SVEP1_MOUSE
ID SVEP1_MOUSE Reviewed; 3567 AA.
AC A2AVA0; Q8C720; Q8CBT2; Q922H0; Q9CUT3; Q9ES77;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1;
DE AltName: Full=Polydom;
DE Flags: Precursor;
GN Name=Svep1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C3H/HeN;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-848 AND 2967-3567.
RC STRAIN=C57BL/6J; TISSUE=Head, Kidney, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2899-3567.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP POSSIBLE FUNCTION, AND TISSUE 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in the cell attachment process.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cytoplasm {ECO:0000250}.
CC Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AVA0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AVA0-2; Sequence=VSP_031629, VSP_031630;
CC -!- TISSUE SPECIFICITY: Present in stromal osteogenic cells. Expressed at
CC much higher level in stromal osteogenic cells at low density compared
CC to cells grown at higher densities (at protein level). Highly expressed
CC in lung and placenta. Also expressed in bone and periosteum, but not in
CC cartilage and skeletal muscle. Weakly or not expressed in other
CC tissues. {ECO:0000269|PubMed:11062057, ECO:0000269|PubMed:16206243}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 11 dpc to 17 dpc in embryos.
CC {ECO:0000269|PubMed:11062057}.
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DR EMBL; AF206329; AAG32160.1; -; mRNA.
DR EMBL; AK052699; BAC35103.1; -; mRNA.
DR EMBL; AK014693; BAB29505.1; -; mRNA.
DR EMBL; AK035333; BAC29036.1; -; mRNA.
DR EMBL; AL805969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008135; AAH08135.1; -; mRNA.
DR CCDS; CCDS18209.1; -. [A2AVA0-1]
DR RefSeq; NP_073725.2; NM_022814.2. [A2AVA0-1]
DR BioGRID; 211104; 1.
DR STRING; 10090.ENSMUSP00000045856; -.
DR GlyGen; A2AVA0; 1 site.
DR iPTMnet; A2AVA0; -.
DR PhosphoSitePlus; A2AVA0; -.
DR jPOST; A2AVA0; -.
DR MaxQB; A2AVA0; -.
DR PaxDb; A2AVA0; -.
DR PRIDE; A2AVA0; -.
DR ProteomicsDB; 257105; -. [A2AVA0-1]
DR ProteomicsDB; 257106; -. [A2AVA0-2]
DR Antibodypedia; 7229; 19 antibodies from 8 providers.
DR DNASU; 64817; -.
DR Ensembl; ENSMUST00000042850; ENSMUSP00000045856; ENSMUSG00000028369. [A2AVA0-1]
DR GeneID; 64817; -.
DR KEGG; mmu:64817; -.
DR UCSC; uc008syr.1; mouse. [A2AVA0-1]
DR UCSC; uc008sys.1; mouse. [A2AVA0-2]
DR CTD; 79987; -.
DR MGI; MGI:1928849; Svep1.
DR VEuPathDB; HostDB:ENSMUSG00000028369; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000156061; -.
DR HOGENOM; CLU_000343_0_0_1; -.
DR InParanoid; A2AVA0; -.
DR OMA; CSAIHCN; -.
DR OrthoDB; 46968at2759; -.
DR PhylomeDB; A2AVA0; -.
DR TreeFam; TF342247; -.
DR BioGRID-ORCS; 64817; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Svep1; mouse.
DR PRO; PR:A2AVA0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AVA0; protein.
DR Bgee; ENSMUSG00000028369; Expressed in vault of skull and 157 other tissues.
DR Genevisible; A2AVA0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; TAS:MGI.
DR GO; GO:0005576; C:extracellular region; ISS:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0008544; P:epidermis development; IMP:MGI.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; ISO:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0003017; P:lymph circulation; IMP:MGI.
DR GO; GO:0001945; P:lymph vessel development; IMP:MGI.
DR GO; GO:0036303; P:lymph vessel morphogenesis; IMP:MGI.
DR GO; GO:0048014; P:Tie signaling pathway; IMP:MGI.
