SVEP1_HUMAN
ID SVEP1_HUMAN Reviewed; 3571 AA.
AC Q4LDE5; Q0P675; Q5D213; Q5T938; Q5VTE4; Q5VTE5; Q7Z387; Q7Z3G3; Q8NBT9;
AC Q96JU7; Q9H284; Q9H8J9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1;
DE AltName: Full=CCP module-containing protein 22;
DE AltName: Full=Polydom;
DE AltName: Full=Selectin-like osteoblast-derived protein;
DE Short=SEL-OB;
DE AltName: Full=Serologically defined breast cancer antigen NY-BR-38;
DE Flags: Precursor;
GN Name=SVEP1; Synonyms=C9orf13, CCP22, SELOB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16206243; DOI=10.1002/jcp.20497;
RA Shur I., Socher R., Hameiri M., Fried A., Benayahu D.;
RT "Molecular and cellular characterization of SEL-OB/SVEP1 in osteogenic
RT cells in vivo and in vitro.";
RL J. Cell. Physiol. 206:420-427(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Mammary gland;
RA Han J., Fang Y., Yan J., Ye Q.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 195-3571 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 318-868 (ISOFORM 2), AND VARIANTS ALA-332 AND VAL-2750.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2131-3571, AND VARIANT ILE-3161.
RC TISSUE=Colon endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2269-2756.
RC TISSUE=Mammary gland;
RX PubMed=12747765;
RA Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O.,
RA Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.;
RT "Humoral immunity to human breast cancer: antigen definition and
RT quantitative analysis of mRNA expression.";
RL Cancer Immun. 1:4-4(2001).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=11062057; DOI=10.1042/bj3520049;
RA Gilges D., Vinit M.-A., Callebaut I., Coulombel L., Cacheux V.,
RA Romeo P.-H., Vigon I.;
RT "Polydom: a secreted protein with pentraxin, complement control protein,
RT epidermal growth factor and von Willebrand factor A domains.";
RL Biochem. J. 352:49-59(2000).
RN [9]
RP GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
CC -!- FUNCTION: May play a role in the cell attachment process.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:16206243}. Membrane {ECO:0000269|PubMed:16206243};
CC Peripheral membrane protein {ECO:0000269|PubMed:16206243}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q4LDE5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4LDE5-2; Sequence=VSP_031626, VSP_031627;
CC Name=3;
CC IsoId=Q4LDE5-3; Sequence=VSP_031625;
CC Name=4;
CC IsoId=Q4LDE5-4; Sequence=VSP_031628;
CC -!- TISSUE SPECIFICITY: Present in mesenchymal primary cultured cell
CC lysates (at protein level). Highly expressed in placenta. Also
CC expressed in marrow stromal cell. Weakly or not expressed in other
CC tissues. {ECO:0000269|PubMed:11062057, ECO:0000269|PubMed:16206243}.
CC -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans.
CC {ECO:0000269|PubMed:22171320}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG48257.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG48257.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB14617.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55420.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ619977; CAF04067.1; -; mRNA.
DR EMBL; AY916667; AAX12481.1; -; mRNA.
DR EMBL; AK023591; BAB14617.1; ALT_INIT; mRNA.
DR EMBL; AK075235; BAC11489.1; -; mRNA.
DR EMBL; AK027870; BAB55420.1; ALT_INIT; mRNA.
DR EMBL; AL158158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL592463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030816; AAH30816.1; -; mRNA.
DR EMBL; BX537918; CAD97901.1; -; mRNA.
DR EMBL; BX538049; CAD97988.1; -; mRNA.
DR EMBL; AF308289; AAG48257.1; ALT_SEQ; mRNA.
DR CCDS; CCDS48004.1; -. [Q4LDE5-1]
DR RefSeq; NP_699197.3; NM_153366.3. [Q4LDE5-1]
DR BioGRID; 123051; 7.
DR IntAct; Q4LDE5; 16.
DR MINT; Q4LDE5; -.
DR STRING; 9606.ENSP00000384917; -.
