Patent Publication Number: US-6335172-B1

Title: Cloned tetrodotoxin-sensitive sodium channel α-subunit and a splice variant thereof

Description:
CROSS REFERENCE TO RELATED APPLICATIONS 
     This application is a divisional of U.S. patent application Ser. No. 09/024,020, filed on Feb. 16, 1998, now U.S. Pat. No. 6,030,810, which in turn claims the benefit under 35 U.S.C. 119(e) of prior provisional U.S. patent application Ser. No. 60/039,447, filed on Feb. 26, 1997. 
    
    
     BACKGROUND OF THE INVENTION 
     1. Field of the Invention 
     This invention relates generally to sodium channel proteins and more particularly to a novel cloned α-subunit of a voltage-gated, tetrodotoxin-sensitive sodium channel protein. This invention further relates to the production of this protein by recombinant technology and nucleic acid sequences encoding for this protein. 
     2. Previous Art 
     The basic unit of information transmitted from one part of the nervous system to another is a single action potential or nerve impulse. The “transmission line” for these impulses is the axon, or nerve fiber. The electrical excitability of the nerve membrane has been shown to depend on the membrane&#39;s voltage-sensitive ionic permeability system that allows it to use energy stored in ionic concentration gradients. Electrical activity of the nerve is triggered by a depolarization of the membrane, which opens channels through the membrane that are highly selective for sodium ions, which are then driven inward by the electrochemical gradient. Of the many ionic channels, the voltage-gated or voltage-sensitive sodium channel is one of the most studied. It is a transmembrane protein that is essential for the generation of action potentials in excitable cells. An excellent review of sodium channels is presented in Catterall,  TINS  16(12):500-506 (1993). 
     The cDNAs for several Na +  channels have been cloned and sequenced. Numa, et al.,  Annals of the New York Academy of Sciences  479:338-355 (1986), describe cDNA from the electric organ of eel and two different cDNAs from rat-brain. Rogart, U.S. Pat. No. 5,380,836, describes cDNA from rat cardiac tissue. See also Rogart, Cribbs, et al.,  Proc. Natl. Acad. Sci ., 86:8170-8174 (1989). A peripheral nerve sodium channel, referred to as PN1, has been detected based on sodium current studies and hybridization to a highly conserved sodium channel probe by D&#39;Arcangelo, et al.,  J. Cell Biol . 122:915-921 (1993), and subsequently cloned from PC12 cells, Toledo-Aral, et al.,  Proc. Nat. Acad. Sci . 94:1527-1532 (1997). The sequence of rat PN1 cloned from dorsal root ganglia and its functional expression have been described, Sangameswaran, et al.,  J. Biol. Chem  272:14805-14809 (1997). Other cloned sodium channels include rat brain types IIa, Auld, et al.,  Neuron  1:449-461 (1988), and III, Kayano, et al.,  FEBS Lett . 228:187-194 (1988), rat skeletal muscle, Trimmer, et al.,  Neuron  3:33-49 (1989), rat NaCh6, Schaller, et al.,  J. Neurosci . 15:3231-3242 (1995), rat peripheral nerve sodium channel type 3 (rPN3), Sangameswaran, et al.,  J. Biol Chem . 271:5953-5956 (1996), also called SNS, Akopian, et al.,  Nature  379:257-262 (1996), rat atypical channel, Felipe, et al.,  J. Biol. Chem . 269:30125-30131 (1994), and the rat glial sodium channel, Akopian, et al.,  FEBS Lett . 400:183-187 (1997). 
     These studies have shown that the amino acid sequence of the Na +  channel has been conserved over a long evolutionary period. These studies have also revealed that the channel is a single polypeptide containing four internal repeats, or homologous domains (domains I-IV), having similar amino acid sequences. Each domain folds into six predicted transmembrane α-helices or segments: five are hydrophobic segments and one segment is highly charged with many lysine and arginine residues. This highly charged segment is the fourth transmembrane segment in each domain (the S4 segment) and is likely to be involved in voltage-gating. The positively charged side chains on the S4 segment are likely to be paired with the negatively charged side chains on the other five segments, such that membrane depolarization could shift the position of one helix relative to the other, thereby opening the channel. Accessory subunits may modify the function of the channel. 
     Therapeutic utilities in recombinant materials derived from the DNA of the numerous sodium channels have been discovered. For example, Cherksey, U.S. Pat. No. 5,132,296, discloses purified Na +  channels that have proven useful as therapeutic and diagnostic tools. 
     Isoforms of sodium channels are divided into “subfamilies”. The term “isoform” is used to mean distinct but closely related sodium channel proteins, i.e., those having an amino acid homology of approximately 60-80%. These isoforms also show strong homology in functions. The term “subfamilies” is used to mean distinct sodium channels that have an amino acid homology of approximately 80-95%. Combinations of several factors are used to determine the distinctions within a subfamily, for example, the speed of a channel, chromosomal location, expression data, homology to other channels within a species, and homology to a channel of the same subfamily across species. Another consideration is an affinity to tetrodotoxin (“TTX”). TTX is a highly potent toxin from the puffer or fugu fish which blocks the conduction of nerve impulses along axons and in excitable membranes of nerve fibers. TTX binds to the Na +  channel and blocks the flow of sodium ions. 
     Studies using TTX as a probe have shed much light on the mechanism and structure of Na +  channels. There are three Na +  channel subtypes that are defined by the affinity for TTX, which can be measured by the IC 50  values: TTX-sensitive Na +  channels (IC 50 ≈1-30 nM), TTX-insensitive N +  channels (IC 50 ≈1-5 μm), and TTX-resistant Na +  channels (IC 50 ≧100 μM). 
     TTX-insensitive action potentials were first studied in rat skeletal muscle. See Redfern, et al.,  Acta Physiol. Scand . 82:70-78 (1971). Subsequently, these action potentials were described in other mammalian tissues, including newborn mammalian skeletal muscle, mammalian cardiac muscle, mouse dorsal root ganglion cells in vitro and in culture, cultured mammalian skeletal muscle, and L6 cells. See Rogart,  Ann. Rev. Physiol . 43:711-725 (1981). 
     Dorsal root ganglia neurons possess both TTX-sensitive (IC 50  ≈0.3 nM) and TTX-resistant (IC 50 ≈100 μM) sodium channel currents, as described in Roy, et al.,  J. Neurosci . 12:2104-2111 (1992). 
     TTX-resistant sodium currents have also been measured in rat nodose and petrosal ganglia, Ikeda, et al.,  J. Neurophysiol . 55:527-539 (1986) and Stea, et al.,  Neurosci . 47:727-736 (1992). 
     SUMMARY OF THE INVENTION 
     One aspect of the present invention is a purified and isolated DNA sequence encoding for a novel TTX-sensitive sodium channel protein, in particular, the α-subunit of this protein. Another embodiment of the invention is a purified and isolated DNA sequence encoding for a splice variant of the novel TTX-sensitive sodium channel. 
     Another aspect of the invention is a method of stabilizing the full length cDNA which encodes the protein sequence of the invention. 
     Also included in this invention are alternate DNA forms, such as genomic DNA, DNA prepared by partial or total chemical synthesis from nucleotides, and DNA having deletions or mutations. 
     Another aspect of the invention is a novel probe based on known sodium channels for screening rat cDNA libraries. 
     Further aspects of the invention include expression vectors comprising the DNA of the invention, host cells transformed or transfected by these vectors, and clonal cell lines expressing the DNA of the invention. Also disclosed is the cDNA and MRNA derived from the DNA sequences of the invention. 
     Another aspect of the present invention are recombinant polynucleotides and oligonucleotides comprising a nucleic acid sequence derived from the DNA sequence of this invention. 
     Still another aspect of the invention is the novel rat TTX-sensitive sodium channel protein and fragments thereof, encoded by the DNA of this invention. 
     Further provided is a method of inhibiting the activity of the novel TTX-sensitive sodium channel comprising administering an effective amount of a compound having an IC 50  of 1 nM or less. 
     Also forming part of this invention is an assay for inhibitors of the sodium channel protein comprising contacting a compound suspected of being an inhibitor with expressed sodium channel and measuring the activity of the sodium channel. 
     Another part of this invention is a method of employing the DNA for forming monoclonal and polyclonal antibodies, for use as molecular targets for drug discovery, highly specific markers for specific antigens, detector molecules, diagnostic assays, and therapeutic uses. 
    
    
     BRIEF DESCRIPTION OF THE SEQ ID&#39;S AND FIGURES 
     SEQ ID NO: 1 depicts an engineered version of the nucleotide cDNA sequence encoding the rat TTX-sensitive peripheral nerve sodium channel type 4 (“PN4”). This version lacks most of the untranslated sequences, thereby comprising a 5934-base open reading frame, from nucleotide residue 22 of the XhoI-HindIII clone, the start site of translation, and ending at residue 5956. 
     SEQ ID NO:2 depicts an engineered version of the nucleotide cDNA sequence encoding the rat TTX-sensitive peripheral nerve sodium channel type 4a (“PN4a”). This version lacks most of the untranslated sequences, thereby comprising a 5964-base open reading frame, beginning at nucleotide residue 22 of the XhoI-HindHIII clone, the start site of translation, and ending at residue 5986. The 30 base pair insert is found at positions 2014-2043. 
     FIGS. 1A-1C (SEQ ID NO:3) depict the deduced amino acid sequence of PN4, represented in the single-letter amino acid code. Shown in FIG. 1A-1C are the homologous domains (I-IV); the putative transmembrane segments (S1-S6); the amino acid conferring sensitivity to TTX (Δ); potential cAMP-phosphorylation site (•); and potential N-glycosylation site (♦). 
     FIGS. 2A-2C (SEQ ID NO:4) depict the deduced amino acid sequence of PN4a, represented in the single-letter amino acid code. Shown in FIGS. 2A-2C are the homologous domains (I-IV); the putative transmembrane segments (S1-S6); the amino acid conferring sensitivity to TTX (Δ); potential cAMP-phosphorylation site (•); and potential N-glycosylation site (♦). 
     FIGS. 3A-3H (SEQ ID NOS:7 and 8 align the base pair sequences of the NaCh6 and the “native” version of the PN4 sodium channel cDNA clones (SEQ ID NOS:7 and 8, including untranslated sequences, depicting the differences in bold. Start and stop codons are underlined and primers are denoted by dashed lines with arrows. 
     FIGS. 4A-4D align the amino acid sequences of the PN4a (SEQ ID NO:4), PN4(SEQ ID NO:3), and NaCh6 sodium channel (SEQ ID NO:9) cDNA clones of FIGS. 3A-3H, depicting the differences in bold. 
     FIG. 5 is a comparison of the conserved region Interdomain I/II between PN4a (SEQ ID NO:10), PN4(SEQ ID NO:11), NaCh6(SEQ ID NO:12), and BrainII sodium channels (SEQ ID NO:13). Differences between PN4 (and PN4a) and NaCh6 are shown in bold type and differences between BrainII and PN4 are underlined. 
     SEQ ID NO:5 depicts the 696 nucleotide cDNA sequence encoding the novel probe CNaD4-2 used to identify the novel sodium channels of the invention. 
     SEQ ID NO:6 depicts the deduced amino acid sequence of probe CNaD4-2, represented in the single-letter amino acid code. 
     FIG. 6 depicts the cloning map of PN4 and PN4a. 
     FIG. 7 shows the properties of currents produced in  Xenopur oocytes  by injection of PN4 cRNA. FIG. 7 a  shows the current produced by sodium channels expressed in an oocyte; FIG. 7 b  shows the current-voltage relationship. 
     FIGS. 8 a  and  8   b  show steady state inactivation of sodium currents produced by PN4 in  Xenopur oocytes  . 
     FIG. 9 demonstrates the effects of the sodium channel β 1  and β 2  subunits upon PN4 function in  Xenopur oocytes  . FIG. 9 a  shows currents produced when the PN4I subunit is injected alone; FIG. 9 b  is with the β 1  subunit; FIG. 9 c  is with the β 2  subunit; and FIG. 9 d  is with both the β 1  and β 2  subunits. 
    
    
     DETAILED DESCRIPTION OF THE INVENTION 
     The present invention relates to novel sodium channel proteins. Specific embodiments include the α-subunit of such sodium channels that are TTX-sensitive. 
     In particular, the present invention relates to a purified and isolated DNA sequence encoding for a novel rat TTX-sensitive sodium channel protein and a splice variant thereof. The term “purified and isolated DNA” refers to DNA that is essentially free, i.e. contains less than about 30%, preferably less than about 10%, and more preferably less than about 1% of the DNA with which the DNA of interest is naturally associated. Techniques for assessing purity are well known to the art and include, for example, restriction mapping, agarose gel electrophoresis, and CsCl gradient centrifugation. The term “DNA” is meant to include cDNA made by reverse transcription of MRNA or by chemical synthesis. 
     Specifically, the invention encompasses DNA having the engineered versions (discussed in detail below) of the nucleotide sequences set forth in SEQ ID NOS:1 and 2 designated herein as nerve sodium channel types 4 and the splice variant 4a (PN4 and PN4a). These versions of the PN4 and PN4a sequence were produced by removing most of the untranslated sequences of the PN4 and PN4a cDNA and cloning into expression vectors for functional analysis. 
     The longer “native” version of PN4 is shown in FIGS. 3A-3H (SEQ ID NO:7). The complete “native” base pair sequence of PN4a has the same sequence shown in FIG.  3  and is labeled rPN4 with the 30 base pair insert after position 2050. The PN4 and PN4a DNA sequences comprise cDNA sequences that encode the α-subunit of novel voltage-gated, TTX-sensitive sodium channels, specifically the amino acid sequences set forth in FIGS. 1A-1C and  2  (SEQ ID NOS:3 and 4). DNA sequences encoding the same or allelic variant or analog sodium channel protein polypeptides of the nervous system, through use of, at least in part, degenerate codons are also contemplated by this invention. 
     The nucleotide sequences of SEQ ID NOS:1 and 2 correspond to the cDNAs from rat. PN4 shares greater than 99% homology with the rat sodium channel NaCh6, previously cloned from brain cDNA (Schaller, et al.,  J. Neurosci . 15:3231-3242 (1995)), and also greater than 99% homology with the orthologous mouse channel, Scn8a (Burgess, et al.,  Nature Genetics  10:61-465 (1995)), discounting the 738 bp deletion in the interdomain I/II region of Scn8a relative to PN4. A homology search provided that the next closest related sodium channel is found in the fugu (puffer fish), with 92% homology. The next closest channels are rat brain types I and II, at 87.9%, and rat brain type III, at 87.3%. Homology to all other known channels drops off significantly thereafter. 
     Additionally, it is believed that the novel voltage-gated, TTX-sensitive sodium channel is also expressed in tissue of other mammalian species such as humans, and that the corresponding gene is highly homologous to the rat sequence. Therefore, the invention includes cDNA encoding a novel mammalian voltage-gated, TTX-sensitive sodium channel. 
     The invention not only includes the entire protein expressed by the cDNA sequences of SEQ ID NOS:1 and 2, but also includes protein fragments. These fragments can be obtained by cleaving the full length proteins or by using smaller DNA sequences or polynucleotides to express the desired fragment. Accordingly, the invention also includes polynucleotides that can be used to make polypeptides of about 10 to 1500, preferably 10 to 100, amino acids in length. The isolation and purification of such recombinant polypeptides can be accomplished by techniques that are well known in the art, for example, preparative chromatographic separations or affinity chromatography. In addition, polypeptides can also be made by synthetic means which are well known in the art. 
     In general, sodium channels comprise an α- and one or more β-subunits. The β-subunits may modulate the function of the channel. However, since the β-subunit is all that is required for the channel to be fully functional, expression of the cDNA in SEQ ID NOS:1 and 2 will each provide a fully functional protein. The gene encoding the β 1 -subunit in nerve tissue was found to be identical to that found in rat heart, brain, and skeletal muscle. The cDNA of the β 1 -subunit is not described herein as it is well known in the art, see Isom, et al.,  Neuron  12:1183-1194 (1994). However, it is to be understood that by combining the known sequence for the β 1 -subunit with the α-subunit sequence described herein, one may obtain complete PN4 and PN4a rat voltage-gated, TTX-sensitive sodium channels. 
     Northern blot analysis indicates that PN4 and PN4a are each encoded by a˜7.5 kb/9.5 kb transcript. The nucleotide sequence analysis of the PN4 cDNA identifies a 5934-base open reading frame, shown in SEQ ID NO: 1, starting at base 22. The nucleotide sequence analysis of the PN4a cDNA identifies a 5964-base open reading frame, shown in SEQ ID NO:2, also starting at base 22. The deduced amino acid sequence of PN4, shown in FIGS. 1A-1C (SEQ ID NO:3), exhibits the primary structural features of an α-subunit of a voltage-gated, TTX-sensitive sodium channel. Shown in FIG. 1A-1C are the homologous domains (I-IV); the putative transmembrane segments (S1-S6); the amino acid conferring sensitivity to TTX (Δ); potential cAMP-phosphorylation site (•); and potential N-glycosylation site (♦). The deduced amino acid sequence of PN4a, shown in FIGS. 2A-2C (SEQ ID NO:4), also exhibits the primary structural features of an α-subunit of a voltage-gated, TTX-sensitive sodium channel. Shown in FIG. 2A-2C are the homologous domains (I-IV); the putative transmembrane segments (S1-S6); the amino acid conferring sensitivity to TTX (Δ); potential cAMP-phosphorylation site (•); and potential N-glycosylation site (♦). 
     Reverse transcription-polymerase chain reaction (degenerate oligonucleotide-primed “RT-PCR”) analysis of RNA from the rat central and peripheral nervous systems, in particular from rat dorsal root ganglia (“DRG”), was performed. Eight main tissue types were screened by f5 RT-PCR for expression of the unique PN4 genes corresponding to positions 4646-5203 of SEQ ID NO:1. PN4 was present in five of the tissues studied: brain, spinal cord, DRG, nodose ganglia, and superior cervical ganglia. PN4 was not present in the remaining tissues studied: sciatic nerve tissue, heart tissue, or skeletal muscle tissue. 
     Three main tissue types were screened by RT-PCR for expression of the unique PN4a genes corresponding to positions 1947-2135 of SEQ ID NO:2. PN4a was present in two of the tissues studied: spinal cord and DRG. PN4a was not present in brain tissue. 
     The invention also pertains to the cloning and functional expression in  Xenopur oocytes  of the novel PN4 and PN4a rat TTX-sensitive sodium channels. Specifically, the α-subunit of the sodium channels was cloned and expressed. Functional expression shows that PN4 and PN4a are voltage-gated, TTX-sensitive sodium channels with properties that are similar to other TTX-sensitive sodium channels. 
     Preferred aspects of this invention are PN4 cDNA sequences which encode for the novel mammalian TTX-sensitive sodium channel proteins that are expressed in brain, spinal cord, dorsal root ganglia, nodose ganglia, and superior cervical ganglia but not in sciatic nerve, heart, or skeletal muscle when assayed by the methods described herein, such as RT-PCR. 
     Also preferred aspects of this invention are PN4a cDNA sequences which encode for the novel mammalian TTX-sensitive sodium channel proteins that are expressed most strongly in DRG, with little expression in spinal cord and almost undetectable expression in brain when assayed by the methods described herein, such as RT-PCR. 
     cDNA sequences which encode for the novel PN4 TTX-sensitive sodium channel proteins that are predominantly expressed in the brain and spinal cord are also contemplated by this invention. cDNA sequences which encode for the novel PN4a TTX-sensitive sodium channel proteins that are predominantly expressed in the DRG are also contemplated by this invention. 
     The term “cDNA”, or complementary DNA, refers to single-stranded or double-stranded DNA sequences obtained by reverse transcription of MRNA isolated from a donor cell. For example, treatment of MRNA with a reverse transcriptase such as AMV reverse transcriptase or M-MuLV reverse transcriptase in the presence of an oligonucleotide primer will furnish an RNA-DNA duplex which can be treated with RNase H, DNA polymerase and DNA ligase to generate double-stranded cDNA. If desired, the double-stranded cDNA can be denatured by conventional techniques such as heating to generate single-stranded cDNA. The term “cDNA” includes cDNA that is a complementary copy of the naturally occurring mRNA, as well as complementary copies of variants of the naturally occurring MRNA, that have the same biological activity. Variants would include, for example, insertions, deletions, and sequences with degenerate codons and alleles. For example, PN4a is a splice variant of PN4, having a 10 amino acid insertion. 
     The term “cRNA” refers to RNA that is a copy of the MRNA transcribed by a cell. cRNA corresponding to MRNA transcribed from a DNA sequence encoding the α-subunit of a novel TTX-sensitive sodium channel protein is contemplated by this invention. 
     The present invention also includes expression vectors comprising the DNA or the cDNA described above, host cells transformed with these expression vectors capable of producing the sodium channel of the invention, and cDNA libraries comprising such host cells. 
     The term “expression vector” refers to any genetic element, e.g., a plasmid, a chromosome, a virus, behaving either as an autonomous unit of polynucleotide expression within a cell or being rendered capable of replication by insertion into a host cell chromosome, having attached to it another polynucleotide segment, so as to bring about the replication and/or expression of the attached segment. Suitable vectors include, but are not limited to, plasmids, bacteriophages, and cosmids. Vectors will contain polynucleotide sequences which are necessary to effect ligation or insertion of the vector into a desired host cell and to effect the expression of the attached segment. Such sequences differ depending on the host organism and will include promoter sequences to effect transcription, enhancer sequences to increase transcription, ribosomal binding site sequences, and transcription and translation termination sequences. 
     The term “host cell” generally refers to prokaryotic or eukaryotic organisms and includes any transformable or transfectable organism which is capable of expressing a protein and can be, or has been, used as a recipient for expression vectors or other transferred DNA. Host cells can also be made to express protein by direct injection with exogenous cRNA translatable into the protein of interest. A preferred host cell is the Xenopus oocyte. 
     The term “transformed” refers to any known method for the insertion of foreign DNA or RNA sequences into a host prokaryotic cell. The term “transfected” refers to any known method for the insertion of foreign DNA or RNA sequences into a host eukaryotic cell. Such transformed or transfected cells include stably transformed or transfected cells in which the inserted DNA is rendered capable of replication in the host cell. They also include transiently expressing cells which express the inserted DNA or RNA for limited periods of time. The transformation or transfection procedure depends on the host cell being transformed. It can include packaging the polynucleotide in a virus, as well as direct uptake of the polynucleotide, such as, for example, lipofection or microinjection. Transformation and transfection can result in incorporation of the inserted DNA into the genome of the host cell or the maintenance of the inserted DNA within the host cell in plasmid form. Methods of transformation are well known in the art and include, but are not limited to, viral infection, electroporation, lipofection, and calcium phosphate mediated direct uptake. 
     It is to be understood that this invention is intended to include other forms of expression vectors, host cells, and transformation techniques which serve equivalent functions and which become known to the art hereto. 
     The term “cDNA library” refers to a collection of clones, usually in a bacteriophage, or less commonly in bacterial plasmids, containing cDNA copies of mRNA sequences derived from a donor cell or tissue. 
     In addition, the present invention contemplates recombinant polynucleotides, of about 15 to 20kb, preferably 10 to l5kb nucleotides in length, comprising a nucleic acid sequence derived from the DNA of the invention. 
     The term “polynucleotide” as used herein refers to a polymeric form of nucleotides of any length, either ribonucleotides or deoxyribonucleotides. This term refers only to the primary structure of the molecule. Thus, this term includes double- and single-stranded DNA, as well as double- and single-stranded RNA. It also includes modified, for example, by methylation and/or by capping, and unmodified forms of the polynucleotide. 
     The term “derived from” a designated sequence, refers to a nucleic acid sequence that is comprised of a sequence of approximately at least 6-8 nucleotides, more preferably at least 10-12 nucleotides, and, even more preferably, at least 15-20 nucleotides that correspond to, i.e., are homologous or complementary to, a region of the designated sequence. The derived sequence is not necessarily physically derived from the nucleotide sequence shown, but may be derived in any manner, including for example, chemical synthesis or DNA replication or reverse transcription, which are based on the information provided by the sequences of bases in the region(s) from which the polynucleotide is derived. 
     Further, the term “polynucleotide” is intended to include a recombinant polynucleotide, which is of genomic, cDNA, semisynthetic, or synthetic origin which, by virtue of its origin or manipulation is not associated with all or a portion of the polynucleotide with which it is associated in nature and/or is linked to a polynucleotide other than that to which it is linked in nature. 
     The “native” version of PN4, and its splice variant PN4a, partially correspond to the sodium channel NaCh6, described in Schaller, K. L. et al.,  J. Neurosci . 15(5):3231-3242 (1995) as shown in FIGS. 3 and 4. In FIG. 3, base pair sequences of the native PN4 and PN4a sodium channel cDNA clones include untranslated sequences. The applicants believe that the published NaCh6 sequence does not correctly provide the sodium channel sequence, and that the sequences for PN4 and PN4a represent the authentic sodium channel sequence for the following reasons. 
     First, most sodium channel gene coding regions, including PN4, begin with an eleven base pair sequence consisting of an out of frame ATG, followed by five base pairs downstream, followed by the ATG initiation codon for the coding region. The DNA sequence alignment (FIG. 3) shows a two base pair deletion in NaCh6 overlapping the second ATG, so that the normally out of frame, upstream ATG becomes the NaCh6 initiation codon, leading to a two amino acid insertion. Start and stop codons are underlined and primers are denoted by dashed lines with arrows. 
     Examination of the DNA sequence alignment (FIG. 3) shows that the bulk of the differences (residues in bold print) between the two sequences that would strongly influence protein function consist of a series of nine single base deletions in the Interdomain I/II region These differences lead to a very different amino acid sequence, as shown in the amino acid alignment of FIGS. 4A-4D, where the differences between the two sequences are again shown in bold print. The applicants&#39; sequencing of multiple isolates resulting from the cloning of up to 1.5kb of the Interdomain I/II region by PCRrepeatedly resulted in sequences which completely agreed with PN4 or PN4a sequences. 
     Comparison of PN4 and PN4a sequences to other sodium channel sequences shows a high degree of homology. For example, FIG. 5 is a comparison of PN4 and PN4a with NaCh6 and rat Brain type II in this region. Whereas PN4 and BrainII share about 50% identity in the region highlighted in bold, NaCh6 is almost completely different. The differences between BrainII and PN4 are underlined. 
     The applicants also employed PCR to look specifically for NaCh6. A sense primer common to both sequences (CAATCGTGGGCGCCCTAATC (SEQ ID NO:14), corresponding to base pair 722-742 of NaCh6 and shown by dashed lines with an arrow in FIGS. 3A-3H at bases 884-904 of PN4) was paired with gene specific antisense primers (TGCTTTCATGCACTGGAATCCCTCT (SEQ ID NO:15), corresponding to base pair 1194-1170 of PN4, and TGCTTTACTGCACTGGAATCCTTCG (SEQ ID NO:10), fs corresponding to base pair 1029-1005 of NaCh6; sequence differences between the two primers are underlined). The antisense primers prime at a three base pair deletion of NaCh6 relative to PN4 and overlap three other sequence differences, as shown in FIGS. 3A-3H. A PCR product of the expected size (about 300 base pairs) was obtained with the PN4 specific antisense primer using pBK-CMV/75-1.4 DNA (described in the description of SEQ ID NO:2) and with rat Brain and rat DRG cDNA templates. No PCR products were obtained from these templates with the NaCh6 specific primer. 
     Any of the sequence differences between PN4 and NaCh6 could result in an inability of the NaCh6 gene to form a functional channel. However, some differences could be ascribed to “base calling.” The applicants have repeatedly sequenced full length versions of PN4 and PN4a to verify the accuracy of the sequence. Of the amino acid differences between PN4 and NaCh6, it appears that the profound differences in the Interdomain I/II region are responsible for the lack of success in expression of the NaCh6 gene. The nine single base deletions in this region appear to shift the reading frame (see FIGS. 3A-3H and FIGS.  4 A- 4 D), leading to a “nonsense” peptide which lacks a number of highly conserved residues (FIG. 5) and which could sufficiently disrupt the structure of the protein to destroy its function. 
     The splice variant PN4a is similar to and occurs in a homologous position to that seen with rat type Brainl and la channels (Schaller, K. L, et al.,  J. Neurosci  12:1370-1381 (1992)). In each case, it appears that the variants make use of the same 3′ splice acceptor sites but alternative 5′sites. Rat BrainIII also has splice variants in this region, using the same 3′ splice site but using alternative 5′ sites more 5′ than the other channels. An amino acid comparison with other rat(r) and human(h) channels is shown below. Not all sodium channels have this splicing pattern. 
     
