 875                 880
AAG ATT CCG GAA CCC CCT AAG ACT CCA GAC GTC CCT AAG CTT CCA GAC     2688
Lys Ile Pro Glu Pro Pro Lys Thr Pro Asp Val Pro Lys Leu Pro Asp
                885                 890                 895
GTC CCT AAG CTT CCA CAC GTC CCT AAG CTT CCA GAT GCA CCG AAG TTA     2736
Val Pro Lys Leu Pro His Val Pro Lys Leu Pro Asp Ala Pro Lys Leu
            900                 905                 910
CCA GAT GGG TTA AAT AAA GTT GGA CAA GCA GTA TTT ACA TCA ACT GAT     2784
Pro Asp Gly Leu Asn Lys Val Gly Gln Ala Val Phe Thr Ser Thr Asp
        915                 920                 925
GGA AAT ACT AAG GTT ACG GTT GTA TTT GAT AAA CCT ACA GAT GCT GAT     2832
Gly Asn Thr Lys Val Thr Val Val Phe Asp Lys Pro Thr Asp Ala Asp
    930                 935                 940
AAG TTA CAT CTC AAG GAA CTA ACG ACG AAA GAG TTG GCT GAT AAA ATT     2880
Lys Leu His Leu Lys Glu Leu Thr Thr Lys Glu Leu Ala Asp Lys Ile
945                 950                 955                 960
GCT CAT AAA ACA GGA GGA GGA ACA GTT CGT GTG TTT GAC TTA TCT CTT     2928
Ala His Lys Thr Gly Gly Gly Thr Val Arg Val Phe Asp Leu Ser Leu
                965                 970                 975
TCT AAA GGA GGC AAG GAA ACA CAT GTC AAT GGA GAA CGA ACT GTT CGG     2976
Ser Lys Gly Gly Lys Glu Thr His Val Asn Gly Glu Arg Thr Val Arg
            980                 985                 990
CTC GCG CTT GGG CAG ACT GGC TCA GAT GTT CAC GTC TAT CAC GTA AAG     3024
Leu Ala Leu Gly Gln Thr Gly Ser Asp Val His Val Tyr His Val Lys
        995                 1000                1005
GAA AAT GGC GAC CTT GAG CGT ATT CCT TCT AAA GTT GAA AAT GGG CAA     3072
Glu Asn Gly Asp Leu Glu Arg Ile Pro Ser Lys Val Glu Asn Gly Gln
    1010                1015                1020
GTT GTT TTT AAA ACG AAC CAC TTC AGT TTG TTT GCG ATT AAG ACA CTT     3120
Val Val Phe Lys Thr Asn His Phe Ser Leu Phe Ala Ile Lys Thr Leu
1025                1030                1035                1040
TCT AAG GAT CAA AAT GTT ACT CCA CCG AAG CAG ACT AAA CCT TCT ACC     3168
Ser Lys Asp Gln Asn Val Thr Pro Pro Lys Gln Thr Lys Pro Ser Thr
                1045                1050                1055
CAA GGC AGT CAA GTA GAG ATT GCA GAG AGT CAA ACT GGA AAA TTC CAG     3216
Gln Gly Ser Gln Val Glu Ile Ala Glu Ser Gln Thr Gly Lys Phe Gln
            1060                1065                1070
AGT AAA GCA GCT AAT CAT AAA GCA CTG GCT ACT GGA AAT GAA ACA GTG     3264
Ser Lys Ala Ala Asn His Lys Ala Leu Ala Thr Gly Asn Glu Thr Val
        1075                1080                1085
GCA AAA GGA AAT CCT ACA TCA ACA ACG GAA AAG AAA CTC GAG CAC CAC     3312
Ala Lys Gly Asn Pro Thr Ser Thr Thr Glu Lys Lys Leu Glu His His
    1090                1095                1100 
           
           
             
               1104 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               not provided 
             
              4
Glu Gly Asp Ile His Met Ser Glu Leu Val Lys Asp Asp Ser Val Lys
  1               5                  10                  15
Thr Thr Glu Val Ala Ala Lys Pro Tyr Pro Ser Met Ala Gln Thr Asp
             20                  25                  30
Gln Gly Asn Asn Ser Ser Ser Ser Glu Leu Glu Thr Thr Arg Met Glu
         35                  40                  45
Ile Pro Thr Thr His Ile Lys Lys Ala Val Glu Pro Val Glu Lys Thr
     50                  55                  60
Ala Gly Glu Thr Ser Ala Thr Asp Thr Gly Lys Arg Glu Lys Gln Leu
 65                  70                  75                  80
Gln Gln Trp Lys Asn Asn Leu Lys Asn Asp Val Asp Asn Thr Ile Leu
                 85                  90                  95
Ser His Glu Gln Lys Asn Glu Phe Lys Thr Lys Ile Asp Glu Thr Asn
            100                 105                 110
Asp Ser Asp Ala Leu Leu Glu Leu Glu Asn Gln Phe Asn Glu Thr Asn
        115                 120                 125
Arg Leu Leu His Ile Lys Gln His Glu Glu Val Glu Lys His Asn Lys
    130                 135                 140
Pro Asn Gln Gln Lys Thr Leu Lys Gln Ser Asp Thr Lys Val Asp Leu
145                 150                 155                 160
Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln Val Glu Ala
                165                 170                 175
Met Ala Glu Gln Ala Gly Ile Thr Asn Glu Asp Lys Asp Ser Met Leu
            180                 185                 190
Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala Asp Lys Lys
        195                 200                 205
Glu Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys Leu Phe Ser
    210                 215                 220
Ser Thr Lys Ala Gly Leu Asp Gln Gln Ile Gln Glu His Val Lys Lys
225                 230                 235                 240
Glu Thr Ser Ser Glu Glu Asn Thr Gln Lys Val Asp Glu His Tyr Ala
                245                 250                 255
Asn Ser Leu Gln Asn Leu Ala Gln Lys Ser Leu Glu Glu Leu Asp Lys
            260                 265                 270
Ala Thr Thr Asn Glu Gln Ala Thr Gln Val Lys Asn Gln Phe Leu Glu
        275                 280                 285
Asn Ala Gln Lys Leu Lys Glu Ile Gln Pro Leu Ile Lys Glu Thr Asn
    290                 295                 300
Val Lys Leu Tyr Lys Ala Met Ser Glu Ser Leu Glu Gln Val Glu Lys
305                 310                 315                 320
Glu Leu Lys His Asn Ser Glu Ala Asn Leu Gln Asp Leu Val Ala Lys
                325                 330                 335
Ser Lys Glu Ile Val Arg Glu Tyr Glu Gly Lys Leu Asn Gln Ser Lys
            340                 345                 350
Asn Leu Pro Glu Leu Lys Gln Leu Glu Glu Glu Ala His Ser Lys Leu
        355                 360                 365
Lys Gln Val Val Glu His Phe Arg Lys Lys Phe Lys Thr Ser Glu Gln
    370                 375                 380
Val Thr Pro Lys Lys Arg Val Lys Arg Asp Leu Ala Ala Asn Glu Asn
385                 390                 395                 400
Asn Gln Gln Lys Ile Glu Leu Thr Val Ser Pro Glu Asn Ile Thr Val
                405                 410                 415
Tyr Glu Gly Glu Asp Val Lys Phe Thr Val Thr Ala Lys Ser Asp Ser
            420                 425                 430
Lys Thr Thr Leu Asp Phe Ser Asp Leu Leu Thr Lys Tyr Asn Pro Ser
        435                 440                 445
Val Ser Asp Arg Ile Ser Thr Asn Tyr Lys Thr Asn Thr Asp Asn His
    450                 455                 460
Lys Ile Ala Glu Ile Thr Ile Lys Asn Leu Lys Leu Asn Gln Ser Gln
465                 470                 475                 480
Thr Val Thr Leu Lys Ala Lys Asp Asp Ser Gly Asn Val Val Glu Lys
                485                 490                 495
Thr Phe Thr Ile Thr Val Gln Lys Lys Glu Glu Lys Gln Val Pro Lys
            500                 505                 510
Thr Pro Glu Gln Lys His Ser Lys Thr Glu Gln Asn Val Pro Gln Glu
        515                 520                 525
Pro Lys Ser Asn Asp Lys Asn Gln Leu Gln Glu Leu Ile Lys Ser Ala
    530                 535                 540
Gln Gln Glu Leu Glu Lys Leu Glu Lys Ala Ile Lys Glu Leu Met Glu
545                 550                 555                 560
Gln Pro Glu Ile Pro Ser Asn Pro Glu Tyr Gly Ile Gln Lys Ser Ile
                565                 570                 575
Trp Glu Ser Gln Lys Glu Pro Ile Gln Glu Ala Ile Thr Ser Phe Asn
            580                 585                 590
Lys Ile Ile Gly Asp Ser Ser Ser Lys Tyr Tyr Thr Glu His Tyr Phe
        595                 600                 605
Asn Lys Tyr Lys Ser His Phe Met Asn Tyr Gln Leu His Ala Gln Met
    610                 615                 620
Glu Ile Leu Thr Arg Lys Val Val Gln Tyr Met Asn Lys Tyr Pro Asp
625                 630                 635                 640
Asn Ala Glu Ile Lys Lys Ile Phe Glu Ser Asp Met Lys Arg Thr Lys
                645                 650                 655
Glu Asp Asn Tyr Gly Ser Leu Glu Asn Asp Ala Leu Lys Gly Tyr Phe
            660                 665                 670
Glu Lys Tyr Phe Leu Thr Pro Phe Asn Lys Ile Lys Gln Ile Val Asp
        675                 680                 685
Asp Leu Asp Lys Lys Val Glu Gln Asp Gln Pro Ala Pro Ile Pro Glu
    690                 695                 700
Asn Ser Glu Met Asp Gln Ala Lys Glu Lys Ala Lys Ile Ala Val Ser
705                 710                 715                 720
Lys Tyr Met Ser Lys Val Leu Asp Gly Val His Gln His Leu Gln Lys
                725                 730                 735
Lys Asn His Ser Lys Ile Val Asp Leu Phe Lys Glu Leu Glu Ala Ile
            740                 745                 750
Lys Gln Gln Thr Ile Phe Asp Ile Asp Asn Ala Lys Thr Glu Val Glu
        755                 760                 765
Ile Asp Asn Leu Val His Asp Ala Phe Ser Lys Met Asn Ala Thr Val
    770                 775                 780
Ala Lys Phe Gln Lys Gly Leu Glu Thr Asn Thr Pro Glu Thr Pro Asp
785                 790                 795                 800
Thr Pro Lys Ile Pro Glu Leu Pro Gln Ala Pro Asp Thr Pro Gln Ala
                805                 810                 815
Pro Asp Thr Pro His Val Pro Glu Ser Pro Lys Ala Pro Glu Ala Pro
            820                 825                 830
Arg Val Pro Glu Ser Pro Asn Thr Pro Glu Ala Pro His Val Pro Glu
        835                 840                 845
Ser Pro Lys Ala Pro Glu Pro Pro Arg Val Pro Glu Ser Pro Asn Thr
    850                 855                 860
Pro Glu Ala Pro His Val Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro
865                 870                 875                 880
Lys Ile Pro Glu Pro Pro Lys Thr Pro Asp Val Pro Lys Leu Pro Asp
                885                 890                 895
Val Pro Lys Leu Pro His Val Pro Lys Leu Pro Asp Ala Pro Lys Leu
            900                 905                 910
Pro Asp Gly Leu Asn Lys Val Gly Gln Ala Val Phe Thr Ser Thr Asp
        915                 920                 925
Gly Asn Thr Lys Val Thr Val Val Phe Asp Lys Pro Thr Asp Ala Asp
    930                 935                 940
Lys Leu His Leu Lys Glu Leu Thr Thr Lys Glu Leu Ala Asp Lys Ile
945                 950                 955                 960
Ala His Lys Thr Gly Gly Gly Thr Val Arg Val Phe Asp Leu Ser Leu
                965                 970                 975
Ser Lys Gly Gly Lys Glu Thr His Val Asn Gly Glu Arg Thr Val Arg
            980                 985                 990
Leu Ala Leu Gly Gln Thr Gly Ser Asp Val His Val Tyr His Val Lys
        995                 1000                1005
Glu Asn Gly Asp Leu Glu Arg Ile Pro Ser Lys Val Glu Asn Gly Gln
    1010                1015                1020
Val Val Phe Lys Thr Asn His Phe Ser Leu Phe Ala Ile Lys Thr Leu
1025                1030                1035                1040
Ser Lys Asp Gln Asn Val Thr Pro Pro Lys Gln Thr Lys Pro Ser Thr
                1045                1050                1055
Gln Gly Ser Gln Val Glu Ile Ala Glu Ser Gln Thr Gly Lys Phe Gln
            1060                1065                1070
Ser Lys Ala Ala Asn His Lys Ala Leu Ala Thr Gly Asn Glu Thr Val
        1075                1080                1085
Ala Lys Gly Asn Pro Thr Ser Thr Thr Glu Lys Lys Leu Glu His His
    1090                1095                1100 
           
           
             