DR GlyConnect; 1781; 17 N-Linked glycans (9 sites).
DR GlyGen; Q4LDE5; 17 sites, 16 N-linked glycans (8 sites), 3 O-linked glycans (6 sites).
DR iPTMnet; Q4LDE5; -.
DR PhosphoSitePlus; Q4LDE5; -.
DR BioMuta; SVEP1; -.
DR DMDM; 296452942; -.
DR EPD; Q4LDE5; -.
DR jPOST; Q4LDE5; -.
DR MassIVE; Q4LDE5; -.
DR MaxQB; Q4LDE5; -.
DR PaxDb; Q4LDE5; -.
DR PeptideAtlas; Q4LDE5; -.
DR PRIDE; Q4LDE5; -.
DR ProteomicsDB; 62229; -. [Q4LDE5-1]
DR ProteomicsDB; 62230; -. [Q4LDE5-2]
DR ProteomicsDB; 62231; -. [Q4LDE5-3]
DR ProteomicsDB; 62232; -. [Q4LDE5-4]
DR Antibodypedia; 7229; 19 antibodies from 8 providers.
DR DNASU; 79987; -.
DR Ensembl; ENST00000374461.1; ENSP00000363585.2; ENSG00000165124.19. [Q4LDE5-2]
DR Ensembl; ENST00000374469.6; ENSP00000363593.2; ENSG00000165124.19. [Q4LDE5-1]
DR GeneID; 79987; -.
DR KEGG; hsa:79987; -.
DR MANE-Select; ENST00000374469.6; ENSP00000363593.2; NM_153366.4; NP_699197.3.
DR UCSC; uc010mtz.4; human. [Q4LDE5-1]
DR CTD; 79987; -.
DR DisGeNET; 79987; -.
DR GeneCards; SVEP1; -.
DR HGNC; HGNC:15985; SVEP1.
DR HPA; ENSG00000165124; Tissue enhanced (adipose tissue, placenta).
DR MIM; 611691; gene.
DR neXtProt; NX_Q4LDE5; -.
DR OpenTargets; ENSG00000165124; -.
DR PharmGKB; PA25971; -.
DR VEuPathDB; HostDB:ENSG00000165124; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000156061; -.
DR HOGENOM; CLU_000343_0_0_1; -.
DR InParanoid; Q4LDE5; -.
DR OMA; CSAIHCN; -.
DR PhylomeDB; Q4LDE5; -.
DR TreeFam; TF342247; -.
DR PathwayCommons; Q4LDE5; -.
DR SignaLink; Q4LDE5; -.
DR BioGRID-ORCS; 79987; 9 hits in 1032 CRISPR screens.
DR ChiTaRS; SVEP1; human.
DR GenomeRNAi; 79987; -.
DR Pharos; Q4LDE5; Tbio.
DR PRO; PR:Q4LDE5; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q4LDE5; protein.
DR Bgee; ENSG00000165124; Expressed in pericardium and 165 other tissues.
DR ExpressionAtlas; Q4LDE5; baseline and differential.
DR Genevisible; Q4LDE5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0008544; P:epidermis development; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0003017; P:lymph circulation; IEA:Ensembl.
DR GO; GO:0036303; P:lymph vessel morphogenesis; IBA:GO_Central.
DR GO; GO:0048014; P:Tie signaling pathway; IEA:Ensembl.
DR GO; GO:0120193; P:tight junction organization; IEA:Ensembl.
DR CDD; cd00033; CCP; 32.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR003410; HYR_dom.
DR InterPro; IPR001759; Pentraxin-related.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF00008; EGF; 6.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07699; Ephrin_rec_like; 4.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02494; HYR; 2.
DR Pfam; PF00354; Pentaxin; 1.
DR Pfam; PF00084; Sushi; 33.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR00895; PENTAXIN.
DR SMART; SM00032; CCP; 34.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 8.
DR SMART; SM00159; PTX; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF57184; SSF57184; 3.
DR SUPFAM; SSF57535; SSF57535; 33.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS00022; EGF_1; 9.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 9.