       
         
           
               
               
               
            
               
                 rPN4 
                 GRLLPE ........... AT.TEVE 
                 (SEQ ID NO:17) 
               
               
                   
               
               
                 rPN4a 
                 GRLLPE VKIDKAAT.DS AT.TEVE 
                 (SEQ ID NO:18) 
               
               
                   
               
               
                 rBRAIN1 
                 GQLLPE VIIDKPATDDN GTTTETE 
                 (SEQ ID NO:19) 
               
               
                   
               
               
                 rBRAIN1a 
                 GQLLPE ........... GTTTETE 
                 (SEQ ID NO:20) 
               
               
                   
               
               
                 rPN1 
                 GQLLPE VIIDKATSDDS GTTNQIH 
                 (SEQ ID NO:21) 
               
               
                   
               
               
                 hNE-Na 
                 GQLLPE ........... GTTNQIH 
                 (SEQ ID NO:22) 
               
               
                   
               
               
                 rBRAIN2 
                 GQLLPE ........... GTTTETE 
                 (SEQ ID NO:23) 
               
               
                   
               
               
                 rBRAIN3 
                 ...... ........... GTTTETE 
                 (SEQ ID NO:24) 
               
               
                   
               
               
                 rCARDIAC 
                 SYLLRP MVLDRPP..DT TTPSEEP 
                 (SEQ ID NO:25) 
               
            
           
         
       
     
     It is interesting to note that the species of rat PN 1 is similar to PN4a in this location, whereas its human orthologue, the neuroendocrine channel, hNE-Na (Klugbauer, et al.,  EMBO J . 14:1084-1090 (1995)), is similar to PN4. Perhaps each of these will be found to be one of a set of splice variants. Whereas the splicing patterns of BrainI, IL and III were found not to vary across a range of tissues (Schaller, K.L., et al.,  J. Neurosci . 12:1370-1381 (1992)), PN4 and PN4a show dramatic abundance differences. PN4 has a gradient of expression with high expression in brain, intermediate in spinal cord, and relatively the least in DRG. PN4a is very low or undetectable in brain, a minor fraction of total PN4 expression in spinal cord, and nearly as abundant as PN4 in DRG. 
     Uses of the Invention 
     Many uses of the invention exist, a few of which are described below. 
     1. Probe for human channel. 
     As mentioned above, it is believed that homologs of the novel rat TTX-sensitive sodium channel described herein are also expressed in mammalian nerve tissue, in particular, human tissue. The entire cDNAs of PN4 and PN4a rat sodium channels of the present invention can be used as a probe to discover whether novel PN4 and PN4a voltage-gated, TTX-sensitive sodium channels exist in human nerve tissue and, if they do, to aid in isolating the cDNAs for the human protein. 
     The human homologues of the rat TTX-sensitive PN4 and PN4a channels can be cloned using a human DRG cDNA library. Human DRG are obtained at autopsy. The frozen tissue is homogenized and the RNA extracted with guanidine isothiocyanate (Chirgwin, et al.,  Biochernistry  18:5294-5299, 1979). The RNA is size-fractionated on a sucrose gradient to enrich for large mRNAs because the sodium channel α-subunits are encoded by large (7-11 kb) transcripts. Double-stranded cDNA is prepared using the SuperScript Choice cDNA kit (GIBCO BRL) with either oligo(dT) or random hexamer primers. EcoRI adapters are ligated onto the double-stranded cDNA, which is then phosphorylated. The cDNA library is constructed by ligating the double-stranded cDNA into the bacteriophage-lambda ZAP II vector (Stratagene) followed by packaging into phage particles. 
     Phage are plated out on 150 mm plates on a lawn of XLI-Blue MRF bacteria (Stratagene) and plaque replicas are made on Hybond N nylon membranes (Amersham). Filters are hybridized to rat PN4 and PN4a cDNA probes by standard procedures and detected by autoradiography or chemiluminescence. The signal produced by the rat PN4 and PN4a probes hybridizing to positive human clones at high stringency should be stronger than obtained with rat brain sodium channel probes hybridizing to these clones. Positive plaques are further purified by limiting dilution and re-screened by hybridization or PCR. Restriction mapping and polymerase chain reaction will identify overlapping clones that can be assembled by standard techniques into the full-length human homologue of rat PN4 and PN4a. The human clone can be expressed by injecting cRNA transcribed in vitro from the full-length cDNA clone into  Xenopur oocytes  , or by transfecting a mammalian cell line with a vector containing the cDNA linked to a suitable promoter. 
     2. Probe for Obtaining Molecular Data. 
     The polynucleotides of the invention can be bound to a reporter molecule to form a polynucleotide probe useful for Northern and Southern blot analysis and in situ hybridization. 
     The term “reporter molecule” refers to a chemical entity capable of being detected by a suitable detection means, including, but not limited to, spectrophotometric, chemiluminescent, immunochemical, or radiochemical means. The polynucleotides of this invention can be conjugated to a reporter molecule by techniques well known in the art. Typically the reporter molecule contains a functional group suitable for attachment to or incorporation into the polynucleotide. The functional groups suitable for attaching the reporter group are usually to activated esters or alkylating agents. Details of techniques for attaching reporter groups are well known in the art. See, for example, Matthews, J. A., Batki, A., Hynds, C., and Kricka, L. J.,  Anal. Biochem ., 151:205-209 (1985) and Engelhardt, et al., European Patent Application No. 0 302 175. 
     3. Antibodies Against PN4 and PN4a. 
     The polypeptides of the invention are highly useful for the development of antibodies against PN4 and PN4a. Such antibodies can be used in affinity chromatography to purify recombinant sodium channel proteins or polypeptides, or they can be used as a research tool. For example, antibodies bound to a reporter molecule can be used in histochemical staining techniques to identify other tissues and cell types where PN4 and PN4a are present, or they can be used to identify epitopic or functional regions of the sodium channel protein of the invention. 
     The antibodies can be monoclonal or polyclonal and can be prepared by techniques that are well known in the art. Polyclonal antibodies are prepared as follows: an immunogenic conjugate comprising PN4, PN4a, or a fragment thereof, optionally linked to a carrier protein, is used to immunize a selected mammal such as a mouse, rabbit, goat, etc. Serum from the immunized mammal is collected and treated according to known procedures to separate the immunoglobulin fraction. 
     Monoclonal antibodies are prepared by standard hybridoma cell technology based on that reported by Kohler and Milstein in  Nature  256:495-497 (1975): spleen cells are obtained from a host animal immunized with the PN4 or PN4a protein or a fragment thereof, optionally linked to a carrier. Hybrid cells are formed by fusing these spleen cells with an appropriate myeloma cell line and cultured. The antibodies produced by the hybrid cells are screened for their ability to bind to expressed PN4 or PN4a proteins. 
     A number of screening techniques well known in the art, such as, for example, forward or reverse enzyme-linked immunosorbent assay screening methods may be employed. The hybrid cells producing such antibodies are then subjected to recloning and high dilution conditions in order to select a hybrid cell that secretes a homogeneous population of antibodies specific to either the PN4 or PN4a protein. 
     In addition, antibodies can be raised by cloning and expressing nucleotide sequences or mutagenized versions thereof coding at least for the amino acid sequences required for specific binding of natural antibodies, and these expressed proteins used as the immunogen. Antibodies may include the complete immunoglobulin or a fragment thereof. Antibodies may be linked to a reporter group such as is described above with reference to polynucleotides. 
     4. Therapeutic Targets for Disorders. 
     The present invention also includes the use of the novel voltage-gated, TTX-sensitive sodium channel α-subunit as a therapeutic target for compounds to treat disorders of the nervous system including, but not limited to, epilepsy, stroke injury, brain injury, allodynia, hyperalgesia, diabetic neuropathy, traumatic injury, and AIDS-associated neuropathy. The invention allows for the manipulation of genetic materials by recombinant technology to produce polypeptides that possess the structural and functional characteristics of the novel voltage-gated, TTX-sensitive sodium channel α-subunit found in nerve tissue, particularly in sensory nerves. Site directed mutagenesis can be used to provide such recombinant polypeptides. For example, synthetic oligonucleotides can be specifically inserted or substituted into the portion of the gene of interest to produce genes encoding for and expressing a specific mutant. Random degenerate oligonucleotides can also be inserted and phage display techniques can be used to identify and isolate polypeptides possessing a functional property of interest. 
     5. Designing Therapeutics based on Inhibiting PN4 and PN4a and Assays thereof. 
     This invention is also directed to inhibiting the activity of PN4 in brain, spinal cord, DRG, nodose ganglia, and superior cervical ganglia tissues. This invention is also directed to inhibiting the activity of PN4a in spinal cord and DRG tissues. However, it is to be understood that further studies may reveal that PN4 and PN4a are present in other tissues, and as such, those tissues can also be targeted areas. For example, the detection of PN4 mRNA in nodose ganglia suggests that PN4 may conduct TTX-sensitive sodium currents in this and other sensory ganglia of the nervous system. 
     In addition, it has been found that proteins not normally expressed in certain tissues are expressed in a disease state. Therefore, this invention is intended to encompass the inhibition of PN4 and PN4a in tissues and cell types where the protein is normally expressed, and in those tissues and cell types where the protein is only expressed during a disease state. 
     The invention also pertains to an assay for inhibitors of the novel TTX-sensitive sodium channel protein comprising contacting a compound suspected of being an inhibitor with expressed sodium channel and measuring the activity of the sodium channel. The compound can be a substantially pure compound of synthetic origin combined in an aqueous medium, or the compound can be a naturally occurring material such that the assay medium is an extract of biological origin, such as, for example, a plant, animal, or microbial cell extract. PN4 and PN4a activity can be measured by methods such as electrophysiology (two electrode voltage clamp or single electrode whole cell patch clamp), guanidinium ion flux assays, and toxin-binding assays. An “inhibitor” is defined as generally that amount that results in greater than 50% decrease in PN4 or PN4a activity, preferably greater than 70% decrease in PN4 or PN4a activity, more preferably greater than 90% decrease in PN4 or PN4a activity. 
     6. Designing and Screening for Additional Therapeutics. 
     Another significant characteristic of PN4 is that it is TTX-sensitive. It is believed that TTX-sensitive sodium channels play a key role in transmitting nerve impulses relating to sensory inputs such as pain and pressure. This will also facilitate the design of therapeutics that can be targeted to a specific area such as nerve tissue. 
     Additionally, the recombinant protein of the present invention can be used to screen for potential therapeutics that have the ability to inhibit the sodium channel of interest. In particular, it would be useful to inhibit selectively the function of sodium channels in nerve tissues responsible for transmitting pain and pressure signals without simultaneously affecting the function of sodium channels in other tissues such as heart and muscle. Such selectivity would allow for the treatment of pain without causing side effects due to cardiac or neuromuscular complications. Therefore, it would be useful to have DNA sequences coding for sodium channels that are selectively expressed in nerve tissue. 
     7. Pain Reliever. 
     Sodium channels in nerve tissue play a large role in the transmission of nerve impulses, and therefore are instrumental in understanding neuropathic pain transmission. Neuropathic pain falls into two categories: allodynia, where a normally non-painful stimulus becomes painful, and hyperalgesia, where a usually normal painful stimulus becomes extremely painful. The ability to inhibit the activity of these sodium channels, i.e., reduce the conduction of nerve impulses, will affect the nerve&#39;s ability to transmit pain. Selective inhibition of sodium channels in sensory neurons such as dorsal root ganglia will allow the blockage of pain impulses without complicating side effects caused by inhibition of sodium channels in other tissues such as brain and heart. In addition, certain diseases are caused by sodium channels that produce impulses at an extremely high frequency. The ability to reduce the activity of the channel can then eliminate or alleviate the disease. Accordingly, potential therapeutic compounds can be screened by methods well known in the art, to discover whether they can inhibit the activity of the recombinant sodium channel of the invention. Barram, M., et al.,  Naun-Schmiedeberg&#39;s Archives of Pharmacology , 347:125-132 (1993) and McNeal, E. T., et al.,  J. Med. Chem ., 28:381-388 (1985). For similar studies with the acetyl choline receptor, see, Claudio, et al., Science, 238:1688-1694 (1987). 
     Accordingly, the present invention encompasses a method of alleviating pain by inhibiting the activity of the novel TTX-sensitive sodium channel comprising administering a therapeutically effective amount of a compound having an IC 50  in the range of 0.1-50 nM, preferably within the range of 1-25 nM, and more preferably within the range of 1-5 nM. Potential therapeutic compounds are identified based on their ability to inhibit the activity of PN4 and PN4a. Therefore, the aforementioned assay can be used to identify compounds having a therapeutically effective IC 50 . 
     The term “IC 50 ” refers to the concentration of a compound that is required to inhibit by 50% the activity of expressed PN4 or PN4a when activity is measured by electrophysiology, flux assays, and toxin-binding assays, as mentioned above. 
     The basic molecular biology techniques employed in accomplishing features of this invention, such as RNA, DNA, and plasmid isolation, restriction enzyme digestion, preparation and probing of a cDNA library, sequencing clones, constructing expression vectors, transforming cells, maintaining and growing cell cultures, and other general techniques are well known in the art, and descriptions of such techniques can be found in general laboratory manuals such as Molecular Cloning: A Laboratory Manual by Sambrook, et al. (Cold Spring Harbor Laboratory Press, 2nd edition, 1989). Accordingly, the following examples are merely illustrative of the techniques by which the invention can be practiced. 
     
       
         
           
               
             
               
                   
               
             
            
               
                 Abbreviations 
               
            
           
           
               
               
            
               
                 BSA 
                 bovine serum albumin 
               
               
                 Denhardt&#39;s 
                 0.02% BSA, 0.02% polyvinyl-pyrrolidone, 0.02% Ficoll 
               
               
                 solution 
                 (0.1 g BSA, 0.1 g Ficoll and 0.1 g polyvinylpyrrolidone 
               
               
                   
                 per 500 ml) 
               
               
                 DRG 
                 dorsal root ganglia 
               
               
                 EDTA 
                 Ethylenediaminetetraacetic acid, tetrasodium salt 
               
               
                 MEN 
                 20 mM MOPS, 1 mM EDTA, 5 mM sodium acetate, 
               
               
                   
                 pH 7.0 
               
               
                 MOPS 
                 3-(N-morpholino)propanesulfonic acid 
               
               
                   
                 (Sigma Chemical Company) 
               
               
                 PN3 
                 peripheral nerve sodium channel type 3 
               
               
                 PNS 
                 peripheral nervous system 
               
               
                 SDS 
                 sodium dodecyl sulfate 
               
               
                 SSC 
                 150 nM NaCl, 15 mM sodium citrate, pH 7.0 
               
               
                 SSPE 
                 80 mM NaCl, 10 mM sodium phosphate, 1 mM 
               
               
                   
                 ethylenediaminetetraacetate, pH 8.0 
               
               
                 TEV 
                 two electrode voltage clamp 
               
               
                 TTX 
                 tetrodotoxin (Sigma Chemical Company) 
               
               
                 UTR 
                 untranslated region 
               
               
                   
               
            
           
         
       
     
     EXAMPLES 
     Each step employed in obtaining the DNA of the novel sodium channel of the invention is described in the detailed examples below. The following is an overview of the steps. Example 1 describes how a novel probe, CNaD4-2, was obtained by designing primers based on known sodium channels. Example 2 describes the construction and screening of a cDNA library with CNaD4-2 to obtain the 3′ end of the novel sodium channel of the invention. Then a known primer was employed to obtain the 5′ end of the DNA of the invention. Example 3 describes how RT-PCR was employed to span the gap, between the 3′ and 5′ ends obtained from the cDNA library. This resulted in a 798 base pair sequence and a splice variant thereof, having a 828 base pair sequence. Example 4 describes assembling the clones into two full-length cDNA clones in expression vectors. The cloning map is illustrated in FIG.  6 . Example 5 discusses the tissue distribution and localization accomplished by RT-PCR. Example 6 discusses the northern analysis of mRNA. Example 7 discloses obtaining expression data from  Xenopur oocytes  , and localization by RT-PCR. 
     Materials 
     The plasmid pBK-CMV was obtained from Stratagene (La Jolla, Calif.); plasmid Litmus 29 was obtained from New England Biolabs (Beverly, Mass.); the oocyte expression vector plasmid pBSTAcIIr was constructed from pBSTA (obtained from A. Goldin at the University of California, Irvine and described by Goldin, et al., in  Methods in Enzymology  (Rudy &amp; Iverson, eds.) 207:279-297) by insertion of a synthetic oligonucleotide linker; the mammalian cell expression vector plasmid pCI-neo was obtained from Promega (Madison, Wis.); plasmid pCRII was obtained from Invitrogen (San Diego, Calif.). Competent  E. Coli  cell lines STBL2TM and SURE® were obtained from GIBCO/BRL and Stratagene, respectively. 
     EXAMPLE 1 
     Identification of a novel channel fragment 
     A novel probe used to identify the novel sodium channels was obtained as follows. Degenerate oligonucleotide primers were designed based on the homologies between known sodium channels in domain IV and used to perform RT-PCR on RNA isolated from rat DRG. The domain IV PCR products were cloned into pCRII, transformed into  E. coli , and single colonies isolated. DNA sequence of the inserts of several of these colonies was obtained, including the following novel sequence from clone pCRII/CNaD4-2 of SEQ ID NO:5, identified as CNaD4-2. SEQ ID NO:6 depicts the deduced amino acid sequence of probe CNaD4-2, represented in the single-letter amino acid code. 
     CNaD4-2 can be made with standard PCR techniques. 
     EXAMPLE 2 
     Construction and screening of cDNA library from rat DRG with probe CNaD4-2 
     EcoRI-adapted cDNA was prepared from normal adult male Sprague-Dawley rat DRG poly(A)+ RNA using the SuperScript Choice System (GIBCO BRL). cDNA (&gt;4kb) was selected by sucrose gradient fractionation as described by Kieffer,  Gene  109:115-119 (1991). The cDNA was then ligated into the Zap Express vector (Stratagene) and packaged with the Gigapack II XL lambda packaging extract (Stratagene). Plate lysates were prepared and screened by PCR using CNaD4-2 specific primers (ACACTCAGAGCAAGCAGATGG (SEQ ID NO: 26) and TCCCTGGGTGCTCTTTGTCCA (SEQ ID NO: 27), corresponding to bases 32 to 52 and 569 to 589 of SEQ ID NO:5, respectively). Phage from one positive lysate were screened by filter hybridization with a  32 P-labeled probe (the 700 base pair EcoRI insert from CNaD4-2). Filters were hybridized in 50% formamide, 5× SSPE, 5× Denhardt&#39;s solution, 0.5% SDS, 250 μg/ml sheared, denatured salmon sperm DNA, and 5OmM sodium phosphate at 42° C. and washed in 0.5×SSC, 0.1% SDS at 50° C. Positive clones were excised in vivo into pBK-CMV using the ExAssist/XLOLR system (Stratagene). 
     Approximately 95% of these clones contained sodium channel sequence under standard screening stringency conditions. The number of clones that are retrieved that contain sodium channel sequence can be increased with increased stringency conditions and careful analysis and interpretation of data. It is well known in the art when screening for a particular type of DNA sequence, other types of DNA sequences will also be hybridized, depending on the specificity of the probe. Here, with the careful designed probe of the invention, the approximate 95% “hit” rate makes this fragment an exceptionally good sodium channel probe. 
     One of these clones, pBK-CMV/PN4.10-1, contained sequence of the CNaD4-2 channel from domain II through the 3′ UTR. The position of the pBK-CMV/PN4.10-1 fragment in the PN4 and PN4a cloning map is shown in FIG.  6 . In FIG. 6, ATG is the start codon, TAG is the stop codon and ∇ is the position of the PN4a splice insert. 
     A degenerate primer designed for sodium channels in domain I (ACCAACTG[T/C]GT[G/A]TT[T/C]ATGAC (SEQ ID NO:28)) was paired with a PN4 specific primer from the domain II region of pBK-CMV/PN4.10-1 (CAGCAGCTACAGTGGCTACA (SEQ ID NO:29)). These primers amplified a ca 1.5kb fragment from rat brain and from rat DRG which was shown by sequencing to represent much of the 5′ end of PN4, thus verifying that the primers would work for screening the library. The primers were then used to screen plate lysates of the DRG cDNA library by PCR. Positive lysates were plated and individual plaques picked and screened by PCR using the same primers. Positive clones were excised in vivo into pBK-CMV using the ExAssist/XLOLR system. One of these, pBK-CMV/75-1.4, was found to contain PN4 sequence from the 5′ UTR to the interdomain I/II region, but not to domain II, possibly due to rearrangement during the excision process. The position of the pBK-CMV/75-1.4 fragment in the PN4 and PN4a cloning map is shown in FIG.  6 . 
     EXAMPLE 3 
     Cloning the interdomain I/II region 
     The gap between pBK-CMV/75-1.4 and pBK-CMV/PN4.10-1 was cloned by RT-PCR on rat DRG and brain total RNA using specific primers: AAAGAGGCCGAGTTCAAGGC (SEQ ID NO:30) (a base pair sequence of pBK-CMV/75-1.4) and TGTCCTTCCGTCCGTAGG (SEQ ID NO:31) (a base pair sequence of pBK-CMV/PN4.10-1). PCR products were cloned into plasmid pCRII and sequenced. Two distinct sequences, FA-2 and FA-7 (see FIG.  6 ), were cloned from DRG. These were found to be identical except for the presence of a 30 base pair insert (found at base pairs 2014-2043 in SEQ ID NO:2 and depicted by an upside triangle at the position of insertion in FA-7, FJ-13, and PN4a in FIG.  6 ), with sequence identity to pBK-CMV/75-1.4 and pBK-CMV/PN4.10-1 in the regions where they overlap. RT-PCR on rat brain RNA yielded only clones which lacked the 30 base pair insert. This insert is homologous to a splice variant of the NaChI channel (NaChIa) and likely results from alternative 5′ splice site usage (Schaller, K. L., et al.,  J. Neurosci . 12:1370-1381 (1992)). 
     Additional RT-PCR was performed on rat DRG RNA using primers TTCATGGGGAACCTTCGAAAC (SEQ ID NO:32) (a base pair sequence of pBK-CMV/75-1.4) and GAACGATGCAGATGGTGATGGCTAA (SEQ ID NO:33) (a base pair sequence of pBK-CMV/PN4.10-1). The 1.5 kb PCR product was cloned into pCRII; six out of twenty isolates were positive for the 30 base pair insert variant by PCR. The sequence obtained for one of these, FJ-13, position shown in FIG. 6, was identical to that expected from the sequences of pBK-CMV/75-1.4, FA-7, and pBK-CMV/PN4. 10-1, thus confirming that these clones all originated from the same transcript. 
     EXAMPLE 4 
     Assembly of full-length PN4 clones in expression vectors 
     Unsuccessful attempts have been made to create and stabilize full-length sodium channel cDNA sequences. In U.S. Pat. No. 5,380,836, the cDNA sequence for a rat cardiac sodium channel protein was contained in three separate plasmids. In order to create full-length functional PN4 genes, the 5′ end was modified: suitable restriction sites were added and the upstream out-of-frame initiation codon was removed. The modified pBK-CMV75-1.4 and FA-2 sequences were fused together, then combined with the remaining portion of PN4 from pBK-CMV/PN4.10-1 in suitable expression vectors. PCR was employed to assemble the 5′ portion of PN4 from the initiation codon to domain II. A 1.43kb PCR fragment was generated from pBK-CMV/75-1.4 using the following primers: (1) 
     GAAGCTCGAGCCCGGGCAAGAGAAGATGGCAGCGCGG (SEQ ID NO:34) (Xho-I Srf-I restriction sites underlined, initiation codon in bold, PN4 homology in italics, a base pair sequence of pBK-CMV/75-1.4) and primer (2) CTCGGAGAGCCTACCCCATC (SEQ ID NO:35) (a base pair sequence of pBK-CMV/75-1.4 and a base pair sequence of FA-2). A 0.69 kb PCR fragment was generated from FA-2 using primer (3) AGAAGGGGAAGATGGGGTAGG (SEQ ID NO:36) (a base pair sequence of FA-2 and a base pair sequence of pBK-CMV/75-1.4) and primer (4) ATTCTGTCCTTCCGTCCGTAG (a base pair sequence of FA-2 and a base pair sequence of pBK-CMV/PN4.10-1). These fragments were gel purified and then a small fraction of each was combined as template in a further PCR reaction using primers (1) and (4). The fragments share a 31 base pair region of overlap at their 3′ and 5′ ends respectively, and therefore can act as primers to fuse the two fragments together (Horton, R. M., et al. (1991) Gene 77:61-68). The 2.1kb PCR product was cloned into pCRII and several isolates were sequenced, one of which, FD-8, had the expected sequence. The position of FD-8 in the PN4 and PN4a clones is shown in the cloning map of FIG.  6 . 
     To facilitate cloning into pBSTA and pCI-neo, it was determined to introduce an XbaI site at the 3′ end. To accomplish this, the PN4 domain II to 3′ UTR region was subcloned from pBK-CMV/PN4.10-1 from the EcoRI site of the vector to the HindIII site 14 base pairs from the PN4 stop codon into EcoRI plus HindIII digested Litmus 29. The resulting clone was labeled FC-1. The position of FC-1 in the PN4 and PN4a clones is shown in the cloning map of FIG.  6 . 
     To assemble the full length PN4, the 5′ portion was subcloned from FD-8 as a 2.0 kb Xho I-Eco NI fragment together with the 3′ portion from FC-1 as a 4.0 kb Eco NI-Xba-I fragment into Xho-I plus Xba-I digested pBSTAcIIr. One of the resulting isolates was found to have the correct sequence and was named pBSTAcII_PN4(FU-7A). 
     The splice variant, PN4a, was assembled by replacing the 1.3kb Sph I—Acc I region of pBSTAcIIr_PN4(FU-7A) with the corresponding fragment from FJ-13, to form pBSTAcIIr_PN4a(FZA-3), and confirmed by DNA sequencing 
     PN4 and PN4a were recloned into pCI-neo as 6.0 kb Xho-I to Xba-I fragments to form pCI-neo-PN4(GAII-1) and pCI-neo-PN4a(GCII-2), respectively, and confirmed by DNA sequencing. The sequences of the coding regions as cloned in the oocyte and mammalian cell expression vectors of PN4 and PN4a are SEQ ID NO:1 and SEQ ID NO:2, respectively. 
     Growth of fragments of PN4 or PN4a was accomplished under standard conditions; however, growth of plasmids containing full length constructs of PN4 and PN4a (in pCIneo or pBSTAcIIr) could not be accomplished without use of special growth media, conditions, and  E. coli  strains. The following proved to be optimal: (1) Use of  E. coli  STBL2™ for primary transformation following ligation reactions; for large scale culturing the primary transformants in STBL2™ cells were used, but secondary transformants in SURE® cells were used later if necessary. These  E. coli  strains have altered genotypes which allow the stable propagation of plasmids containing unstable inserts. (2) Solid media was 1/2× FM (see below) plus either 1× YENB (Bacto Yeast Extract, 0.75%, Bacto Nutrient Broth, 0.8%; Sharma, R. C. and Schimike, R. T., Biotechniques 20: 42-44, 1996), 1× YET (Bacto Yeast Extract, 0.75%, Bacto Tryptone, 0.8%), or 1× LB (Tryptone, 1%, Yeast Extract, 0.5%, NaCl, 0.5%), plus 15 g/L agar. (3)Liquid media optimally was 1× FM plus 1/2× LB. (4) Carbenicillin, 100μg/ml, was used for all media, as it is metabolized less rapidly than ampicillin. However, carbenicillin may be used within the range of 50-200 μg/ml; and more preferably within the range of 75-125 μg/ml. (5) Temperature for growth should be no greater than 30° C., usually 28° C.; this necessitated longer growth periods than normally employed, from 36 to 48 hours. 
     The recipe for 2× Freezing Medium (2×FM) is K2HPO4, 12.6 g; Na3Citrate, 0.9 g; MgSO4.7H20, 0.18 g; (NH4)2SO4, 1.8 g; KH2PO4, 3.6 g; Glycerol, 88 g; H2O, qs to 1 L. 
     2×FM and the remaining media components are prepared separately, sterilized by autoclaving, cooled to at least 60° C., and added together to form the final medium. Carbenicillin is prepared at 25 mg/ml H2O and sterilized by filtration. 2×FM was first described for preparation of frozen stocks of bacterial cells (Practical Methods in Molecular Biology, Schleif, R. F. and Wensink, P. C., Springer-Verlag, New York (1981) pp201-202). 
     EXAMPLE 5 
     Tissue distribution by RT-PCR 
     Brain, spinal cord, DRG, nodose ganglia, superior cervical ganglia, sciatic nerve, hearts and skeletal muscle tissue were isolated from anesthetized, normal adult male Sprague-Dawley rats and were stored at −80° C. RNA was isolated from each tissue using RNAzol (Tel-Test, Inc.). Random-primed cDNA was reverse transcribed from 500 ng of RNA from each tissue. The CNaD4-2 specific primers ACACTCAGAGCAAGCAGATGG (SEQ ID NO:38) and TCCCTGGGTGCTCTTTGTCCA (SEQ ID NO:39) (see above) defined a 558 base pair amplicon and would not discriminate between PN4 and PN4a. Thermal cycler parameters were 30 s/94° C., 30 s/64° C., 1 min/72° C. (24 cycles (confirmation experiment: 34 cycles)), 30 s/94° C., 30 s/64° C., 30 s/64° C. (1 cycle). A positive control (pCRII/CNaD4-2) and a no-template control were also included. cDNA from each tissue was also PCR amplified using primers specific for glyceraldehyde-3-phosphate dehydrogenase to demonstrate template viability, as described by Tso, et al.,  Nucleic Acid Res . 13:2485-2502 (1985). 
     Tissue distribution profile of PN4 by analysis of RNA from selected rat tissues by RT-PCR was as follows: 
     