               3384 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA 
             
             
               not provided 
             
             
               CDS 
                1..3384 
             
              5
ATG AGT GAG CTT GTA AAG GAC GAT AGT GTG AAG ACT ACC GAG GTT GCA       48
Met Ser Glu Leu Val Lys Asp Asp Ser Val Lys Thr Thr Glu Val Ala
  1               5                  10                  15
GCT AAG CCC TAT CCA AGT ATG GCT CAA ACA GAT CAA GGA AAT AAT TCA       96
Ala Lys Pro Tyr Pro Ser Met Ala Gln Thr Asp Gln Gly Asn Asn Ser
             20                  25                  30
TCA TCC TCG GAA CTT GAG ACA ACA AGG ATG GAA ATT CCT ACA ACA GAC      144
Ser Ser Ser Glu Leu Glu Thr Thr Arg Met Glu Ile Pro Thr Thr Asp
         35                  40                  45
ATA AAA AAA GCT GTT GAA CCG GTC GAG AAA ACA GCT GGG GAA ACA TCT      192
Ile Lys Lys Ala Val Glu Pro Val Glu Lys Thr Ala Gly Glu Thr Ser
     50                  55                  60
GCC ACT GAT ACT GGA AAA CGA GAG AAA CAA TTA CAA CAA TGG AAA AAT      240
Ala Thr Asp Thr Gly Lys Arg Glu Lys Gln Leu Gln Gln Trp Lys Asn
 65                  70                  75                  80
AAT CTA AAA AAT GAT GTG GAT AAC ACA ATT CTA TCT CAT GAA CAG AAA      288
Asn Leu Lys Asn Asp Val Asp Asn Thr Ile Leu Ser His Glu Gln Lys
                 85                  90                  95
AAT GAG TTT AAA ACA AAA ATT GAT GAA ACA AAT GAT TCT GAT GCA TTA      336
Asn Glu Phe Lys Thr Lys Ile Asp Glu Thr Asn Asp Ser Asp Ala Leu
            100                 105                 110
TTA GAA TTA GAA AAT CAA TTT AAC GAA ACT AAT AGA CTG TTA CAC ATC      384
Leu Glu Leu Glu Asn Gln Phe Asn Glu Thr Asn Arg Leu Leu His Ile
        115                 120                 125
AAA CAA CAT GAA GAA GTT GAG AAA GAT AAG AAA GCT AAG CAA CAG AAA      432
Lys Gln His Glu Glu Val Glu Lys Asp Lys Lys Ala Lys Gln Gln Lys
    130                 135                 140
ACT CTG AAA CAG TCA GAT ACG AAA GTA GAT CTA AGC AAT ATT GAC AAA      480
Thr Leu Lys Gln Ser Asp Thr Lys Val Asp Leu Ser Asn Ile Asp Lys
145                 150                 155                 160
GAG CTT AAT CAT CAA AAA AGT CCA GTT GAA AAA ATG GCA GAG CCA AAG      528
Glu Leu Asn His Gln Lys Ser Pro Val Glu Lys Met Ala Glu Pro Lys
                165                 170                 175
GGA ATC ACA AAT GAA GAT AAA GAT TCT ATG CTG AAA AAA ATC GAA GAT      576
Gly Ile Thr Asn Glu Asp Lys Asp Ser Met Leu Lys Lys Ile Glu Asp
            180                 185                 190
ATT CGT AAA CAA GCT CAA CAA GCA GAT AAA AAA GAA GAT GCC GAA GTA      624
Ile Arg Lys Gln Ala Gln Gln Ala Asp Lys Lys Glu Asp Ala Glu Val
        195                 200                 205
AAG GTT CGT GAA GAA CTA GGT AAA CTC TTT AGT TCA ACT AAA GCT GGT      672
Lys Val Arg Glu Glu Leu Gly Lys Leu Phe Ser Ser Thr Lys Ala Gly
    210                 215                 220
CTG GAT CAA GAA ATT CAT GAG CAT GTG AAG AAA GAA ACG AGT AGT GAG      720
Leu Asp Gln Glu Ile His Glu His Val Lys Lys Glu Thr Ser Ser Glu
225                 230                 235                 240
GAA AAT ACT CAG AAA GTT GAT GAA CAC TAT GCT AAT AGC CTT CAG AAC      768
Glu Asn Thr Gln Lys Val Asp Glu His Tyr Ala Asn Ser Leu Gln Asn
                245                 250                 255
CTT GCT CAA AAA TCT CTT GAA GAA CTA GAT AAG GCA ACT ACC AAT GAA      816
Leu Ala Gln Lys Ser Leu Glu Glu Leu Asp Lys Ala Thr Thr Asn Glu
            260                 265                 270
CAA GCT ACA CAA GTT AAA AAT CAA TTC TTA GAA AAC GCT CAA AAG CTC      864
Gln Ala Thr Gln Val Lys Asn Gln Phe Leu Glu Asn Ala Gln Lys Leu
        275                 280                 285
AAA GAA ATG CAA CCT CTT ATC AAA GAA ACG AAT GTG AAA TTG TAT AAG      912
Lys Glu Met Gln Pro Leu Ile Lys Glu Thr Asn Val Lys Leu Tyr Lys
    290                 295                 300
GCT ATG AGT GAG AGC TTG GAG CAG GTT GAG AAG GAA TTA AAA CAT AAT      960
Ala Met Ser Glu Ser Leu Glu Gln Val Glu Lys Glu Leu Lys His Asn
305                 310                 315                 320
TCG GAA GCT AAT TTA GAA GAT TTG GTT GCG AAA TCT AAA GAA ATC GTA     1008
Ser Glu Ala Asn Leu Glu Asp Leu Val Ala Lys Ser Lys Glu Ile Val
                325                 330                 335
AGA GAA TAC GAA GGA AAA CTT AAT CAA TCT AAA AAT CTT CCA GAA TTA     1056
Arg Glu Tyr Glu Gly Lys Leu Asn Gln Ser Lys Asn Leu Pro Glu Leu
            340                 345                 350
AAG CAA CTA GAA GAG GAA GCT CAT TCG AAG TTG AAA CAA GTT GTG GAG     1104
Lys Gln Leu Glu Glu Glu Ala His Ser Lys Leu Lys Gln Val Val Glu
        355                 360                 365
GAT TTT AGA AAA AAA TTT AAA ACG TCA GAG CAA GTG ACA CCA AAA AAA     1152
Asp Phe Arg Lys Lys Phe Lys Thr Ser Glu Gln Val Thr Pro Lys Lys
    370                 375                 380
CGT GTC AAA CGA GAT TTA GCT GCT AAT GAA AAT AAT CAA CAA AAG ATT     1200
Arg Val Lys Arg Asp Leu Ala Ala Asn Glu Asn Asn Gln Gln Lys Ile
385                 390                 395                 400
GAG TTA ACA GTT TCA CCA GAG AAT ATC ACT GTA TAT GAA GGT GAA GAC     1248
Glu Leu Thr Val Ser Pro Glu Asn Ile Thr Val Tyr Glu Gly Glu Asp
                405                 410                 415
GTG AAA TTT ACA GTC ACA GCT AAA AGT GAT TCG AAG ACG ACG TTG GAC     1296
Val Lys Phe Thr Val Thr Ala Lys Ser Asp Ser Lys Thr Thr Leu Asp
            420                 425                 430
TTC AGT GAT CTT TTA ACA AAA TAT AAT CCG TCT GTA TCA GAT AGA ATT     1344
Phe Ser Asp Leu Leu Thr Lys Tyr Asn Pro Ser Val Ser Asp Arg Ile
        435                 440                 445
AGT ACA AAT TAT AAG ACT AAC ACG GAT AAT CAT AAG ATT GCC GAA ATC     1392
Ser Thr Asn Tyr Lys Thr Asn Thr Asp Asn His Lys Ile Ala Glu Ile
    450                 455                 460
ACT ATC AAG AAT TTG AAG CTA AAT GAA AGT CAA ACA GTG ACT CTA AAA     1440
Thr Ile Lys Asn Leu Lys Leu Asn Glu Ser Gln Thr Val Thr Leu Lys
465                 470                 475                 480
GCT AAA GAT GAT TCT GGC AAT GTA GTT GAA AAA ACA TTC ACT ATT ACA     1488
Ala Lys Asp Asp Ser Gly Asn Val Val Glu Lys Thr Phe Thr Ile Thr
                485                 490                 495
GTG CAA AAG AAA GAG GAG AAA CAA GTT CCT AAA ACA CCA GAG CAG AAA     1536
Val Gln Lys Lys Glu Glu Lys Gln Val Pro Lys Thr Pro Glu Gln Lys
            500                 505                 510
GAT TCT AAA ACG GAA GAA AAG GTT CCT CAA GAA CCA AAA TCA AAT GAC     1584
Asp Ser Lys Thr Glu Glu Lys Val Pro Gln Glu Pro Lys Ser Asn Asp
        515                 520                 525
AAG AAT CAA TTA CAA GAG TTG ATT AAA TCA GCT CAA CAA GAA CTG GAA     1632
Lys Asn Gln Leu Gln Glu Leu Ile Lys Ser Ala Gln Gln Glu Leu Glu
    530                 535                 540
AAG TTA GAA AAA GCA ATA AAA GAA TTA ATG GAG CAA CCA GAG ATT CCA     1680
Lys Leu Glu Lys Ala Ile Lys Glu Leu Met Glu Gln Pro Glu Ile Pro
545                 550                 555                 560
TCC AAT CCA GAG TAT GGT ATT CAA AAA TCT ATT TGG GAG TCA CAA AAA     1728
Ser Asn Pro Glu Tyr Gly Ile Gln Lys Ser Ile Trp Glu Ser Gln Lys
                565                 570                 575
GAG CCT ATC CAG GAA GCC ATA ACA AGT TTT AAG AAG ATT ATT GGT GAT     1776
Glu Pro Ile Gln Glu Ala Ile Thr Ser Phe Lys Lys Ile Ile Gly Asp
            580                 585                 590
TCA TCT TCA AAA TAC TAC ACA GAG CAC TAT TTT AAC AAA TAT AAA TCT     1824
Ser Ser Ser Lys Tyr Tyr Thr Glu His Tyr Phe Asn Lys Tyr Lys Ser
        595                 600                 605
GAT TTT ATG AAT TAT CAA CTT CAT GCA CAA ATG GAG ATG CTG ACT AGA     1872
Asp Phe Met Asn Tyr Gln Leu His Ala Gln Met Glu Met Leu Thr Arg
    610                 615                 620
AAA GTG GTT CAG TAT ATG AAC AAA TAT CCT GAT AAT GCA GAA ATT AAA     1920
Lys Val Val Gln Tyr Met Asn Lys Tyr Pro Asp Asn Ala Glu Ile Lys
625                 630                 635                 640
AAG ATA TTT GAG TCA GAT ATG AAG AGA ACG AAA GAA GAT AAT TAC GGA     1968
Lys Ile Phe Glu Ser Asp Met Lys Arg Thr Lys Glu Asp Asn Tyr Gly
                645                 650                 655
AGT TTA GAA AAT GAT GCT TTG AAA GGC TAT TTT GAG AAA TAT TTC CTT     2016
Ser Leu Glu Asn Asp Ala Leu Lys Gly Tyr Phe Glu Lys Tyr Phe Leu
            660                 665                 670
ACA CCA TTT AAT AAA ATT AAG CAG ATT GTA GAT GAT TTG GAT AAA AAA     2064
Thr Pro Phe Asn Lys Ile Lys Gln Ile Val Asp Asp Leu Asp Lys Lys
        675                 680                 685
GTA GAA CAA GAT CAG CCA GCA CCA ATT CCG GAA AAT TCA GAA ATG GAT     2112
Val Glu Gln Asp Gln Pro Ala Pro Ile Pro Glu Asn Ser Glu Met Asp
    690                 695                 700
CAG GCT AAG GAA AAG GCT AAG ATT GCT GTA TCG AAG TAT ATG AGT AAG     2160
Gln Ala Lys Glu Lys Ala Lys Ile Ala Val Ser Lys Tyr Met Ser Lys
705                 710                 715                 720
GTT TTA GAT GGA GTT CAT CAA CAT CTG CAG AAG AAA AAT CAC AGT AAA     2208
Val Leu Asp Gly Val His Gln His Leu Gln Lys Lys Asn His Ser Lys
                725                 730                 735
ATT GTT GAT CTT TTT AAG GAA CTT GAA GCG ATT AAA CAA CAA ACT ATT     2256
Ile Val Asp Leu Phe Lys Glu Leu Glu Ala Ile Lys Gln Gln Thr Ile
            740                 745                 750
TTT GAT ATT GAC AAT GCA AAG ACT GAA GTA GAG ATT GAT AAC TTA GTA     2304
Phe Asp Ile Asp Asn Ala Lys Thr Glu Val Glu Ile Asp Asn Leu Val
        755                 760                 765
CAC GAT GCA TTC TCA AAA ATG AAT GCT ACT GTT GCT AAA TTT CAA AAA     2352
His Asp Ala Phe Ser Lys Met Asn Ala Thr Val Ala Lys Phe Gln Lys
    770                 775                 780
GGT CTA GAG ACA AAT ACG CCA GAA ACT CCA GAT ACA CCG AAG ATT CCA     2400
Gly Leu Glu Thr Asn Thr Pro Glu Thr Pro Asp Thr Pro Lys Ile Pro
785                 790                 795                 800
GAG CTA CCT CAA GCC CCA GAT ACA CCG CAG GCT CCA GAC ACA CCG CAT     2448
Glu Leu Pro Gln Ala Pro Asp Thr Pro Gln Ala Pro Asp Thr Pro His
                805                 810                 815
GTT CCG GAA TCA CCA AAG GCC CCA GAA GCA CCG CGT GTT CCG GAA TCA     2496
Val Pro Glu Ser Pro Lys Ala Pro Glu Ala Pro Arg Val Pro Glu Ser
            820                 825                 830
CCA AAG ACT CCA GAA GCA CCG CAT GTT CCG GAA TCA CCA AAG GCC CCA     2544
Pro Lys Thr Pro Glu Ala Pro His Val Pro Glu Ser Pro Lys Ala Pro
        835                 840                 845
GAA GCA CCG CGT GTT CCG GAA TCA CCA AAG ACT CCA GAA GCA CCG CAT     2592
Glu Ala Pro Arg Val Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro His
    850                 855                 860
GTT CCG GAA TCA CCA AAG ACT CCA GAA GCA CCA AAG ATT CCG GAA CCC     2640
Val Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro Lys Ile Pro Glu Pro
865                 870                 875                 880
CCT AAG ACT CCG GAC GTC CCT AAG CTT CCA GAC GTC CCT AAG CTT CCA     2688
Pro Lys Thr Pro Asp Val Pro Lys Leu Pro Asp Val Pro Lys Leu Pro
                885                 890                 895
GAC GTC CCT AAG CTT CCA GAT GCA CCG AAG TTA CCA GAT GGG TTA AAT     2736
Asp Val Pro Lys Leu Pro Asp Ala Pro Lys Leu Pro Asp Gly Leu Asn
            900                 905                 910
AAA GTT GGA CAA GCA GTA TTT ACA TCA ACT GAT GGA AAT ACT AAG GTT     2784
Lys Val Gly Gln Ala Val Phe Thr Ser Thr Asp Gly Asn Thr Lys Val
        915                 920                 925
ACG GTT GTA TTT GAT AAA CCT ACA GAT GCT GAT AAG TTA CAT CTC AAG     2832
Thr Val Val Phe Asp Lys Pro Thr Asp Ala Asp Lys Leu His Leu Lys
    930                 935                 940
GAA GTA ACG ACG AAA GAG TTG GCT GAT AAA ATT GCT CAT AAA ACA GGA     2880
Glu Val Thr Thr Lys Glu Leu Ala Asp Lys Ile Ala His Lys Thr Gly
945                 950                 955                 960
GGA GGA ACA GTT CGT GTG TTT GAC TTA TCT CTT TCT AAA GGA GGC AAG     2928
Gly Gly Thr Val Arg Val Phe Asp Leu Ser Leu Ser Lys Gly Gly Lys
                965                 970                 975
GAA ACA CAT GTC AAT GGA GAA CGA ACT GTT CGG CTC GCG CTT GGG CAG     2976
Glu Thr His Val Asn Gly Glu Arg Thr Val Arg Leu Ala Leu Gly Gln
            980                 985                 990
ACT GGC TCA GAT GTT CAC GTC TAT CAC GTA AAG GAA AAT GGC GAC CTT     3024
Thr Gly Ser Asp Val His Val Tyr His Val Lys Glu Asn Gly Asp Leu
        995                 1000                1005
GAG CGT ATT CCT TCT AAA GTT GAA AAT GGG CAA GTT GTT TTT AAA ACG     3072
Glu Arg Ile Pro Ser Lys Val Glu Asn Gly Gln Val Val Phe Lys Thr
    1010                1015                1020
AAC CAC TTC AGT TTG TTT GCG ATT AAG ACA CTT TCT AAG GAT CAA AAT     3120
Asn His Phe Ser Leu Phe Ala Ile Lys Thr Leu Ser Lys Asp Gln Asn
1025                1030                1035                1040
GTT ACT CCA CCG AAG CAG ACT AAA CCT TCT ACC CAA GGC AGT CAA GTA     3168
Val Thr Pro Pro Lys Gln Thr Lys Pro Ser Thr Gln Gly Ser Gln Val
                1045                1050                1055
GAG ATT GCA GAG AGT CAA ACT GGA AAA TTC CAG AGT AAA GCA GCT AAT     3216
Glu Ile Ala Glu Ser Gln Thr Gly Lys Phe Gln Ser Lys Ala Ala Asn
            1060                1065                1070
CAT AAA GCA CTG GCT ACT GGA AAT GAA ACA GTG GCA AAA GGA AAT CCT     3264
His Lys Ala Leu Ala Thr Gly Asn Glu Thr Val Ala Lys Gly Asn Pro
        1075                1080                1085
ACA TCA ACA ACG GAA AAG AAA TTG CCA TAT ACA GGA GTG GCA TCT AAT     3312
Thr Ser Thr Thr Glu Lys Lys Leu Pro Tyr Thr Gly Val Ala Ser Asn
    1090                1095                1100
CTA GTT CTT GAA ATT ATG GGT CTC CTT GGT TTG ATT GGA ACT TCA TTC     3360
Leu Val Leu Glu Ile Met Gly Leu Leu Gly Leu Ile Gly Thr Ser Phe
1105                1110                1115                1120
ATC GCA ATG AAA AGA AGA AAA TCA                                     3384
Ile Ala Met Lys Arg Arg Lys Ser
                1125 
           