DR PROSITE; PS01187; EGF_CA; 6.
DR PROSITE; PS50825; HYR; 2.
DR PROSITE; PS51828; PTX_2; 1.
DR PROSITE; PS50923; SUSHI; 34.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cytoplasm; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Secreted; Signal; Sushi.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..3571
FT /note="Sushi, von Willebrand factor type A, EGF and
FT pentraxin domain-containing protein 1"
FT /id="PRO_0000320179"
FT DOMAIN 83..264
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 376..435
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 436..495
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 496..561
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 560..642
FT /note="HYR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00113"
FT DOMAIN 643..724
FT /note="HYR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00113"
FT DOMAIN 725..789
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1193..1229
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1231..1267
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1269..1305
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1307..1343
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1345..1381
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1383..1419
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1424..1628
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT DOMAIN 1629..1687
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1688..1745
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1745..1784
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1787..1844
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1845..1902
FT /note="Sushi 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1903..1960
FT /note="Sushi 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1961..2018
FT /note="Sushi 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2019..2080
FT /note="Sushi 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2081..2143
FT /note="Sushi 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2144..2201
FT /note="Sushi 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2202..2261
FT /note="Sushi 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2262..2320
FT /note="Sushi 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2321..2378
FT /note="Sushi 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2379..2437
FT /note="Sushi 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2438..2495
FT /note="Sushi 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2496..2553
FT /note="Sushi 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2554..2610
FT /note="Sushi 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2663..2714
FT /note="Sushi 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2715..2772
FT /note="Sushi 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2773..2830