DR GO; GO:0120193; P:tight junction organization; IMP:MGI.
DR CDD; cd00033; CCP; 33.
DR CDD; cd00152; PTX; 1.
DR Gene3D; 2.60.40.10; -; 1.
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; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR003410; HYR_dom.
DR InterPro; IPR013783; Ig-like_fold.
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; 5.
DR Pfam; PF12947; EGF_3; 1.
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; 12.
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..3567
FT /note="Sushi, von Willebrand factor type A, EGF and
FT pentraxin domain-containing protein 1"
FT /id="PRO_5000057616"
FT DOMAIN 84..265
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 377..436
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 437..496
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 497..561
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 560..644
FT /note="HYR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00113"
FT DOMAIN 645..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 1192..1228
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1230..1266
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1268..1304
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1306..1342
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1344..1380
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1382..1418
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1423..1627
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT DOMAIN 1628..1686
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1687..1744
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1744..1783
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1780..1843
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1844..1901
FT /note="Sushi 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1902..1959
FT /note="Sushi 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1960..2017
FT /note="Sushi 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2018..2079
FT /note="Sushi 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2080..2142
FT /note="Sushi 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2143..2200
FT /note="Sushi 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2201..2260
FT /note="Sushi 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2261..2319
FT /note="Sushi 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2320..2377
FT /note="Sushi 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2378..2436
FT /note="Sushi 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2437..2494
FT /note="Sushi 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2495..2552
FT /note="Sushi 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2553..2609
FT /note="Sushi 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2660..2711
FT /note="Sushi 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2712..2769
FT /note="Sushi 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2770..2827
FT /note="Sushi 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2828..2885