       
         
           
               
               
               
             
               
                   
                   
               
               
                   
                 Tissue 
                 RT-PCR (35 cycles) 
               
               
                   
                   
               
             
            
               
                   
                 Brain 
                 + + + + + 
               
               
                   
                 Spinal cord 
                 + + + 
               
               
                   
                 DRG 
                 + + 
               
               
                   
                 Nodose ganglia 
                 + + 
               
               
                   
                 Superior cervical ganglia 
                 + 
               
               
                   
                 Sciatic nerve 
                 − 
               
               
                   
                 Heart 
                 − 
               
               
                   
                 Skeletal muscle 
                 − 
               
               
                   
                   
               
            
           
         
       
     
     PN4 was also detected after only 25 cycles (24+1) in the same five tissues as above in the same relative abundance. 
     Since PN4 differs from PN4a by only 30 base pairs, a new sense primer, GGTGGACTGCAACGGCGTA (SEQ ID NO:40) (corresponding to the same base pair sequences of FA-2 and FA-7), was employed. RT-PCR using this primer together with primer ATTCTGTCCTTCCGTCCGTAG (SEQ ID NO:41) (primer 4 above) gave amplicons of 159 base pairs from PN4 and 189 base pairs from PN4a. Thermal cycler parameters were 1 min/95° C., 20sec/94° C., 30 sec/60° C., 1 min/72° C., 8 cycles, 20sec/94° C., 30 sec/58° C., 1 min/72° C., 27 cycles, 3 min/72° C. PN4a was nearly as abundant as PN4 in DRG, much less abundant than PN4 in spinal cord, and almost undetectable in brain. This correlates well with cloning data; based on sequenced, cloned RT-PCR fragments which included the 30 base pair insert region, PN4a was found in 40% of isolates from DRG (9/24), but not found from brain (0/4). 
     
       
         
           
               
               
               
            
               
                   
                   
               
               
                   
                 RT-PCR (35 cycles) 
                   
               
            
           
           
               
               
               
               
            
               
                   
                 Tissue 
                 PN4 
                 PN4a 
               
               
                   
                   
               
               
                   
                 Brain 
                 + + + + + 
                 (+/−) 
               
               
                   
                 Spinal cord 
                 + + + 
                 + 
               
               
                   
                 DRG 
                 + + 
                 + + 
               
               
                   
                   
               
            
           
         
       
     
     EXAMPLE 6 
     Northern Analysis of MRNA from rat DRG 
     Lumbar DRG #4 and #5 (L4 and L5), brain, and spinal cord were removed from anesthetized adult male Sprague-Dawley rats under a dissecting microscope. The tissues were frozen in dry ice and homogenized with a Polytron homogenizer; the RNA was extracted by the guanidine isothiocyanate procedure (Chomczynksi, et al.,  Anal. Biochemistry  162:156-159, (1987)). Total RNA (5 μg of each sample) was dissolved in MEN buffer containing 50% formamide, 6.6% formaldehyde and denatured at 65° C. for 5-10 minutes. The RNA was electrophoresed through a 0.8% agarose gel containing 8.3% formaldehyde in MEN buffer. The electrode buffer was MEN buffer containing 3.7% formaldehyde; the gel was run at 50 V for 12-18 hours. 
     After electrophoresis, the gel was rinsed in 2×SSC and the RNA was transferred to a Duralose membrane (Stratagene) with 20×SSC by capillary action; the membrane was baked under vacuum at 80° C. for 1 hour. The membrane was prehybridized in 50% formamide, 5×SSC, 50 mM sodium phosphate, pH 7.1, 1× Denhardt&#39;s solution, 0.5% SDS, and sheared, heat-denatured salmon sperm DNA (1 mg/ml) for 16 hours at 42° C. The membrane was hybridized in 50% formamide, 5×SSC, 50 mM sodium phosphate, pH 7.1, 1× Denhardt&#39;s solution, 0.5% SDS, and sheared, heat-denatured salmon sperm DNA (200 μg/ml) with a  32 P-labeled cRNA probe (ca. 1-3×10 6  cpm/ml). The probe was the cloned fragment, CNaD4-2, which contains the Domain 4 sequence of PN4 sodium channel α-subunit sequence. The probe was hybridized for 18 hours at 42° C. The cRNA probe was synthesized by excising and subcloning the fragment into pBluescript KS+ vector, purchased from Stratagene. The cRNA was transcribed in vitro using T3 RNA polymerase, purchased from Promega, after linearizing the plasmid with Xbal, purchased from Boehringer Mannheim. Protocols for each procedure mentioned above can be found in  Molecular Cloning: A Laboratory Manual  by Sambrook, et al. (Cold Spring Harbor Laboratory Press, 2nd edition, 1989). 
     The membrane was washed three times with 2×SSC, 0.1% SDS at room temperature for 20 minutes and then washed once with 0.1×SSC, 0.1% SDS at 68° C. for 30 minutes. The filter was exposed against Kodak X-omat AR film at −80° C. with intensifying screens for up to two weeks. 
     Size markers, including ribosomal 18S and 28S RNAs and RNA markers (GIBCO BRL), were run in parallel lanes of the gel. Their positions were determined by staining the excised lane with ethidium bromide (0.5 μg/ml) followed by photography under UV light. The CNaD4-2 probe hybridized to RNA from the brain, cerebellum, dorsal, and ventral horn of the spinal cord with sizes of 11 kb, 9.5 kb, 7.5 kb, and 6.5 kb, estimated on the basis of their positions relative to the standards. 
     Bands of the same size were detected in a blot containing total RNA from DRG from neuropathic pain model. However, no signal was detected with RNA from naive DRG. 
     PN4 constitutes a subfamily of novel sodium channel genes; these genes are different from those detectable with other probes (e.g., PEAF8 and PN3 probes), as discussed in copending application no. 08/511,828. Sequence comparison of PN4 with NaCh6 (MRNA size=9.5kb) (Schaller, et al.,  J. Neurosci . 15:3231-3242 (1995)), Scn8a (Burgess, et al.,  Nature Genetics  10:461465 (1995)), and cardiac-specific sodium channel for which only a partial sequence is available (mRNA size=7kb) (Sills, et al.,  J. Clin. Invest . 84:331-336 (1989)) indicates that these genes share a higher homology among themselves than with members of other sodium channel subfamilies such as the brain-type sodium channels, the TTX-insensitive cardiac sodium channel, and the TTX-resistant PN3 (copending application no. 08/511,828). 
     Semiquantitation of the signal intensity of the various bands detected in the blot containing RNAs from the neuropathic pain model indicated that the level cf 7.5kb transcript was upregulated ˜35 fold as compared with the DRG from the sham operated side on day 1 after the surgery, wherein the sciatic nerve was ligated with four loose ligatures causing a constriction injury. None of the other transcripts detected by the CNaD4-2 probe was regulated so dramatically. By day 2, the regulation was reduced to ˜5 fold as compared with the sham operated side. The experiment was performed with DRG pooled from 6 rats. This experimental data suggests that PN4, or its splice variant, PN4a, is involved in the pathophysiology of neuropathic pain. 
     EXAMPLE 7 
     Expression of full length PN4 and PN4a clones in  Xenopur oocytes    
     After linearization with NotI, cRNA was prepared from pBSTAcIIr_PN4, pBSTAcIr_PN4a, and constructs of rat β 1  and rat β 2  in pBSTA, using a T7 in vitro transcription kit (mMessage mMachine, Ambion), and was injected into stage V and VI  Xenopur oocytes  using a Nanojector (Drummond), as described in Goldin, supra. After 1.5 days at 20° C., the oocytes were impaled with agarose-cushion electrodes (0.3-0.8 MOhm) and voltage-clamped with a Geneclamp 500 amplifier (Axon Instruments) in TEV mode; see Schreibmayer, et al.,  Pflugers Arch . 426:453-458 (1994). Stimulation and recording were controlled by a computer running pClamp (Axon Instruments), Kegel, et al.,  J. Neurosci. Meth . 12:317-330 (1982). Oocytes were perfused with a solution containing: 81 mM NaCl, 2 mM KC1, 1 mM MgCl 2 , 0.3 mM CaCl 2 , 20 mM Hepes-NaOH, pH 7.5. The data collected is shown in the FIGS. 7-9 and is described hereinafter. 
     FIG. 7 a  shows the currents produced from a PN4 sodium channel expressed in aXenopus oocyte using P/−4 leak subtraction (Benzanilla and Armstrong  J. Gen. Physiol . 70:549-566 (1977)), filtered at 5 kHz with a 4-pole Bessel filter, and sampled at 50 kHz. The x-axis denotes time in milliseconds. 
     FIG. 7 b  illustrates the voltage to current relationship of the PN4 sodium channel expressed in a Xenopus oocyte. In the expression of PN4, 0.2 ng of cRNA gave 1.4±0.19 μA (n=9). In the expression of PN4a, 0.1 ng gave 1.8±0.23 μA (n=6). 
     FIGS. 8 a  and  b  show steady state inactivation of sodium currents produced by PN4 in  Xenopur oocytes  , using 10 second conditioning prepulses. In FIG. 8 a , the x-axis denotes time in milliseconds. Leak currents were measured during long pulses to −100 mV and −120 mV, and the test currents corrected assuming that the leak currents had a linear current-voltage relationship. In FIG. 8 b , the x-axis is conditioning potential in millivolts and the y-axis is current in μA. For the steady state inactivation of PN4, we found V ½ =−70.7±0.71 mV, k=5.5±0.55 mV (n=3) For the steady state inactivation of PN4a, we found V ½ =−73.3±0.97 mV, k=5.5±0.28 mV (n=4). Under these conditions, a V ½  for inactivation of about −70 mV is similar to most sodium channels. 
     FIG. 9 demonstrates the effects of the β 1  and βsubunits upon PN4 function in Xenopus oocytes. Shown are currents produced when the PN4 α subunit is injected (a) alone; (b) with the β 1  subunit; (c) with the β 2  subunit; and (d) with both the β 1  and β 2  subunits. The x-axis in each of these figures denotes time in milliseconds. As these figures show, the inactivation kinetics of functionally active PN4 channels are accelerated by the β 1  subunit. No obvious effects are seen with the β 2  subunit. 
     As is seen in FIGS. 7 a  and  7   b , expression of PN4 produced an inward current with slow inactivation kinetics, similar to that of the rBIIa (Patton, et al.,  Neuron  7:637-647 (1991)) and rSkM1 α-subunits expressed in the absence of the β 1 -subunit. Co-injection of rat β 1  cRNA (1 ng/oocyte) with PN4 cRNA accelerated inactivation kinetics of the channel, as seen in FIGS. 9 a  and 9 b . Acceleration of inactivation kinetics of rBIIa and rSkml expressed in oocytes by co-expression of rat PI has been reported (Isom, et al.,  Science  256:839-842 (1992); and Waliner, et al.,  FEBS Lett . 336:535-539 1993)). 
     Sodium channels are distinctively sensitive or insensitive to neurotoxins such as TTX. The TTX-sensitive brain and skeletal muscle sodium channels are blocked by nanomolar TTX concentrations, whereas the TTX-insensitive cardiac sodium channels are blocked by micromolar TTX concentrations. In rat heart sodium channel 1, Cys 374  is a critical determinant of TTX-insensitivity, as shown in Satin, et al.,  Science  256:1202-1205(1992); in the TTX-sensitive rBI, rBII, rBIII, and rSkM1, the corresponding residue is either Phe or Tyr. In PN4 and PN4a, this residue is Tyr. When expressed in  Xenopur oocytes  , we found the PN4 sodium current to be inhibited in a concentration-dependent manner by 0.1-10 nM TTX, with IC 50  values of 0.4 nM and 1.6 nM in two oocytes. 
     All publications and patent applications mentioned in this specification are herein incorporated by reference to the same extent as if each individual publication or patent application was specifically and individually indicated to be incorporated by reference. 
     Although the foregoing invention has been described in some detail by way of illustration and example for purposes of clarity and understanding, it will be obvious that certain changes and modifications may be practiced within the scope of the appended claims. 
     
       
         
           
             43 
           
           
             
               5977 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             1
CTCGAGCCCG GGCAAGAGAA GATGGCAGCG CGGCTGCTCG CACCACCAGG CCCTGATAGT     60
TTCAAGCCTT TCACCCCTGA GTCGCTGGCA AACATCGAGA GGCGTATTGC CGAGAGCAAG    120
CTCAAGAAAC CACCAAAGGC GGATGGCAGC CACCGGGAGG ACGATGAAGA CAGCAAGCCC    180
AAGCCAAACA GTGACCTGGA GGCTGGGAAG AGTTTGCCTT TCATCTACGG GGACATCCCG    240
CAAGGCCTGG TTGCGGTTCC CCTGGAGGAC TTTGACCCTT ACTATTTGAC GCAGAAAACC    300
TTTGTAGTAT TAAACAGAGG GAAAACTCTC TTCAGATTTA GTGCCACACC TGCCTTGTAC    360
ATTTTAAGCC CTTTTAACCT GATAAGAAGA ATAGCTATTA AAATTTTGAT ACACTCAGTT    420
TTCAGCATGA TCATCATGTG CACCATCCTG ACCAACTGTG TGTTCATGAC CTTTAGTAAC    480
CCTCCAGAAT GGTCCAAGAA TGTGGAGTAC ACATTCACAG GGATTTACAC ATTTGAATCA    540
CTAGTGAAAA TCATCGCAAG AGGTTTCTGC ATAGACGGCT TCACCTTCTT GCGAGACCCG    600
TGGAACTGGT TAGACTTCAG TGTCATCATG ATGGCATATG TGACAGAGTT TGTGGACCTG    660
GGCAATGTCT CAGCGCTGAG AACATTCAGG GTTCTCCGAG CTTTGAAAAC TATCTCTGTA    720
ATTCCAGGCC TGAAGACAAT CGTGGGCGCC CTAATCCAGT CCGTGAAGAA GCTGTCGGAC    780
GTGATGATCC TGACAGTGTT CTGCCTGAGT GTTTTCGCCC TGATTGGCCT GCAGCTCTTC    840
ATGGGGAACC TTCGAAACAA GTGTGTCGTG TGGCCCATAA ACTTCAACGA GAGCTACCTG    900
GAGAACGGCA CCAGAGGCTT TGACTGGGAG GAATATATCA ACAATAAAAC AAACTTTTAC    960
ATGGTTCCTG GCATGCTAGA ACCCTTGCTC TGCGGGAACA GTTCTGATGC TGGGCAATGC   1020
CCAGAGGGAT TCCAGTGCAT GAAAGCAGGA AGGAACCCCA ACTACGGTTA CACCAGCTTT   1080
GACACCTTCA GCTGGGCCTT CTTGGCATTA TTCCGCCTTA TGACCCAGGA CTATTGGGAG   1140
AACTTATACC AGCTGACCTT ACGAGCCGCT GGGAAAACGT ACATGATCTT CTTTGTCTTG   1200
GTCATCTTCG TGGGTTCTTT CTATCTGGTG AACTTGATCT TGGCTGTGGT GGCCATGGCT   1260
TATGAGGAAC AGAACCAGGC AACACTGGAG GAGGCAGAGC AAAAAGAGGC CGAGTTCAAG   1320
GCAATGCTGG AGCAACTCAA GAAGCAGCAG GAGGAGGCAC AGGCTGCTGC AATGGCCACC   1380
TCAGCGGGCA CTGTCTCGGA AGACGCCATT GAAGAAGAAG GGGAAGATGG GGTAGGCTCT   1440
CCGAGGAGCT CTTCTGAACT GTCTAAACTC AGTTCCAAGA GCGCGAAGGA GCGGCGGAAC   1500
CGACGGAAGA AGAGGAAGCA GAAGGAGCTC TCTGAAGGCG AGGAGAAAGG GGACCCGGAG   1560
AAGGTGTTTA AGTCAGAGTC GGAAGACGGT ATGAGAAGGA AGGCCTTCCG GCTGCCAGAC   1620
AACAGGATAG GGAGGAAGTT TTCCATCATG AATCAGTCGC TGCTCAGCAT TCCAGGCTCG   1680
CCCTTCCTCT CCCGACATAA CAGCAAAAGC AGCATCTTCA GCTTCCGGGG ACCCGGTCGG   1740
TTCCGGGACC CCGGCTCTGA GAATGAGTTC GCAGACGATG AACACAGCAC CGTGGAGGAG   1800
AGCGAGGGCC GGCGTGACTC GCTCTTCATC CCGATCCGCG CCCGCGAGCG CCGCAGCAGC   1860
TACAGTGGCT ACAGCGGCTA CAGCCAGTGC AGCCGCTCGT CGCGCATCTT CCCCAGCCTG   1920
CGGCGCAGCG TGAAGCGCAA CAGCACGGTG GACTGCAACG GCGTAGTGTC ACTCATCGGG   1980
CCCGGCTCAC ACATCGGGCG GCTCCTGCCT GAGGCAACGA CTGAGGTGGA AATTAAGAAG   2040
AAAGGCCCTG GATCTCTTTT AGTTTCTATG GACCAACTCG CCTCCTACGG ACGGAAGGAC   2100
AGAATCAACA GCATAATGAG CGTGGTCACA AACACGCTAG TGGAAGAGCT GGAAGAGTCT   2160
CAGAGAAAGT GCCCACCGTG CTGGTATAAG TTTGCCAACA CTTTCCTCAT CTGGGAGTGT   2220
CACCCCTACT GGATAAAACT GAAGGAGATC GTGAACTTAA TCGTCATGGA CCCTTTTGTA   2280
GACTTAGCCA TCACCATCTG CATCGTTCTG AATACGCTAT TTATGGCAAT GGAGCACCAT   2340
CCCATGACAC CACAGTTCGA ACACGTCTTG GCCGTAGGAA ATCTGGTGTT CACCGGGATC   2400
TTCACGGCGG AAATGTTTCT GAAGCTCATA GCCATGGACC CCTACTATTA TTTCCAAGAA   2460
GGCTGGAACA TTTTTGACGG ATTTATTGTC TCCCTCAGTT TAATGGAGCT GAGTCTCGCA   2520
GATGTGGAGG GGCTCTCAGT GCTGCGGTCT TTCCGACTGC TCCGAGTCTT CAAGCTGGCC   2580
AAGTCCTGGC CCACCCTGAA CATGCTGATC AAGATCATCG GGAACTCCGT GGGTGCCCTG   2640
GGCAACCTGA CCCTGGTGCT GGCCATCATC GTCTTCATCT TCGCCGTGGT GGGGATGCAG   2700
CTGTTTGGAA AGAGTTACAA GGAGTGCGTC TGTAAGATCA ACCAGGAGTG CAAGCTCCCG   2760
CGCTGGCACA TGAACGACTT CTTCCACTCC TTCCTCATCG TCTTCCGAGT GCTGTGTGGG   2820
GAGTGGATCG AGACCATGTG GGACTGCATG GAGGTGGCCG GCCAGGCCAT GTGCCTCATT   2880
GTCTTCATGA TGGTTATGGT CATTGGCAAC CTGGTGGTGC TGAATCTATT CCTGGCCTTG   2940
CTTCTGAGCT CCTTCAGCGC AGACAACCTG GCGGCCACAG ACGACGACGG GGAAATGAAC   3000
AACCTGCAGA TCTCAGTGAT CCGGATCAAG AAGGGCGTGG CCTGGACCAA AGTGAAGGTG   3060
CACGCCTTCA TGCAGGCTCA CTTCAAGCAG CGGGAGGCGG ATGAAGTGAA ACCCCTCGAC   3120
GAGCTGTATG AGAAGAAGGC CAACTGCATC GCCAACCACA CGGGCGTGGA TATCCACCGG   3180
AACGGCGACT TCCAGAAGAA CGGGAACGGA ACCACCAGCG GCATCGGCAG CAGCGTGGAG   3240
AAGTACATCA TCGACGAGGA CCACATGTCC TTCATTAACA ACCCAAACCT GACCGTCCGG   3300
GTGCCCATTG CTGTGGGCGA GTCTGACTTC GAGAACCTCA ACACAGAGGA TGTTAGCAGC   3360
GAATCAGACC CTGAAGGCAG CAAAGATAAA CTGGACGATA CCAGCTCCTC AGAAGGAAGT   3420
ACCATCGACA TCAAGCCTGA GGTGGAAGAA GTTCCCGTGG AGCAACCTGA GGAATACTTG   3480
GATCCGGACG CCTGCTTTAC AGAGGGTTGC GTCCAGCGGT TCAAGTGCTG CCAGGTCAAC   3540
ATCGAGGAAG GACTAGGCAA GTCGTGGTGG ATCTTGCGGA AAACCTGCTT CCTCATTGTG   3600
GAGCACAATT GGTTTGAGAC CTTCATCATC TTCATGATTC TGCTCAGCAG TGGCGCCCTG   3660
GCCTTTGAGG ACATCTACAT TGAGCAGAGG AAGACCATCC GCACCATCCT GGAGTATGCG   3720
GACAAGGTCT TCACCTACAT CTTCATCCTG GAGATGTTGC TCAAGTGGAC AGCCTACGGC   3780
TTCGTCAAGT TCTTCACCAA TGCCTGGTGC TGGTTGGACT TCCTCATTGT GGCTGTCTCT   3840
TTAGTCAGCC TTATAGCTAA TGCCCTGGGC TACTCGGAAC TAGGTGCCAT AAAGTCCCTT   3900
AGGACCCTAA GAGCTTTGAG ACCCTTAAGA GCCTTATCAC GATTTGAAGG GATGAGGGTG   3960
GTGGTGAATG CCTTGGTGGG CGCCATCCCC TCCATCATGA ATGTGCTGCT GGTGTGTCTC   4020
ATCTTCTGGC TGATTTTCAG CATCATGGGA GTTAACCTGT TTGCGGGGAA ATACCACTAC   4080
TGCTTTAATG AGACTTCTGA AATCCGGTTC GAAATCGATA TTGTCAACAA TAAAACGGAC   4140
TGTGAGAAGC TCATGGAGGG CAACAGCACG GAGATCCGAT GGAAGAATGT CAAGATCAAC   4200
TTTGACAATG TCGGAGCAGG GTACCTGGCC CTTCTTCAAG TGGCAACCTT CAAAGGCTGG   4260
ATGGACATCA TGTATGCGGC TGTAGATTCC CGAAAGCCAG ACGAGCAGCC TGACTACGAG   4320
GGCAACATCT ACATGTACAT CTACTTCGTC ATCTTCATCA TCTTCGGCTC CTTCTTCACC   4380
CTCAACCTGT TCATCGGTGT CATCATCGAC AACTTCAACC AGCAGAAGAA AAAGTTTGGA   4440
GGTCAGGACA TCTTCATGAC AGAGGAACAG AAGAAGTACT ACAATGCCAT GAAAAAGCTG   4500
GGCTCCAAGA AGCCACAGAA GCCCATCCCC CGACCCTTGA ACAAAATCCA AGGGATTGTC   4560
TTTGATTTCG TCACTCAACA AGCCTTTGAC ATTGTGATCA TGATGCTCAT CTGCCTTAAC   4620
ATGGTGACAA TGATGGTGGA GACAGACACT CAGAGCAAGC AGATGGAGAA CATTCTTTAC   4680
TGGATTAATC TGGTCTTTGT CATCTTCTTC ACCTGCGAGT GTGTGCTCAA AATGTTTGCC   4740
TTGAGACACT ACTATTTCAC CATTGGCTGG AACATCTTTG ACTTTGTGGT GGTCATCCTC   4800
TCCATTGTGG GAATGTTCCT GGCTGATATC ATTGAGAAGT ACTTCGTCTC CCCAACCCTA   4860
TTCCGAGTTA TCCGATTGGC CCGTATTGGG CGCATCTTGC GTCTGATCAA GGGCGCCAAA   4920
GGGATCCGCA CCCTGCTCTT TGCCTTAATG ATGTCGCTGC CCGCCCTGTT CAACATCGGC   4980
CTCCTGCTCT TCCTCGTCAT GTTCATCTTC TCCATTTTTG GCATGTCCAA CTTCGCATAC   5040
GTGAAGCACG AGGCCGGCAT TGACGACATG TTCAACTTCG AGACATTTGG CAACAGCATG   5100
ATCTGTTTGT TCCAGATCAC AACGTCTGCT GGCTGGGATG GCCTGCTGCT GCCAATCCTG   5160
AACCGCCCCC CTGACTGCAG CTTGGACAAA GAGCACCCAG GGAGTGGCTT CAAAGGGGAC   5220
TGTGGGAACC CCTCGGTGGG CATCTTCTTC TTTGTGAGCT ACATCATCAT CTCCTTCCTG   5280
ATTGTGGTGA ACATGTACAT CGCCATCATC CTGGAGAACT TCAGCGTGGC CACCGAGGAG   5340
AGCGCCGACC CTCTGAGTGA GGATGACTTC GAGACTTTCT ATGAGATCTG GGAGAAGTTT   5400
GACCCAGACG CCACCCAGTT CATCGAGTAC TGTAAGCTGG CAGACTTTGC CGACGCCCTG   5460
GAGCACCCGC TCCGAGTACC CAAGCCCAAC ACCATCGAGC TCATCGCCAT GGACCTGCCC   5520
ATGGTGAGCG GAGATCGCAT CCACTGCTTG GACATCCTTT TCGCCTTCAC CAAGCGAGTC   5580
CTGGGAGACA GTGGGGAGTT GGACATCCTG CGGCAGCAGA TGGAGGAGCG GTTCGTGGCA   5640
TCCAATCCTT CCAAAGTGTC TTACGAGCCT ATCACAACCA CTCTGCGGCG CAAGCAGGAG   5700
GAGGTGTCTG CAGTGGTCCT GCAGCGTGCC TACAGGGGAC ACTTGGCTAG GCGGGGCTTC   5760
ATCTGCAGAA AGATGGCCTC CAACAAGCTG GAGAATGGAG GCACACACAG AGACAAGAAG   5820
GAGAGCACCC CGTCCACAGC CTCCCTCCCC TCTTACGACA GCGTCACAAA GCCAGACAAG   5880
GAGAAGCAGC AGCGTGCGGA GGAGGGCAGA AGGGAAAGAG CCAAGAGGCA AAAAGAGGTC   5940
AGGGAGTCCA AGTGCTAGAG GAGGGGAAAG GAAGCTT                            5977
 