FT /note="Sushi 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2831..2888
FT /note="Sushi 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2889..2946
FT /note="Sushi 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2947..3004
FT /note="Sushi 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3005..3061
FT /note="Sushi 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3062..3119
FT /note="Sushi 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3120..3178
FT /note="Sushi 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3179..3238
FT /note="Sushi 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3239..3296
FT /note="Sushi 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3297..3354
FT /note="Sushi 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3355..3413
FT /note="Sushi 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3414..3470
FT /note="Sushi 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3500..3532
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3533..3564
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 887..894
FT /note="O-glycosylated at one site"
FT MOTIF 2845..2847
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 847
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3018
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 378..420
FT /evidence="ECO:0000250"
FT DISULFID 406..433
FT /evidence="ECO:0000250"
FT DISULFID 438..480
FT /evidence="ECO:0000250"
FT DISULFID 466..493
FT /evidence="ECO:0000250"
FT DISULFID 498..544
FT /evidence="ECO:0000250"
FT DISULFID 529..559
FT /evidence="ECO:0000250"
FT DISULFID 727..769
FT /evidence="ECO:0000250"
FT DISULFID 753..787
FT /evidence="ECO:0000250"
FT DISULFID 1197..1208
FT /evidence="ECO:0000250"
FT DISULFID 1202..1217
FT /evidence="ECO:0000250"
FT DISULFID 1219..1228
FT /evidence="ECO:0000250"
FT DISULFID 1235..1246
FT /evidence="ECO:0000250"
FT DISULFID 1240..1255
FT /evidence="ECO:0000250"
FT DISULFID 1257..1266
FT /evidence="ECO:0000250"
FT DISULFID 1273..1284
FT /evidence="ECO:0000250"
FT DISULFID 1278..1293
FT /evidence="ECO:0000250"
FT DISULFID 1295..1304
FT /evidence="ECO:0000250"
FT DISULFID 1311..1322
FT /evidence="ECO:0000250"
FT DISULFID 1316..1331
FT /evidence="ECO:0000250"
FT DISULFID 1333..1342
FT /evidence="ECO:0000250"
FT DISULFID 1349..1360
FT /evidence="ECO:0000250"
FT DISULFID 1354..1369
FT /evidence="ECO:0000250"
FT DISULFID 1371..1380
FT /evidence="ECO:0000250"
FT DISULFID 1387..1398
FT /evidence="ECO:0000250"
FT DISULFID 1392..1407
FT /evidence="ECO:0000250"
FT DISULFID 1409..1418
FT /evidence="ECO:0000250"
FT DISULFID 1631..1672
FT /evidence="ECO:0000250"
FT DISULFID 1658..1685
FT /evidence="ECO:0000250"
FT DISULFID 1690..1730
FT /evidence="ECO:0000250"
FT DISULFID 1716..1743
FT /evidence="ECO:0000250"
FT DISULFID 1749..1761
FT /evidence="ECO:0000250"
FT DISULFID 1755..1770