FT /note="Sushi 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2886..2943
FT /note="Sushi 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 2944..3001
FT /note="Sushi 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3002..3057
FT /note="Sushi 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3058..3115
FT /note="Sushi 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3116..3174
FT /note="Sushi 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3175..3234
FT /note="Sushi 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3235..3292
FT /note="Sushi 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3293..3350
FT /note="Sushi 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3351..3409
FT /note="Sushi 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3410..3466
FT /note="Sushi 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 3496..3528
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3529..3560
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 379..421
FT /evidence="ECO:0000250"
FT DISULFID 407..434
FT /evidence="ECO:0000250"
FT DISULFID 439..481
FT /evidence="ECO:0000250"
FT DISULFID 467..494
FT /evidence="ECO:0000250"
FT DISULFID 499..544
FT /evidence="ECO:0000250"
FT DISULFID 530..559
FT /evidence="ECO:0000250"
FT DISULFID 727..769
FT /evidence="ECO:0000250"
FT DISULFID 753..787
FT /evidence="ECO:0000250"
FT DISULFID 1196..1207
FT /evidence="ECO:0000250"
FT DISULFID 1201..1216
FT /evidence="ECO:0000250"
FT DISULFID 1218..1227
FT /evidence="ECO:0000250"
FT DISULFID 1234..1245
FT /evidence="ECO:0000250"
FT DISULFID 1239..1254
FT /evidence="ECO:0000250"
FT DISULFID 1256..1265
FT /evidence="ECO:0000250"
FT DISULFID 1272..1283
FT /evidence="ECO:0000250"
FT DISULFID 1277..1292
FT /evidence="ECO:0000250"
FT DISULFID 1294..1303
FT /evidence="ECO:0000250"
FT DISULFID 1310..1321
FT /evidence="ECO:0000250"
FT DISULFID 1315..1330
FT /evidence="ECO:0000250"
FT DISULFID 1332..1341
FT /evidence="ECO:0000250"
FT DISULFID 1348..1359
FT /evidence="ECO:0000250"
FT DISULFID 1353..1368
FT /evidence="ECO:0000250"
FT DISULFID 1370..1379
FT /evidence="ECO:0000250"
FT DISULFID 1386..1397
FT /evidence="ECO:0000250"
FT DISULFID 1391..1406
FT /evidence="ECO:0000250"
FT DISULFID 1408..1417
FT /evidence="ECO:0000250"
FT DISULFID 1630..1671
FT /evidence="ECO:0000250"
FT DISULFID 1657..1684
FT /evidence="ECO:0000250"
FT DISULFID 1689..1729
FT /evidence="ECO:0000250"
FT DISULFID 1715..1742
FT /evidence="ECO:0000250"
FT DISULFID 1748..1760
FT /evidence="ECO:0000250"
FT DISULFID 1754..1769
FT /evidence="ECO:0000250"
FT DISULFID 1771..1782
FT /evidence="ECO:0000250"
FT DISULFID 1788..1828
FT /evidence="ECO:0000250"
FT DISULFID 1814..1841
FT /evidence="ECO:0000250"
FT DISULFID 1846..1886
FT /evidence="ECO:0000250"
FT DISULFID 1872..1899
FT /evidence="ECO:0000250"
FT DISULFID 1904..1944
FT /evidence="ECO:0000250"
FT DISULFID 1930..1957
FT /evidence="ECO:0000250"
FT DISULFID 1962..2002
FT /evidence="ECO:0000250"
FT DISULFID 1988..2015
FT /evidence="ECO:0000250"