           
             
               1128 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               not provided 
             
              6
Met Ser Glu Leu Val Lys Asp Asp Ser Val Lys Thr Thr Glu Val Ala
  1               5                  10                  15
Ala Lys Pro Tyr Pro Ser Met Ala Gln Thr Asp Gln Gly Asn Asn Ser
             20                  25                  30
Ser Ser Ser Glu Leu Glu Thr Thr Arg Met Glu Ile Pro Thr Thr Asp
         35                  40                  45
Ile Lys Lys Ala Val Glu Pro Val Glu Lys Thr Ala Gly Glu Thr Ser
     50                  55                  60
Ala Thr Asp Thr Gly Lys Arg Glu Lys Gln Leu Gln Gln Trp Lys Asn
 65                  70                  75                  80
Asn Leu Lys Asn Asp Val Asp Asn Thr Ile Leu Ser His Glu Gln Lys
                 85                  90                  95
Asn Glu Phe Lys Thr Lys Ile Asp Glu Thr Asn Asp Ser Asp Ala Leu
            100                 105                 110
Leu Glu Leu Glu Asn Gln Phe Asn Glu Thr Asn Arg Leu Leu His Ile
        115                 120                 125
Lys Gln His Glu Glu Val Glu Lys Asp Lys Lys Ala Lys Gln Gln Lys
    130                 135                 140
Thr Leu Lys Gln Ser Asp Thr Lys Val Asp Leu Ser Asn Ile Asp Lys
145                 150                 155                 160
Glu Leu Asn His Gln Lys Ser Pro Val Glu Lys Met Ala Glu Pro Lys
                165                 170                 175
Gly Ile Thr Asn Glu Asp Lys Asp Ser Met Leu Lys Lys Ile Glu Asp
            180                 185                 190
Ile Arg Lys Gln Ala Gln Gln Ala Asp Lys Lys Glu Asp Ala Glu Val
        195                 200                 205
Lys Val Arg Glu Glu Leu Gly Lys Leu Phe Ser Ser Thr Lys Ala Gly
    210                 215                 220
Leu Asp Gln Glu Ile His Glu His Val Lys Lys Glu Thr Ser Ser Glu
225                 230                 235                 240
Glu Asn Thr Gln Lys Val Asp Glu His Tyr Ala Asn Ser Leu Gln Asn
                245                 250                 255
Leu Ala Gln Lys Ser Leu Glu Glu Leu Asp Lys Ala Thr Thr Asn Glu
            260                 265                 270
Gln Ala Thr Gln Val Lys Asn Gln Phe Leu Glu Asn Ala Gln Lys Leu
        275                 280                 285
Lys Glu Met Gln Pro Leu Ile Lys Glu Thr Asn Val Lys Leu Tyr Lys
    290                 295                 300
Ala Met Ser Glu Ser Leu Glu Gln Val Glu Lys Glu Leu Lys His Asn
305                 310                 315                 320
Ser Glu Ala Asn Leu Glu Asp Leu Val Ala Lys Ser Lys Glu Ile Val
                325                 330                 335
Arg Glu Tyr Glu Gly Lys Leu Asn Gln Ser Lys Asn Leu Pro Glu Leu
            340                 345                 350
Lys Gln Leu Glu Glu Glu Ala His Ser Lys Leu Lys Gln Val Val Glu
        355                 360                 365
Asp Phe Arg Lys Lys Phe Lys Thr Ser Glu Gln Val Thr Pro Lys Lys
    370                 375                 380
Arg Val Lys Arg Asp Leu Ala Ala Asn Glu Asn Asn Gln Gln Lys Ile
385                 390                 395                 400
Glu Leu Thr Val Ser Pro Glu Asn Ile Thr Val Tyr Glu Gly Glu Asp
                405                 410                 415
Val Lys Phe Thr Val Thr Ala Lys Ser Asp Ser Lys Thr Thr Leu Asp
            420                 425                 430
Phe Ser Asp Leu Leu Thr Lys Tyr Asn Pro Ser Val Ser Asp Arg Ile
        435                 440                 445
Ser Thr Asn Tyr Lys Thr Asn Thr Asp Asn His Lys Ile Ala Glu Ile
    450                 455                 460
Thr Ile Lys Asn Leu Lys Leu Asn Glu Ser Gln Thr Val Thr Leu Lys
465                 470                 475                 480
Ala Lys Asp Asp Ser Gly Asn Val Val Glu Lys Thr Phe Thr Ile Thr
                485                 490                 495
Val Gln Lys Lys Glu Glu Lys Gln Val Pro Lys Thr Pro Glu Gln Lys
            500                 505                 510
Asp Ser Lys Thr Glu Glu Lys Val Pro Gln Glu Pro Lys Ser Asn Asp
        515                 520                 525
Lys Asn Gln Leu Gln Glu Leu Ile Lys Ser Ala Gln Gln Glu Leu Glu
    530                 535                 540
Lys Leu Glu Lys Ala Ile Lys Glu Leu Met Glu Gln Pro Glu Ile Pro
545                 550                 555                 560
Ser Asn Pro Glu Tyr Gly Ile Gln Lys Ser Ile Trp Glu Ser Gln Lys
                565                 570                 575
Glu Pro Ile Gln Glu Ala Ile Thr Ser Phe Lys Lys Ile Ile Gly Asp
            580                 585                 590
Ser Ser Ser Lys Tyr Tyr Thr Glu His Tyr Phe Asn Lys Tyr Lys Ser
        595                 600                 605
Asp Phe Met Asn Tyr Gln Leu His Ala Gln Met Glu Met Leu Thr Arg
    610                 615                 620
Lys Val Val Gln Tyr Met Asn Lys Tyr Pro Asp Asn Ala Glu Ile Lys
625                 630                 635                 640
Lys Ile Phe Glu Ser Asp Met Lys Arg Thr Lys Glu Asp Asn Tyr Gly
                645                 650                 655
Ser Leu Glu Asn Asp Ala Leu Lys Gly Tyr Phe Glu Lys Tyr Phe Leu
            660                 665                 670
Thr Pro Phe Asn Lys Ile Lys Gln Ile Val Asp Asp Leu Asp Lys Lys
        675                 680                 685
Val Glu Gln Asp Gln Pro Ala Pro Ile Pro Glu Asn Ser Glu Met Asp
    690                 695                 700
Gln Ala Lys Glu Lys Ala Lys Ile Ala Val Ser Lys Tyr Met Ser Lys
705                 710                 715                 720
Val Leu Asp Gly Val His Gln His Leu Gln Lys Lys Asn His Ser Lys
                725                 730                 735
Ile Val Asp Leu Phe Lys Glu Leu Glu Ala Ile Lys Gln Gln Thr Ile
            740                 745                 750
Phe Asp Ile Asp Asn Ala Lys Thr Glu Val Glu Ile Asp Asn Leu Val
        755                 760                 765
His Asp Ala Phe Ser Lys Met Asn Ala Thr Val Ala Lys Phe Gln Lys
    770                 775                 780
Gly Leu Glu Thr Asn Thr Pro Glu Thr Pro Asp Thr Pro Lys Ile Pro
785                 790                 795                 800
Glu Leu Pro Gln Ala Pro Asp Thr Pro Gln Ala Pro Asp Thr Pro His
                805                 810                 815
Val Pro Glu Ser Pro Lys Ala Pro Glu Ala Pro Arg Val Pro Glu Ser
            820                 825                 830
Pro Lys Thr Pro Glu Ala Pro His Val Pro Glu Ser Pro Lys Ala Pro
        835                 840                 845
Glu Ala Pro Arg Val Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro His
    850                 855                 860
Val Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro Lys Ile Pro Glu Pro
865                 870                 875                 880
Pro Lys Thr Pro Asp Val Pro Lys Leu Pro Asp Val Pro Lys Leu Pro
                885                 890                 895
Asp Val Pro Lys Leu Pro Asp Ala Pro Lys Leu Pro Asp Gly Leu Asn
            900                 905                 910
Lys Val Gly Gln Ala Val Phe Thr Ser Thr Asp Gly Asn Thr Lys Val
        915                 920                 925
Thr Val Val Phe Asp Lys Pro Thr Asp Ala Asp Lys Leu His Leu Lys
    930                 935                 940
Glu Val Thr Thr Lys Glu Leu Ala Asp Lys Ile Ala His Lys Thr Gly
945                 950                 955                 960
Gly Gly Thr Val Arg Val Phe Asp Leu Ser Leu Ser Lys Gly Gly Lys
                965                 970                 975
Glu Thr His Val Asn Gly Glu Arg Thr Val Arg Leu Ala Leu Gly Gln
            980                 985                 990
Thr Gly Ser Asp Val His Val Tyr His Val Lys Glu Asn Gly Asp Leu
        995                 1000                1005
Glu Arg Ile Pro Ser Lys Val Glu Asn Gly Gln Val Val Phe Lys Thr
    1010                1015                1020
Asn His Phe Ser Leu Phe Ala Ile Lys Thr Leu Ser Lys Asp Gln Asn
1025                1030                1035                1040
Val Thr Pro Pro Lys Gln Thr Lys Pro Ser Thr Gln Gly Ser Gln Val
                1045                1050                1055
Glu Ile Ala Glu Ser Gln Thr Gly Lys Phe Gln Ser Lys Ala Ala Asn
            1060                1065                1070
His Lys Ala Leu Ala Thr Gly Asn Glu Thr Val Ala Lys Gly Asn Pro
        1075                1080                1085
Thr Ser Thr Thr Glu Lys Lys Leu Pro Tyr Thr Gly Val Ala Ser Asn
    1090                1095                1100
Leu Val Leu Glu Ile Met Gly Leu Leu Gly Leu Ile Gly Thr Ser Phe
1105                1110                1115                1120
Ile Ala Met Lys Arg Arg Lys Ser
                1125 
           