FT /evidence="ECO:0000250"
FT DISULFID 1772..1783
FT /evidence="ECO:0000250"
FT DISULFID 1789..1829
FT /evidence="ECO:0000250"
FT DISULFID 1815..1842
FT /evidence="ECO:0000250"
FT DISULFID 1847..1887
FT /evidence="ECO:0000250"
FT DISULFID 1873..1900
FT /evidence="ECO:0000250"
FT DISULFID 1905..1945
FT /evidence="ECO:0000250"
FT DISULFID 1931..1958
FT /evidence="ECO:0000250"
FT DISULFID 1963..2003
FT /evidence="ECO:0000250"
FT DISULFID 1989..2016
FT /evidence="ECO:0000250"
FT DISULFID 2021..2061
FT /evidence="ECO:0000250"
FT DISULFID 2047..2078
FT /evidence="ECO:0000250"
FT DISULFID 2083..2126
FT /evidence="ECO:0000250"
FT DISULFID 2112..2141
FT /evidence="ECO:0000250"
FT DISULFID 2146..2186
FT /evidence="ECO:0000250"
FT DISULFID 2172..2199
FT /evidence="ECO:0000250"
FT DISULFID 2204..2245
FT /evidence="ECO:0000250"
FT DISULFID 2231..2259
FT /evidence="ECO:0000250"
FT DISULFID 2264..2304
FT /evidence="ECO:0000250"
FT DISULFID 2290..2318
FT /evidence="ECO:0000250"
FT DISULFID 2323..2363
FT /evidence="ECO:0000250"
FT DISULFID 2349..2376
FT /evidence="ECO:0000250"
FT DISULFID 2381..2422
FT /evidence="ECO:0000250"
FT DISULFID 2408..2435
FT /evidence="ECO:0000250"
FT DISULFID 2440..2480
FT /evidence="ECO:0000250"
FT DISULFID 2466..2493
FT /evidence="ECO:0000250"
FT DISULFID 2498..2538
FT /evidence="ECO:0000250"
FT DISULFID 2524..2551
FT /evidence="ECO:0000250"
FT DISULFID 2556..2596
FT /evidence="ECO:0000250"
FT DISULFID 2582..2608
FT /evidence="ECO:0000250"
FT DISULFID 2685..2712
FT /evidence="ECO:0000250"
FT DISULFID 2717..2757
FT /evidence="ECO:0000250"
FT DISULFID 2743..2770
FT /evidence="ECO:0000250"
FT DISULFID 2775..2815
FT /evidence="ECO:0000250"
FT DISULFID 2801..2828
FT /evidence="ECO:0000250"
FT DISULFID 2833..2873
FT /evidence="ECO:0000250"
FT DISULFID 2859..2886
FT /evidence="ECO:0000250"
FT DISULFID 2891..2931
FT /evidence="ECO:0000250"
FT DISULFID 2917..2944
FT /evidence="ECO:0000250"
FT DISULFID 2949..2989
FT /evidence="ECO:0000250"
FT DISULFID 2975..3002
FT /evidence="ECO:0000250"
FT DISULFID 3007..3046
FT /evidence="ECO:0000250"
FT DISULFID 3032..3059
FT /evidence="ECO:0000250"
FT DISULFID 3064..3104
FT /evidence="ECO:0000250"
FT DISULFID 3090..3117
FT /evidence="ECO:0000250"
FT DISULFID 3122..3163
FT /evidence="ECO:0000250"
FT DISULFID 3148..3176
FT /evidence="ECO:0000250"
FT DISULFID 3181..3221
FT /evidence="ECO:0000250"
FT DISULFID 3207..3236
FT /evidence="ECO:0000250"
FT DISULFID 3241..3281
FT /evidence="ECO:0000250"
FT DISULFID 3267..3294
FT /evidence="ECO:0000250"
FT DISULFID 3299..3339
FT /evidence="ECO:0000250"
FT DISULFID 3325..3352
FT /evidence="ECO:0000250"
FT DISULFID 3384..3411
FT /evidence="ECO:0000250"
FT DISULFID 3416..3456
FT /evidence="ECO:0000250"
FT DISULFID 3442..3468
FT /evidence="ECO:0000250"
FT DISULFID 3504..3514
FT /evidence="ECO:0000250"
FT DISULFID 3508..3520