FT DISULFID 2020..2060
FT /evidence="ECO:0000250"
FT DISULFID 2046..2077
FT /evidence="ECO:0000250"
FT DISULFID 2082..2125
FT /evidence="ECO:0000250"
FT DISULFID 2111..2140
FT /evidence="ECO:0000250"
FT DISULFID 2145..2185
FT /evidence="ECO:0000250"
FT DISULFID 2171..2198
FT /evidence="ECO:0000250"
FT DISULFID 2203..2244
FT /evidence="ECO:0000250"
FT DISULFID 2230..2258
FT /evidence="ECO:0000250"
FT DISULFID 2263..2303
FT /evidence="ECO:0000250"
FT DISULFID 2289..2317
FT /evidence="ECO:0000250"
FT DISULFID 2322..2362
FT /evidence="ECO:0000250"
FT DISULFID 2348..2375
FT /evidence="ECO:0000250"
FT DISULFID 2380..2421
FT /evidence="ECO:0000250"
FT DISULFID 2407..2434
FT /evidence="ECO:0000250"
FT DISULFID 2439..2479
FT /evidence="ECO:0000250"
FT DISULFID 2465..2492
FT /evidence="ECO:0000250"
FT DISULFID 2497..2537
FT /evidence="ECO:0000250"
FT DISULFID 2523..2550
FT /evidence="ECO:0000250"
FT DISULFID 2555..2595
FT /evidence="ECO:0000250"
FT DISULFID 2581..2607
FT /evidence="ECO:0000250"
FT DISULFID 2682..2709
FT /evidence="ECO:0000250"
FT DISULFID 2714..2754
FT /evidence="ECO:0000250"
FT DISULFID 2740..2767
FT /evidence="ECO:0000250"
FT DISULFID 2772..2812
FT /evidence="ECO:0000250"
FT DISULFID 2798..2825
FT /evidence="ECO:0000250"
FT DISULFID 2830..2870
FT /evidence="ECO:0000250"
FT DISULFID 2856..2883
FT /evidence="ECO:0000250"
FT DISULFID 2888..2928
FT /evidence="ECO:0000250"
FT DISULFID 2914..2941
FT /evidence="ECO:0000250"
FT DISULFID 2946..2986
FT /evidence="ECO:0000250"
FT DISULFID 2972..2999
FT /evidence="ECO:0000250"
FT DISULFID 3004..3043
FT /evidence="ECO:0000250"
FT DISULFID 3029..3055
FT /evidence="ECO:0000250"
FT DISULFID 3060..3100
FT /evidence="ECO:0000250"
FT DISULFID 3086..3113
FT /evidence="ECO:0000250"
FT DISULFID 3118..3159
FT /evidence="ECO:0000250"
FT DISULFID 3144..3172
FT /evidence="ECO:0000250"
FT DISULFID 3177..3217
FT /evidence="ECO:0000250"
FT DISULFID 3203..3232
FT /evidence="ECO:0000250"
FT DISULFID 3237..3277
FT /evidence="ECO:0000250"
FT DISULFID 3263..3290
FT /evidence="ECO:0000250"
FT DISULFID 3295..3335
FT /evidence="ECO:0000250"
FT DISULFID 3321..3348
FT /evidence="ECO:0000250"
FT DISULFID 3353..3394
FT /evidence="ECO:0000250"
FT DISULFID 3380..3407
FT /evidence="ECO:0000250"
FT DISULFID 3412..3452
FT /evidence="ECO:0000250"
FT DISULFID 3438..3464
FT /evidence="ECO:0000250"
FT DISULFID 3500..3510
FT /evidence="ECO:0000250"
FT DISULFID 3504..3516
FT /evidence="ECO:0000250"
FT DISULFID 3518..3527
FT /evidence="ECO:0000250"
FT DISULFID 3532..3542
FT /evidence="ECO:0000250"
FT DISULFID 3536..3548
FT /evidence="ECO:0000250"
FT DISULFID 3550..3559
FT /evidence="ECO:0000250"
FT VAR_SEQ 436..440
FT /note="VRTCP -> GMESG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031629"
FT VAR_SEQ 441..3567
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031630"
FT CONFLICT 1480
FT /note="F -> S (in Ref. 1; AAG32160)"
FT /evidence="ECO:0000305"
FT CONFLICT 1528
FT /note="D -> N (in Ref. 1; AAG32160)"
FT /evidence="ECO:0000305"
FT CONFLICT 3143