           
             
               3294 base pairs 
               nucleic acid 
               double 
               linear 
             
             
               cDNA 
             
             
               not provided 
             
             
               CDS 
                1..3294 
             
              7
GAA GGA GAT ATA CAT ATG AGT GAG CTT GTA AAG GAC GAT AGT GTG AAG       48
Glu Gly Asp Ile His Met Ser Glu Leu Val Lys Asp Asp Ser Val Lys
  1               5                  10                  15
ACT ACC GAG GTT GCA GCT AAG CCC TAT CCA AGT ATG GCT CAA ACA GAT       96
Thr Thr Glu Val Ala Ala Lys Pro Tyr Pro Ser Met Ala Gln Thr Asp
             20                  25                  30
CAA GGA AAT AAT TCA TCA TCC TCG GAA CTT GAG ACA ACA AGG ATG GAA      144
Gln Gly Asn Asn Ser Ser Ser Ser Glu Leu Glu Thr Thr Arg Met Glu
         35                  40                  45
ATT CCT ACA ACA GAC ATA AAA AAA GCT GTT GAA CCG GTC GAG AAA ACA      192
Ile Pro Thr Thr Asp Ile Lys Lys Ala Val Glu Pro Val Glu Lys Thr
     50                  55                  60
GCT GGG GAA ACA TCT GCC ACT CAT ACT GGA AAA CGA GAG AAA CAA TTA      240
Ala Gly Glu Thr Ser Ala Thr His Thr Gly Lys Arg Glu Lys Gln Leu
 65                  70                  75                  80
CAA CAA TGG AAA AAT AAT CTA AAA AAT GAT GTG GAT AAC ACA ATT CTA      288
Gln Gln Trp Lys Asn Asn Leu Lys Asn Asp Val Asp Asn Thr Ile Leu
                 85                  90                  95
TCT CAT GAA CAG AAA AAT GAG TTT AAA ACA AAA ATT GAT GAA ACA AAT      336
Ser His Glu Gln Lys Asn Glu Phe Lys Thr Lys Ile Asp Glu Thr Asn
            100                 105                 110
GAT TCT GAT GCA TTA TTA GAA TTA GAA AAT CAA TTT AAC GAA ACT AAT      384
Asp Ser Asp Ala Leu Leu Glu Leu Glu Asn Gln Phe Asn Glu Thr Asn
        115                 120                 125
AGA CTG TTA CAC ATC AAA CAA CAT GAA GAA GTT GAG AAA GAT AAG AAA      432
Arg Leu Leu His Ile Lys Gln His Glu Glu Val Glu Lys Asp Lys Lys
    130                 135                 140
GCT AAG CAA CAG AAA ACT CTG AAA CAG TCA GAT ACG AAA GTA GAT CTA      480
Ala Lys Gln Gln Lys Thr Leu Lys Gln Ser Asp Thr Lys Val Asp Leu
145                 150                 155                 160
AGC AAT ATT GAC AAA GAG CTT AAT CAT CAA AAA AGT CAA GAA GCG GGA      528
Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln Glu Ala Gly
                165                 170                 175
ATC ACA AAT GAA GAT AAA GAT TCT ATG CTG AAA AAA ATC GAA GAT ATT      576
Ile Thr Asn Glu Asp Lys Asp Ser Met Leu Lys Lys Ile Glu Asp Ile
            180                 185                 190
CGT AAA CAA GCT CAA CAA CCA GAT AAA AAA GAA GAT GCC GAA GTA AAG      624
Arg Lys Gln Ala Gln Gln Pro Asp Lys Lys Glu Asp Ala Glu Val Lys
        195                 200                 205
GTT CGT GAA GAA CTA GGT AAA CTC TTT AGT TCA ACT AAA GCT GGT CTG      672
Val Arg Glu Glu Leu Gly Lys Leu Phe Ser Ser Thr Lys Ala Gly Leu
    210                 215                 220
GAT CAA GAA ATT CAA GAG CAT GTG AAG AAA GAA ACG AGT AGT GAG GAA      720
Asp Gln Glu Ile Gln Glu His Val Lys Lys Glu Thr Ser Ser Glu Glu
225                 230                 235                 240
AAT ACT CAG AAA GTT GAT GAA CAC TAT GCT AAT AGC CTT CAG AAC CTT      768
Asn Thr Gln Lys Val Asp Glu His Tyr Ala Asn Ser Leu Gln Asn Leu
                245                 250                 255
GCT CAA AAA TCT CTT GAA GAA CTA GAT AAG GCA ACT ACC AAT GAA CAA      816
Ala Gln Lys Ser Leu Glu Glu Leu Asp Lys Ala Thr Thr Asn Glu Gln
            260                 265                 270
GCT ACA CAA GTT AAA AAT CAA TTC TTA GAA AAC GCT CAA AAG CTC AAA      864
Ala Thr Gln Val Lys Asn Gln Phe Leu Glu Asn Ala Gln Lys Leu Lys
        275                 280                 285
GAA ATA CAA CCT CTT ATC AAA GAA ACG AAT GTG AAA TTG TAT AAG GCT      912
Glu Ile Gln Pro Leu Ile Lys Glu Thr Asn Val Lys Leu Tyr Lys Ala
    290                 295                 300
ATG AGT GAG AGC TTG GAG CAG GTT GAG AAG GAA TTA AAA CAT AAT TCG      960
Met Ser Glu Ser Leu Glu Gln Val Glu Lys Glu Leu Lys His Asn Ser
305                 310                 315                 320
GAA GCT AAT TTA GAA GAT TTG GTT GCG AAA TCT AAA GAA ATC GTA AGA     1008
Glu Ala Asn Leu Glu Asp Leu Val Ala Lys Ser Lys Glu Ile Val Arg
                325                 330                 335
GAA TAC GAA GGA AAA CTT AAT CAA TCT AAA AAT CTT CCA GAA TTA AAG     1056
Glu Tyr Glu Gly Lys Leu Asn Gln Ser Lys Asn Leu Pro Glu Leu Lys
            340                 345                 350
CAA CTA GAA GAG GAA GCT CAT TCG AAG TTG AAA CAA GTT GTG GAG GAT     1104
Gln Leu Glu Glu Glu Ala His Ser Lys Leu Lys Gln Val Val Glu Asp
        355                 360                 365
TTT AGA AAA AAA TTT AAA ACG TCA GAG CAA GTG ACA CCA AAA AAA CGT     1152
Phe Arg Lys Lys Phe Lys Thr Ser Glu Gln Val Thr Pro Lys Lys Arg
    370                 375                 380
CTC AAA CGA GAT TTA GCT GCT AAT GAA AAT AAT CAA CAA AAG ATT GAG     1200
Leu Lys Arg Asp Leu Ala Ala Asn Glu Asn Asn Gln Gln Lys Ile Glu
385                 390                 395                 400
TTA ACA GTT TCA CCA GAG AAT ATC ACT GTA TAT GAA GGT GAA GAC GTG     1248
Leu Thr Val Ser Pro Glu Asn Ile Thr Val Tyr Glu Gly Glu Asp Val
                405                 410                 415
AAA TTT ACA GTC ACA GCT AAA AGT GAT TCG AAG ACG ACG TTG GAC TTC     1296
Lys Phe Thr Val Thr Ala Lys Ser Asp Ser Lys Thr Thr Leu Asp Phe
            420                 425                 430
AGT GAT CTT TTA ACA AAA TAT AAT CCG TCT GTA TCA GAT AGA ATT AGT     1344
Ser Asp Leu Leu Thr Lys Tyr Asn Pro Ser Val Ser Asp Arg Ile Ser
        435                 440                 445
ACA AAT TAT AAG ACT AAC ACG GAT AAT CAT AAG ATT GCC GAA ATC ACT     1392
Thr Asn Tyr Lys Thr Asn Thr Asp Asn His Lys Ile Ala Glu Ile Thr
    450                 455                 460
ATC AAG AAT TTG AAG CTA AAT GAA AGT CAA ACA GTG ACT CTA AAA GCT     1440
Ile Lys Asn Leu Lys Leu Asn Glu Ser Gln Thr Val Thr Leu Lys Ala
465                 470                 475                 480
AAA GAT GAT TCT GGC AAT GTA GTT GAA AAA ACA TTC ACT ATT ACA GTG     1488
Lys Asp Asp Ser Gly Asn Val Val Glu Lys Thr Phe Thr Ile Thr Val
                485                 490                 495
CAA AAG AAA GAG GAG AAA CAA GTT CCT AAA ACA CCA GAG CAG AAA GAT     1536
Gln Lys Lys Glu Glu Lys Gln Val Pro Lys Thr Pro Glu Gln Lys Asp
            500                 505                 510
TCT AAA ACG GAA GAA AAG GTT CCT CAA GAA CCA AAA TCA AAT GAC AAG     1584
Ser Lys Thr Glu Glu Lys Val Pro Gln Glu Pro Lys Ser Asn Asp Lys
        515                 520                 525
AAT CAA TTA CAA GAG TTG ATT AAA TCA GCT CAA CAA GAA CTG GAA AAG     1632
Asn Gln Leu Gln Glu Leu Ile Lys Ser Ala Gln Gln Glu Leu Glu Lys
    530                 535                 540
TTA GAA AAA GCA ATA AAA GAA TTA ATG GAG CAA CCA GAG ATT CCA TCC     1680
Leu Glu Lys Ala Ile Lys Glu Leu Met Glu Gln Pro Glu Ile Pro Ser
545                 550                 555                 560
AAT CCA GAG TAT GGT ATT CAA AAA TCT ATT TGG GAG TCA CAA AAA GAG     1728
Asn Pro Glu Tyr Gly Ile Gln Lys Ser Ile Trp Glu Ser Gln Lys Glu
                565                 570                 575
CCT ATC CAG GAA GCC ATA ACA AGT TTT AAG AAG ATT ATT GGT GAT TCA     1776
Pro Ile Gln Glu Ala Ile Thr Ser Phe Lys Lys Ile Ile Gly Asp Ser
            580                 585                 590
TCT TCA AAA TAC TAC ACA GAG CAC TAT TTT AAC AAA TAT AAA TCT CAT     1824
Ser Ser Lys Tyr Tyr Thr Glu His Tyr Phe Asn Lys Tyr Lys Ser His
        595                 600                 605
TTT ATG AAT TAT CAA CTT CAT GCA CAA ATG GAG ATG CTG ACT AGA AAA     1872
Phe Met Asn Tyr Gln Leu His Ala Gln Met Glu Met Leu Thr Arg Lys
    610                 615                 620
GTG GTT CAG TAT ATG AAC AAA TAT CCT GAT AAT GCA GAA ATT AAA AAG     1920
Val Val Gln Tyr Met Asn Lys Tyr Pro Asp Asn Ala Glu Ile Lys Lys
625                 630                 635                 640
ATA TTT GAG TCA GAT ATG AAG AGA ACG AAA GAA GAT AAT TAC GGA AGT     1968
Ile Phe Glu Ser Asp Met Lys Arg Thr Lys Glu Asp Asn Tyr Gly Ser
                645                 650                 655
TTA GAA AAT GAT GCT TTG AAA GGC TAT TTT GAG AAA TAT TTC CTT ACA     2016
Leu Glu Asn Asp Ala Leu Lys Gly Tyr Phe Glu Lys Tyr Phe Leu Thr
            660                 665                 670
CCA TTT AAT AAA ATT AAG CAG ATT GTA GAT GAT TTC GAT AAA AAA GTA     2064
Pro Phe Asn Lys Ile Lys Gln Ile Val Asp Asp Phe Asp Lys Lys Val
        675                 680                 685
GAA CAA GAT CAG CCA GCA CCA ATT CCG GAA AAT TCA GAA ATG GAT CAG     2112
Glu Gln Asp Gln Pro Ala Pro Ile Pro Glu Asn Ser Glu Met Asp Gln
    690                 695                 700
GCT AAG GAA AAG GCT AAG ATT GCT GTA TCG AAG TAT ATG AGT AAG GTT     2160
Ala Lys Glu Lys Ala Lys Ile Ala Val Ser Lys Tyr Met Ser Lys Val
705                 710                 715                 720
TTA GAT GGA GTT CAT CAA CAT CTG CAG AAG AAA AAT CAC AGT AAA ATT     2208
Leu Asp Gly Val His Gln His Leu Gln Lys Lys Asn His Ser Lys Ile
                725                 730                 735
GTT GAT CTT TTT AAG GAA CTT GAA GCG ATT AAA CAA CAA ACT ATT TTT     2256
Val Asp Leu Phe Lys Glu Leu Glu Ala Ile Lys Gln Gln Thr Ile Phe
            740                 745                 750
GAT ATT GAC AAT GCA AAG ACT GAA GTA GAG ATT GAT AAC TTA GTA CAC     2304
Asp Ile Asp Asn Ala Lys Thr Glu Val Glu Ile Asp Asn Leu Val His
        755                 760                 765
GAT GCA TTC TCA AAA ATG AAT GCT ACT GTT GCT AAA TTT CAA AAA GGT     2352
Asp Ala Phe Ser Lys Met Asn Ala Thr Val Ala Lys Phe Gln Lys Gly
    770                 775                 780
CTA GAG ACA AAT ACG CCA GAA ACT CCA GAT ACA CCG AAG ATT CCA GAG     2400
Leu Glu Thr Asn Thr Pro Glu Thr Pro Asp Thr Pro Lys Ile Pro Glu
785                 790                 795                 800
CTA CCT CAA GCC CCA GAT ACA CCG CAG GCT CCA GAC ACA CCG CAT GTT     2448
Leu Pro Gln Ala Pro Asp Thr Pro Gln Ala Pro Asp Thr Pro His Val
                805                 810                 815
CCG CAA TCA CCA AAG GCC CCA GAA GCA CCG CGT GTT CCG GAA TCA CCA     2496
Pro Gln Ser Pro Lys Ala Pro Glu Ala Pro Arg Val Pro Glu Ser Pro
            820                 825                 830
AAG ACT CCA GAA GCA CCC CAT GTT CCG GAA TCA CCA AAG GCC CCA GAA     2544
Lys Thr Pro Glu Ala Pro His Val Pro Glu Ser Pro Lys Ala Pro Glu
        835                 840                 845
GCA CCG CGT GTT CCG GAA TCA CCA AAG ACT CCA GAA GCA CCG CAT GTT     2592
Ala Pro Arg Val Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro His Val
    850                 855                 860
CCG GAA TCA CCA AAG ACT CCA GAA GCA CCA AAG ATT CCG GAA CCC CCT     2640
Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro Lys Ile Pro Glu Pro Pro
865                 870                 875                 880
AAG ACT CCA GAC GTC CCT AAC CTT CCA GAC GTC CCT AAG CTT CCA GAC     2688
Lys Thr Pro Asp Val Pro Asn Leu Pro Asp Val Pro Lys Leu Pro Asp
                885                 890                 895
GTC CCT AAG CTT CCA GAT GCA CCG AAG TTA CCA CAT GGG TTA AAT AAA     2736
Val Pro Lys Leu Pro Asp Ala Pro Lys Leu Pro His Gly Leu Asn Lys
            900                 905                 910
GTT GGA CAA GCA GTA TTT ACA TCA ACT GAT GGA AAT ACT AAG GTT ACG     2784
Val Gly Gln Ala Val Phe Thr Ser Thr Asp Gly Asn Thr Lys Val Thr
        915                 920                 925
GTT GTA TTT GAT AAA CCT ACA GAT GCT GAT AAG TTA CAT CTC AAG GAA     2832
Val Val Phe Asp Lys Pro Thr Asp Ala Asp Lys Leu His Leu Lys Glu
    930                 935                 940
GTA ACG ACG AAA GAG TTG GCT GAT AAA ATT GCT CAT AAA ACA GGA GGA     2880
Val Thr Thr Lys Glu Leu Ala Asp Lys Ile Ala His Lys Thr Gly Gly
945                 950                 955                 960
GGA ACA GTT CGT GTG TTT GAC TTA TCT CTT TCT AAA GGA GGC AAG GAA     2928
Gly Thr Val Arg Val Phe Asp Leu Ser Leu Ser Lys Gly Gly Lys Glu
                965                 970                 975
ACA CAT GTC AAT GGA GAA CGA ACT GTT CGG CTC GCG CTT GGG CAG ACT     2976
Thr His Val Asn Gly Glu Arg Thr Val Arg Leu Ala Leu Gly Gln Thr
            980                 985                 990
GGC TCA GAT GTT CAC GTC TAT CAC GTA AAG GAA AAT GGC GAC CTT GAG     3024
Gly Ser Asp Val His Val Tyr His Val Lys Glu Asn Gly Asp Leu Glu
        995                 1000                1005
CGT ATT CCT TCT AAA GTT GAA AAT GGG CAA GTT GTT TTT AAA ACG AAC     3072
Arg Ile Pro Ser Lys Val Glu Asn Gly Gln Val Val Phe Lys Thr Asn
    1010                1015                1020
CAC TTC AGT TTG TTT GCG ATT AAG ACA CTT TCT AAG GAT CAA AAT GTT     3120
His Phe Ser Leu Phe Ala Ile Lys Thr Leu Ser Lys Asp Gln Asn Val
1025                1030                1035                1040
ACT CCA CCG AAG CAG ACT AAA CCT TCT ACC CAA GGC AGT CAA GTA GAG     3168
Thr Pro Pro Lys Gln Thr Lys Pro Ser Thr Gln Gly Ser Gln Val Glu
                1045                1050                1055
ATT GCA GAG AGT CAA ACT GGA AAA TTC CAG ACT AAA GCA GCT AAT CAT     3216
Ile Ala Glu Ser Gln Thr Gly Lys Phe Gln Thr Lys Ala Ala Asn His
            1060                1065                1070
AAA CCA CTG GCT ACT GGA AAT GAA ACA GTG GCA AAA GGA AAT CCT ACA     3264
Lys Pro Leu Ala Thr Gly Asn Glu Thr Val Ala Lys Gly Asn Pro Thr
        1075                1080                1085
TCA ACA ACG GAA AAG AAA CTC GAG CAC CAC                             3294
Ser Thr Thr Glu Lys Lys Leu Glu His His
    1090                1095 
           