           
           
             
               6007 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             2
CTCGAGCCCG GGCAAGAGAA GATGGCAGCG CGGCTGCTCG CACCACCAGG CCCTGATAGT     60
TTCAAGCCTT TCACCCCTGA GTCGCTGGCA AACATCGAGA GGCGTATTGC CGAGAGCAAG    120
CTCAAGAAAC CACCAAAGGC GGATGGCAGC CACCGGGAGG ACGATGAAGA CAGCAAGCCC    180
AAGCCAAACA GTGACCTGGA GGCTGGGAAG AGTTTGCCTT TCATCTACGG GGACATCCCG    240
CAAGGCCTGG TTGCGGTTCC CCTGGAGGAC TTTGACCCTT ACTATTTGAC GCAGAAAACC    300
TTTGTAGTAT TAAACAGAGG GAAAACTCTC TTCAGATTTA GTGCCACACC TGCCTTGTAC    360
ATTTTAAGCC CTTTTAACCT GATAAGAAGA ATAGCTATTA AAATTTTGAT ACACTCAGTT    420
TTCAGCATGA TCATCATGTG CACCATCCTG ACCAACTGTG TGTTCATGAC CTTTAGTAAC    480
CCTCCAGAAT GGTCCAAGAA TGTGGAGTAC ACATTCACAG GGATTTACAC ATTTGAATCA    540
CTAGTGAAAA TCATCGCAAG AGGTTTCTGC ATAGACGGCT TCACCTTCTT GCGAGACCCG    600
TGGAACTGGT TAGACTTCAG TGTCATCATG ATGGCATATG TGACAGAGTT TGTGGACCTG    660
GGCAATGTCT CAGCGCTGAG AACATTCAGG GTTCTCCGAG CTTTGAAAAC TATCTCTGTA    720
ATTCCAGGCC TGAAGACAAT CGTGGGCGCC CTAATCCAGT CCGTGAAGAA GCTGTCGGAC    780
GTGATGATCC TGACAGTGTT CTGCCTGAGT GTTTTCGCCC TGATTGGCCT GCAGCTCTTC    840
ATGGGGAACC TTCGAAACAA GTGTGTCGTG TGGCCCATAA ACTTCAACGA GAGCTACCTG    900
GAGAACGGCA CCAGAGGCTT TGACTGGGAG GAATATATCA ACAATAAAAC AAACTTTTAC    960
ATGGTTCCTG GCATGCTAGA ACCCTTGCTC TGCGGGAACA GTTCTGATGC TGGGCAATGC   1020
CCAGAGGGAT TCCAGTGCAT GAAAGCAGGA AGGAACCCCA ACTACGGTTA CACCAGCTTT   1080
GACACCTTCA GCTGGGCCTT CTTGGCATTA TTCCGCCTTA TGACCCAGGA CTATTGGGAG   1140
AACTTATACC AGCTGACCTT ACGAGCCGCT GGGAAAACGT ACATGATCTT CTTTGTCTTG   1200
GTCATCTTCG TGGGTTCTTT CTATCTGGTG AACTTGATCT TGGCTGTGGT GGCCATGGCT   1260
TATGAGGAAC AGAACCAGGC AACACTGGAG GAGGCAGAGC AAAAAGAGGC CGAGTTCAAG   1320
GCAATGCTGG AGCAACTCAA GAAGCAGCAG GAGGAGGCAC AGGCTGCTGC AATGGCCACC   1380
TCAGCGGGCA CTGTCTCGGA AGACGCCATT GAAGAAGAAG GGGAAGATGG GGTAGGCTCT   1440
CCGAGGAGCT CTTCTGAACT GTCTAAACTC AGTTCCAAGA GCGCGAAGGA GCGGCGGAAC   1500
CGACGGAAGA AGAGGAAGCA GAAGGAGCTC TCTGAAGGCG AGGAGAAAGG GGACCCGGAG   1560
AAGGTGTTTA AGTCAGAGTC GGAAGACGGT ATGAGAAGGA AGGCCTTCCG GCTGCCAGAC   1620
AACAGGATAG GGAGGAAGTT TTCCATCATG AATCAGTCGC TGCTCAGCAT TCCAGGCTCG   1680
CCCTTCCTCT CCCGACATAA CAGCAAAAGC AGCATCTTCA GCTTCCGGGG ACCCGGTCGG   1740
TTCCGGGACC CCGGCTCTGA GAATGAGTTC GCAGACGATG AACACAGCAC CGTGGAGGAG   1800
AGCGAGGGCC GGCGTGACTC GCTCTTCATC CCGATCCGCG CCCGCGAGCG CCGCAGCAGC   1860
TACAGTGGCT ACAGCGGCTA CAGCCAGTGC AGCCGCTCGT CGCGCATCTT CCCCAGCCTG   1920
CGGCGCAGCG TGAAGCGCAA CAGCACGGTG GACTGCAACG GCGTAGTGTC ACTCATCGGG   1980
CCCGGCTCAC ACATCGGGCG GCTCCTGCCT GAGGTGAAAA TAGATAAGGC AGCTACGGAC   2040
AGCGCAACGA CTGAGGTGGA AATTAAGAAG AAAGGCCCTG GATCTCTTTT AGTTTCTATG   2100
GACCAACTCG CCTCCTACGG ACGGAAGGAC AGAATCAACA GCATAATGAG CGTGGTCACA   2160
AACACGCTAG TGGAAGAGCT GGAAGAGTCT CAGAGAAAGT GCCCACCGTG CTGGTATAAG   2220
TTTGCCAACA CTTTCCTCAT CTGGGAGTGT CACCCCTACT GGATAAAACT GAAGGAGATC   2280
GTGAACTTAA TCGTCATGGA CCCTTTTGTA GACTTAGCCA TCACCATCTG CATCGTTCTG   2340
AATACGCTAT TTATGGCAAT GGAGCACCAT CCCATGACAC CACAGTTCGA ACACGTCTTG   2400
GCCGTAGGAA ATCTGGTGTT CACCGGGATC TTCACGGCGG AAATGTTTCT GAAGCTCATA   2460
GCCATGGACC CCTACTATTA TTTCCAAGAA GGCTGGAACA TTTTTGACGG ATTTATTGTC   2520
TCCCTCAGTT TAATGGAGCT GAGTCTCGCA GATGTGGAGG GGCTCTCAGT GCTGCGGTCT   2580
TTCCGACTGC TCCGAGTCTT CAAGCTGGCC AAGTCCTGGC CCACCCTGAA CATGCTGATC   2640
AAGATCATCG GGAACTCCGT GGGTGCCCTG GGCAACCTGA CCCTGGTGCT GGCCATCATC   2700
GTCTTCATCT TCGCCGTGGT GGGGATGCAG CTGTTTGGAA AGAGTTACAA GGAGTGCGTC   2760
TGTAAGATCA ACCAGGAGTG CAAGCTCCCG CGCTGGCACA TGAACGACTT CTTCCACTCC   2820
TTCCTCATCG TCTTCCGAGT GCTGTGTGGG GAGTGGATCG AGACCATGTG GGACTGCATG   2880
GAGGTGGCCG GCCAGGCCAT GTGCCTCATT GTCTTCATGA TGGTTATGGT CATTGGCAAC   2940
CTGGTGGTGC TGAATCTATT CCTGGCCTTG CTTCTGAGCT CCTTCAGCGC AGACAACCTG   3000
GCGGCCACAG ACGACGACGG GGAAATGAAC AACCTGCAGA TCTCAGTGAT CCGGATCAAG   3060
AAGGGCGTGG CCTGGACCAA AGTGAAGGTG CACGCCTTCA TGCAGGCTCA CTTCAAGCAG   3120
CGGGAGGCGG ATGAAGTGAA ACCCCTCGAC GAGCTGTATG AGAAGAAGGC CAACTGCATC   3180
GCCAACCACA CGGGCGTGGA TATCCACCGG AACGGCGACT TCCAGAAGAA CGGGAACGGA   3240
ACCACCAGCG GCATCGGCAG CAGCGTGGAG AAGTACATCA TCGACGAGGA CCACATGTCC   3300
TTCATTAACA ACCCAAACCT GACCGTCCGG GTGCCCATTG CTGTGGGCGA GTCTGACTTC   3360
GAGAACCTCA ACACAGAGGA TGTTAGCAGC GAATCAGACC CTGAAGGCAG CAAAGATAAA   3420
CTGGACGATA CCAGCTCCTC AGAAGGAAGT ACCATCGACA TCAAGCCTGA GGTGGAAGAA   3480
GTTCCCGTGG AGCAACCTGA GGAATACTTG GATCCGGACG CCTGCTTTAC AGAGGGTTGC   3540
GTCCAGCGGT TCAAGTGCTG CCAGGTCAAC ATCGAGGAAG GACTAGGCAA GTCGTGGTGG   3600
ATCTTGCGGA AAACCTGCTT CCTCATTGTG GAGCACAATT GGTTTGAGAC CTTCATCATC   3660
TTCATGATTC TGCTCAGCAG TGGCGCCCTG GCCTTTGAGG ACATCTACAT TGAGCAGAGG   3720
AAGACCATCC GCACCATCCT GGAGTATGCG GACAAGGTCT TCACCTACAT CTTCATCCTG   3780
GAGATGTTGC TCAAGTGGAC AGCCTACGGC TTCGTCAAGT TCTTCACCAA TGCCTGGTGC   3840
TGGTTGGACT TCCTCATTGT GGCTGTCTCT TTAGTCAGCC TTATAGCTAA TGCCCTGGGC   3900
TACTCGGAAC TAGGTGCCAT AAAGTCCCTT AGGACCCTAA GAGCTTTGAG ACCCTTAAGA   3960
GCCTTATCAC GATTTGAAGG GATGAGGGTG GTGGTGAATG CCTTGGTGGG CGCCATCCCC   4020
TCCATCATGA ATGTGCTGCT GGTGTGTCTC ATCTTCTGGC TGATTTTCAG CATCATGGGA   4080
GTTAACCTGT TTGCGGGGAA ATACCACTAC TGCTTTAATG AGACTTCTGA AATCCGGTTC   4140
GAAATCGATA TTGTCAACAA TAAAACGGAC TGTGAGAAGC TCATGGAGGG CAACAGCACG   4200
GAGATCCGAT GGAAGAATGT CAAGATCAAC TTTGACAATG TCGGAGCAGG GTACCTGGCC   4260
CTTCTTCAAG TGGCAACCTT CAAAGGCTGG ATGGACATCA TGTATGCGGC TGTAGATTCC   4320
CGAAAGCCAG ACGAGCAGCC TGACTACGAG GGCAACATCT ACATGTACAT CTACTTCGTC   4380
ATCTTCATCA TCTTCGGCTC CTTCTTCACC CTCAACCTGT TCATCGGTGT CATCATCGAC   4440
AACTTCAACC AGCAGAAGAA AAAGTTTGGA GGTCAGGACA TCTTCATGAC AGAGGAACAG   4500
AAGAAGTACT ACAATGCCAT GAAAAAGCTG GGCTCCAAGA AGCCACAGAA GCCCATCCCC   4560
CGACCCTTGA ACAAAATCCA AGGGATTGTC TTTGATTTCG TCACTCAACA AGCCTTTGAC   4620
ATTGTGATCA TGATGCTCAT CTGCCTTAAC ATGGTGACAA TGATGGTGGA GACAGACACT   4680
CAGAGCAAGC AGATGGAGAA CATTCTTTAC TGGATTAATC TGGTCTTTGT CATCTTCTTC   4740
ACCTGCGAGT GTGTGCTCAA AATGTTTGCC TTGAGACACT ACTATTTCAC CATTGGCTGG   4800
AACATCTTTG ACTTTGTGGT GGTCATCCTC TCCATTGTGG GAATGTTCCT GGCTGATATC   4860
ATTGAGAAGT ACTTCGTCTC CCCAACCCTA TTCCGAGTTA TCCGATTGGC CCGTATTGGG   4920
CGCATCTTGC GTCTGATCAA GGGCGCCAAA GGGATCCGCA CCCTGCTCTT TGCCTTAATG   4980
ATGTCGCTGC CCGCCCTGTT CAACATCGGC CTCCTGCTCT TCCTCGTCAT GTTCATCTTC   5040
TCCATTTTTG GCATGTCCAA CTTCGCATAC GTGAAGCACG AGGCCGGCAT TGACGACATG   5100
TTCAACTTCG AGACATTTGG CAACAGCATG ATCTGTTTGT TCCAGATCAC AACGTCTGCT   5160
GGCTGGGATG GCCTGCTGCT GCCAATCCTG AACCGCCCCC CTGACTGCAG CTTGGACAAA   5220
GAGCACCCAG GGAGTGGCTT CAAAGGGGAC TGTGGGAACC CCTCGGTGGG CATCTTCTTC   5280
TTTGTGAGCT ACATCATCAT CTCCTTCCTG ATTGTGGTGA ACATGTACAT CGCCATCATC   5340
CTGGAGAACT TCAGCGTGGC CACCGAGGAG AGCGCCGACC CTCTGAGTGA GGATGACTTC   5400
GAGACTTTCT ATGAGATCTG GGAGAAGTTT GACCCAGACG CCACCCAGTT CATCGAGTAC   5460
TGTAAGCTGG CAGACTTTGC CGACGCCCTG GAGCACCCGC TCCGAGTACC CAAGCCCAAC   5520
ACCATCGAGC TCATCGCCAT GGACCTGCCC ATGGTGAGCG GAGATCGCAT CCACTGCTTG   5580
GACATCCTTT TCGCCTTCAC CAAGCGAGTC CTGGGAGACA GTGGGGAGTT GGACATCCTG   5640
CGGCAGCAGA TGGAGGAGCG GTTCGTGGCA TCCAATCCTT CCAAAGTGTC TTACGAGCCT   5700
ATCACAACCA CTCTGCGGCG CAAGCAGGAG GAGGTGTCTG CAGTGGTCCT GCAGCGTGCC   5760
TACAGGGGAC ACTTGGCTAG GCGGGGCTTC ATCTGCAGAA AGATGGCCTC CAACAAGCTG   5820
GAGAATGGAG GCACACACAG AGACAAGAAG GAGAGCACCC CGTCCACAGC CTCCCTCCCC   5880
TCTTACGACA GCGTCACAAA GCCAGACAAG GAGAAGCAGC AGCGTGCGGA GGAGGGCAGA   5940
AGGGAAAGAG CCAAGAGGCA AAAAGAGGTC AGGGAGTCCA AGTGCTAGAG GAGGGGAAAG   6000
GAAGCTT                                                             6007
 
           
           
             
               1978 amino acids 
               amino acid 
               single 
               linear 
             