FT /evidence="ECO:0000250"
FT DISULFID 3522..3531
FT /evidence="ECO:0000250"
FT DISULFID 3536..3546
FT /evidence="ECO:0000250"
FT DISULFID 3540..3552
FT /evidence="ECO:0000250"
FT DISULFID 3554..3563
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..2074
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_031625"
FT VAR_SEQ 868
FT /note="P -> N (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_031626"
FT VAR_SEQ 869..3571
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_031627"
FT VAR_SEQ 1547..3571
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031628"
FT VARIANT 332
FT /note="G -> A (in dbSNP:rs3818764)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_039153"
FT VARIANT 428
FT /note="G -> S (in dbSNP:rs10980419)"
FT /id="VAR_039154"
FT VARIANT 507
FT /note="V -> I (in dbSNP:rs872665)"
FT /id="VAR_039155"
FT VARIANT 581
FT /note="Q -> H (in dbSNP:rs10817033)"
FT /id="VAR_039156"
FT VARIANT 637
FT /note="I -> V (in dbSNP:rs13286541)"
FT /id="VAR_039157"
FT VARIANT 899
FT /note="K -> R (in dbSNP:rs10817025)"
FT /id="VAR_039158"
FT VARIANT 1157
FT /note="I -> V (in dbSNP:rs7038903)"
FT /id="VAR_039159"
FT VARIANT 1330
FT /note="L -> M (in dbSNP:rs10817021)"
FT /id="VAR_039160"
FT VARIANT 1416
FT /note="K -> Q (in dbSNP:rs1889323)"
FT /id="VAR_039161"
FT VARIANT 1444
FT /note="M -> L (in dbSNP:rs7863519)"
FT /id="VAR_039162"
FT VARIANT 1648
FT /note="L -> V (in dbSNP:rs7852962)"
FT /id="VAR_039163"
FT VARIANT 1810
FT /note="E -> A (in dbSNP:rs2986671)"
FT /id="VAR_039164"
FT VARIANT 1953
FT /note="R -> K (in dbSNP:rs17204832)"
FT /id="VAR_039165"
FT VARIANT 2607
FT /note="T -> A (in dbSNP:rs3802433)"
FT /id="VAR_039166"
FT VARIANT 2750
FT /note="A -> V (in dbSNP:rs7030192)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_039167"
FT VARIANT 2922
FT /note="I -> V (in dbSNP:rs16914996)"
FT /id="VAR_039168"
FT VARIANT 3161
FT /note="F -> I (in dbSNP:rs3739451)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_039169"
FT VARIANT 3230
FT /note="P -> T (in dbSNP:rs16914992)"
FT /id="VAR_039170"
FT VARIANT 3559
FT /note="T -> M (in dbSNP:rs17204533)"
FT /id="VAR_039171"
FT CONFLICT 429
FT /note="S -> L (in Ref. 1; CAF04067 and 3; BAB55420)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="H -> R (in Ref. 3; BAB14617)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="F -> L (in Ref. 3; BAB14617)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="C -> W (in Ref. 1; CAF04067 and 3; BAB55420)"
FT /evidence="ECO:0000305"
FT CONFLICT 980
FT /note="E -> G (in Ref. 1; CAF04067 and 3; BAB55420)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063
FT /note="Y -> C (in Ref. 1; CAF04067 and 3; BAB55420)"
FT /evidence="ECO:0000305"
FT CONFLICT 1442
FT /note="D -> V (in Ref. 1; CAF04067 and 3; BAB55420)"
FT /evidence="ECO:0000305"
FT CONFLICT 1546
FT /note="P -> PGMF (in Ref. 1; CAF04067)"