           
             
               1098 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               not provided 
             
              8
Glu Gly Asp Ile His Met Ser Glu Leu Val Lys Asp Asp Ser Val Lys
  1               5                  10                  15
Thr Thr Glu Val Ala Ala Lys Pro Tyr Pro Ser Met Ala Gln Thr Asp
             20                  25                  30
Gln Gly Asn Asn Ser Ser Ser Ser Glu Leu Glu Thr Thr Arg Met Glu
         35                  40                  45
Ile Pro Thr Thr Asp Ile Lys Lys Ala Val Glu Pro Val Glu Lys Thr
     50                  55                  60
Ala Gly Glu Thr Ser Ala Thr His Thr Gly Lys Arg Glu Lys Gln Leu
 65                  70                  75                  80
Gln Gln Trp Lys Asn Asn Leu Lys Asn Asp Val Asp Asn Thr Ile Leu
                 85                  90                  95
Ser His Glu Gln Lys Asn Glu Phe Lys Thr Lys Ile Asp Glu Thr Asn
            100                 105                 110
Asp Ser Asp Ala Leu Leu Glu Leu Glu Asn Gln Phe Asn Glu Thr Asn
        115                 120                 125
Arg Leu Leu His Ile Lys Gln His Glu Glu Val Glu Lys Asp Lys Lys
    130                 135                 140
Ala Lys Gln Gln Lys Thr Leu Lys Gln Ser Asp Thr Lys Val Asp Leu
145                 150                 155                 160
Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln Glu Ala Gly
                165                 170                 175
Ile Thr Asn Glu Asp Lys Asp Ser Met Leu Lys Lys Ile Glu Asp Ile
            180                 185                 190
Arg Lys Gln Ala Gln Gln Pro Asp Lys Lys Glu Asp Ala Glu Val Lys
        195                 200                 205
Val Arg Glu Glu Leu Gly Lys Leu Phe Ser Ser Thr Lys Ala Gly Leu
    210                 215                 220
Asp Gln Glu Ile Gln Glu His Val Lys Lys Glu Thr Ser Ser Glu Glu
225                 230                 235                 240
Asn Thr Gln Lys Val Asp Glu His Tyr Ala Asn Ser Leu Gln Asn Leu
                245                 250                 255
Ala Gln Lys Ser Leu Glu Glu Leu Asp Lys Ala Thr Thr Asn Glu Gln
            260                 265                 270
Ala Thr Gln Val Lys Asn Gln Phe Leu Glu Asn Ala Gln Lys Leu Lys
        275                 280                 285
Glu Ile Gln Pro Leu Ile Lys Glu Thr Asn Val Lys Leu Tyr Lys Ala
    290                 295                 300
Met Ser Glu Ser Leu Glu Gln Val Glu Lys Glu Leu Lys His Asn Ser
305                 310                 315                 320
Glu Ala Asn Leu Glu Asp Leu Val Ala Lys Ser Lys Glu Ile Val Arg
                325                 330                 335
Glu Tyr Glu Gly Lys Leu Asn Gln Ser Lys Asn Leu Pro Glu Leu Lys
            340                 345                 350
Gln Leu Glu Glu Glu Ala His Ser Lys Leu Lys Gln Val Val Glu Asp
        355                 360                 365
Phe Arg Lys Lys Phe Lys Thr Ser Glu Gln Val Thr Pro Lys Lys Arg
    370                 375                 380
Leu Lys Arg Asp Leu Ala Ala Asn Glu Asn Asn Gln Gln Lys Ile Glu
385                 390                 395                 400
Leu Thr Val Ser Pro Glu Asn Ile Thr Val Tyr Glu Gly Glu Asp Val
                405                 410                 415
Lys Phe Thr Val Thr Ala Lys Ser Asp Ser Lys Thr Thr Leu Asp Phe
            420                 425                 430
Ser Asp Leu Leu Thr Lys Tyr Asn Pro Ser Val Ser Asp Arg Ile Ser
        435                 440                 445
Thr Asn Tyr Lys Thr Asn Thr Asp Asn His Lys Ile Ala Glu Ile Thr
    450                 455                 460
Ile Lys Asn Leu Lys Leu Asn Glu Ser Gln Thr Val Thr Leu Lys Ala
465                 470                 475                 480
Lys Asp Asp Ser Gly Asn Val Val Glu Lys Thr Phe Thr Ile Thr Val
                485                 490                 495
Gln Lys Lys Glu Glu Lys Gln Val Pro Lys Thr Pro Glu Gln Lys Asp
            500                 505                 510
Ser Lys Thr Glu Glu Lys Val Pro Gln Glu Pro Lys Ser Asn Asp Lys
        515                 520                 525
Asn Gln Leu Gln Glu Leu Ile Lys Ser Ala Gln Gln Glu Leu Glu Lys
    530                 535                 540
Leu Glu Lys Ala Ile Lys Glu Leu Met Glu Gln Pro Glu Ile Pro Ser
545                 550                 555                 560
Asn Pro Glu Tyr Gly Ile Gln Lys Ser Ile Trp Glu Ser Gln Lys Glu
                565                 570                 575
Pro Ile Gln Glu Ala Ile Thr Ser Phe Lys Lys Ile Ile Gly Asp Ser
            580                 585                 590
Ser Ser Lys Tyr Tyr Thr Glu His Tyr Phe Asn Lys Tyr Lys Ser His
        595                 600                 605
Phe Met Asn Tyr Gln Leu His Ala Gln Met Glu Met Leu Thr Arg Lys
    610                 615                 620
Val Val Gln Tyr Met Asn Lys Tyr Pro Asp Asn Ala Glu Ile Lys Lys
625                 630                 635                 640
Ile Phe Glu Ser Asp Met Lys Arg Thr Lys Glu Asp Asn Tyr Gly Ser
                645                 650                 655
Leu Glu Asn Asp Ala Leu Lys Gly Tyr Phe Glu Lys Tyr Phe Leu Thr
            660                 665                 670
Pro Phe Asn Lys Ile Lys Gln Ile Val Asp Asp Phe Asp Lys Lys Val
        675                 680                 685
Glu Gln Asp Gln Pro Ala Pro Ile Pro Glu Asn Ser Glu Met Asp Gln
    690                 695                 700
Ala Lys Glu Lys Ala Lys Ile Ala Val Ser Lys Tyr Met Ser Lys Val
705                 710                 715                 720
Leu Asp Gly Val His Gln His Leu Gln Lys Lys Asn His Ser Lys Ile
                725                 730                 735
Val Asp Leu Phe Lys Glu Leu Glu Ala Ile Lys Gln Gln Thr Ile Phe
            740                 745                 750
Asp Ile Asp Asn Ala Lys Thr Glu Val Glu Ile Asp Asn Leu Val His
        755                 760                 765
Asp Ala Phe Ser Lys Met Asn Ala Thr Val Ala Lys Phe Gln Lys Gly
    770                 775                 780
Leu Glu Thr Asn Thr Pro Glu Thr Pro Asp Thr Pro Lys Ile Pro Glu
785                 790                 795                 800
Leu Pro Gln Ala Pro Asp Thr Pro Gln Ala Pro Asp Thr Pro His Val
                805                 810                 815
Pro Gln Ser Pro Lys Ala Pro Glu Ala Pro Arg Val Pro Glu Ser Pro
            820                 825                 830
Lys Thr Pro Glu Ala Pro His Val Pro Glu Ser Pro Lys Ala Pro Glu
        835                 840                 845
Ala Pro Arg Val Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro His Val
    850                 855                 860
Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro Lys Ile Pro Glu Pro Pro
865                 870                 875                 880
Lys Thr Pro Asp Val Pro Asn Leu Pro Asp Val Pro Lys Leu Pro Asp
                885                 890                 895
Val Pro Lys Leu Pro Asp Ala Pro Lys Leu Pro His Gly Leu Asn Lys
            900                 905                 910
Val Gly Gln Ala Val Phe Thr Ser Thr Asp Gly Asn Thr Lys Val Thr
        915                 920                 925
Val Val Phe Asp Lys Pro Thr Asp Ala Asp Lys Leu His Leu Lys Glu
    930                 935                 940
Val Thr Thr Lys Glu Leu Ala Asp Lys Ile Ala His Lys Thr Gly Gly
945                 950                 955                 960
Gly Thr Val Arg Val Phe Asp Leu Ser Leu Ser Lys Gly Gly Lys Glu
                965                 970                 975
Thr His Val Asn Gly Glu Arg Thr Val Arg Leu Ala Leu Gly Gln Thr
            980                 985                 990
Gly Ser Asp Val His Val Tyr His Val Lys Glu Asn Gly Asp Leu Glu
        995                 1000                1005
Arg Ile Pro Ser Lys Val Glu Asn Gly Gln Val Val Phe Lys Thr Asn
    1010                1015                1020
His Phe Ser Leu Phe Ala Ile Lys Thr Leu Ser Lys Asp Gln Asn Val
1025                1030                1035                1040
Thr Pro Pro Lys Gln Thr Lys Pro Ser Thr Gln Gly Ser Gln Val Glu
                1045                1050                1055
Ile Ala Glu Ser Gln Thr Gly Lys Phe Gln Thr Lys Ala Ala Asn His
            1060                1065                1070
Lys Pro Leu Ala Thr Gly Asn Glu Thr Val Ala Lys Gly Asn Pro Thr
        1075                1080                1085
Ser Thr Thr Glu Lys Lys Leu Glu His His
    1090                1095 
           