             
               peptide 
             
             3
Met Ala Ala Arg Leu Leu Ala Pro Pro Gly Pro Asp Ser Phe Lys Pro
1               5                   10                  15
Phe Thr Pro Glu Ser Leu Ala Asn Ile Glu Arg Arg Ile Ala Glu Ser
            20                  25                  30
Lys Leu Lys Lys Pro Pro Lys Ala Asp Gly Ser His Arg Glu Asp Asp
        35                  40                  45
Glu Asp Ser Lys Pro Lys Pro Asn Ser Asp Leu Glu Ala Gly Lys Ser
    50                  55                  60
Leu Pro Phe Ile Tyr Gly Asp Ile Pro Gln Gly Leu Val Ala Val Pro
65                  70                  75                  80
Leu Glu Asp Phe Asp Pro Tyr Tyr Leu Thr Gln Lys Thr Phe Val Val
                85                  90                  95
Leu Asn Arg Gly Lys Thr Leu Phe Arg Phe Ser Ala Thr Pro Ala Leu
            100                 105                 110
Tyr Ile Leu Ser Pro Phe Asn Leu Ile Arg Arg Ile Ala Ile Lys Ile
        115                 120                 125
Leu Ile His Ser Val Phe Ser Met Ile Ile Met Cys Thr Ile Leu Thr
    130                 135                 140
Asn Cys Val Phe Met Thr Phe Ser Asn Pro Pro Glu Trp Ser Lys Asn
145                 150                 155                 160
Val Glu Tyr Thr Phe Thr Gly Ile Tyr Thr Phe Glu Ser Leu Val Lys
                165                 170                 175
Ile Ile Ala Arg Gly Phe Cys Ile Asp Gly Phe Thr Phe Leu Arg Asp
            180                 185                 190
Pro Trp Asn Trp Leu Asp Phe Ser Val Ile Met Met Ala Tyr Val Thr
        195                 200                 205
Glu Phe Val Asp Leu Gly Asn Val Ser Ala Leu Arg Thr Phe Arg Val
    210                 215                 220
Leu Arg Ala Leu Lys Thr Ile Ser Val Ile Pro Gly Leu Lys Thr Ile
225                 230                 235                 240
Val Gly Ala Leu Ile Gln Ser Val Lys Lys Leu Ser Asp Val Met Ile
                245                 250                 255
Leu Thr Val Phe Cys Leu Ser Val Phe Ala Leu Ile Gly Leu Gln Leu
            260                 265                 270
Phe Met Gly Asn Leu Arg Asn Lys Cys Val Val Trp Pro Ile Asn Phe
        275                 280                 285
Asn Glu Ser Tyr Leu Glu Asn Gly Thr Arg Gly Phe Asp Trp Glu Glu
    290                 295                 300
Tyr Ile Asn Asn Lys Thr Asn Phe Tyr Met Val Pro Gly Met Leu Glu
305                 310                 315                 320
Pro Leu Leu Cys Gly Asn Ser Ser Asp Ala Gly Gln Cys Pro Glu Gly
                325                 330                 335
Phe Gln Cys Met Lys Ala Gly Arg Asn Pro Asn Tyr Gly Tyr Thr Ser
            340                 345                 350
Phe Asp Thr Phe Ser Trp Ala Phe Leu Ala Leu Phe Arg Leu Met Thr
        355                 360                 365
Gln Asp Tyr Trp Glu Asn Leu Tyr Gln Leu Thr Leu Arg Ala Ala Gly
    370                 375                 380
Lys Thr Tyr Met Ile Phe Phe Val Leu Val Ile Phe Val Gly Ser Phe
385                 390                 395                 400
Tyr Leu Val Asn Leu Ile Leu Ala Val Val Ala Met Ala Tyr Glu Glu
                405                 410                 415
Gln Asn Gln Ala Thr Leu Glu Glu Ala Glu Gln Lys Glu Ala Glu Phe
            420                 425                 430
Lys Ala Met Leu Glu Gln Leu Lys Lys Gln Gln Glu Glu Ala Gln Ala
        435                 440                 445
Ala Ala Met Ala Thr Ser Ala Gly Thr Val Ser Glu Asp Ala Ile Glu
    450                 455                 460
Glu Glu Gly Glu Asp Gly Val Gly Ser Pro Arg Ser Ser Ser Glu Leu
465                 470                 475                 480
Ser Lys Leu Ser Ser Lys Ser Ala Lys Glu Arg Arg Asn Arg Arg Lys
                485                 490                 495
Lys Arg Lys Gln Lys Glu Leu Ser Glu Gly Glu Glu Lys Gly Asp Pro
            500                 505                 510
Glu Lys Val Phe Lys Ser Glu Ser Glu Asp Gly Met Arg Arg Lys Ala
        515                 520                 525
Phe Arg Leu Pro Asp Asn Arg Ile Gly Arg Lys Phe Ser Ile Met Asn
    530                 535                 540
Gln Ser Leu Leu Ser Ile Pro Gly Ser Pro Phe Leu Ser Arg His Asn
545                 550                 555                 560
Ser Lys Ser Ser Ile Phe Ser Phe Arg Gly Pro Gly Arg Phe Arg Asp
                565                 570                 575
Pro Gly Ser Glu Asn Glu Phe Ala Asp Asp Glu His Ser Thr Val Glu
            580                 585                 590
Glu Ser Glu Gly Arg Arg Asp Ser Leu Phe Ile Pro Ile Arg Ala Arg
        595                 600                 605
Glu Arg Arg Ser Ser Tyr Ser Gly Tyr Ser Gly Tyr Ser Gln Cys Ser
    610                 615                 620
Arg Ser Ser Arg Ile Phe Pro Ser Leu Arg Arg Ser Val Lys Arg Asn
625                 630                 635                 640
Ser Thr Val Asp Cys Asn Gly Val Val Ser Leu Ile Gly Pro Gly Ser
                645                 650                 655
His Ile Gly Arg Leu Leu Pro Glu Ala Thr Thr Glu Val Glu Ile Lys
            660                 665                 670
Lys Lys Gly Pro Gly Ser Leu Leu Val Ser Met Asp Gln Leu Ala Ser
        675                 680                 685
Tyr Gly Arg Lys Asp Arg Ile Asn Ser Ile Met Ser Val Val Thr Asn
    690                 695                 700
Thr Leu Val Glu Glu Leu Glu Glu Ser Gln Arg Lys Cys Pro Pro Cys
705                 710                 715                 720
Trp Tyr Lys Phe Ala Asn Thr Phe Leu Ile Trp Glu Cys His Pro Tyr
                725                 730                 735
Trp Ile Lys Leu Lys Glu Ile Val Asn Leu Ile Val Met Asp Pro Phe
            740                 745                 750
Val Asp Leu Ala Ile Thr Ile Cys Ile Val Leu Asn Thr Leu Phe Met
        755                 760                 765
Ala Met Glu His His Pro Met Thr Pro Gln Phe Glu His Val Leu Ala
    770                 775                 780
Val Gly Asn Leu Val Phe Thr Gly Ile Phe Thr Ala Glu Met Phe Leu
785                 790                 795                 800
Lys Leu Ile Ala Met Asp Pro Tyr Tyr Tyr Phe Gln Glu Gly Trp Asn
                805                 810                 815
Ile Phe Asp Gly Phe Ile Val Ser Leu Ser Leu Met Glu Leu Ser Leu
            820                 825                 830
Ala Asp Val Glu Gly Leu Ser Val Leu Arg Ser Phe Arg Leu Leu Arg
        835                 840                 845
Val Phe Lys Leu Ala Lys Ser Trp Pro Thr Leu Asn Met Leu Ile Lys
    850                 855                 860
Ile Ile Gly Asn Ser Val Gly Ala Leu Gly Asn Leu Thr Leu Val Leu
865                 870                 875                 880
Ala Ile Ile Val Phe Ile Phe Ala Val Val Gly Met Gln Leu Phe Gly
                885                 890                 895
Lys Ser Tyr Lys Glu Cys Val Cys Lys Ile Asn Gln Glu Cys Lys Leu
            900                 905                 910
Pro Arg Trp His Met Asn Asp Phe Phe His Ser Phe Leu Ile Val Phe
        915                 920                 925
Arg Val Leu Cys Gly Glu Trp Ile Glu Thr Met Trp Asp Cys Met Glu
    930                 935                 940
Val Ala Gly Gln Ala Met Cys Leu Ile Val Phe Met Met Val Met Val
945                 950                 955                 960
Ile Gly Asn Leu Val Val Leu Asn Leu Phe Leu Ala Leu Leu Leu Ser
                965                 970                 975
Ser Phe Ser Ala Asp Asn Leu Ala Ala Thr Asp Asp Asp Gly Glu Met
            980                 985                 990
Asn Asn Leu Gln Ile Ser Val Ile Arg Ile Lys Lys Gly Val Ala Trp
        995                 1000                1005
Thr Lys Val Lys Val His Ala Phe Met Gln Ala His Phe Lys Gln Arg
    1010                1015                1020
Glu Ala Asp Glu Val Lys Pro Leu Asp Glu Leu Tyr Glu Lys Lys Ala
1025                1030                1035                1040
Asn Cys Ile Ala Asn His Thr Gly Val Asp Ile His Arg Asn Gly Asp
                1045                1050                1055
Phe Gln Lys Asn Gly Asn Gly Thr Thr Ser Gly Ile Gly Ser Ser Val
            1060                1065                1070
Glu Lys Tyr Ile Ile Asp Glu Asp His Met Ser Phe Ile Asn Asn Pro
        1075                1080                1085
Asn Leu Thr Val Arg Val Pro Ile Ala Val Gly Glu Ser Asp Phe Glu
    1090                1095                1100
Asn Leu Asn Thr Glu Asp Val Ser Ser Glu Ser Asp Pro Glu Gly Ser
1105                1110                1115                1120
Lys Asp Lys Leu Asp Asp Thr Ser Ser Ser Glu Gly Ser Thr Ile Asp
                1125                1130                1135
Ile Lys Pro Glu Val Glu Glu Val Pro Val Glu Gln Pro Glu Glu Tyr
            1140                1145                1150
Leu Asp Pro Asp Ala Cys Phe Thr Glu Gly Cys Val Gln Arg Phe Lys
        1155                1160                1165
Cys Cys Gln Val Asn Ile Glu Glu Gly Leu Gly Lys Ser Trp Trp Ile
    1170                1175                1180
Leu Arg Lys Thr Cys Phe Leu Ile Val Glu His Asn Trp Phe Glu Thr
1185                1190                1195                1200
Phe Ile Ile Phe Met Ile Leu Leu Ser Ser Gly Ala Leu Ala Phe Glu
                1205                1210                1215
Asp Ile Tyr Ile Glu Gln Arg Lys Thr Ile Arg Thr Ile Leu Glu Tyr
            1220                1225                1230
Ala Asp Lys Val Phe Thr Tyr Ile Phe Ile Leu Glu Met Leu Leu Lys
        1235                1240                1245
Trp Thr Ala Tyr Gly Phe Val Lys Phe Phe Thr Asn Ala Trp Cys Trp
    1250                1255                1260
Leu Asp Phe Leu Ile Val Ala Val Ser Leu Val Ser Leu Ile Ala Asn
1265                1270                1275                1280
Ala Leu Gly Tyr Ser Glu Leu Gly Ala Ile Lys Ser Leu Arg Thr Leu
                1285                1290                1295
Arg Ala Leu Arg Pro Leu Arg Ala Leu Ser Arg Phe Glu Gly Met Arg
            1300                1305                1310
Val Val Val Asn Ala Leu Val Gly Ala Ile Pro Ser Ile Met Asn Val
        1315                1320                1325
Leu Leu Val Cys Leu Ile Phe Trp Leu Ile Phe Ser Ile Met Gly Val
    1330                1335                1340
Asn Leu Phe Ala Gly Lys Tyr His Tyr Cys Phe Asn Glu Thr Ser Glu
1345                1350                1355                1360
Ile Arg Phe Glu Ile Asp Ile Val Asn Asn Lys Thr Asp Cys Glu Lys
                1365                1370                1375
Leu Met Glu Gly Asn Ser Thr Glu Ile Arg Trp Lys Asn Val Lys Ile
            1380                1385                1390
Asn Phe Asp Asn Val Gly Ala Gly Tyr Leu Ala Leu Leu Gln Val Ala
        1395                1400                1405
Thr Phe Lys Gly Trp Met Asp Ile Met Tyr Ala Ala Val Asp Ser Arg
    1410                1415                1420
Lys Pro Asp Glu Gln Pro Asp Tyr Glu Gly Asn Ile Tyr Met Tyr Ile
1425                1430                1435                1440
Tyr Phe Val Ile Phe Ile Ile Phe Gly Ser Phe Phe Thr Leu Asn Leu
                1445                1450                1455
Phe Ile Gly Val Ile Ile Asp Asn Phe Asn Gln Gln Lys Lys Lys Phe
            1460                1465                1470
Gly Gly Gln Asp Ile Phe Met Thr Glu Glu Gln Lys Lys Tyr Tyr Asn
        1475                1480                1485
Ala Met Lys Lys Leu Gly Ser Lys Lys Pro Gln Lys Pro Ile Pro Arg
    1490                1495                1500
Pro Leu Asn Lys Ile Gln Gly Ile Val Phe Asp Phe Val Thr Gln Gln
1505                1510                1515                1520
Ala Phe Asp Ile Val Ile Met Met Leu Ile Cys Leu Asn Met Val Thr
                1525                1530                1535
Met Met Val Glu Thr Asp Thr Gln Ser Lys Gln Met Glu Asn Ile Leu
            1540                1545                1550
Tyr Trp Ile Asn Leu Val Phe Val Ile Phe Phe Thr Cys Glu Cys Val
        1555                1560                1565
Leu Lys Met Phe Ala Leu Arg His Tyr Tyr Phe Thr Ile Gly Trp Asn
    1570                1575                1580
Ile Phe Asp Phe Val Val Val Ile Leu Ser Ile Val Gly Met Phe Leu
1585                1590                1595                1600
Ala Asp Ile Ile Glu Lys Tyr Phe Val Ser Pro Thr Leu Phe Arg Val
                1605                1610                1615
Ile Arg Leu Ala Arg Ile Gly Arg Ile Leu Arg Leu Ile Lys Gly Ala
            1620                1625                1630
Lys Gly Ile Arg Thr Leu Leu Phe Ala Leu Met Met Ser Leu Pro Ala
        1635                1640                1645
Leu Phe Asn Ile Gly Leu Leu Leu Phe Leu Val Met Phe Ile Phe Ser
    1650                1655                1660
Ile Phe Gly Met Ser Asn Phe Ala Tyr Val Lys His Glu Ala Gly Ile
1665                1670                1675                1680
Asp Asp Met Phe Asn Phe Glu Thr Phe Gly Asn Ser Met Ile Cys Leu
                1685                1690                1695
Phe Gln Ile Thr Thr Ser Ala Gly Trp Asp Gly Leu Leu Leu Pro Ile
            1700                1705                1710
Leu Asn Arg Pro Pro Asp Cys Ser Leu Asp Lys Glu His Pro Gly Ser
        1715                1720                1725
Gly Phe Lys Gly Asp Cys Gly Asn Pro Ser Val Gly Ile Phe Phe Phe
    1730                1735                1740
Val Ser Tyr Ile Ile Ile Ser Phe Leu Ile Val Val Asn Met Tyr Ile
1745                1750                1755                1760
Ala Ile Ile Leu Glu Asn Phe Ser Val Ala Thr Glu Glu Ser Ala Asp
                1765                1770                1775
Pro Leu Ser Glu Asp Asp Phe Glu Thr Phe Tyr Glu Ile Trp Glu Lys
            1780                1785                1790
Phe Asp Pro Asp Ala Thr Gln Phe Ile Glu Tyr Cys Lys Leu Ala Asp
        1795                1800                1805
Phe Ala Asp Ala Leu Glu His Pro Leu Arg Val Pro Lys Pro Asn Thr
    1810                1815                1820
Ile Glu Leu Ile Ala Met Asp Leu Pro Met Val Ser Gly Asp Arg Ile
1825                1830                1835                1840
His Cys Leu Asp Ile Leu Phe Ala Phe Thr Lys Arg Val Leu Gly Asp
                1845                1850                1855
Ser Gly Glu Leu Asp Ile Leu Arg Gln Gln Met Glu Glu Arg Phe Val
            1860                1865                1870
Ala Ser Asn Pro Ser Lys Val Ser Tyr Glu Pro Ile Thr Thr Thr Leu
        1875                1880                1885
Arg Arg Lys Gln Glu Glu Val Ser Ala Val Val Leu Gln Arg Ala Tyr
    1890                1895                1900
Arg Gly His Leu Ala Arg Arg Gly Phe Ile Cys Arg Lys Met Ala Ser
1905                1910                1915                1920
Asn Lys Leu Glu Asn Gly Gly Thr His Arg Asp Lys Lys Glu Ser Thr
                1925                1930                1935
Pro Ser Thr Ala Ser Leu Pro Ser Tyr Asp Ser Val Thr Lys Pro Asp
            1940                1945                1950
Lys Glu Lys Gln Gln Arg Ala Glu Glu Gly Arg Arg Glu Arg Ala Lys
        1955                1960                1965
Arg Gln Lys Glu Val Arg Glu Ser Lys Cys
    1970                1975
 
           
           
             
               1988 amino acids 
               amino acid 
               single 
               linear 
             
             
               peptide 
             
             4
Met Ala Ala Arg Leu Leu Ala Pro Pro Gly Pro Asp Ser Phe Lys Pro
1               5                   10                  15
Phe Thr Pro Glu Ser Leu Ala Asn Ile Glu Arg Arg Ile Ala Glu Ser
            20                  25                  30
Lys Leu Lys Lys Pro Pro Lys Ala Asp Gly Ser His Arg Glu Asp Asp
        35                  40                  45
Glu Asp Ser Lys Pro Lys Pro Asn Ser Asp Leu Glu Ala Gly Lys Ser
    50                  55                  60
Leu Pro Phe Ile Tyr Gly Asp Ile Pro Gln Gly Leu Val Ala Val Pro
65                  70                  75                  80
Leu Glu Asp Phe Asp Pro Tyr Tyr Leu Thr Gln Lys Thr Phe Val Val
                85                  90                  95
Leu Asn Arg Gly Lys Thr Leu Phe Arg Phe Ser Ala Thr Pro Ala Leu
            100                 105                 110
Tyr Ile Leu Ser Pro Phe Asn Leu Ile Arg Arg Ile Ala Ile Lys Ile
        115                 120                 125
Leu Ile His Ser Val Phe Ser Met Ile Ile Met Cys Thr Ile Leu Thr
    130                 135                 140
Asn Cys Val Phe Met Thr Phe Ser Asn Pro Pro Glu Trp Ser Lys Asn
145                 150                 155                 160
Val Glu Tyr Thr Phe Thr Gly Ile Tyr Thr Phe Glu Ser Leu Val Lys
                165                 170                 175
Ile Ile Ala Arg Gly Phe Cys Ile Asp Gly Phe Thr Phe Leu Arg Asp
            180                 185                 190
Pro Trp Asn Trp Leu Asp Phe Ser Val Ile Met Met Ala Tyr Val Thr
        195                 200                 205
Glu Phe Val Asp Leu Gly Asn Val Ser Ala Leu Arg Thr Phe Arg Val
    210                 215                 220
Leu Arg Ala Leu Lys Thr Ile Ser Val Ile Pro Gly Leu Lys Thr Ile
225                 230                 235                 240
Val Gly Ala Leu Ile Gln Ser Val Lys Lys Leu Ser Asp Val Met Ile
                245                 250                 255
Leu Thr Val Phe Cys Leu Ser Val Phe Ala Leu Ile Gly Leu Gln Leu
            260                 265                 270
Phe Met Gly Asn Leu Arg Asn Lys Cys Val Val Trp Pro Ile Asn Phe
        275                 280                 285
Asn Glu Ser Tyr Leu Glu Asn Gly Thr Arg Gly Phe Asp Trp Glu Glu
    290                 295                 300
Tyr Ile Asn Asn Lys Thr Asn Phe Tyr Met Val Pro Gly Met Leu Glu
305                 310                 315                 320
Pro Leu Leu Cys Gly Asn Ser Ser Asp Ala Gly Gln Cys Pro Glu Gly
                325                 330                 335
Phe Gln Cys Met Lys Ala Gly Arg Asn Pro Asn Tyr Gly Tyr Thr Ser
            340                 345                 350
Phe Asp Thr Phe Ser Trp Ala Phe Leu Ala Leu Phe Arg Leu Met Thr
        355                 360                 365
Gln Asp Tyr Trp Glu Asn Leu Tyr Gln Leu Thr Leu Arg Ala Ala Gly
    370                 375                 380
Lys Thr Tyr Met Ile Phe Phe Val Leu Val Ile Phe Val Gly Ser Phe
385                 390                 395                 400
Tyr Leu Val Asn Leu Ile Leu Ala Val Val Ala Met Ala Tyr Glu Glu
                405                 410                 415
Gln Asn Gln Ala Thr Leu Glu Glu Ala Glu Gln Lys Glu Ala Glu Phe
            420                 425                 430
Lys Ala Met Leu Glu Gln Leu Lys Lys Gln Gln Glu Glu Ala Gln Ala
        435                 440                 445
Ala Ala Met Ala Thr Ser Ala Gly Thr Val Ser Glu Asp Ala Ile Glu
    450                 455                 460
Glu Glu Gly Glu Asp Gly Val Gly Ser Pro Arg Ser Ser Ser Glu Leu
465                 470                 475                 480
Ser Lys Leu Ser Ser Lys Ser Ala Lys Glu Arg Arg Asn Arg Arg Lys
                485                 490                 495
Lys Arg Lys Gln Lys Glu Leu Ser Glu Gly Glu Glu Lys Gly Asp Pro
            500                 505                 510
Glu Lys Val Phe Lys Ser Glu Ser Glu Asp Gly Met Arg Arg Lys Ala
        515                 520                 525
Phe Arg Leu Pro Asp Asn Arg Ile Gly Arg Lys Phe Ser Ile Met Asn
    530                 535                 540
Gln Ser Leu Leu Ser Ile Pro Gly Ser Pro Phe Leu Ser Arg His Asn
545                 550                 555                 560
Ser Lys Ser Ser Ile Phe Ser Phe Arg Gly Pro Gly Arg Phe Arg Asp
                565                 570                 575
Pro Gly Ser Glu Asn Glu Phe Ala Asp Asp Glu His Ser Thr Val Glu
            580                 585                 590
Glu Ser Glu Gly Arg Arg Asp Ser Leu Phe Ile Pro Ile Arg Ala Arg
        595                 600                 605
Glu Arg Arg Ser Ser Tyr Ser Gly Tyr Ser Gly Tyr Ser Gln Cys Ser
    610                 615                 620
Arg Ser Ser Arg Ile Phe Pro Ser Leu Arg Arg Ser Val Lys Arg Asn
625                 630                 635                 640
Ser Thr Val Asp Cys Asn Gly Val Val Ser Leu Ile Gly Pro Gly Ser
                645                 650                 655
His Ile Gly Arg Leu Leu Pro Glu Val Lys Ile Asp Lys Ala Ala Thr
            660                 665                 670
Asp Ser Ala Thr Thr Glu Val Glu Ile Lys Lys Lys Gly Pro Gly Ser
        675                 680                 685
Leu Leu Val Ser Met Asp Gln Leu Ala Ser Tyr Gly Arg Lys Asp Arg
    690                 695                 700
Ile Asn Ser Ile Met Ser Val Val Thr Asn Thr Leu Val Glu Glu Leu
705                 710                 715                 720
Glu Glu Ser Gln Arg Lys Cys Pro Pro Cys Trp Tyr Lys Phe Ala Asn
                725                 730                 735
Thr Phe Leu Ile Trp Glu Cys His Pro Tyr Trp Ile Lys Leu Lys Glu
            740                 745                 750
Ile Val Asn Leu Ile Val Met Asp Pro Phe Val Asp Leu Ala Ile Thr
        755                 760                 765
Ile Cys Ile Val Leu Asn Thr Leu Phe Met Ala Met Glu His His Pro
    770                 775                 780
Met Thr Pro Gln Phe Glu His Val Leu Ala Val Gly Asn Leu Val Phe
785                 790                 795                 800
Thr Gly Ile Phe Thr Ala Glu Met Phe Leu Lys Leu Ile Ala Met Asp
                805                 810                 815
Pro Tyr Tyr Tyr Phe Gln Glu Gly Trp Asn Ile Phe Asp Gly Phe Ile
            820                 825                 830
Val Ser Leu Ser Leu Met Glu Leu Ser Leu Ala Asp Val Glu Gly Leu
        835                 840                 845
Ser Val Leu Arg Ser Phe Arg Leu Leu Arg Val Phe Lys Leu Ala Lys
    850                 855                 860
Ser Trp Pro Thr Leu Asn Met Leu Ile Lys Ile Ile Gly Asn Ser Val
865                 870                 875                 880
Gly Ala Leu Gly Asn Leu Thr Leu Val Leu Ala Ile Ile Val Phe Ile
                885                 890                 895
Phe Ala Val Val Gly Met Gln Leu Phe Gly Lys Ser Tyr Lys Glu Cys
            900                 905                 910
Val Cys Lys Ile Asn Gln Glu Cys Lys Leu Pro Arg Trp His Met Asn
        915                 920                 925
Asp Phe Phe His Ser Phe Leu Ile Val Phe Arg Val Leu Cys Gly Glu
    930                 935                 940
Trp Ile Glu Thr Met Trp Asp Cys Met Glu Val Ala Gly Gln Ala Met
945                 950                 955                 960
Cys Leu Ile Val Phe Met Met Val Met Val Ile Gly Asn Leu Val Val
                965                 970                 975
Leu Asn Leu Phe Leu Ala Leu Leu Leu Ser Ser Phe Ser Ala Asp Asn
            980                 985                 990
Leu Ala Ala Thr Asp Asp Asp Gly Glu Met Asn Asn Leu Gln Ile Ser
        995                 1000                1005
Val Ile Arg Ile Lys Lys Gly Val Ala Trp Thr Lys Val Lys Val His
    1010                1015                1020
Ala Phe Met Gln Ala His Phe Lys Gln Arg Glu Ala Asp Glu Val Lys
1025                1030                1035                1040
Pro Leu Asp Glu Leu Tyr Glu Lys Lys Ala Asn Cys Ile Ala Asn His
                1045                1050                1055
Thr Gly Val Asp Ile His Arg Asn Gly Asp Phe Gln Lys Asn Gly Asn
            1060                1065                1070
Gly Thr Thr Ser Gly Ile Gly Ser Ser Val Glu Lys Tyr Ile Ile Asp
        1075                1080                1085
Glu Asp His Met Ser Phe Ile Asn Asn Pro Asn Leu Thr Val Arg Val
    1090                1095                1100
Pro Ile Ala Val Gly Glu Ser Asp Phe Glu Asn Leu Asn Thr Glu Asp
1105                1110                1115                1120
Val Ser Ser Glu Ser Asp Pro Glu Gly Ser Lys Asp Lys Leu Asp Asp
                1125                1130                1135
Thr Ser Ser Ser Glu Gly Ser Thr Ile Asp Ile Lys Pro Glu Val Glu
            1140                1145                1150
Glu Val Pro Val Glu Gln Pro Glu Glu Tyr Leu Asp Pro Asp Ala Cys
        1155                1160                1165
Phe Thr Glu Gly Cys Val Gln Arg Phe Lys Cys Cys Gln Val Asn Ile
    1170                1175                1180
Glu Glu Gly Leu Gly Lys Ser Trp Trp Ile Leu Arg Lys Thr Cys Phe
1185                1190                1195                1200
Leu Ile Val Glu His Asn Trp Phe Glu Thr Phe Ile Ile Phe Met Ile
                1205                1210                1215
Leu Leu Ser Ser Gly Ala Leu Ala Phe Glu Asp Ile Tyr Ile Glu Gln
            1220                1225                1230
Arg Lys Thr Ile Arg Thr Ile Leu Glu Tyr Ala Asp Lys Val Phe Thr
        1235                1240                1245
Tyr Ile Phe Ile Leu Glu Met Leu Leu Lys Trp Thr Ala Tyr Gly Phe
    1250                1255                1260
Val Lys Phe Phe Thr Asn Ala Trp Cys Trp Leu Asp Phe Leu Ile Val
1265                1270                1275                1280
Ala Val Ser Leu Val Ser Leu Ile Ala Asn Ala Leu Gly Tyr Ser Glu
                1285                1290                1295
Leu Gly Ala Ile Lys Ser Leu Arg Thr Leu Arg Ala Leu Arg Pro Leu
            1300                1305                1310
Arg Ala Leu Ser Arg Phe Glu Gly Met Arg Val Val Val Asn Ala Leu
        1315                1320                1325
Val Gly Ala Ile Pro Ser Ile Met Asn Val Leu Leu Val Cys Leu Ile
    1330                1335                1340
Phe Trp Leu Ile Phe Ser Ile Met Gly Val Asn Leu Phe Ala Gly Lys
1345                1350                1355                1360
Tyr His Tyr Cys Phe Asn Glu Thr Ser Glu Ile Arg Phe Glu Ile Asp
                1365                1370                1375
Ile Val Asn Asn Lys Thr Asp Cys Glu Lys Leu Met Glu Gly Asn Ser
            1380                1385                1390
Thr Glu Ile Arg Trp Lys Asn Val Lys Ile Asn Phe Asp Asn Val Gly
        1395                1400                1405
Ala Gly Tyr Leu Ala Leu Leu Gln Val Ala Thr Phe Lys Gly Trp Met
    1410                1415                1420
Asp Ile Met Tyr Ala Ala Val Asp Ser Arg Lys Pro Asp Glu Gln Pro
1425                1430                1435                1440
Asp Tyr Glu Gly Asn Ile Tyr Met Tyr Ile Tyr Phe Val Ile Phe Ile
                1445                1450                1455
Ile Phe Gly Ser Phe Phe Thr Leu Asn Leu Phe Ile Gly Val Ile Ile
            1460                1465                1470
Asp Asn Phe Asn Gln Gln Lys Lys Lys Phe Gly Gly Gln Asp Ile Phe
        1475                1480                1485
Met Thr Glu Glu Gln Lys Lys Tyr Tyr Asn Ala Met Lys Lys Leu Gly
    1490                1495                1500
Ser Lys Lys Pro Gln Lys Pro Ile Pro Arg Pro Leu Asn Lys Ile Gln
1505                1510                1515                1520
Gly Ile Val Phe Asp Phe Val Thr Gln Gln Ala Phe Asp Ile Val Ile
                1525                1530                1535
Met Met Leu Ile Cys Leu Asn Met Val Thr Met Met Val Glu Thr Asp
            1540                1545                1550
Thr Gln Ser Lys Gln Met Glu Asn Ile Leu Tyr Trp Ile Asn Leu Val
        1555                1560                1565
Phe Val Ile Phe Phe Thr Cys Glu Cys Val Leu Lys Met Phe Ala Leu
    1570                1575                1580
Arg His Tyr Tyr Phe Thr Ile Gly Trp Asn Ile Phe Asp Phe Val Val
1585                1590                1595                1600
Val Ile Leu Ser Ile Val Gly Met Phe Leu Ala Asp Ile Ile Glu Lys
                1605                1610                1615
Tyr Phe Val Ser Pro Thr Leu Phe Arg Val Ile Arg Leu Ala Arg Ile
            1620                1625                1630
Gly Arg Ile Leu Arg Leu Ile Lys Gly Ala Lys Gly Ile Arg Thr Leu
        1635                1640                1645
Leu Phe Ala Leu Met Met Ser Leu Pro Ala Leu Phe Asn Ile Gly Leu
    1650                1655                1660
Leu Leu Phe Leu Val Met Phe Ile Phe Ser Ile Phe Gly Met Ser Asn
1665                1670                1675                1680
Phe Ala Tyr Val Lys His Glu Ala Gly Ile Asp Asp Met Phe Asn Phe
                1685                1690                1695
Glu Thr Phe Gly Asn Ser Met Ile Cys Leu Phe Gln Ile Thr Thr Ser
            1700                1705                1710
Ala Gly Trp Asp Gly Leu Leu Leu Pro Ile Leu Asn Arg Pro Pro Asp
        1715                1720                1725
Cys Ser Leu Asp Lys Glu His Pro Gly Ser Gly Phe Lys Gly Asp Cys
    1730                1735                1740
Gly Asn Pro Ser Val Gly Ile Phe Phe Phe Val Ser Tyr Ile Ile Ile
1745                1750                1755                1760
Ser Phe Leu Ile Val Val Asn Met Tyr Ile Ala Ile Ile Leu Glu Asn
                1765                1770                1775
Phe Ser Val Ala Thr Glu Glu Ser Ala Asp Pro Leu Ser Glu Asp Asp
            1780                1785                1790
Phe Glu Thr Phe Tyr Glu Ile Trp Glu Lys Phe Asp Pro Asp Ala Thr
        1795                1800                1805
Gln Phe Ile Glu Tyr Cys Lys Leu Ala Asp Phe Ala Asp Ala Leu Glu
    1810                1815                1820
His Pro Leu Arg Val Pro Lys Pro Asn Thr Ile Glu Leu Ile Ala Met
1825                1830                1835                1840
Asp Leu Pro Met Val Ser Gly Asp Arg Ile His Cys Leu Asp Ile Leu
                1845                1850                1855
Phe Ala Phe Thr Lys Arg Val Leu Gly Asp Ser Gly Glu Leu Asp Ile
            1860                1865                1870
Leu Arg Gln Gln Met Glu Glu Arg Phe Val Ala Ser Asn Pro Ser Lys
        1875                1880                1885
Val Ser Tyr Glu Pro Ile Thr Thr Thr Leu Arg Arg Lys Gln Glu Glu
    1890                1895                1900
Val Ser Ala Val Val Leu Gln Arg Ala Tyr Arg Gly His Leu Ala Arg
1905                1910                1915                1920
Arg Gly Phe Ile Cys Arg Lys Met Ala Ser Asn Lys Leu Glu Asn Gly
                1925                1930                1935
Gly Thr His Arg Asp Lys Lys Glu Ser Thr Pro Ser Thr Ala Ser Leu
            1940                1945                1950
Pro Ser Tyr Asp Ser Val Thr Lys Pro Asp Lys Glu Lys Gln Gln Arg
        1955                1960                1965
Ala Glu Glu Gly Arg Arg Glu Arg Ala Lys Arg Gln Lys Glu Val Arg
    1970                1975                1980
Glu Ser Lys Cys
1985
 