FT /evidence="ECO:0000305"
FT CONFLICT 1775
FT /note="P -> S (in Ref. 1; CAF04067)"
FT /evidence="ECO:0000305"
FT CONFLICT 2179
FT /note="K -> E (in Ref. 6; CAD97901)"
FT /evidence="ECO:0000305"
FT CONFLICT 2189
FT /note="T -> S (in Ref. 3; BAC11489)"
FT /evidence="ECO:0000305"
FT CONFLICT 2237
FT /note="S -> P (in Ref. 3; BAC11489)"
FT /evidence="ECO:0000305"
FT CONFLICT 2246
FT /note="Q -> H (in Ref. 3; BAC11489)"
FT /evidence="ECO:0000305"
FT CONFLICT 2259
FT /note="C -> W (in Ref. 3; BAC11489)"
FT /evidence="ECO:0000305"
FT CONFLICT 2299
FT /note="D -> G (in Ref. 6; CAD97988)"
FT /evidence="ECO:0000305"
FT CONFLICT 2454
FT /note="Q -> R (in Ref. 3; BAC11489)"
FT /evidence="ECO:0000305"
FT CONFLICT 2519
FT /note="T -> I (in Ref. 6; CAD97901)"
FT /evidence="ECO:0000305"
FT CONFLICT 2623
FT /note="D -> A (in Ref. 7; AAG48257)"
FT /evidence="ECO:0000305"
FT CONFLICT 2705
FT /note="W -> R (in Ref. 3; BAC11489)"
FT /evidence="ECO:0000305"
FT CONFLICT 2753
FT /note="D -> G (in Ref. 3; BAC11489)"
FT /evidence="ECO:0000305"
FT CONFLICT 2833
FT /note="C -> R (in Ref. 3; BAC11489)"
FT /evidence="ECO:0000305"
FT CONFLICT 2857
FT /note="Y -> H (in Ref. 6; CAD97901)"
FT /evidence="ECO:0000305"
FT CONFLICT 3005
FT /note="C -> F (in Ref. 3; BAC11489)"
FT /evidence="ECO:0000305"
FT CONFLICT 3186
FT /note="N -> S (in Ref. 6; CAD97988)"
FT /evidence="ECO:0000305"
FT CONFLICT 3302
FT /note="P -> Q (in Ref. 1; CAF04067 and 3; BAC11489)"
FT /evidence="ECO:0000305"
FT CONFLICT 3398
FT /note="C -> Y (in Ref. 1; CAF04067 and 3; BAC11489)"
FT /evidence="ECO:0000305"
FT CONFLICT 3565
FT /note="R -> G (in Ref. 6; CAD97988)"
FT /evidence="ECO:0000305"
FT CONFLICT 3567
FT /note="R -> G (in Ref. 6; CAD97988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3571 AA; 390170 MW; 8F52DE456CED5DED CRC64;
MWPRLAFCCW GLALVSGWAT FQQMSPSRNF SFRLFPETAP GAPGSIPAPP APGDEAAGSR
VERLGQAFRR RVRLLRELSE RLELVFLVDD SSSVGEVNFR SELMFVRKLL SDFPVVPTAT
RVAIVTFSSK NYVVPRVDYI STRRARQHKC ALLLQEIPAI SYRGGGTYTK GAFQQAAQIL
LHARENSTKV VFLITDGYSN GGDPRPIAAS LRDSGVEIFT FGIWQGNIRE LNDMASTPKE
EHCYLLHSFE EFEALARRAL HEDLPSGSFI QDDMVHCSYL CDEGKDCCDR MGSCKCGTHT
GHFECICEKG YYGKGLQYEC TACPSGTYKP EGSPGGISSC IPCPDENHTS PPGSTSPEDC
VCREGYRASG QTCELVHCPA LKPPENGYFI QNTCNNHFNA ACGVRCHPGF DLVGSSIILC
LPNGLWSGSE SYCRVRTCPH LRQPKHGHIS CSTREMLYKT TCLVACDEGY RLEGSDKLTC
QGNSQWDGPE PRCVERHCST FQMPKDVIIS PHNCGKQPAK FGTICYVSCR QGFILSGVKE
MLRCTTSGKW NVGVQAAVCK DVEAPQINCP KDIEAKTLEQ QDSANVTWQI PTAKDNSGEK
VSVHVHPAFT PPYLFPIGDV AIVYTATDLS GNQASCIFHI KVIDAEPPVI DWCRSPPPVQ
VSEKVHAASW DEPQFSDNSG AELVITRSHT QGDLFPQGET IVQYTATDPS GNNRTCDIHI
VIKGSPCEIP FTPVNGDFIC TPDNTGVNCT LTCLEGYDFT EGSTDKYYCA YEDGVWKPTY
TTEWPDCAKK RFANHGFKSF EMFYKAARCD DTDLMKKFSE AFETTLGKMV PSFCSDAEDI
DCRLEENLTK KYCLEYNYDY ENGFAIGPGG WGAANRLDYS YDDFLDTVQE TATSIGNAKS
SRIKRSAPLS DYKIKLIFNI TASVPLPDER NDTLEWENQQ RLLQTLETIT NKLKRTLNKD