           
             
               3492 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA 
             
             
               not provided 
             
             
               CDS 
                1..3492 
             
              9
ATG TTT AAA TCT AAT TAT GAA AGA AAA ATG CGT TAT TCC ATT CGT AAA       48
Met Phe Lys Ser Asn Tyr Glu Arg Lys Met Arg Tyr Ser Ile Arg Lys
  1               5                  10                  15
TTT AGT GTA GGA GTA GCT AGT GTA GCG GTA GCT AGT TTG TTC ATG GGA       96
Phe Ser Val Gly Val Ala Ser Val Ala Val Ala Ser Leu Phe Met Gly
             20                  25                  30
AGC GTT GCT CAT GCA AGT GAG CTT GTA AAG CAC GAT AGT GTG AAG ACT      144
Ser Val Ala His Ala Ser Glu Leu Val Lys His Asp Ser Val Lys Thr
         35                  40                  45
ACC GAG GTT GCA GCT AAG CCC TAT CCA AGT ATG GCT CAA ACA GAT CAA      192
Thr Glu Val Ala Ala Lys Pro Tyr Pro Ser Met Ala Gln Thr Asp Gln
     50                  55                  60
GGA AAT AAT TCA TCA TCC TCG GAA CTT GAG ACA ACA AAG ATC GAA ATT      240
Gly Asn Asn Ser Ser Ser Ser Glu Leu Glu Thr Thr Lys Ile Glu Ile
 65                  70                  75                  80
CCT ACA ACA GAC ATA AAA AAA GCT GTT GAA CCG CTC GAG AAA ACA GCT      288
Pro Thr Thr Asp Ile Lys Lys Ala Val Glu Pro Leu Glu Lys Thr Ala
                 85                  90                  95
GGG GAA ACA TCT GCC ACT GAT ACT GGA AAA CGA GAG AAA CAA TTA CAA      336
Gly Glu Thr Ser Ala Thr Asp Thr Gly Lys Arg Glu Lys Gln Leu Gln
            100                 105                 110
CAA TGG AAA AAT AAT CTA AAA AAT GAT GTG CAT AAC ACA ATT CTA TCT      384
Gln Trp Lys Asn Asn Leu Lys Asn Asp Val His Asn Thr Ile Leu Ser
        115                 120                 125
CAT GAA CAG AAA AAT GAG TTT AAA ACA AAA ATT GAT GAA ACA AAT GAT      432
His Glu Gln Lys Asn Glu Phe Lys Thr Lys Ile Asp Glu Thr Asn Asp
    130                 135                 140
TCT GAT GCA TTA TTA GAA TTA GAA AAT CAA TTT AAC GAA ACT AAT AGA      480
Ser Asp Ala Leu Leu Glu Leu Glu Asn Gln Phe Asn Glu Thr Asn Arg
145                 150                 155                 160
CTG TTA CAC ATC AAA CAA CAT GAA GAA GTT GAG AAA GAT AAG AAA GCT      528
Leu Leu His Ile Lys Gln His Glu Glu Val Glu Lys Asp Lys Lys Ala
                165                 170                 175
AAG CAA CAG AAA ACT CTG AAA CAG TCA GAT ACC AAA GTA GAT CTA AGC      576
Lys Gln Gln Lys Thr Leu Lys Gln Ser Asp Thr Lys Val Asp Leu Ser
            180                 185                 190
AAT ATT GAC AAA GAG CTT AAT CAT CAA AAA AGT CAA GTT GAA ACC ATG      624
Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln Val Glu Thr Met
        195                 200                 205
GCA GAG CAA CTC GGG ATC ACA AAT GAA GAT AAA GAT TCT ATG CTG AAA      672
Ala Glu Gln Leu Gly Ile Thr Asn Glu Asp Lys Asp Ser Met Leu Lys
    210                 215                 220
AAA ATC GAA GAT ATT CGT AAA CAA GCT CAA CAA GCA GAT AAA AAA GAA      720
Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala Asp Lys Lys Glu
225                 230                 235                 240
GAT GCC GAA GTA AAG GTT CGT GAA GAA CTA GGT AAA CTC TTT ACT TCA      768
Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys Leu Phe Thr Ser
                245                 250                 255
ACT AAA GCT GGT CTG GAT CAA GAA ATT CAA GAG CAT GTG AAG AAA GAA      816
Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln Glu His Val Lys Lys Glu
            260                 265                 270
ACG ACT AGT GAG GAA AAT ACT CAG AAA GTT GAT GAA CAC TAT CCT AAT      864
Thr Thr Ser Glu Glu Asn Thr Gln Lys Val Asp Glu His Tyr Pro Asn
        275                 280                 285
AGC CTT CAG AAC CTT GCT CAA AAA TCT CTT GAA GAA CTA GAT AAG GCA      912
Ser Leu Gln Asn Leu Ala Gln Lys Ser Leu Glu Glu Leu Asp Lys Ala
    290                 295                 300
ACT ACC AAT GAA CAA GCT ACA CAA GTT AAA AAT CAA TTC TTA GAA AAC      960
Thr Thr Asn Glu Gln Ala Thr Gln Val Lys Asn Gln Phe Leu Glu Asn
305                 310                 315                 320
GCT CAA AAG CTC AAA GAA ATA CAA CCT CTT ATC AAA GAA ACG AAT GTG     1008
Ala Gln Lys Leu Lys Glu Ile Gln Pro Leu Ile Lys Glu Thr Asn Val
                325                 330                 335
AAA TTG TAT AAG GCT ATG AGT GAG AGC TTG GAG CAG GTT GAG AAG CAA     1056
Lys Leu Tyr Lys Ala Met Ser Glu Ser Leu Glu Gln Val Glu Lys Gln
            340                 345                 350
TTA AAA CAT AAT TCG CAA GCT AAT TTA GAA GAT TTG GTT GCG AAA TCT     1104
Leu Lys His Asn Ser Gln Ala Asn Leu Glu Asp Leu Val Ala Lys Ser
        355                 360                 365
AAA GAA ATC GTA AGA GAA TAC GAA GGA AAA CTT AAT CAA TCT AAA AAT     1152
Lys Glu Ile Val Arg Glu Tyr Glu Gly Lys Leu Asn Gln Ser Lys Asn
    370                 375                 380
CTT CCA GAA TTA AAG CAA CTA GAA GAG GAA GCT CAT TCG AAG TTG AAA     1200
Leu Pro Glu Leu Lys Gln Leu Glu Glu Glu Ala His Ser Lys Leu Lys
385                 390                 395                 400
CAA GTT GTG GAG GAT TTT AGA AAA AAA TTT AAA ACC TCA GAG CAA GTG     1248
Gln Val Val Glu Asp Phe Arg Lys Lys Phe Lys Thr Ser Glu Gln Val
                405                 410                 415
ACA CCA AAA AAA CGT GTC AAA CGA GAT TTA GCT GCT AAT GAA AAT AAT     1296
Thr Pro Lys Lys Arg Val Lys Arg Asp Leu Ala Ala Asn Glu Asn Asn
            420                 425                 430
CAA CAA AAG ATT GAG TTA ACA GTT TCA CCA GAG AAT ATC ACT GTA TAT     1344
Gln Gln Lys Ile Glu Leu Thr Val Ser Pro Glu Asn Ile Thr Val Tyr
        435                 440                 445
GAA GGT GAA GAC CTG AAA TTT ACA CTC ACA GCT AAA AGT GAT TCG AAG     1392
Glu Gly Glu Asp Leu Lys Phe Thr Leu Thr Ala Lys Ser Asp Ser Lys
    450                 455                 460
ACG ACG TTG GAC TTC AGT GAT CTT TTA ACA AAA TAT AAT CCG TCT GTA     1440
Thr Thr Leu Asp Phe Ser Asp Leu Leu Thr Lys Tyr Asn Pro Ser Val
465                 470                 475                 480
TCA GAT AGA ATT AGT ACA AAT TAT AAG ACT AAC ACG GAT AAT CAT AAG     1488
Ser Asp Arg Ile Ser Thr Asn Tyr Lys Thr Asn Thr Asp Asn His Lys
                485                 490                 495
ATT GCC GAA ATC ACT ATC AAG AAT TTG AAG CTA AAT GAA AGT CAA ACA     1536
Ile Ala Glu Ile Thr Ile Lys Asn Leu Lys Leu Asn Glu Ser Gln Thr
            500                 505                 510
GTG ACT CTA AAA GCT AAA GAT GAT TCT GGC AAT GTA GTT CAA AAA ACA     1584
Val Thr Leu Lys Ala Lys Asp Asp Ser Gly Asn Val Val Gln Lys Thr
        515                 520                 525
TTC ACT ATT ACA GTG CAA AAG AAA GAG GAG AAA CAA GTT CCT AAA ACA     1632
Phe Thr Ile Thr Val Gln Lys Lys Glu Glu Lys Gln Val Pro Lys Thr
    530                 535                 540
CCA GAG CAG AAA GAT TCT AAA ACG GAA GAA AAG GTT CCT CAA GAA CCA     1680
Pro Glu Gln Lys Asp Ser Lys Thr Glu Glu Lys Val Pro Gln Glu Pro
545                 550                 555                 560
AAA TCA AAT GAC AAG AAT CAA TTA CAA GAG TTG ATT AAA TCA GCT CAA     1728
Lys Ser Asn Asp Lys Asn Gln Leu Gln Glu Leu Ile Lys Ser Ala Gln
                565                 570                 575
CAA CAA CTG GAA AAG TTA GAA AAA GCA ATA AAA GAA TTA ATG GAG CAA     1776
Gln Gln Leu Glu Lys Leu Glu Lys Ala Ile Lys Glu Leu Met Glu Gln
            580                 585                 590
CCA GAG ATT CCA TCC AAT CCA GAG TAT GGT ATT CAA AAA TCT ATT TGG     1824
Pro Glu Ile Pro Ser Asn Pro Glu Tyr Gly Ile Gln Lys Ser Ile Trp
        595                 600                 605
GAG TCA CAA AAA GAG CCT ATC CAG GAA GCC ATA ACA AGT TTT AAG AAG     1872
Glu Ser Gln Lys Glu Pro Ile Gln Glu Ala Ile Thr Ser Phe Lys Lys
    610                 615                 620
ATT ATT GGT GAT TCA TCT TCA AAA TAC TAC ACA GAG CAC TAT TTT AAC     1920
Ile Ile Gly Asp Ser Ser Ser Lys Tyr Tyr Thr Glu His Tyr Phe Asn
625                 630                 635                 640
AAA TAT AAA TCT GAT TTT ATG AAT TAT CAA CTT CAT GCA CAA ATG GAG     1968
Lys Tyr Lys Ser Asp Phe Met Asn Tyr Gln Leu His Ala Gln Met Glu
                645                 650                 655
ATG CTG ACT AGA AAA GTG GTT CAG TAT ATC AAC AAA TAT CCT GAT AAT     2016
Met Leu Thr Arg Lys Val Val Gln Tyr Ile Asn Lys Tyr Pro Asp Asn
            660                 665                 670
GCA GAA ATT AAA AAG ATA TTT GAG TCA GAT ATG AAG AGA ACG AAA GAA     2064
Ala Glu Ile Lys Lys Ile Phe Glu Ser Asp Met Lys Arg Thr Lys Glu
        675                 680                 685
GAT AAT TAC GGA AGT TTA GAA AAT GAT GCT TTG AAA GGC TAT TTT GAG     2112
Asp Asn Tyr Gly Ser Leu Glu Asn Asp Ala Leu Lys Gly Tyr Phe Glu
    690                 695                 700
AAA TAT TTC CTT ACA CCA TTT AAT AAA ATT AAG CAG ATT GTA GAT GAT     2160
Lys Tyr Phe Leu Thr Pro Phe Asn Lys Ile Lys Gln Ile Val Asp Asp
705                 710                 715                 720
TTG GAT AAA AAA GTA GAA CAA GAT CAG CCA GCA CCA ATT CCG GAA AAT     2208
Leu Asp Lys Lys Val Glu Gln Asp Gln Pro Ala Pro Ile Pro Glu Asn
                725                 730                 735
TCA GAA ATG GAT CAG GCT AAG GAA AAG GCT AAG ATT GCT GTA TCG AAG     2256
Ser Glu Met Asp Gln Ala Lys Glu Lys Ala Lys Ile Ala Val Ser Lys
            740                 745                 750
TAT ATG AGT AAG GTT TTA GAT GGA GTT CAT CAA CAT CTG CAG AAG AAA     2304
Tyr Met Ser Lys Val Leu Asp Gly Val His Gln His Leu Gln Lys Lys
        755                 760                 765
AAT AAC ACT AAA ATT GTT GAT CTT TTT AAG GAA CTT GAA GCG ATT AAA     2352
Asn Asn Thr Lys Ile Val Asp Leu Phe Lys Glu Leu Glu Ala Ile Lys
    770                 775                 780
CAA CAA ACT ATT TTT GAT ATT GAC AAT GCA AAG ACT GAA GTA GAG ATT     2400
Gln Gln Thr Ile Phe Asp Ile Asp Asn Ala Lys Thr Glu Val Glu Ile
785                 790                 795                 800
GAT AAC TTA GTA CAC GAT GCA TTC TCA AAA ATG AAT GCT ACT GTT GCT     2448
Asp Asn Leu Val His Asp Ala Phe Ser Lys Met Asn Ala Thr Val Ala
                805                 810                 815
AAA TTT CAA AAA GGT CTA GAG ACA AAT ACG CCA GAA ACT CCA CAT ACA     2496
Lys Phe Gln Lys Gly Leu Glu Thr Asn Thr Pro Glu Thr Pro His Thr
            820                 825                 830
CCC AAG ATT CCA GAG CTA CCT CAA GCC CCA GAT ACA CCG CAG GCT CCA     2544
Pro Lys Ile Pro Glu Leu Pro Gln Ala Pro Asp Thr Pro Gln Ala Pro
        835                 840                 845
GAC ACA CCG CAT GTT CCG GAA TCA CCA AAG GCC CCA GAA GCA CCC CGT     2592
Asp Thr Pro His Val Pro Glu Ser Pro Lys Ala Pro Glu Ala Pro Arg
    850                 855                 860
GTT CCG GAA TCA CCA AAC ACT CCA GAA GCA CCG CAT GTT CCC CAA TCA     2640
Val Pro Glu Ser Pro Asn Thr Pro Glu Ala Pro His Val Pro Gln Ser
865                 870                 875                 880
CCA AAG GCC CCA GAA GCA CCG CGT GTT CCG GAA TCA CCA AAC ACT CCA     2688
Pro Lys Ala Pro Glu Ala Pro Arg Val Pro Glu Ser Pro Asn Thr Pro
                885                 890                 895
GAA GCA CCG CAT GTT CCG GAA TCA CCA AAG ACT CCA GAA GCA CCA AAG     2736
Glu Ala Pro His Val Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro Lys
            900                 905                 910
ATT CCG GAA CCC CCT AAG ACT CCA GAC GTC CCT AAG CTT CCA GAC GTC     2784
Ile Pro Glu Pro Pro Lys Thr Pro Asp Val Pro Lys Leu Pro Asp Val
        915                 920                 925
CCT AAG CTT CCA GAC GTC CCT AAG CTT CCA GAT GCA CCC AAG TTA CCA     2832
Pro Lys Leu Pro Asp Val Pro Lys Leu Pro Asp Ala Pro Lys Leu Pro
    930                 935                 940
GAT GGG TTA AAT AAA GTT GGA CAA GCA GTA TTT ACA TCA ACT GAT GGA     2880
Asp Gly Leu Asn Lys Val Gly Gln Ala Val Phe Thr Ser Thr Asp Gly
945                 950                 955                 960
AAT ACT AAG GTT ACG GTT GTA TTT GAT AAA CCT ACA GAT GCT GAT AAG     2928
Asn Thr Lys Val Thr Val Val Phe Asp Lys Pro Thr Asp Ala Asp Lys
                965                 970                 975
TTA CAT CTC AAG GAA CTA ACG ACG AAA GAG TTG GCT GAT AAA ATT GCT     2976
Leu His Leu Lys Glu Leu Thr Thr Lys Glu Leu Ala Asp Lys Ile Ala
            980                 985                 990
CAT AAA ACA GGA GGA GGA ACA GTT CGT GTG TTT GAC TTA TCT CTT TCT     3024
His Lys Thr Gly Gly Gly Thr Val Arg Val Phe Asp Leu Ser Leu Ser
        995                 1000                1005
AAA GGA GGC AAG GAA ACA CAT GTC AAT GGA CAA CGA ACT GTT CGG CTC     3072
Lys Gly Gly Lys Glu Thr His Val Asn Gly Gln Arg Thr Val Arg Leu
    1010                1015                1020
GCG CTT GGG CAG ACT GGC TCA GAT GTT CAC GTC TAT CAC GTA AAG GAA     3120
Ala Leu Gly Gln Thr Gly Ser Asp Val His Val Tyr His Val Lys Glu
1025                1030                1035                1040
AAT GGC GAC CTT GAG CGT ATT CCT TCT AAA GTT GAA AAT GGG CAA GTT     3168
Asn Gly Asp Leu Glu Arg Ile Pro Ser Lys Val Glu Asn Gly Gln Val
                1045                1050                1055
GTT TTT AAA ACG AAC CAC TTC AGT TTG TTT GCG ATT AAG ACA CTT TCT     3216
Val Phe Lys Thr Asn His Phe Ser Leu Phe Ala Ile Lys Thr Leu Ser
            1060                1065                1070
AAG GAT CAA AAT GTT ACT CCA CCG AAG CAG ACT AAA CCT TCT ACC CAA     3264
Lys Asp Gln Asn Val Thr Pro Pro Lys Gln Thr Lys Pro Ser Thr Gln
        1075                1080                1085
GGC AGT CAA GTA GAG ATT GCA GAG AGT CAA ACT GGA AAA TTC CAG AGT     3312
Gly Ser Gln Val Glu Ile Ala Glu Ser Gln Thr Gly Lys Phe Gln Ser
    1090                1095                1100
AAA GCA GCT AAT CAT AAA GCA CTC GCT ACT GGA AAT GAA ACA GTG GCA     3360
Lys Ala Ala Asn His Lys Ala Leu Ala Thr Gly Asn Glu Thr Val Ala
1105                1110                1115                1120
AAA GGA AAT CCT ACA TCA ACA ACG CAA AAG AAA TTG CCA TAT ACA GGA     3408
Lys Gly Asn Pro Thr Ser Thr Thr Gln Lys Lys Leu Pro Tyr Thr Gly
                1125                1130                1135
GTG GCA TCT AAT CTA GTT CTT GAA ATT ATG GGT CTC CTT GGT TTG ATT     3456
Val Ala Ser Asn Leu Val Leu Glu Ile Met Gly Leu Leu Gly Leu Ile
            1140                1145                1150
GGA ACT TCA TTC ATC GCA ATG AAA AGA AGA AAA TCA                     3492
Gly Thr Ser Phe Ile Ala Met Lys Arg Arg Lys Ser
        1155                1160 
           