           
           
             
               696 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             5
CTCAACATGG TTACTATGAT GGTGGAGACA GACACTCAGA GCAAGCAGAT GGAGAACATT     60
CTTTACTGGA TTAATCTGGT CTTTGTCATC TTCTTCACCT GCGAGTGTGT GCTCAAAATG    120
TTTGCCTTGA GACACTACTA TTTCACCATT GGCTGGAACA TCTTTGACTT TGTGGTGGTC    180
ATCCTCTCCA TTGTGGGAAT GTTCCTGGCT GATATCATTG AGAAGTACTT CGTCTCCCCA    240
ACCCTATTCC GAGTTATCCG ATTGGCCCGT ATTGGGCGCA TCTTGCGTCT GATCAAGGGG    300
GCCAAAGGGA TCCGCACCCT GCTCTTTGGC CTTAATGATG TCGCTGGCCG CCCTGTTCAA    360
CATCGCCTCC TGCTCTTCCT CGTCATGTTC ATCTTCTCCA TTTTTGGCAT GTCCAACTTC    420
GCATACGTGA AGCACGAGGC CGGCATTGAC GACATGTTCA ACTTCGAGAC ATTTGGCAAC    480
AGCATGATCT GTTTGTTCCA GATCACAACG TCTGCTGGCT GGGATGGCCT GCTGCTGCCA    540
ATCCTGAACC GCCCCCCTGA CTGCAGCTTG GACAAAGAGC ACCCAGGGAG TGGCTTCAAA    600
GGGGACTGTG GGAACCCCTC GGTGGGCATC TTCTTCTTTG TGAGCTACAT CATCATCTCC    660
TTCCTGATTG TGGTGAACAT GTACATCGCA GTCATC                              696
 
           
           
             
               232 amino acids 
               amino acid 
               single 
               linear 
             
             
               peptide 
             
             6
Leu Asn Met Val Thr Met Met Val Glu Thr Asp Thr Gln Ser Lys Gln
1               5                   10                  15
Met Glu Asn Ile Leu Tyr Trp Ile Asn Leu Val Phe Val Ile Phe Phe
            20                  25                  30
Thr Cys Glu Cys Val Leu Lys Met Phe Ala Leu Arg His Tyr Tyr Phe
        35                  40                  45
Thr Ile Gly Trp Asn Ile Phe Asp Phe Val Val Val Ile Leu Ser Ile
    50                  55                  60
Val Gly Met Phe Leu Ala Asp Ile Ile Glu Lys Tyr Phe Val Ser Pro
65                  70                  75                  80
Thr Leu Phe Arg Val Ile Arg Leu Ala Arg Ile Gly Arg Ile Leu Arg
                85                  90                  95
Leu Ile Lys Gly Ala Lys Gly Ile Arg Thr Leu Leu Phe Gly Leu Asn
            100                 105                 110
Asp Val Ala Gly Arg Pro Val Gln His Arg Leu Leu Leu Phe Leu Val
        115                 120                 125
Met Phe Ile Phe Ser Ile Phe Gly Met Ser Asn Phe Ala Tyr Val Lys
    130                 135                 140
His Glu Ala Gly Ile Asp Asp Met Phe Asn Phe Glu Thr Phe Gly Asn
145                 150                 155                 160
Ser Met Ile Cys Leu Phe Gln Ile Thr Thr Ser Ala Gly Trp Asp Gly
                165                 170                 175
Leu Leu Leu Pro Ile Leu Asn Arg Pro Pro Asp Cys Ser Leu Asp Lys
            180                 185                 190
Glu His Pro Gly Ser Gly Phe Lys Gly Asp Cys Gly Asn Pro Ser Val
        195                 200                 205
Gly Ile Phe Phe Phe Val Ser Tyr Ile Ile Ile Ser Phe Leu Ile Val
    210                 215                 220
Val Asn Met Tyr Ile Ala Val Ile
225                 230
 
           
           
             
               6556 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             7
CCAAGATGGC GCCCACCGCA GTCCCGCCCG CCGCAGCCTC GGCGCCTCTG CAGTCCGGCC     60
GCGCCTCCCG GGCCCCGCGC TAGGGCCGCT GCCGCCTCGC CCGCCGCCGC CGCCGCCAGC    120
TGACCTGTCC CGGACACATA ACTAACGAAG CTGCTGCAGG ATGAGAAGAT GGCAGCGCGG    180
CTGCTCGCAC CACCAGGCCC TGATAGTTTC AAGCCTTTCA CCCCTGAGTC GCTGGCAAAC    240
ATCGAGAGGC GTATTGCCGA GAGCAAGCTC AAGAAACCAC CAAAGGCGGA TGGCAGCCAC    300
CGGGAGGACG ATGAAGACAG CAAGCCCAAG CCAAACAGTG ACCTGGAGGC TGGGAAGAGT    360
TTGCCTTTCA TCTACGGGGA CATCCCGCAA GGCCTGGTTG CGGTTCCCCT GGAGGACTTT    420
GACCCTTACT ATTTGACGCA GAAAACCTTT GTAGTATTAA ACAGAGGGAA AACTCTCTTC    480
AGATTTAGTG CCACACCTGC CTTGTACATT TTAAGCCCTT TTAACCTGAT AAGAAGAATA    540
GCTATTAAAA TTTTGATACA CTCAGTTTTC AGCATGATCA TCATGTGCAC CATCCTGACC    600
AACTGTGTGT TCATGACCTT TAGTAACCCT CCAGAATGGT CCAAGAATGT GGAGTACACA    660
TTCACAGGGA TTTACACATT TGAATCACTA GTGAAAATCA TCGCAAGAGG TTTCTGCATA    720
GACGGCTTCA CCTTCTTGCG AGACCCGTGG AACTGGTTAG ACTTCAGTGT CATCATGATG    780
GCATATGTGA CAGAGTTTGT GGACCTGGGC AATGTCTCAG CGCTGAGAAC ATTCAGGGTT    840
CTCCGAGCTT TGAAAACTAT CTCTGTAATT CCAGGCCTGA AGACAATCGT GGGCGCCCTA    900
ATCCAGTCCG TGAAGAAGCT GTCGGACGTG ATGATCCTGA CAGTGTTCTG CCTGAGTGTT    960
TTCGCCCTGA TTGGCCTGCA GCTCTTCATG GGGAACCTTC GAAACAAGTG TGTCGTGTGG   1020
CCCATAAACT TCAACGAGAG CTACCTGGAG AACGGCACCA GAGGCTTTGA CTGGGAGGAA   1080
TATATCAACA ATAAAACAAA CTTTTACATG GTTCCTGGCA TGCTAGAACC CTTGCTCTGC   1140
GGGAACAGTT CTGATGCTGG GCAATGCCCA GAGGGATTCC AGTGCATGAA AGCAGGAAGG   1200
AACCCCAACT ACGGTTACAC CAGCTTTGAC ACCTTCAGCT GGGCCTTCTT GGCATTATTC   1260
CGCCTTATGA CCCAGGACTA TTGGGAGAAC TTATACCAGC TGACCTTACG AGCCGCTGGG   1320
AAAACGTACA TGATCTTCTT TGTCTTGGTC ATCTTCGTGG GTTCTTTCTA TCTGGTGAAC   1380
TTGATCTTGG CTGTGGTGGC CATGGCTTAT GAGGAACAGA ACCAGGCAAC ACTGGAGGAG   1440
GCAGAGCAAA AAGAGGCCGA GTTCAAGGCA ATGCTGGAGC AACTCAAGAA GCAGCAGGAG   1500
GAGGCACAGG CTGCTGCAAT GGCCACCTCA GCGGGCACTG TCTCGGAAGA CGCCATTGAA   1560
GAAGAAGGGG AAGATGGGGT AGGCTCTCCG AGGAGCTCTT CTGAACTGTC TAAACTCAGT   1620
TCCAAGAGCG CGAAGGAGCG GCGGAACCGA CGGAAGAAGA GGAAGCAGAA GGAGCTCTCT   1680
GAAGGCGAGG AGAAAGGGGA CCCGGAGAAG GTGTTTAAGT CAGAGTCGGA AGACGGTATG   1740
AGAAGGAAGG CCTTCCGGCT GCCAGACAAC AGGATAGGGA GGAAGTTTTC CATCATGAAT   1800
CAGTCGCTGC TCAGCATTCC AGGCTCGCCC TTCCTCTCCC GACATAACAG CAAAAGCAGC   1860
ATCTTCAGCT TCCGGGGACC CGGTCGGTTC CGGGACCCCG GCTCTGAGAA TGAGTTCGCA   1920
GACGATGAAC ACAGCACCGT GGAGGAGAGC GAGGGCCGGC GTGACTCGCT CTTCATCCCG   1980
ATCCGCGCCC GCGAGCGCCG CAGCAGCTAC AGTGGCTACA GCGGCTACAG CCAGTGCAGC   2040
CGCTCGTCGC GCATCTTCCC CAGCCTGCGG CGCAGCGTGA AGCGCAACAG CACGGTGGAC   2100
TGCAACGGCG TAGTGTCACT CATCGGGCCC GGCTCACACA TCGGGCGGCT CCTGCCTGAG   2160
GCAACGACTG AGGTGGAAAT TAAGAAGAAA GGCCCTGGAT CTCTTTTAGT TTCTATGGAC   2220
CAACTCGCCT CCTACGGACG GAAGGACAGA ATCAACAGCA TAATGAGCGT GGTCACAAAC   2280
ACGCTAGTGG AAGAGCTGGA AGAGTCTCAG AGAAAGTGCC CACCGTGCTG GTATAAGTTT   2340
GCCAACACTT TCCTCATCTG GGAGTGTCAC CCCTACTGGA TAAAACTGAA GGAGATCGTG   2400
AACTTAATCG TCATGGACCC TTTTGTAGAC TTAGCCATCA CCATCTGCAT CGTTCTGAAT   2460
ACGCTATTTA TGGCAATGGA GCACCATCCC ATGACACCAC AGTTCGAACA CGTCTTGGCC   2520
GTAGGAAATC TGGTGTTCAC CGGGATCTTC ACGGCGGAAA TGTTTCTGAA GCTCATAGCC   2580
ATGGACCCCT ACTATTATTT CCAAGAAGGC TGGAACATTT TTGACGGATT TATTGTCTCC   2640
CTCAGTTTAA TGGAGCTGAG TCTCGCAGAT GTGGAGGGGC TCTCAGTGCT GCGGTCTTTC   2700
CGACTGCTCC GAGTCTTCAA GCTGGCCAAG TCCTGGCCCA CCCTGAACAT GCTGATCAAG   2760
ATCATCGGGA ACTCCGTGGG TGCCCTGGGC AACCTGACCC TGGTGCTGGC CATCATCGTC   2820
TTCATCTTCG CCGTGGTGGG GATGCAGCTG TTTGGAAAGA GTTACAAGGA GTGCGTCTGT   2880
AAGATCAACC AGGAGTGCAA GCTCCCGCGC TGGCACATGA ACGACTTCTT CCACTCCTTC   2940
CTCATCGTCT TCCGAGTGCT GTGTGGGGAG TGGATCGAGA CCATGTGGGA CTGCATGGAG   3000
GTGGCCGGCC AGGCCATGTG CCTCATTGTC TTCATGATGG TTATGGTCAT TGGCAACCTG   3060
GTGGTGCTGA ATCTATTCCT GGCCTTGCTT CTGAGCTCCT TCAGCGCAGA CAACCTGGCG   3120
GCCACAGACG ACGACGGGGA AATGAACAAC CTGCAGATCT CAGTGATCCG GATCAAGAAG   3180
GGCGTGGCCT GGACCAAAGT GAAGGTGCAC GCCTTCATGC AGGCTCACTT CAAGCAGCGG   3240
GAGGCGGATG AAGTGAAACC CCTCGACGAG CTGTATGAGA AGAAGGCCAA CTGCATCGCC   3300
AACCACACGG GCGTGGATAT CCACCGGAAC GGCGACTTCC AGAAGAACGG GAACGGAACC   3360
ACCAGCGGCA TCGGCAGCAG CGTGGAGAAG TACATCATCG ACGAGGACCA CATGTCCTTC   3420
ATTAACAACC CAAACCTGAC CGTCCGGGTG CCCATTGCTG TGGGCGAGTC TGACTTCGAG   3480
AACCTCAACA CAGAGGATGT TAGCAGCGAA TCAGACCCTG AAGGCAGCAA AGATAAACTG   3540
GACGATACCA GCTCCTCAGA AGGAAGTACC ATCGACATCA AGCCTGAGGT GGAAGAAGTT   3600
CCCGTGGAGC AACCTGAGGA ATACTTGGAT CCGGACGCCT GCTTTACAGA GGGTTGCGTC   3660
CAGCGGTTCA AGTGCTGCCA GGTCAACATC GAGGAAGGAC TAGGCAAGTC GTGGTGGATC   3720
TTGCGGAAAA CCTGCTTCCT CATTGTGGAG CACAATTGGT TTGAGACCTT CATCATCTTC   3780
ATGATTCTGC TCAGCAGTGG CGCCCTGGCC TTTGAGGACA TCTACATTGA GCAGAGGAAG   3840
ACCATCCGCA CCATCCTGGA GTATGCGGAC AAGGTCTTCA CCTACATCTT CATCCTGGAG   3900
ATGTTGCTCA AGTGGACAGC CTACGGCTTC GTCAAGTTCT TCACCAATGC CTGGTGCTGG   3960
TTGGACTTCC TCATTGTGGC TGTCTCTTTA GTCAGCCTTA TAGCTAATGC CCTGGGCTAC   4020
TCGGAACTAG GTGCCATAAA GTCCCTTAGG ACCCTAAGAG CTTTGAGACC CTTAAGAGCC   4080
TTATCACGAT TTGAAGGGAT GAGGGTGGTG GTGAATGCCT TGGTGGGCGC CATCCCCTCC   4140
ATCATGAATG TGCTGCTGGT GTGTCTCATC TTCTGGCTGA TTTTCAGCAT CATGGGAGTT   4200
AACCTGTTTG CGGGGAAATA CCACTACTGC TTTAATGAGA CTTCTGAAAT CCGGTTCGAA   4260
ATCGATATTG TCAACAATAA AACGGACTGT GAGAAGCTCA TGGAGGGCAA CAGCACGGAG   4320
ATCCGATGGA AGAATGTCAA GATCAACTTT GACAATGTCG GAGCAGGGTA CCTGGCCCTT   4380
CTTCAAGTGG CAACCTTCAA AGGCTGGATG GACATCATGT ATGCGGCTGT AGATTCCCGA   4440
AAGCCAGACG AGCAGCCTGA CTACGAGGGC AACATCTACA TGTACATCTA CTTCGTCATC   4500
TTCATCATCT TCGGCTCCTT CTTCACCCTC AACCTGTTCA TCGGTGTCAT CATCGACAAC   4560
TTCAACCAGC AGAAGAAAAA GTTTGGAGGT CAGGACATCT TCATGACAGA GGAACAGAAG   4620
AAGTACTACA ATGCCATGAA AAAGCTGGGC TCCAAGAAGC CACAGAAGCC CATCCCCCGA   4680
CCCTTGAACA AAATCCAAGG GATTGTCTTT GATTTCGTCA CTCAACAAGC CTTTGACATT   4740
GTGATCATGA TGCTCATCTG CCTTAACATG GTGACAATGA TGGTGGAGAC AGACACTCAG   4800
AGCAAGCAGA TGGAGAACAT TCTTTACTGG ATTAATCTGG TCTTTGTCAT CTTCTTCACC   4860
TGCGAGTGTG TGCTCAAAAT GTTTGCCTTG AGACACTACT ATTTCACCAT TGGCTGGAAC   4920
ATCTTTGACT TTGTGGTGGT CATCCTCTCC ATTGTGGGAA TGTTCCTGGC TGATATCATT   4980
GAGAAGTACT TCGTCTCCCC AACCCTATTC CGAGTTATCC GATTGGCCCG TATTGGGCGC   5040
ATCTTGCGTC TGATCAAGGG CGCCAAAGGG ATCCGCACCC TGCTCTTTGC CTTAATGATG   5100
TCGCTGCCCG CCCTGTTCAA CATCGGCCTC CTGCTCTTCC TCGTCATGTT CATCTTCTCC   5160
ATTTTTGGCA TGTCCAACTT CGCATACGTG AAGCACGAGG CCGGCATTGA CGACATGTTC   5220
AACTTCGAGA CATTTGGCAA CAGCATGATC TGTTTGTTCC AGATCACAAC GTCTGCTGGC   5280
TGGGATGGCC TGCTGCTGCC AATCCTGAAC CGCCCCCCTG ACTGCAGCTT GGACAAAGAG   5340
CACCCAGGGA GTGGCTTCAA AGGGGACTGT GGGAACCCCT CGGTGGGCAT CTTCTTCTTT   5400
GTGAGCTACA TCATCATCTC CTTCCTGATT GTGGTGAACA TGTACATCGC CATCATCCTG   5460
GAGAACTTCA GCGTGGCCAC CGAGGAGAGC GCCGACCCTC TGAGTGAGGA TGACTTCGAG   5520
ACTTTCTATG AGATCTGGGA GAAGTTTGAC CCAGACGCCA CCCAGTTCAT CGAGTACTGT   5580
AAGCTGGCAG ACTTTGCCGA CGCCCTGGAG CACCCGCTCC GAGTACCCAA GCCCAACACC   5640
ATCGAGCTCA TCGCCATGGA CCTGCCCATG GTGAGCGGAG ATCGCATCCA CTGCTTGGAC   5700
ATCCTTTTCG CCTTCACCAA GCGAGTCCTG GGAGACAGTG GGGAGTTGGA CATCCTGCGG   5760
CAGCAGATGG AGGAGCGGTT CGTGGCATCC AATCCTTCCA AAGTGTCTTA CGAGCCTATC   5820
ACAACCACTC TGCGGCGCAA GCAGGAGGAG GTGTCTGCAG TGGTCCTGCA GCGTGCCTAC   5880
AGGGGACACT TGGCTAGGCG GGGCTTCATC TGCAGAAAGA TGGCCTCCAA CAAGCTGGAG   5940
AATGGAGGCA CACACAGAGA CAAGAAGGAG AGCACCCCGT CCACAGCCTC CCTCCCCTCT   6000
TACGACAGCG TCACAAAGCC AGACAAGGAG AAGCAGCAGC GTGCGGAGGA GGGCAGAAGG   6060
GAAAGAGCCA AGAGGCAAAA AGAGGTCAGG GAGTCCAAGT GCTAGAGGAG GGGAAAGGAA   6120
GCTTACCCCG GCTGAACACT GGCAAGTGAA AGCTTGTTTA CAAACTTCCG AATCTCACGG   6180
ATGCAGAGCA GCTGTGCAGA CGCTCGCTGT ACTGGAAGAC CTATACCAAA CATAGTCTGC   6240
TTACATGTGA CATGGTGGCA TCCTGAGCGG TGACTGCTGG GGACAAAGGA CCCTGCTCCC   6300
TGGACTCACA GATCTCCTAT CGCTTGGGCA GACGGTTACT GCATGTTCCA CACTTAGTCA   6360
ATGCAACTTA GGACTAAACT AACCAGGATA CAAAACCGAG GCGGCTGCCG GGACCAGCAG   6420
ATCACCGCTG CAGCCAAATG GATTTTATTT TTTCATTTTG TTGATTCTCA GAAGCAGAAA   6480
GCATCACTTT AAAAGTTTGT TTGTTCATNC AAACAATATT TGAATTCTTA CATTAGTTAA   6540
GCTAAGCANC AAAAAG                                                   6556
 
           
           