PMYSFQLASE ILIADSNSLE TKKASPFCRP GSVLRGRMCV NCPLGTYYNL EHFTCESCRI
GSYQDEEGQL ECKLCPSGMY TEYIHSRNIS DCKAQCKQGT YSYSGLETCE SCPLGTYQPK
FGSRSCLSCP ENTSTVKRGA VNISACGVPC PEGKFSRSGL MPCHPCPRDY YQPNAGKAFC
LACPFYGTTP FAGSRSITEC SSFSSTFSAA EESVVPPASL GHIKKRHEIS SQVFHECFFN
PCHNSGTCQQ LGRGYVCLCP LGYTGLKCET DIDECSPLPC LNNGVCKDLV GEFICECPSG
YTGQRCEENI NECSSSPCLN KGICVDGVAG YRCTCVKGFV GLHCETEVNE CQSNPCLNNA
VCEDQVGGFL CKCPPGFLGT RCGKNVDECL SQPCKNGATC KDGANSFRCL CAAGFTGSHC
ELNINECQSN PCRNQATCVD ELNSYSCKCQ PGFSGKRCET EQSTGFNLDF EVSGIYGYVM
LDGMLPSLHA LTCTFWMKSS DDMNYGTPIS YAVDNGSDNT LLLTDYNGWV LYVNGREKIT
NCPSVNDGRW HHIAITWTSA NGIWKVYIDG KLSDGGAGLS VGLPIPGGGA LVLGQEQDKK
GEGFSPAESF VGSISQLNLW DYVLSPQQVK SLATSCPEEL SKGNVLAWPD FLSGIVGKVK
IDSKSIFCSD CPRLGGSVPH LRTASEDLKP GSKVNLFCDP GFQLVGNPVQ YCLNQGQWTQ
PLPHCERISC GVPPPLENGF HSADDFYAGS TVTYQCNNGY YLLGDSRMFC TDNGSWNGVS
PSCLDVDECA VGSDCSEHAS CLNVDGSYIC SCVPPYTGDG KNCAEPIKCK APGNPENGHS
SGEIYTVGAE VTFSCQEGYQ LMGVTKITCL ESGEWNHLIP YCKAVSCGKP AIPENGCIEE
LAFTFGSKVT YRCNKGYTLA GDKESSCLAN SSWSHSPPVC EPVKCSSPEN INNGKYILSG
LTYLSTASYS CDTGYSLQGP SIIECTASGI WDRAPPACHL VFCGEPPAIK DAVITGNNFT
FRNTVTYTCK EGYTLAGLDT IECLADGKWS RSDQQCLAVS CDEPPIVDHA SPETAHRLFG
DIAFYYCSDG YSLADNSQLL CNAQGKWVPP EGQDMPRCIA HFCEKPPSVS YSILESVSKA
KFAAGSVVSF KCMEGFVLNT SAKIECMRGG QWNPSPMSIQ CIPVRCGEPP SIMNGYASGS
NYSFGAMVAY SCNKGFYIKG EKKSTCEATG QWSSPIPTCH PVSCGEPPKV ENGFLEHTTG
RIFESEVRYQ CNPGYKSVGS PVFVCQANRH WHSESPLMCV PLDCGKPPPI QNGFMKGENF
EVGSKVQFFC NEGYELVGDS SWTCQKSGKW NKKSNPKCMP AKCPEPPLLE NQLVLKELTT
EVGVVTFSCK EGHVLQGPSV LKCLPSQQWN DSFPVCKIVL CTPPPLISFG VPIPSSALHF
GSTVKYSCVG GFFLRGNSTT LCQPDGTWSS PLPECVPVEC PQPEEIPNGI IDVQGLAYLS
TALYTCKPGF ELVGNTTTLC GENGHWLGGK PTCKAIECLK PKEILNGKFS YTDLHYGQTV
TYSCNRGFRL EGPSALTCLE TGDWDVDAPS CNAIHCDSPQ PIENGFVEGA DYSYGAIIIY
SCFPGFQVAG HAMQTCEESG WSSSIPTCMP IDCGLPPHID FGDCTKLKDD QGYFEQEDDM
MEVPYVTPHP PYHLGAVAKT WENTKESPAT HSSNFLYGTM VSYTCNPGYE LLGNPVLICQ
EDGTWNGSAP SCISIECDLP TAPENGFLRF TETSMGSAVQ YSCKPGHILA GSDLRLCLEN
RKWSGASPRC EAISCKKPNP VMNGSIKGSN YTYLSTLYYE CDPGYVLNGT ERRTCQDDKN
WDEDEPICIP VDCSSPPVSA NGQVRGDEYT FQKEIEYTCN EGFLLEGARS RVCLANGSWS
GATPDCVPVR CATPPQLANG VTEGLDYGFM KEVTFHCHEG YILHGAPKLT CQSDGNWDAE
IPLCKPVNCG PPEDLAHGFP NGFSFIHGGH IQYQCFPGYK LHGNSSRRCL SNGSWSGSSP
SCLPCRCSTP VIEYGTVNGT DFDCGKAARI QCFKGFKLLG LSEITCEADG QWSSGFPHCE
HTSCGSLPMI PNAFISETSS WKENVITYSC RSGYVIQGSS DLICTEKGVW SQPYPVCEPL
SCGSPPSVAN AVATGEAHTY ESEVKLRCLE GYTMDTDTDT FTCQKDGRWF PERISCSPKK
CPLPENITHI LVHGDDFSVN RQVSVSCAEG YTFEGVNISV CQLDGTWEPP FSDESCSPVS
CGKPESPEHG FVVGSKYTFE STIIYQCEPG YELEGNRERV CQENRQWSGG VAICKETRCE
TPLEFLNGKA DIENRTTGPN VVYSCNRGYS LEGPSEAHCT ENGTWSHPVP LCKPNPCPVP
FVIPENALLS EKEFYVDQNV SIKCREGFLL QGHGIITCNP DETWTQTSAK CEKISCGPPA
HVENAIARGV HYQYGDMITY SCYSGYMLEG FLRSVCLENG TWTSPPICRA VCRFPCQNGG
ICQRPNACSC PEGWMGRLCE EPICILPCLN GGRCVAPYQC DCPPGWTGSR CHTAVCQSPC
LNGGKCVRPN RCHCLSSWTG HNCSRKRRTG F