           
             
               1164 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               not provided 
             
              10
Met Phe Lys Ser Asn Tyr Glu Arg Lys Met Arg Tyr Ser Ile Arg Lys
  1               5                  10                  15
Phe Ser Val Gly Val Ala Ser Val Ala Val Ala Ser Leu Phe Met Gly
             20                  25                  30
Ser Val Ala His Ala Ser Glu Leu Val Lys His Asp Ser Val Lys Thr
         35                  40                  45
Thr Glu Val Ala Ala Lys Pro Tyr Pro Ser Met Ala Gln Thr Asp Gln
     50                  55                  60
Gly Asn Asn Ser Ser Ser Ser Glu Leu Glu Thr Thr Lys Ile Glu Ile
 65                  70                  75                  80
Pro Thr Thr Asp Ile Lys Lys Ala Val Glu Pro Leu Glu Lys Thr Ala
                 85                  90                  95
Gly Glu Thr Ser Ala Thr Asp Thr Gly Lys Arg Glu Lys Gln Leu Gln
            100                 105                 110
Gln Trp Lys Asn Asn Leu Lys Asn Asp Val His Asn Thr Ile Leu Ser
        115                 120                 125
His Glu Gln Lys Asn Glu Phe Lys Thr Lys Ile Asp Glu Thr Asn Asp
    130                 135                 140
Ser Asp Ala Leu Leu Glu Leu Glu Asn Gln Phe Asn Glu Thr Asn Arg
145                 150                 155                 160
Leu Leu His Ile Lys Gln His Glu Glu Val Glu Lys Asp Lys Lys Ala
                165                 170                 175
Lys Gln Gln Lys Thr Leu Lys Gln Ser Asp Thr Lys Val Asp Leu Ser
            180                 185                 190
Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln Val Glu Thr Met
        195                 200                 205
Ala Glu Gln Leu Gly Ile Thr Asn Glu Asp Lys Asp Ser Met Leu Lys
    210                 215                 220
Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala Asp Lys Lys Glu
225                 230                 235                 240
Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys Leu Phe Thr Ser
                245                 250                 255
Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln Glu His Val Lys Lys Glu
            260                 265                 270
Thr Thr Ser Glu Glu Asn Thr Gln Lys Val Asp Glu His Tyr Pro Asn
        275                 280                 285
Ser Leu Gln Asn Leu Ala Gln Lys Ser Leu Glu Glu Leu Asp Lys Ala
    290                 295                 300
Thr Thr Asn Glu Gln Ala Thr Gln Val Lys Asn Gln Phe Leu Glu Asn
305                 310                 315                 320
Ala Gln Lys Leu Lys Glu Ile Gln Pro Leu Ile Lys Glu Thr Asn Val
                325                 330                 335
Lys Leu Tyr Lys Ala Met Ser Glu Ser Leu Glu Gln Val Glu Lys Gln
            340                 345                 350
Leu Lys His Asn Ser Gln Ala Asn Leu Glu Asp Leu Val Ala Lys Ser
        355                 360                 365
Lys Glu Ile Val Arg Glu Tyr Glu Gly Lys Leu Asn Gln Ser Lys Asn
    370                 375                 380
Leu Pro Glu Leu Lys Gln Leu Glu Glu Glu Ala His Ser Lys Leu Lys
385                 390                 395                 400
Gln Val Val Glu Asp Phe Arg Lys Lys Phe Lys Thr Ser Glu Gln Val
                405                 410                 415
Thr Pro Lys Lys Arg Val Lys Arg Asp Leu Ala Ala Asn Glu Asn Asn
            420                 425                 430
Gln Gln Lys Ile Glu Leu Thr Val Ser Pro Glu Asn Ile Thr Val Tyr
        435                 440                 445
Glu Gly Glu Asp Leu Lys Phe Thr Leu Thr Ala Lys Ser Asp Ser Lys
    450                 455                 460
Thr Thr Leu Asp Phe Ser Asp Leu Leu Thr Lys Tyr Asn Pro Ser Val
465                 470                 475                 480
Ser Asp Arg Ile Ser Thr Asn Tyr Lys Thr Asn Thr Asp Asn His Lys
                485                 490                 495
Ile Ala Glu Ile Thr Ile Lys Asn Leu Lys Leu Asn Glu Ser Gln Thr
            500                 505                 510
Val Thr Leu Lys Ala Lys Asp Asp Ser Gly Asn Val Val Gln Lys Thr
        515                 520                 525
Phe Thr Ile Thr Val Gln Lys Lys Glu Glu Lys Gln Val Pro Lys Thr
    530                 535                 540
Pro Glu Gln Lys Asp Ser Lys Thr Glu Glu Lys Val Pro Gln Glu Pro
545                 550                 555                 560
Lys Ser Asn Asp Lys Asn Gln Leu Gln Glu Leu Ile Lys Ser Ala Gln
                565                 570                 575
Gln Gln Leu Glu Lys Leu Glu Lys Ala Ile Lys Glu Leu Met Glu Gln
            580                 585                 590
Pro Glu Ile Pro Ser Asn Pro Glu Tyr Gly Ile Gln Lys Ser Ile Trp
        595                 600                 605
Glu Ser Gln Lys Glu Pro Ile Gln Glu Ala Ile Thr Ser Phe Lys Lys
    610                 615                 620
Ile Ile Gly Asp Ser Ser Ser Lys Tyr Tyr Thr Glu His Tyr Phe Asn
625                 630                 635                 640
Lys Tyr Lys Ser Asp Phe Met Asn Tyr Gln Leu His Ala Gln Met Glu
                645                 650                 655
Met Leu Thr Arg Lys Val Val Gln Tyr Ile Asn Lys Tyr Pro Asp Asn
            660                 665                 670
Ala Glu Ile Lys Lys Ile Phe Glu Ser Asp Met Lys Arg Thr Lys Glu
        675                 680                 685
Asp Asn Tyr Gly Ser Leu Glu Asn Asp Ala Leu Lys Gly Tyr Phe Glu
    690                 695                 700
Lys Tyr Phe Leu Thr Pro Phe Asn Lys Ile Lys Gln Ile Val Asp Asp
705                 710                 715                 720
Leu Asp Lys Lys Val Glu Gln Asp Gln Pro Ala Pro Ile Pro Glu Asn
                725                 730                 735
Ser Glu Met Asp Gln Ala Lys Glu Lys Ala Lys Ile Ala Val Ser Lys
            740                 745                 750
Tyr Met Ser Lys Val Leu Asp Gly Val His Gln His Leu Gln Lys Lys
        755                 760                 765
Asn Asn Thr Lys Ile Val Asp Leu Phe Lys Glu Leu Glu Ala Ile Lys
    770                 775                 780
Gln Gln Thr Ile Phe Asp Ile Asp Asn Ala Lys Thr Glu Val Glu Ile
785                 790                 795                 800
Asp Asn Leu Val His Asp Ala Phe Ser Lys Met Asn Ala Thr Val Ala
                805                 810                 815
Lys Phe Gln Lys Gly Leu Glu Thr Asn Thr Pro Glu Thr Pro His Thr
            820                 825                 830
Pro Lys Ile Pro Glu Leu Pro Gln Ala Pro Asp Thr Pro Gln Ala Pro
        835                 840                 845
Asp Thr Pro His Val Pro Glu Ser Pro Lys Ala Pro Glu Ala Pro Arg
    850                 855                 860
Val Pro Glu Ser Pro Asn Thr Pro Glu Ala Pro His Val Pro Gln Ser
865                 870                 875                 880
Pro Lys Ala Pro Glu Ala Pro Arg Val Pro Glu Ser Pro Asn Thr Pro
                885                 890                 895
Glu Ala Pro His Val Pro Glu Ser Pro Lys Thr Pro Glu Ala Pro Lys
            900                 905                 910
Ile Pro Glu Pro Pro Lys Thr Pro Asp Val Pro Lys Leu Pro Asp Val
        915                 920                 925
Pro Lys Leu Pro Asp Val Pro Lys Leu Pro Asp Ala Pro Lys Leu Pro
    930                 935                 940
Asp Gly Leu Asn Lys Val Gly Gln Ala Val Phe Thr Ser Thr Asp Gly
945                 950                 955                 960
Asn Thr Lys Val Thr Val Val Phe Asp Lys Pro Thr Asp Ala Asp Lys
                965                 970                 975
Leu His Leu Lys Glu Leu Thr Thr Lys Glu Leu Ala Asp Lys Ile Ala
            980                 985                 990
His Lys Thr Gly Gly Gly Thr Val Arg Val Phe Asp Leu Ser Leu Ser
        995                 1000                1005
Lys Gly Gly Lys Glu Thr His Val Asn Gly Gln Arg Thr Val Arg Leu
    1010                1015                1020
Ala Leu Gly Gln Thr Gly Ser Asp Val His Val Tyr His Val Lys Glu
1025                1030                1035                1040
Asn Gly Asp Leu Glu Arg Ile Pro Ser Lys Val Glu Asn Gly Gln Val
                1045                1050                1055
Val Phe Lys Thr Asn His Phe Ser Leu Phe Ala Ile Lys Thr Leu Ser
            1060                1065                1070
Lys Asp Gln Asn Val Thr Pro Pro Lys Gln Thr Lys Pro Ser Thr Gln
        1075                1080                1085
Gly Ser Gln Val Glu Ile Ala Glu Ser Gln Thr Gly Lys Phe Gln Ser
    1090                1095                1100
Lys Ala Ala Asn His Lys Ala Leu Ala Thr Gly Asn Glu Thr Val Ala
1105                1110                1115                1120
Lys Gly Asn Pro Thr Ser Thr Thr Gln Lys Lys Leu Pro Tyr Thr Gly
                1125                1130                1135
Val Ala Ser Asn Leu Val Leu Glu Ile Met Gly Leu Leu Gly Leu Ile
            1140                1145                1150
Gly Thr Ser Phe Ile Ala Met Lys Arg Arg Lys Ser
        1155                1160 
           