             
               6826 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             8
ATGAGAAGAT CGGCGCGGCT GCTCGCACCA CCAGGCCCTG ATAGTTTCAA GCCTTTCACC     60
CCTGAGTCGC TGGCAAACAT CGAGAGGCGT ATTGCCGAGA GCAAGCTCAA GAAACCACCA    120
AAGGCGGATG GCAGCCACCG GGAGGACGAT GAAGACAGCA AGCCCAAGCC AAACAGTGAC    180
CTGGAGGCTG GGAAGAGTTT GCCTTTCATC TACGGGGACA TCCCGCAAGG CCTGGTTGCG    240
GTTCCCCTGG AGGACTTTGA CCCTTACTAT TTGACGCAGA AAACCTTTGT AGTATTAAAC    300
AGAGGGAAAA CTCTCTTCAG ATTTAGTGCC ACACCTGCCT TGTACATTTT AAGCCCTTTT    360
AACCTGATAA GAAGAATAGC TATTAAAATT TTGATACACT CAGTTTTCAG CATGATCATC    420
ATGTGCACCA TCCTGACCAA CTGTGTGTTC ATGACCTTTA GTAACCCTCC AGAATGGTCC    480
AAGAATGTGG AGTACACATT CACAGGGATT TACACATTTG AATCACTAGT GAAAATCATC    540
GCAAGAGGTT TCTGCATAGA CGGCTTCACC TTCTTACGAG ACCCGTGGAA CTGGTTAGAC    600
TTCAGTGTCA TCATGATGGC ATATGTGACA GAGTTTGTGG ACCTGGGCAA TGTCTCAGCG    660
CTGAGAACAT TCAGGGTTCT CCGAGCTTTG AAAACTATCT CTGTAATTCC AGGCCTGAAG    720
ACAATCGTGG GCGCCCTAAT CCAGTCCGTG AAGAAGCTGT CGGACGTGAT GATCCTGACA    780
GTGTTCTGCC TGAGTGTTTT CGCCCTGATT GGCCTGCAGC TCTTTCATGG GAACCTTTCG    840
AAACAGTGTG TCGTGTGGCC CATAAACTTC AACGAGAGCT ACCTGGAGAA CGGCACCAGA    900
GGCTTTGACT GGGAGGAATA TATCAACAAT AAAACAAACT TTTACATGGT TCCTGGCATG    960
CTAGAACCCT TGCTCTGCGG GAACAGTTCT GATGCTGGGC AATGCGAAGG ATTCCAGTGC   1020
AGTAAAGCAG GAAGGAACCC CAACTACGGT TACACCAGCT TTGACACCTT CAGCTGGGCC   1080
TTCTTGGCAT TATTCCGCCT TATGACCCAG GACTATTGGG AGAACTTATA CCAGCTGACC   1140
TTACGAGCCG CTGGGAAAAC GTACATGATC TTCTTTGTCT TGGTCATCTT CGTGGGTTCT   1200
TTCTATCCGG TGAACTTGAT CTTGGCTGTG GTGGCCATGG CTTATGAGGA ACAGAACCAG   1260
GCAACACTGG AGGAGGCAGA GCAAAAAGAG GCCGAGTTCA AGGCAATGCT GGAGCAACTC   1320
AAGAAGCAGC AGGAGGAGGC ACAGGCTGCT GCAATGGCCA CCTCAGCGGG CACTGTCTCG   1380
GAAGACGCCA TTGAAGAAGA AGGGGAAGAT GGGGTAGGCT CTCCGAGGAG CTCTTCTGAA   1440
CTGTCTAAAC TCAGTTCCAA GAGCGCGAAG GAGCGGCGGA ACCGACGGAA GAAGAGGAAG   1500
CAGAAGGAGC TCTCTGAAGG CGAGGAGAAA GGGGACCCGG AGAAGGTGTT TAAGTCAGAG   1560
TCGGAATACG GTATGAGAAG GAAGGCCTTC CGGCTGCCAG ACAACAGGAT AGGGAGGAAG   1620
TTTTCCATCA TGAATCAGTC GCTGCTCAGC ATTCCAGGCT CGCCCTTCCT CTCCCGACAT   1680
AACAGCAAAA GCAGCATCTT CAGCTTCGGG GACCCGTCGG TTCGGGACCC CGGCTCTGAG   1740
AATGAGTTCG CAGACGATGA ACACAGCACC GTGGAGGAGA GCGAGGGCCG GCGTGACTCG   1800
CTCTTCATCC CGATCCGCGC CCGCGAGCGC CGCAGCAGCT ACAGTGGCTA CAGCGGCTAC   1860
AGCCAGTGCA GCCGCTCGTC GCGCATCTCC CCAGCCTGCG CGCAGCGTGA AGCCAACAGC   1920
ACGGTGGACT GCAACGGCGT AGTGTCACTC ATCGGGCCCG GCTCACACAT CGGGCGGCTC   1980
CTGCTGAGGC AACGACTGAG GTGGAAATTA AGAAGAAAGG CCCTGGACTC TTTTAGTTTC   2040
TATGGACCAA CTCGCCTCCT ACGGACGGAA GGACAGAATC AACAGCATAA TGAGCGTGGT   2100
CACAAACACG CTAGTGAAGA GCTGGAAGAG TCTCAGAGAA AGTGCCCACC GTGCTGGTAT   2160
AAGTTTGCCA ACACTTTCCT CATCTGGGAG TGTCACCCCT ACTGGATAAA ACTGAAGGAG   2220
ATCGTGAACT TAATCGTCAT GGACCCTTTT GTAGACTTAG CCATCACCAT CTGCATCGTT   2280
CTGAATACGC TATTTATGGC AATGGAGCAC CATCCCATGA CACCACAGTT CGAACACGTC   2340
TTGGCCGTAG GAAATCTGGT GTTCACCGGG ATCTTCACGG CGGAAATGTT TCTGAAGCTC   2400
ATAGCCATGG ACCCCTACTA TTATTTCCAA GAAGGCTGGA ACATTTTTGA CGGATTTATT   2460
GTCTCCCTCA GTTTAATGGA GCTGAGTCTC GCAGATGTGG AGGGGCTCTC AGTGCTGCGG   2520
TCTTTCCGAC TGCTCCGAGT CTTCAAGCTG GCCAAGTCCT GGCCCACCCT GAACATGCTG   2580
ATCAAGATCA TCGGGAACTC CGTGGGTGCC CTGGGCAACC TGACCCTGGT GCTGGCCATC   2640
ATCGTCTTCA TCTTCGCCGT GGTGGGGATG CAGCTGTTTG GAAAGAGTTA CAAGGAGTGC   2700
GTCTGTAAGA TCAACCAGGA GTGCAAGCTC CCGCGCTGGC ACATGAACGA CTTCTTCCAC   2760
TCCTTCCTCA TCGTCTTCCG AGTGCTGTGT GGGGAGTGGA TCGAGACCAT GTGGGACTGC   2820
ATGGAGGTGG CCGGCCAGGC CATGTGCCTC ATTGTCTTCA TGATGGTTAT GGTCATTGGC   2880
AACCTGGTGG TGCTGAATCT ATTCCTGGCC TTGCTTCTGA GCTCCTTCAG CGCAGACAAC   2940
CTGGCGGCCA CAGACGACGA CGGGGAAATG AACAACCTGC AGATCTCAGT GATCCGGATC   3000
AAGAAGGGCG TGGCCTGGAC CAAAGTGAAG GTGCACGCCT TCATGCAGGC TCACTTCAAG   3060
CAGCGGGAGG CGGATGAAGT GAAACCCCTC GACGAGCTGT ATGAGAAGAA GGCCAACTGC   3120
ATCGCCAACC ACACGGGCGT GGATATCCAC CGGAACGGCG ACTTCCAGAA GAACGGGAAC   3180
GGAACCACCA GCGGCATCGG CAGCAGCGTG GAGAAGTACA TCATCGACGA GGACCACATG   3240
TCCTTCATTA ACAACCCAAA CCTGACCGTC CGGGTGCCCA TTGCTGTGGG CGAGTCTGAC   3300
TTCGAGAACC TCAACACAGA GGATGTTAGC AGCGAATCAG ACCCTGAAGG CAGCAAAGAT   3360
AAACTGGACG ATACCAGCTC CTCAGAAGGA AGTACCATCG ACATCAAGCC TGAGGTGGAA   3420
GAAGTTCCCG TGGAGCAACC TGAGGAATAC TTGGATCCGG ACGCCTGCTT TACAGAGGGT   3480
TGCGTCCAGC GGTTCAAGTG CTGCCAGGTC AACATCGAGG AAGGACTAGG CAAGTCGTGG   3540
TGGATCTTGC GGAAAACCTG CTTCCTCATT GTGGAGCACA ATTGGTTTGA GACCTTCATC   3600
ATCTTCATGA TTCTGCTCAG CAGTGGCGCC CTGGCCTTTG AGGACATCTA CATTGAGCAG   3660
AGGAAGACCA TCCGCACCAT CCTGGAGTAT GCGGACAAGG TCTTCACCTA CATCTTCATC   3720
CTGGAGATGT TGCTCAAGTG GACCACGTAC GGCTTCGTCA AGTTCTTCAC CAATGCCTGG   3780
TGCTGGTTGG ACTTCCTCAT TGTGGCTGTC TCTTTAGTCA GCCTTATAGC TAATGCCCTG   3840
GGCTACTCGG AACTAGGTGC CATAAAGTCC CTTAGGACCC TAAGAGCTTT GAGACCCTTA   3900
AGAGCCTTAT CACGATTTGA AGGGATGAGG GTGGTGGTGA ATGCCTTGGT GGGTGCCATC   3960
CCCTCCATCA TGAATGTGCT GCTGGTGTGT CTCATCTTCT GGCTGATTTT CAGCATCATG   4020
GGAGTTAACC TGTTTGCGGG GAAATACCAC TACTGCTTTA ATGAGACTTC TGAAATCCGG   4080
TTCGAAATCG ATATTGTCAA CAATAAAACG GACTGTGAGA AGCTCATGGA GGGCAACAGC   4140
ACGGAGATCC GATGGAAGAA TGTCAAGATC AACTTTGACA ATGTCGGAGC AGGGTACCTG   4200
GCCCTTCTTC AAGTGGCAAC CTTCAAAGGC TGGATGGACA TCATGTATGC GGCTGTAGAT   4260
TCCCGAAAGC CAGACGAGCA GCCTGACTAC GAGGGCAACA TCTACATGTA CATCTACTTC   4320
GTCATCTTCA TCATCTTCGG CTCCTTCTTC ACCCTCAACC TGTTCATCGG TGTCATCATC   4380
GACAACTTCA ACCAGCAGAA GAAAAAGTTT GGAGGTCAGG ACATCTTCAT GACAGAGGAA   4440
CAGAAGAAGT ACTATAATGC CATGAAAAAG CTGGGCTCCA AGAAGCCACA GAAGCCCATC   4500
CCCCGACCCT TGAACAAAAT CCAAGGGATT GTCTTTGATT TCGTCACTCA ACAAGCCTTT   4560
GACATTGTGA TCATGATGCT CATCTGCCTT AACATGGTGA CAATGATGGT GGAGACAGAC   4620
ACTCAGAGCA AGCAGATGGA GAACATTCTT TACTGGATTA ATCTGGTCTT TGTCATCTTC   4680
TTCACCTGCG AGTGTGTGCT CAAAATGTTT GCCTTGAGAC ACTACTACTT CACCATTGGC   4740
TGGAACATCT TTGACTTTGT GGTGGTCATC CTCTCCATTG TGGGAATGTT CCTGGCTGAT   4800
ATCATTGAGA AGTACTTCGT CTCCCCAACC CTATTCCGAG TTATCCGATT GGCCCGTATT   4860
GGGCGCATCT TGCGTCTGAT CAAGGGCGCC AAAGGGATCC GCACTCTGCT CTTTGCTCTG   4920
ATGATGTCGC TGCCCGCCCT GTTCAACATC GGCCTCCTGC TCTTCCTCGT CATGTTCATC   4980
TTCTCCATTT TTGGCATGTC CAACTTCGCA TACGTGAAGC ACGAGGCCGG CATTGACGAC   5040
ATGTTCAACT TCGAGACATT TGGCAACAGC ATGATCTGTT TGTTCCAGAT CACAACGTCT   5100
GCTGGCTGGG ATGGCCTGCT GCTGCCAATC CTGAACCGCC CCCCTGACTG CAGCTTGGAC   5160
AAAGAGCACC CAGGGAGTGG CTTCAAAGGG GACTGTGGGA ACCCCTCGGT GGGCATCTTC   5220
TTCTTTGTGA GCTACATCAT CATCTCCTTC CTGATTGTGG TGAACATGTG CATCGCCATC   5280
ATCCTGGAGA ACTTCAGCGT GGCCACCGAG GAGAGCGCCG ACCCTCTGAG TGAGGATGAC   5340
TTCGAGACTT TCTATGAGAT CTGGGAGAAG TTTGACCCAG ACGCCACCCA GTTCATCGAG   5400
TACTGTAAGC TGGCAGACTT TGCCGACGCC CTGGAGCACC CGCTCCGAGT ACCCAAGCCC   5460
AACACCATCG AGCTCATCGC CATGGACCTG CCCATGGTGA GCGGAGATCG CATCCACTGC   5520
TTGGACATCC TTTTCGCCTT CACCAAGGCA GTCCTGGGAG ACAGTGGGGA GTTGGACATC   5580
CTGCGGCAGC AGATGGAGGA GCGGTTCGTG GCATCCAATC CTTCCAAAGT GTCTTACGAA   5640
GCCTATCACA CCACTCTGCG GCGCAACGAG GAGGAGGTGT CTGCAGTGGT CCTGCAGCGT   5700
GCCTACAGGG GACACTTGGC TAGGCGGGGC TTCATCTGCA GAAAGATGGC CTCCAACAAG   5760
CTGGAGAATG GAGGCACACA CAGAGACAAG AAGGAGAGCA CCCCGTCCAC AGCCTCCCTC   5820
CCCTCTTACG ACAGCGTCAC AAAGCCAGAC AAGGAGAAGC AGCAGCGTGC GGAGGAGGGC   5880
AGAAGGGAAA GAGCCAAGAG GCAAAAAGAG GTCAGGGAGT CCAAGTGCTA GAGGAGGGGA   5940
AAGGAAGCTT ACCCCGGCTG AACACTGGCA AGTGAAAGCT TGTTTACAAA CTTCCGAATC   6000
TCACGGATGC AGACAGCTGT GCAGACGCTC GCTGTACTGG AAGACCTATA CCAAACATAG   6060
TCTGCTTACA TGTGACATGG TGGCATCCTG AGCGGTGACT GCTGCTGGGG ACAAAGGACC   6120
CTGCTCCCTG GACTCACAGA TCTCCTATCG CTTGGGCAGA CGGTTACTGC ATGTTCCACA   6180
CTTAGTCAAT GCAACTTAGG ACTAAACTAA CCAGGATACA AAACCGAGGC GGCTGGCGAC   6240
CAGCAGATCA CCGCTGCAGC CAAATGGATT TTATTTTTTC ATTTTGTTGA TTCTCAGAAG   6300
CAGAAAGCAT CACTTTAAAA GTTTGTTTGT TCATGCAAAC AATATTTGAA TTCTTACATT   6360
AGTTAAGCTA AGCAGCAAAA AGAAACACAC ACGCACACAG ACACACAAAG ACACACACAC   6420
ATTCAGCCTA TGTCACTAAT CGTCTGTTTC TTTAACATAA CAGCATCTTC TCCACACGAG   6480
CGGCACGTGG TTTGGAGATG GGTGGGGGAA AATCAGGGTT TCAGGCTGAG GAGGACTTGC   6540
TCAGGCCAAT CCCAAATATG TGCTCGTTCA ATGCATAGAA GTGACCTGCA TGATGGCATG   6600
CTGTGTTCAG AAGTCATGCA TGAGACCCAC ACACCACAAG ACACTAGTAC TCCTGTNNCC   6660
ATCCACAGGC TCAGCCTGCG GACAGGACCA GCCCTGCACC GTTCACTGTA TTTGGAGAAA   6720
TGGTAAGAGT TCCACACCGG CTGCAGTCCT CTCAGTGTAG GATTCTTTCG TACACCTCTG   6780
GGTAGGGAGA CATAATTAAC CAATTGACCA CTACCAACAA AACAAT                  6826
 
           
           
             
               1976 amino acids 
               amino acid 
               single 
               linear 
             
             
               peptide 
             
             9
Met Arg Arg Ser Ala Arg Leu Leu Ala Pro Pro Gly Pro Asp Ser Phe
1               5                   10                  15
Lys Pro Phe Thr Pro Glu Ser Leu Ala Asn Ile Glu Arg Arg Ile Ala
            20                  25                  30
Glu Ser Lys Leu Lys Lys Pro Pro Lys Ala Asp Gly Ser His Arg Glu
        35                  40                  45
Asp Asp Glu Asp Ser Lys Pro Lys Pro Asn Ser Asp Leu Glu Ala Gly
    50                  55                  60
Lys Ser Leu Pro Phe Ile Tyr Gly Asp Ile Pro Gln Gly Leu Val Ala
65                  70                  75                  80
Val Pro Leu Glu Asp Phe Asp Pro Tyr Tyr Leu Thr Gln Lys Thr Phe
                85                  90                  95
Val Val Leu Asn Arg Gly Lys Thr Leu Phe Arg Phe Ser Ala Thr Pro
            100                 105                 110
Ala Leu Tyr Ile Leu Ser Pro Phe Asn Leu Ile Arg Arg Ile Ala Ile
        115                 120                 125
Lys Ile Leu Ile His Ser Val Phe Ser Met Ile Ile Met Cys Thr Ile
    130                 135                 140
Leu Thr Asn Cys Val Phe Met Thr Phe Ser Asn Pro Pro Glu Trp Ser
145                 150                 155                 160
Lys Asn Val Glu Tyr Thr Phe Thr Gly Ile Tyr Thr Phe Glu Ser Leu
                165                 170                 175
Val Lys Ile Ile Ala Arg Gly Phe Cys Ile Asp Gly Phe Thr Phe Leu
            180                 185                 190
Arg Asp Pro Trp Asn Trp Leu Asp Phe Ser Val Ile Met Met Ala Tyr
        195                 200                 205
Val Thr Glu Phe Val Asp Leu Gly Asn Val Ser Ala Leu Arg Thr Phe
    210                 215                 220
Arg Val Leu Arg Ala Leu Lys Thr Ile Ser Val Ile Pro Gly Leu Lys
225                 230                 235                 240
Thr Ile Val Gly Ala Leu Ile Gln Ser Val Lys Lys Leu Ser Asp Val
                245                 250                 255
Met Ile Leu Thr Val Phe Cys Leu Ser Val Phe Ala Leu Ile Gly Leu
            260                 265                 270
Gln Leu Phe His Gly Asn Leu Ser Lys Gln Cys Val Val Trp Pro Ile
        275                 280                 285
Asn Phe Asn Glu Ser Tyr Leu Glu Asn Gly Thr Arg Gly Phe Asp Trp
    290                 295                 300
Glu Glu Tyr Ile Asn Asn Lys Thr Asn Phe Tyr Met Val Pro Gly Met
305                 310                 315                 320
Leu Glu Pro Leu Leu Cys Gly Asn Ser Ser Asp Ala Gly Gln Cys Glu
                325                 330                 335
Gly Phe Gln Cys Ser Lys Ala Gly Arg Asn Pro Asn Tyr Gly Tyr Thr
            340                 345                 350
Ser Phe Asp Thr Phe Ser Trp Ala Phe Leu Ala Leu Phe Arg Leu Met
        355                 360                 365
Thr Gln Asp Tyr Trp Glu Asn Leu Tyr Gln Leu Thr Leu Arg Ala Ala
    370                 375                 380
Gly Lys Thr Tyr Met Ile Phe Phe Val Leu Val Ile Phe Val Gly Ser
385                 390                 395                 400
Phe Tyr Pro Val Asn Leu Ile Leu Ala Val Val Ala Met Ala Tyr Glu
                405                 410                 415
Glu Gln Asn Gln Ala Thr Leu Glu Glu Ala Glu Gln Lys Glu Ala Glu
            420                 425                 430
Phe Lys Ala Met Leu Glu Gln Leu Lys Lys Gln Gln Glu Glu Ala Gln
        435                 440                 445
Ala Ala Ala Met Ala Thr Ser Ala Gly Thr Val Ser Glu Asp Ala Ile
    450                 455                 460
Glu Glu Glu Gly Glu Asp Gly Val Gly Ser Pro Arg Ser Ser Ser Glu
465                 470                 475                 480
Leu Ser Lys Leu Ser Ser Lys Ser Ala Lys Glu Arg Arg Asn Arg Arg
                485                 490                 495
Lys Lys Arg Lys Gln Lys Glu Leu Ser Glu Gly Glu Glu Lys Gly Asp
            500                 505                 510
Pro Glu Lys Val Phe Lys Ser Glu Ser Glu Tyr Gly Met Arg Arg Lys
        515                 520                 525
Ala Phe Arg Leu Pro Asp Asn Arg Ile Gly Arg Lys Phe Ser Ile Met
    530                 535                 540
Asn Gln Ser Leu Leu Ser Ile Pro Gly Ser Pro Phe Leu Ser Arg His
545                 550                 555                 560
Asn Ser Lys Ser Ser Ile Phe Ser Phe Gly Asp Pro Ser Val Arg Asp
                565                 570                 575
Pro Gly Ser Glu Asn Glu Phe Ala Asp Asp Glu His Ser Thr Val Glu
            580                 585                 590
Glu Ser Glu Gly Arg Arg Asp Ser Leu Phe Ile Pro Ile Arg Ala Arg
        595                 600                 605
Glu Arg Arg Ser Ser Tyr Ser Gly Tyr Ser Gly Tyr Ser Gln Cys Ser
    610                 615                 620
Arg Ser Ser Arg Ile Ser Pro Ala Cys Ala Gln Arg Glu Ala Asn Ser
625                 630                 635                 640
Thr Val Asp Cys Asn Gly Val Val Ser Leu Ile Gly Pro Gly Ser His
                645                 650                 655
Ile Gly Arg Leu Leu Leu Arg Gln Arg Leu Arg Trp Lys Leu Arg Arg
            660                 665                 670
Lys Ala Leu Asp Ser Phe Ser Phe Tyr Gly Pro Thr Arg Leu Leu Arg
        675                 680                 685
Thr Glu Gly Gln Asn Gln Gln His Asn Glu Arg Gly His Lys His Ala
    690                 695                 700
Ser Glu Glu Leu Glu Glu Ser Gln Arg Lys Cys Pro Pro Cys Trp Tyr
705                 710                 715                 720
Lys Phe Ala Asn Thr Phe Leu Ile Trp Glu Cys His Pro Tyr Trp Ile
                725                 730                 735
Lys Leu Lys Glu Ile Val Asn Leu Ile Val Met Asp Pro Phe Val Asp
            740                 745                 750
Leu Ala Ile Thr Ile Cys Ile Val Leu Asn Thr Leu Phe Met Ala Met
        755                 760                 765
Glu His His Pro Met Thr Pro Gln Phe Glu His Val Leu Ala Val Gly
    770                 775                 780
Asn Leu Val Phe Thr Gly Ile Phe Thr Ala Glu Met Phe Leu Lys Leu
785                 790                 795                 800
Ile Ala Met Asp Pro Tyr Tyr Tyr Phe Gln Glu Gly Trp Asn Ile Phe
                805                 810                 815
Asp Gly Phe Ile Val Ser Leu Ser Leu Met Glu Leu Ser Leu Ala Asp
            820                 825                 830
Val Glu Gly Leu Ser Val Leu Arg Ser Phe Arg Leu Leu Arg Val Phe
        835                 840                 845
Lys Leu Ala Lys Ser Trp Pro Thr Leu Asn Met Leu Ile Lys Ile Ile
    850                 855                 860
Gly Asn Ser Val Gly Ala Leu Gly Asn Leu Thr Leu Val Leu Ala Ile
865                 870                 875                 880
Ile Val Phe Ile Phe Ala Val Val Gly Met Gln Leu Phe Gly Lys Ser
                885                 890                 895
Tyr Lys Glu Cys Val Cys Lys Ile Asn Gln Glu Cys Lys Leu Pro Arg
            900                 905                 910
Trp His Met Asn Asp Phe Phe His Ser Phe Leu Ile Val Phe Arg Val
        915                 920                 925
Leu Cys Gly Glu Trp Ile Glu Thr Met Trp Asp Cys Met Glu Val Ala
    930                 935                 940
Gly Gln Ala Met Cys Leu Ile Val Phe Met Met Val Met Val Ile Gly
945                 950                 955                 960
Asn Leu Val Val Leu Asn Leu Phe Leu Ala Leu Leu Leu Ser Ser Phe
                965                 970                 975
Ser Ala Asp Asn Leu Ala Ala Thr Asp Asp Asp Gly Glu Met Asn Asn
            980                 985                 990
Leu Gln Ile Ser Val Ile Arg Ile Lys Lys Gly Val Ala Trp Thr Lys
        995                 1000                1005
Val Lys Val His Ala Phe Met Gln Ala His Phe Lys Gln Arg Glu Ala
    1010                1015                1020
Asp Glu Val Lys Pro Leu Asp Glu Leu Tyr Glu Lys Lys Ala Asn Cys
1025                1030                1035                1040
Ile Ala Asn His Thr Gly Val Asp Ile His Arg Asn Gly Asp Phe Gln
                1045                1050                1055
Lys Asn Gly Asn Gly Thr Thr Ser Gly Ile Gly Ser Ser Val Glu Lys
            1060                1065                1070
Tyr Ile Ile Asp Glu Asp His Met Ser Phe Ile Asn Asn Pro Asn Leu
        1075                1080                1085
Thr Val Arg Val Pro Ile Ala Val Gly Glu Ser Asp Phe Glu Asn Leu
    1090                1095                1100
Asn Thr Glu Asp Val Ser Ser Glu Ser Asp Pro Glu Gly Ser Lys Asp
1105                1110                1115                1120
Lys Leu Asp Asp Thr Ser Ser Ser Glu Gly Ser Thr Ile Asp Ile Lys
                1125                1130                1135
Pro Glu Val Glu Glu Val Pro Val Glu Gln Pro Glu Glu Tyr Leu Asp
            1140                1145                1150
Pro Asp Ala Cys Phe Thr Glu Gly Cys Val Gln Arg Phe Lys Cys Cys
        1155                1160                1165
Gln Val Asn Ile Glu Glu Gly Leu Gly Lys Ser Trp Trp Ile Leu Arg
    1170                1175                1180
Lys Thr Cys Phe Leu Ile Val Glu His Asn Trp Phe Glu Thr Phe Ile
1185                1190                1195                1200
Ile Phe Met Ile Leu Leu Ser Ser Gly Ala Leu Ala Phe Glu Asp Ile
                1205                1210                1215
Tyr Ile Glu Gln Arg Lys Thr Ile Arg Thr Ile Leu Glu Tyr Ala Asp
            1220                1225                1230
Lys Val Phe Thr Tyr Ile Phe Ile Leu Glu Met Leu Leu Lys Trp Thr
        1235                1240                1245
Thr Tyr Gly Phe Val Lys Phe Phe Thr Asn Ala Trp Cys Trp Leu Asp
    1250                1255                1260
Phe Leu Ile Val Ala Val Ser Leu Val Ser Leu Ile Ala Asn Ala Leu
1265                1270                1275                1280
Gly Tyr Ser Glu Leu Gly Ala Ile Lys Ser Leu Arg Thr Leu Arg Ala
                1285                1290                1295
Leu Arg Pro Leu Arg Ala Leu Ser Arg Phe Glu Gly Met Arg Val Val
            1300                1305                1310
Val Asn Ala Leu Val Gly Ala Ile Pro Ser Ile Met Asn Val Leu Leu
        1315                1320                1325
Val Cys Leu Ile Phe Trp Leu Ile Phe Ser Ile Met Gly Val Asn Leu
    1330                1335                1340
Phe Ala Gly Lys Tyr His Tyr Cys Phe Asn Glu Thr Ser Glu Ile Arg
1345                1350                1355                1360
Phe Glu Ile Asp Ile Val Asn Asn Lys Thr Asp Cys Glu Lys Leu Met
                1365                1370                1375
Glu Gly Asn Ser Thr Glu Ile Arg Trp Lys Asn Val Lys Ile Asn Phe
            1380                1385                1390
Asp Asn Val Gly Ala Gly Tyr Leu Ala Leu Leu Gln Val Ala Thr Phe
        1395                1400                1405
Lys Gly Trp Met Asp Ile Met Tyr Ala Ala Val Asp Ser Arg Lys Pro
    1410                1415                1420
Asp Glu Gln Pro Asp Tyr Glu Gly Asn Ile Tyr Met Tyr Ile Tyr Phe
1425                1430                1435                1440
Val Ile Phe Ile Ile Phe Gly Ser Phe Phe Thr Leu Asn Leu Phe Ile
                1445                1450                1455
Gly Val Ile Ile Asp Asn Phe Asn Gln Gln Lys Lys Lys Phe Gly Gly
            1460                1465                1470
Gln Asp Ile Phe Met Thr Glu Glu Gln Lys Lys Tyr Tyr Asn Ala Met
        1475                1480                1485
Lys Lys Leu Gly Ser Lys Lys Pro Gln Lys Pro Ile Pro Arg Pro Leu
    1490                1495                1500
Asn Lys Ile Gln Gly Ile Val Phe Asp Phe Val Thr Gln Gln Ala Phe
1505                1510                1515                1520
Asp Ile Val Ile Met Met Leu Ile Cys Leu Asn Met Val Thr Met Met
                1525                1530                1535
Val Glu Thr Asp Thr Gln Ser Lys Gln Met Glu Asn Ile Leu Tyr Trp
            1540                1545                1550
Ile Asn Leu Val Phe Val Ile Phe Phe Thr Cys Glu Cys Val Leu Lys
        1555                1560                1565
Met Phe Ala Leu Arg His Tyr Tyr Phe Thr Ile Gly Trp Asn Ile Phe
    1570                1575                1580
Asp Phe Val Val Val Ile Leu Ser Ile Val Gly Met Phe Leu Ala Asp
1585                1590                1595                1600
Ile Ile Glu Lys Tyr Phe Val Ser Pro Thr Leu Phe Arg Val Ile Arg
                1605                1610                1615
Leu Ala Arg Ile Gly Arg Ile Leu Arg Leu Ile Lys Gly Ala Lys Gly
            1620                1625                1630
Ile Arg Thr Leu Leu Phe Ala Leu Met Met Ser Leu Pro Ala Leu Phe
        1635                1640                1645
Asn Ile Gly Leu Leu Leu Phe Leu Val Met Phe Ile Phe Ser Ile Phe
    1650                1655                1660
Gly Met Ser Asn Phe Ala Tyr Val Lys His Glu Ala Gly Ile Asp Asp
1665                1670                1675                1680
Met Phe Asn Phe Glu Thr Phe Gly Asn Ser Met Ile Cys Leu Phe Gln
                1685                1690                1695
Ile Thr Thr Ser Ala Gly Trp Asp Gly Leu Leu Leu Pro Ile Leu Asn
            1700                1705                1710
Arg Pro Pro Asp Cys Ser Leu Asp Lys Glu His Pro Gly Ser Gly Phe
        1715                1720                1725
Lys Gly Asp Cys Gly Asn Pro Ser Val Gly Ile Phe Phe Phe Val Ser
    1730                1735                1740
Tyr Ile Ile Ile Ser Phe Leu Ile Val Val Asn Met Cys Ile Ala Ile
1745                1750                1755                1760
Ile Leu Glu Asn Phe Ser Val Ala Thr Glu Glu Ser Ala Asp Pro Leu
                1765                1770                1775
Ser Glu Asp Asp Phe Glu Thr Phe Tyr Glu Ile Trp Glu Lys Phe Asp
            1780                1785                1790
Pro Asp Ala Thr Gln Phe Ile Glu Tyr Cys Lys Leu Ala Asp Phe Ala
        1795                1800                1805
Asp Ala Leu Glu His Pro Leu Arg Val Pro Lys Pro Asn Thr Ile Glu
    1810                1815                1820
Leu Ile Ala Met Asp Leu Pro Met Val Ser Gly Asp Arg Ile His Cys
1825                1830                1835                1840
Leu Asp Ile Leu Phe Ala Phe Thr Lys Ala Val Leu Gly Asp Ser Gly
                1845                1850                1855
Glu Leu Asp Ile Leu Arg Gln Gln Met Glu Glu Arg Phe Val Ala Ser
            1860                1865                1870
Asn Pro Ser Lys Val Ser Tyr Glu Ala Tyr His Thr Thr Leu Arg Arg
        1875                1880                1885
Asn Glu Glu Glu Val Ser Ala Val Val Leu Gln Arg Ala Tyr Arg Gly
    1890                1895                1900
His Leu Ala Arg Arg Gly Phe Ile Cys Arg Lys Met Ala Ser Asn Lys
1905                1910                1915                1920
Leu Glu Asn Gly Gly Thr His Arg Asp Lys Lys Glu Ser Thr Pro Ser
                1925                1930                1935
Thr Ala Ser Leu Pro Ser Tyr Asp Ser Val Thr Lys Pro Asp Lys Glu
            1940                1945                1950
Lys Gln Gln Arg Ala Glu Glu Gly Arg Arg Glu Arg Ala Lys Arg Gln
        1955                1960                1965
Lys Glu Val Arg Glu Ser Lys Cys
    1970                1975
 
           
           
             
               150 amino acids 
               amino acid 
               single 
               linear 
             
             
               peptide 
             
             10
Asp Ser Leu Phe Ile Pro Ile Arg Ala Arg Glu Arg Arg Ser Ser Tyr
1               5                   10                  15
Ser Gly Tyr Ser Gly Tyr Ser Gln Cys Ser Arg Ser Ser Arg Ile Phe
            20                  25                  30
Pro Ser Leu Arg Arg Ser Val Lys Arg Asn Ser Thr Val Asp Cys Asn
        35                  40                  45
Gly Val Val Ser Leu Ile Gly Pro Gly Ser His Ile Gly Arg Leu Leu
    50                  55                  60
Pro Glu Val Lys Ile Asp Lys Ala Ala Thr Asp Ser Ala Thr Thr Glu
65                  70                  75                  80
Val Glu Ile Lys Lys Lys Gly Pro Gly Ser Leu Leu Val Ser Met Asp
                85                  90                  95
Gln Leu Ala Ser Tyr Gly Arg Lys Asp Arg Ile Asn Ser Ile Met Ser
            100                 105                 110
Val Val Thr Asn Thr Leu Val Glu Glu Leu Glu Glu Ser Gln Arg Lys
        115                 120                 125
Cys Pro Pro Cys Trp Tyr Lys Phe Ala Asn Thr Phe Leu Ile Trp Glu
    130                 135                 140
Cys His Pro Tyr Trp Ile
145                 150
 
           
           
             
               140 amino acids 
               amino acid 
               single 
               linear 
             
             
               peptide 
             
             11
Asp Ser Leu Phe Ile Pro Ile Arg Ala Arg Glu Arg Arg Ser Ser Tyr
1               5                   10                  15
Ser Gly Tyr Ser Gly Tyr Ser Gln Cys Ser Arg Ser Ser Arg Ile Phe
            20                  25                  30
Pro Ser Leu Arg Arg Ser Val Lys Arg Asn Ser Thr Val Asp Cys Asn
        35                  40                  45
Gly Val Val Ser Leu Ile Gly Pro Gly Ser His Ile Gly Arg Leu Leu
    50                  55                  60
Pro Glu Ala Thr Thr Glu Val Glu Ile Lys Lys Lys Gly Pro Gly Ser
65                  70                  75                  80
Leu Leu Val Ser Met Asp Gln Leu Ala Ser Tyr Gly Arg Lys Asp Arg
                85                  90                  95
Ile Asn Ser Ile Met Ser Val Val Thr Asn Thr Leu Val Glu Glu Leu
            100                 105                 110
Glu Glu Ser Gln Arg Lys Cys Pro Pro Cys Trp Tyr Lys Phe Ala Asn
        115                 120                 125
Thr Phe Leu Ile Trp Glu Cys His Pro Tyr Trp Ile
    130                 135                 140
 
           
           
             
               138 amino acids 
               amino acid 
               single 
               linear 
             
             
               peptide 
             
             12
Asp Ser Leu Phe Ile Pro Ile Arg Ala Arg Glu Arg Arg Ser Ser Tyr
1               5                   10                  15
Ser Gly Tyr Ser Gly Tyr Ser Gln Cys Ser Arg Ser Ser Arg Ile Ser
            20                  25                  30
Pro Ala Cys Ala Gln Arg Glu Ala Asn Ser Thr Val Asp Cys Asn Gly
        35                  40                  45
Val Val Ser Leu Ile Gly Pro Gly Ser His Ile Gly Arg Leu Leu Leu
    50                  55                  60
Arg Gln Arg Leu Arg Trp Lys Leu Arg Arg Lys Ala Leu Asp Ser Phe
65                  70                  75                  80
Ser Phe Tyr Gly Pro Thr Arg Leu Leu Arg Thr Glu Gly Gln Asn Gln
                85                  90                  95
Gln His Asn Glu Arg Gly His Lys His Ala Ser Glu Glu Leu Glu Glu
            100                 105                 110
Ser Gln Arg Lys Cys Pro Pro Cys Trp Tyr Lys Phe Ala Asn Thr Phe
        115                 120                 125
Leu Ile Trp Glu Cys His Pro Tyr Trp Ile
    130                 135
 
           
           
             
               138 amino acids 
               amino acid 
               single 
               linear 
             
             
               peptide 
             
             13
Asp Ser Leu Phe Val Pro His Arg His Gly Glu Arg Arg Pro Ser Asn
1               5                   10                  15
Val Ser Gln Ala Ser Arg Ala Ser Arg Gly Ile Pro Thr Leu Pro Met
            20                  25                  30
Asn Gly Lys Met His Ser Ala Val Asp Cys Asn Gly Val Val Ser Leu
        35                  40                  45
Val Gly Gly Pro Ser Ala Leu Thr Ser Pro Val Gly Gln Leu Leu Pro
    50                  55                  60
Glu Gly Thr Thr Thr Glu Thr Glu Ile Arg Lys Arg Arg Ser Ser Ser
65                  70                  75                  80
Tyr His Val Ser Met Asp Leu Leu Glu Asp Pro Ser Arg Gln Arg Ala
                85                  90                  95
Met Ser Ile Ala Ser Ile Leu Thr Asn Thr Met Glu Glu Leu Glu Glu
            100                 105                 110
Ser Arg Gln Lys Cys Pro Pro Cys Trp Tyr Lys Phe Ala Asn Met Cys
        115                 120                 125
Leu Ile Trp Asp Cys Cys Lys Pro Trp Leu
    130                 135
 
           
           
             
               20 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             14
CAATCGTGGG CGCCCTAATC                                                 20
 
           
           
             
               25 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             15
TGCTTTCATG CACTGGAATC CCTCT                                           25
 
           
           
             
               25 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             16
TGCTTTACTG CACTGGAATC CTTCG                                           25
 
           
           
             
               12 amino acids 
               amino acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             17
Gly Arg Leu Leu Pro Glu Ala Thr Thr Glu Val Glu
1               5                   10
 
           
           
             
               22 amino acids 
               amino acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             18
Gly Arg Leu Leu Pro Glu Val Lys Ile Asp Lys Ala Ala Thr Asp Ser
1               5                   10                  15
Ala Thr Thr Glu Val Glu
            20
 
           
           
             
               24 amino acids 
               amino acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             19
Gly Gln Leu Leu Pro Glu Val Ile Ile Asp Lys Pro Ala Thr Asp Asp
1               5                   10                  15
Asn Gly Thr Thr Thr Glu Thr Glu
            20
 
           
           
             
               13 amino acids 
               amino acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             20
Gly Gln Leu Leu Pro Glu Gly Thr Thr Thr Glu Thr Glu
1               5                   10
 
           
           
             
               24 amino acids 
               amino acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             21
Gly Gln Leu Leu Pro Glu Val Ile Ile Asp Lys Ala Thr Ser Asp Asp
1               5                   10                  15
Ser Gly Thr Thr Asn Gln Met Arg
            20
 
           
           
             
               13 amino acids 
               amino acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             22
Gly Gln Leu Leu Pro Glu Gly Thr Thr Asn Gln Ile His
1               5                   10
 
           
           
             
               13 amino acids 
               amino acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             23
Gly Gln Leu Leu Pro Glu Gly Thr Thr Thr Glu Thr Glu
1               5                   10
 
           
           
             
               7 amino acids 
               amino acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             24
Gly Thr Thr Thr Glu Thr Glu
1               5
 
           
           
             
               7 amino acids 
               amino acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             25
Thr Thr Pro Ser Glu Glu Pro
1               5
 
           
           
             
               21 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             26
ACACTCAGAG CAAGCAGATG G                                               21
 
           
           
             
               21 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             27
TCCCTGGGTG CTCTTTGTCC A                                               21
 
           
           
             
               20 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             
               misc_difference 
                replace(9, “”) 
                /note= “This position is T or C.”
 
             
             
               misc_difference 
                replace(12, “”) 
                /note= “This position is G or A.”
 
             
             
               misc_difference 
                replace(15, “”) 
                /note= “This position is T or C.”
 
             
             28
ACCAACTGYG TRTTYATGAC                                                 20
 
           
           
             
               20 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             29
CAGCAGCTAC AGTGGCTACA                                                 20
 
           
           
             
               20 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             30
AAAGAGGCCG AGTTCAAGGC                                                 20
 
           
           
             
               18 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             31
TGTCCTTCCG TCCGTAGG                                                   18
 
           
           
             
               21 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             32
TTCATGGGGA ACCTTCGAAA C                                               21
 
           
           
             
               25 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             33
GAACGATGCA GATGGTGATG GCTAA                                           25
 
           
           
             
               37 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             34
GAAGCTCGAG CCCGGGCAAG AGAAGATGGC AGCGCGG                              37
 
           
           
             
               20 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             35
CTCGGAGAGC CTACCCCATC                                                 20
 
           
           
             
               21 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             36
AGAAGGGGAA GATGGGGTAG G                                               21
 
           
           
             
               21 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             37
ATTCTGTCCT TCCGTCCGTA G                                               21
 
           
           
             
               21 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             38
ACACTCAGAG CAAGCAGATG G                                               21
 
           
           
             
               21 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             39
TCCCTGGGTG CTCTTTGTCC A                                               21
 
           
           
             
               19 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             40
GGTGGACTGC AACGGCGTA                                                  19
 
           
           
             
               21 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             41
ATTCTGTCCT TCCGTCCGTA G                                               21
 
           
           
             
               30 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             42
GTGAAAATAG ATAAGGCAGC TACGGACAGC                                      30
 
           
           
             
               6586 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               DNA (genomic) 
             
             43
CCAAGATGGC GCCCACCGCA GTCCCGCCCG CCGCAGCCTC GGCGCCTCTG CAGTCCGGCC     60
GCGCCTCCCG GGCCCCGCGC TAGGGCCGCT GCCGCCTCGC CCGCCGCCGC CGCCGCCAGC    120
TGACCTGTCC CGGACACATA ACTAACGAAG CTGCTGCAGG ATGAGAAGAT GGCAGCGCGG    180
CTGCTCGCAC CACCAGGCCC TGATAGTTTC AAGCCTTTCA CCCCTGAGTC GCTGGCAAAC    240
ATCGAGAGGC GTATTGCCGA GAGCAAGCTC AAGAAACCAC CAAAGGCGGA TGGCAGCCAC    300
CGGGAGGACG ATGAAGACAG CAAGCCCAAG CCAAACAGTG ACCTGGAGGC TGGGAAGAGT    360
TTGCCTTTCA TCTACGGGGA CATCCCGCAA GGCCTGGTTG CGGTTCCCCT GGAGGACTTT    420
GACCCTTACT ATTTGACGCA GAAAACCTTT GTAGTATTAA ACAGAGGGAA AACTCTCTTC    480
AGATTTAGTG CCACACCTGC CTTGTACATT TTAAGCCCTT TTAACCTGAT AAGAAGAATA    540
GCTATTAAAA TTTTGATACA CTCAGTTTTC AGCATGATCA TCATGTGCAC CATCCTGACC    600
AACTGTGTGT TCATGACCTT TAGTAACCCT CCAGAATGGT CCAAGAATGT GGAGTACACA    660
TTCACAGGGA TTTACACATT TGAATCACTA GTGAAAATCA TCGCAAGAGG TTTCTGCATA    720
GACGGCTTCA CCTTCTTGCG AGACCCGTGG AACTGGTTAG ACTTCAGTGT CATCATGATG    780
GCATATGTGA CAGAGTTTGT GGACCTGGGC AATGTCTCAG CGCTGAGAAC ATTCAGGGTT    840
CTCCGAGCTT TGAAAACTAT CTCTGTAATT CCAGGCCTGA AGACAATCGT GGGCGCCCTA    900
ATCCAGTCCG TGAAGAAGCT GTCGGACGTG ATGATCCTGA CAGTGTTCTG CCTGAGTGTT    960
TTCGCCCTGA TTGGCCTGCA GCTCTTCATG GGGAACCTTC GAAACAAGTG TGTCGTGTGG   1020
CCCATAAACT TCAACGAGAG CTACCTGGAG AACGGCACCA GAGGCTTTGA CTGGGAGGAA   1080
TATATCAACA ATAAAACAAA CTTTTACATG GTTCCTGGCA TGCTAGAACC CTTGCTCTGC   1140
GGGAACAGTT CTGATGCTGG GCAATGCCCA GAGGGATTCC AGTGCATGAA AGCAGGAAGG   1200
AACCCCAACT ACGGTTACAC CAGCTTTGAC ACCTTCAGCT GGGCCTTCTT GGCATTATTC   1260
CGCCTTATGA CCCAGGACTA TTGGGAGAAC TTATACCAGC TGACCTTACG AGCCGCTGGG   1320
AAAACGTACA TGATCTTCTT TGTCTTGGTC ATCTTCGTGG GTTCTTTCTA TCTGGTGAAC   1380
TTGATCTTGG CTGTGGTGGC CATGGCTTAT GAGGAACAGA ACCAGGCAAC ACTGGAGGAG   1440
GCAGAGCAAA AAGAGGCCGA GTTCAAGGCA ATGCTGGAGC AACTCAAGAA GCAGCAGGAG   1500
GAGGCACAGG CTGCTGCAAT GGCCACCTCA GCGGGCACTG TCTCGGAAGA CGCCATTGAA   1560
GAAGAAGGGG AAGATGGGGT AGGCTCTCCG AGGAGCTCTT CTGAACTGTC TAAACTCAGT   1620
TCCAAGAGCG CGAAGGAGCG GCGGAACCGA CGGAAGAAGA GGAAGCAGAA GGAGCTCTCT   1680
GAAGGCGAGG AGAAAGGGGA CCCGGAGAAG GTGTTTAAGT CAGAGTCGGA AGACGGTATG   1740
AGAAGGAAGG CCTTCCGGCT GCCAGACAAC AGGATAGGGA GGAAGTTTTC CATCATGAAT   1800
CAGTCGCTGC TCAGCATTCC AGGCTCGCCC TTCCTCTCCC GACATAACAG CAAAAGCAGC   1860
ATCTTCAGCT TCCGGGGACC CGGTCGGTTC CGGGACCCCG GCTCTGAGAA TGAGTTCGCA   1920
GACGATGAAC ACAGCACCGT GGAGGAGAGC GAGGGCCGGC GTGACTCGCT CTTCATCCCG   1980
ATCCGCGCCC GCGAGCGCCG CAGCAGCTAC AGTGGCTACA GCGGCTACAG CCAGTGCAGC   2040
CGCTCGTCGC GTGAAAATAG ATAAGGCAGC TACGGACAGC GCATCTTCCC CAGCCTGCGG   2100
CGCAGCGTGA AGCGCAACAG CACGGTGGAC TGCAACGGCG TAGTGTCACT CATCGGGCCC   2160
GGCTCACACA TCGGGCGGCT CCTGCCTGAG GCAACGACTG AGGTGGAAAT TAAGAAGAAA   2220
GGCCCTGGAT CTCTTTTAGT TTCTATGGAC CAACTCGCCT CCTACGGACG GAAGGACAGA   2280
ATCAACAGCA TAATGAGCGT GGTCACAAAC ACGCTAGTGG AAGAGCTGGA AGAGTCTCAG   2340
AGAAAGTGCC CACCGTGCTG GTATAAGTTT GCCAACACTT TCCTCATCTG GGAGTGTCAC   2400
CCCTACTGGA TAAAACTGAA GGAGATCGTG AACTTAATCG TCATGGACCC TTTTGTAGAC   2460
TTAGCCATCA CCATCTGCAT CGTTCTGAAT ACGCTATTTA TGGCAATGGA GCACCATCCC   2520
ATGACACCAC AGTTCGAACA CGTCTTGGCC GTAGGAAATC TGGTGTTCAC CGGGATCTTC   2580
ACGGCGGAAA TGTTTCTGAA GCTCATAGCC ATGGACCCCT ACTATTATTT CCAAGAAGGC   2640
TGGAACATTT TTGACGGATT TATTGTCTCC CTCAGTTTAA TGGAGCTGAG TCTCGCAGAT   2700
GTGGAGGGGC TCTCAGTGCT GCGGTCTTTC CGACTGCTCC GAGTCTTCAA GCTGGCCAAG   2760
TCCTGGCCCA CCCTGAACAT GCTGATCAAG ATCATCGGGA ACTCCGTGGG TGCCCTGGGC   2820
AACCTGACCC TGGTGCTGGC CATCATCGTC TTCATCTTCG CCGTGGTGGG GATGCAGCTG   2880
TTTGGAAAGA GTTACAAGGA GTGCGTCTGT AAGATCAACC AGGAGTGCAA GCTCCCGCGC   2940
TGGCACATGA ACGACTTCTT CCACTCCTTC CTCATCGTCT TCCGAGTGCT GTGTGGGGAG   3000
TGGATCGAGA CCATGTGGGA CTGCATGGAG GTGGCCGGCC AGGCCATGTG CCTCATTGTC   3060
TTCATGATGG TTATGGTCAT TGGCAACCTG GTGGTGCTGA ATCTATTCCT GGCCTTGCTT   3120
CTGAGCTCCT TCAGCGCAGA CAACCTGGCG GCCACAGACG ACGACGGGGA AATGAACAAC   3180
CTGCAGATCT CAGTGATCCG GATCAAGAAG GGCGTGGCCT GGACCAAAGT GAAGGTGCAC   3240
GCCTTCATGC AGGCTCACTT CAAGCAGCGG GAGGCGGATG AAGTGAAACC CCTCGACGAG   3300
CTGTATGAGA AGAAGGCCAA CTGCATCGCC AACCACACGG GCGTGGATAT CCACCGGAAC   3360
GGCGACTTCC AGAAGAACGG GAACGGAACC ACCAGCGGCA TCGGCAGCAG CGTGGAGAAG   3420
TACATCATCG ACGAGGACCA CATGTCCTTC ATTAACAACC CAAACCTGAC CGTCCGGGTG   3480
CCCATTGCTG TGGGCGAGTC TGACTTCGAG AACCTCAACA CAGAGGATGT TAGCAGCGAA   3540
TCAGACCCTG AAGGCAGCAA AGATAAACTG GACGATACCA GCTCCTCAGA AGGAAGTACC   3600
ATCGACATCA AGCCTGAGGT GGAAGAAGTT CCCGTGGAGC AACCTGAGGA ATACTTGGAT   3660
CCGGACGCCT GCTTTACAGA GGGTTGCGTC CAGCGGTTCA AGTGCTGCCA GGTCAACATC   3720
GAGGAAGGAC TAGGCAAGTC GTGGTGGATC TTGCGGAAAA CCTGCTTCCT CATTGTGGAG   3780
CACAATTGGT TTGAGACCTT CATCATCTTC ATGATTCTGC TCAGCAGTGG CGCCCTGGCC   3840
TTTGAGGACA TCTACATTGA GCAGAGGAAG ACCATCCGCA CCATCCTGGA GTATGCGGAC   3900
AAGGTCTTCA CCTACATCTT CATCCTGGAG ATGTTGCTCA AGTGGACAGC CTACGGCTTC   3960
GTCAAGTTCT TCACCAATGC CTGGTGCTGG TTGGACTTCC TCATTGTGGC TGTCTCTTTA   4020
GTCAGCCTTA TAGCTAATGC CCTGGGCTAC TCGGAACTAG GTGCCATAAA GTCCCTTAGG   4080
ACCCTAAGAG CTTTGAGACC CTTAAGAGCC TTATCACGAT TTGAAGGGAT GAGGGTGGTG   4140
GTGAATGCCT TGGTGGGCGC CATCCCCTCC ATCATGAATG TGCTGCTGGT GTGTCTCATC   4200
TTCTGGCTGA TTTTCAGCAT CATGGGAGTT AACCTGTTTG CGGGGAAATA CCACTACTGC   4260
TTTAATGAGA CTTCTGAAAT CCGGTTCGAA ATCGATATTG TCAACAATAA AACGGACTGT   4320
GAGAAGCTCA TGGAGGGCAA CAGCACGGAG ATCCGATGGA AGAATGTCAA GATCAACTTT   4380
GACAATGTCG GAGCAGGGTA CCTGGCCCTT CTTCAAGTGG CAACCTTCAA AGGCTGGATG   4440
GACATCATGT ATGCGGCTGT AGATTCCCGA AAGCCAGACG AGCAGCCTGA CTACGAGGGC   4500
AACATCTACA TGTACATCTA CTTCGTCATC TTCATCATCT TCGGCTCCTT CTTCACCCTC   4560
AACCTGTTCA TCGGTGTCAT CATCGACAAC TTCAACCAGC AGAAGAAAAA GTTTGGAGGT   4620
CAGGACATCT TCATGACAGA GGAACAGAAG AAGTACTACA ATGCCATGAA AAAGCTGGGC   4680
TCCAAGAAGC CACAGAAGCC CATCCCCCGA CCCTTGAACA AAATCCAAGG GATTGTCTTT   4740
GATTTCGTCA CTCAACAAGC CTTTGACATT GTGATCATGA TGCTCATCTG CCTTAACATG   4800
GTGACAATGA TGGTGGAGAC AGACACTCAG AGCAAGCAGA TGGAGAACAT TCTTTACTGG   4860
ATTAATCTGG TCTTTGTCAT CTTCTTCACC TGCGAGTGTG TGCTCAAAAT GTTTGCCTTG   4920
AGACACTACT ATTTCACCAT TGGCTGGAAC ATCTTTGACT TTGTGGTGGT CATCCTCTCC   4980
ATTGTGGGAA TGTTCCTGGC TGATATCATT GAGAAGTACT TCGTCTCCCC AACCCTATTC   5040
CGAGTTATCC GATTGGCCCG TATTGGGCGC ATCTTGCGTC TGATCAAGGG CGCCAAAGGG   5100
ATCCGCACCC TGCTCTTTGC CTTAATGATG TCGCTGCCCG CCCTGTTCAA CATCGGCCTC   5160
CTGCTCTTCC TCGTCATGTT CATCTTCTCC ATTTTTGGCA TGTCCAACTT CGCATACGTG   5220
AAGCACGAGG CCGGCATTGA CGACATGTTC AACTTCGAGA CATTTGGCAA CAGCATGATC   5280
TGTTTGTTCC AGATCACAAC GTCTGCTGGC TGGGATGGCC TGCTGCTGCC AATCCTGAAC   5340
CGCCCCCCTG ACTGCAGCTT GGACAAAGAG CACCCAGGGA GTGGCTTCAA AGGGGACTGT   5400
GGGAACCCCT CGGTGGGCAT CTTCTTCTTT GTGAGCTACA TCATCATCTC CTTCCTGATT   5460
GTGGTGAACA TGTACATCGC CATCATCCTG GAGAACTTCA GCGTGGCCAC CGAGGAGAGC   5520
GCCGACCCTC TGAGTGAGGA TGACTTCGAG ACTTTCTATG AGATCTGGGA GAAGTTTGAC   5580
CCAGACGCCA CCCAGTTCAT CGAGTACTGT AAGCTGGCAG ACTTTGCCGA CGCCCTGGAG   5640
CACCCGCTCC GAGTACCCAA GCCCAACACC ATCGAGCTCA TCGCCATGGA CCTGCCCATG   5700
GTGAGCGGAG ATCGCATCCA CTGCTTGGAC ATCCTTTTCG CCTTCACCAA GCGAGTCCTG   5760
GGAGACAGTG GGGAGTTGGA CATCCTGCGG CAGCAGATGG AGGAGCGGTT CGTGGCATCC   5820
AATCCTTCCA AAGTGTCTTA CGAGCCTATC ACAACCACTC TGCGGCGCAA GCAGGAGGAG   5880
GTGTCTGCAG TGGTCCTGCA GCGTGCCTAC AGGGGACACT TGGCTAGGCG GGGCTTCATC   5940
TGCAGAAAGA TGGCCTCCAA CAAGCTGGAG AATGGAGGCA CACACAGAGA CAAGAAGGAG   6000
AGCACCCCGT CCACAGCCTC CCTCCCCTCT TACGACAGCG TCACAAAGCC AGACAAGGAG   6060
AAGCAGCAGC GTGCGGAGGA GGGCAGAAGG GAAAGAGCCA AGAGGCAAAA AGAGGTCAGG   6120
GAGTCCAAGT GCTAGAGGAG GGGAAAGGAA GCTTACCCCG GCTGAACACT GGCAAGTGAA   6180
AGCTTGTTTA CAAACTTCCG AATCTCACGG ATGCAGAGCA GCTGTGCAGA CGCTCGCTGT   6240
ACTGGAAGAC CTATACCAAA CATAGTCTGC TTACATGTGA CATGGTGGCA TCCTGAGCGG   6300
TGACTGCTGG GGACAAAGGA CCCTGCTCCC TGGACTCACA GATCTCCTAT CGCTTGGGCA   6360
GACGGTTACT GCATGTTCCA CACTTAGTCA ATGCAACTTA GGACTAAACT AACCAGGATA   6420
CAAAACCGAG GCGGCTGCCG GGACCAGCAG ATCACCGCTG CAGCCAAATG GATTTTATTT   6480
TTTCATTTTG TTGATTCTCA GAAGCAGAAA GCATCACTTT AAAAGTTTGT TTGTTCATNC   6540
AAACAATATT TGAATTCTTA CATTAGTTAA GCTAAGCANC AAAAAG                  6586