           
             
               106 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              11
Leu Leu His Ile Lys Gln His Glu Glu Val Glu Lys Asp Lys Lys Ala
1               5                   10                  15
Lys Gln Gln Lys Thr Leu Lys Gln Ser Asp Thr Lys Val Asp Leu Ser
            20                  25                  30
Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln Val Glu Lys Met
        35                  40                  45
Ala Glu Gln Lys Gly Ile Thr Asn Glu Asp Lys Asp Ser Met Leu Lys
    50                  55                  60
Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala Asp Lys Lys Glu
65                  70                  75                  80
Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys Leu Phe Ser Ser
                85                  90                  95
Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln
            100                 105 
           
           
             
               147 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              12
Asp Ser Asp Ala Leu Leu Glu Leu Glu Asn Gln Phe Asn Glu Thr Asn
1               5                   10                  15
Arg Leu Leu His Ile Lys Gln His Glu Glu Val Glu Lys Asp Lys Lys
            20                  25                  30
Ala Lys Gln Gln Lys Thr Leu Lys Gln Ser Asp Thr Lys Val Asp Leu
        35                  40                  45
Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln Val Glu Lys
    50                  55                  60
Met Ala Glu Gln Lys Gly Ile Thr Asn Glu Asp Lys Asp Ser Met Leu
65                  70                  75                  80
Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala Asp Lys Lys
                85                  90                  95
Glu Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys Leu Phe Ser
            100                 105                 110
Ser Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln Glu His Val Lys Lys
        115                 120                 125
Glu Thr Ser Ser Glu Glu Asn Thr Gln Lys Val Asp Glu His Tyr Ala
    130                 135                 140
Asn Ser Leu
145 
           
           
             
               147 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              13
Asp Ser Asp Ala Leu Leu Glu Leu Glu Asn Gln Phe Asn Glu Thr Asn
1               5                   10                  15
Arg Leu Leu His Ile Lys Gln His Glu Glu Val Glu Lys Asp Lys Lys
            20                  25                  30
Ala Lys Gln Gln Lys Thr Leu Lys Gln Ser Asp Thr Lys Val Asp Leu
        35                  40                  45
Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln Val Glu Lys
    50                  55                  60
Met Ala Glu Gln Lys Gly Ile Thr Asn Glu Asp Lys Asp Ser Met Leu
65                  70                  75                  80
Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala Asp Lys Lys
                85                  90                  95
Glu Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys Leu Phe Ser
            100                 105                 110
Ser Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln Glu His Val Lys Lys
        115                 120                 125
Glu Thr Ser Ser Glu Glu Asn Thr Gln Lys Val Asp Glu His Tyr Ala
    130                 135                 140
Asn Ser Leu
145 
           
           
             
               111 amino acids 
               amino acid 
               single 
               linear 
             
             
               peptide 
             
             
               not provided 
             
              14
Val Asp Leu Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln
1               5                   10                  15
Val Glu Lys Met Ala Glu Gln Lys Gly Ile Thr Asn Glu Asp Lys Asp
            20                  25                  30
Ser Met Leu Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala
        35                  40                  45
Asp Lys Lys Glu Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys
    50                  55                  60
Leu Phe Ser Ser Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln Glu His
65                  70                  75                  80
Val Lys Lys Glu Thr Ser Ser Glu Glu Asn Thr Gln Lys Val Asp Glu
                85                  90                  95
His Tyr Ala Asn Ser Leu Gln Asn Leu Ala Gln Lys Ser Leu Glu
            100                 105                 110 
           
           
             
               111 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              15
Val Asp Leu Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln
1               5                   10                  15
Val Glu Lys Met Ala Glu Gln Lys Gly Ile Thr Asn Glu Asp Lys Asp
            20                  25                  30
Ser Met Leu Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala
        35                  40                  45
Asp Lys Lys Glu Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys
    50                  55                  60
Leu Phe Ser Ser Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln Glu His
65                  70                  75                  80
Val Lys Lys Glu Thr Ser Ser Glu Glu Asn Thr Gln Lys Val Asp Glu
                85                  90                  95
His Tyr Ala Asn Ser Leu Gln Asn Leu Ala Gln Lys Ser Leu Glu
            100                 105                 110 
           
           
             
               120 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              16
Val Asp Leu Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln
1               5                   10                  15
Val Glu Lys Met Ala Glu Gln Lys Gly Ile Thr Asn Glu Asp Lys Asp
            20                  25                  30
Ser Met Leu Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala
        35                  40                  45
Asp Lys Lys Glu Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys
    50                  55                  60
Leu Phe Ser Ser Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln Glu His
65                  70                  75                  80
Val Lys Lys Glu Thr Ser Ser Glu Glu Asn Thr Gln Lys Val Asp Glu
                85                  90                  95
His Tyr Ala Asn Ser Leu Gln Asn Leu Ala Gln Lys Ser Leu Glu Glu
            100                 105                 110
Leu Asp Lys Ala Thr Thr Asn Glu
        115                 120 
           
           
             
               120 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              17
Val Asp Leu Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln
1               5                   10                  15
Val Glu Lys Met Ala Glu Gln Lys Gly Ile Thr Asn Glu Asp Lys Asp
            20                  25                  30
Ser Met Leu Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala
        35                  40                  45
Asp Lys Lys Glu Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys
    50                  55                  60
Leu Phe Ser Ser Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln Glu His
65                  70                  75                  80
Val Lys Lys Glu Thr Ser Ser Glu Glu Asn Thr Gln Lys Val Asp Glu
                85                  90                  95
His Tyr Ala Asn Ser Leu Gln Asn Leu Ala Gln Lys Ser Leu Glu Glu
            100                 105                 110
Leu Asp Lys Ala Thr Thr Asn Glu
        115                 120 
           
           
             
               58 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              18
Val Asp Leu Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln
1               5                   10                  15
Val Glu Lys Met Ala Glu Gln Lys Gly Ile Thr Asn Glu Asp Lys Asp
            20                  25                  30
Ser Met Leu Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala
        35                  40                  45
Asp Lys Lys Glu Asp Ala Glu Val Lys Val
    50                  55 
           
           
             
               58 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              19
Val Asp Leu Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln
1               5                   10                  15
Val Glu Lys Met Ala Glu Gln Lys Gly Ile Thr Asn Glu Asp Lys Asp
            20                  25                  30
Ser Met Leu Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala
        35                  40                  45
Asp Lys Lys Glu Asp Ala Glu Val Lys Val
    50                  55 
           
           
             
               102 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              20
Val Asp Leu Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln
1               5                   10                  15
Val Glu Lys Met Ala Glu Gln Lys Gly Ile Thr Asn Glu Asp Lys Asp
            20                  25                  30
Ser Met Leu Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala
        35                  40                  45
Asp Lys Lys Glu Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys
    50                  55                  60
Leu Phe Ser Ser Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln Glu His
65                  70                  75                  80
Val Lys Lys Glu Thr Ser Ser Glu Glu Asn Thr Gln Lys Val Asp Glu
                85                  90                  95
His Tyr Ala Asn Ser Leu
            100 
           
           
             
               78 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              21
Val Asp Leu Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Pro
1               5                   10                  15
Val Glu Lys Met Ala Glu Pro Lys Gly Ile Thr Asn Glu Asp Lys Asp
            20                  25                  30
Ser Met Leu Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala
        35                  40                  45
Asp Lys Lys Glu Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys
    50                  55                  60
Leu Phe Ser Ser Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln
65                  70                  75 
           
           
             
               78 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              22
Val Asp Leu Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln
1               5                   10                  15
Val Glu Ala Met Ala Glu Gln Ala Gly Ile Thr Asn Glu Asp Lys Asp
            20                  25                  30
Ser Met Leu Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala
        35                  40                  45
Asp Lys Lys Glu Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys
    50                  55                  60
Leu Phe Ser Ser Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln
65                  70                  75 
           
           
             
               72 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              23
Val Asp Leu Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln
1               5                   10                  15
Glu Ala Gly Ile Thr Asn Glu Asp Lys Asp Ser Met Leu Lys Lys Ile
            20                  25                  30
Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala Asp Lys Lys Glu Asp Ala
        35                  40                  45
Glu Val Lys Val Arg Glu Glu Leu Gly Lys Leu Phe Ser Ser Thr Lys
    50                  55                  60
Ala Gly Leu Asp Gln Glu Ile Gln
65                  70 
           
           
             
               78 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              24
Val Asp Leu Ser Asn Ile Asp Lys Glu Leu Asn His Gln Lys Ser Gln
1               5                   10                  15
Val Glu Thr Met Ala Glu Gln Leu Gly Ile Thr Asn Glu Asp Lys Asp
            20                  25                  30
Ser Met Leu Lys Lys Ile Glu Asp Ile Arg Lys Gln Ala Gln Gln Ala
        35                  40                  45
Asp Lys Lys Glu Asp Ala Glu Val Lys Val Arg Glu Glu Leu Gly Lys
    50                  55                  60
Leu Phe Ser Ser Thr Lys Ala Gly Leu Asp Gln Glu Ile Gln
65                  70                  75 
           
           
             
               9 amino acids 
               amino acid 
               single 
               Not Relevant 
             
             
               peptide 
             
             
               not provided 
             
              25
Glu Leu Ile Lys Ser Ala Gln Gln Glu
1               5 
           
           
             
               40 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA 
             
             
               not provided 
             
              26
GTTGAAGCAA TGGCAGAGCA AGCGGGAATC ACAAATGAAG                           40 
           
           
             
               42 base pairs 
               nucleic acid 
               single 
               Not Relevant 
             
             
               cDNA 
             
             
               not provided 
             
              27
GATTCCCGCT TGCTCTGCCA TTGCTTCAAC TTGACTTTTT TG                        42 
           
           
             
               30 base pairs 
               nucleic acid 
               single 
               Not Relevant 
             
             
               cDNA 
             
             
               not provided 
             
              28
AAGGATCCAA GTGAGCTTGT AAAGGACGAT                                      30 
           
           
             
               32 base pairs 
               nucleic acid 
               single 
               Not Relevant 
             
             
               cDNA 
             
             
               not provided 
             
              29
AAAACTCGAG TTTCTTTTCC GTTGTTGATG TA                                   32 
           
           
             
               15 amino acids 
               amino acid 
               single 
               linear 
             
             
               cDNA 
             
             
               not provided 
             
              30
Asn His Gln Lys Ser Gln Val Glu Lys Met Ala Glu Gln Lys Gly
1               5                   10                  15 
           
           
             
               57 base pairs 
               nucleic acid 
               double 
               linear 
             
             
               cDNA 
             
             
               not provided 
             
             
               CDS 
                1..54 
             
              31
AGA TCT CGA TCC CGC GAA ATT AAT ACG ACT CAC TAT AGG GGA ATT GTG       48
Arg Ser Arg Ser Arg Glu Ile Asn Thr Thr His Tyr Arg Gly Ile Val
  1               5                  10                  15
AGC GGA TAA                                                           57
Ser Gly 
           
           
             
               18 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               not provided 
             
              32
Arg Ser Arg Ser Arg Glu Ile Asn Thr Thr His Tyr Arg Gly Ile Val
  1               5                  10                  15
Ser Gly 
           
           
             
               30 base pairs 
               nucleic acid 
               double 
               linear 
             
             
               cDNA 
             
             
               not provided 
             
             
               CDS 
                1..27 
             
              33
CAA TTC CCC TCT AGA AAT AAT TTT GTT TAA                               30
Gln Phe Pro Ser Arg Asn Asn Phe Val
  1               5 
           
           
             
               9 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               not provided 
             
              34
Gln Phe Pro Ser Arg Asn Asn Phe Val
  1               5