FT /note="R -> K (in Ref. 2; BAB29505)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3567 AA; 387457 MW; 8E10297DFB8392EE CRC64;
MWSRLAFCCW ALALVSGWTN FQPVAPSLNF SFRLFPEASP GALGRLAVPP ASSEEEAAGS
KVERLGRAFR SRVRRLRELS GSLELVFLVD ESSSVGQTNF LNELKFVRKL LSDFPVVSTA
TRVAIVTFSS KNNVVARVDY ISTSRAHQHK CALLSREIPA ITYRGGGTYT KGAFQQAAQI
LRHSRENSTK VIFLITDGYS NGGDPRPIAA SLRDFGVEIF TFGIWQGNIR ELNDMASTPK
EEHCYLLHSF EEFEALARRA LHEDLPSGSF IQEDMARCSY LCEAGKDCCD RMASCKCGTH
TGQFECICEK GYYGKGLQHE CTACPSGTYK PEASPGGIST CIPCPDVSHT SPPGSTSPED
CVCREGYQRS GQTCEVVHCP ALKPPENGFF IQNTCKNHFN AACGVRCRPG FDLVGSSIHL
CQPNGLWSGT ESFCRVRTCP HLRQPKHGHI SCSTAEMSYN TLCLVTCNEG YRLEGSTRLT
CQGNAQWDGP EPRCVERHCA TFQKPKGVII SPPSCGKQPA RPGMTCQLSC RQGYILSGVR
EVRCATSGKW SAKVQTAVCK DVEAPQISCP NDIEAKTGEQ QDSANVTWQV PTAKDNSGEK
VSVHVHPAFT PPYLFPIGDV AITYTATDSS GNQASCTFYI KVIDVEPPVI DWCRSPPPIQ
VVEKEHPASW DEPQFSDNSG AELVITSSHT QGDMFPHGET VVWYTATDPS GNNRTCDIHI
VIKGSPCEVP FTPVNGDFIC AQDSAGVNCS LSCKEGYDFT EGSTEKYYCA FEDGIWRPPY
STEWPDCAIK RFANHGFKSF EMLYKTTRCD DMDLFKKFSA AFETTLGNMV PSFCNDADDI
DCRLEDLTKK YCIEYNYNYE NGFAIGPGGW GAGNRLDYSY DHFLDVVQET PTDVGKARSS
RIKRTVPLSD PKIQLIFNIT ASVPLPEERN DTLELENQQR LIKTLETITN RLKSTLNKEP
MYSFQLASET VVADSNSLET EKAFLFCRPG SVLRGRMCVN CPLGTSYSLE HSTCESCLMG
SYQDEEGQLE CKLCPPRTHT EYLHSRSVSE CKAQCKQGTY SSSGLETCES CPLGTYQPEF
GSRSCLLCPE TTTTVKRGAV DISACGVPCP VGEFSRSGLT PCYPCPRDYY QPNAGKSFCL
ACPFYGTTTI TGATSITDCS SFSSTFSAAE ESIVPLVAPG HSQNKYEVSS QVFHECFLNP
CHNSGTCQQL GRGYVCLCPP GYTGLKCETD IDECSSLPCL NGGICRDQVG GFTCECSLGY
SGQICEENIN ECISSPCLNK GTCTDGLASY RCTCVKGYMG VHCETDVNEC QSSPCLNNAV
CKDQVGGFSC KCPPGFLGTR CEKNVDECLS QPCQNGATCK DGANSFRCQC PAGFTGTHCE
LNINECQSNP CRNQATCVDE LNSYSCKCQP GFSGHRCETE QPSGFNLDFE VSGIYGYVLL
DGVLPTLHAI TCAFWMKSSD VINYGTPISY ALEDDKDNTF LLTDYNGWVL YVNGKEKITN
CPSVNDGIWH HIAITWTSTG GAWRVYIDGE LSDGGTGLSI GKAIPGGGAL VLGQEQDKKG
EGFNPAESFV GSISQLNLWD YVLSPQQVKL LASSCPEELS RGNVLAWPDF LSGITGKVKV
DSSSMFCSDC PSLEGSVPHL RPASGNRKPG SKVSLFCDPG FQMVGNPVQY CLNQGQWTQP
LPHCERIRCG LPPALENGFY SAEDFHAGST VTYQCTSGYY LLGDSRMFCT DNGSWNGISP
SCLDVDECAV GSDCSEHASC LNTNGSYVCS CNPPYTGDGK NCAEPVKCKA PENPENGHSS
GEIYTVGTAV TFSCDEGHEL VGVSTITCLE TGEWDRLRPS CEAISCGVPP VPENGGVDGS
AFTYGSKVVY RCDKGYTLSG DEESACLASG SWSHSSPVCE LVKCSQPEDI NNGKYILSGL
TYLSIASYSC ENGYSLQGPS LLECTASGSW DRAPPSCQLV SCGEPPIVKD AVITGSNFTF
GNTVAYTCKE GYTLAGPDTI VCQANGKWNS SNHQCLAVSC DEPPNVDHAS PETAHRLFGD
TAFYYCADGY SLADNSQLIC NAQGNWVPPA GQAVPRCIAH FCEKPPSVSY SILESVSKAK
FAAGSVVSFK CMEGFVLNTS AKIECLRGGE WSPSPLSVQC IPVRCGEPPS IANGYPSGTN
YSFGAVVAYS CHKGFYIKGE KKSTCEATGQ WSKPTPTCHP VSCNEPPKVE NGFLEHTTGR
TFESEARFQC NPGYKAAGSP VFVCQANRHW HSDAPLSCTP LNCGKPPPIQ NGFLKGESFE
VGSKVQFVCN EGYELVGDNS WTCQKSGKWS KKPSPKCVPT KCAEPPLLEN QLVLKELASE
VGVMTISCKE GHALQGPSVL KCLPSGQWNG SFPICKMVLC PSPPLIPFGV PASSGALHFG
STVKYLCVDG FFLRGSPTIL CQADSTWSSP LPECVPVECP QPEEILNGII HVQGLAYLST
TLYTCKPGFE LVGNATTLCG ENGQWLGGKP MCKPIECPEP KEILNGQFSS VSFQYGQTIT
YFCDRGFRLE GPKSLTCLET GDWDMDPPSC DAIHCSDPQP IENGFVEGAD YRYGAMIIYS
CFPGFQVLGH AMQTCEESGW SSSSPTCVPI DCGLPPHIDF GDCTKVRDGQ GHFDQEDDMM
EVPYLAHPQH LEATAKALEN TKESPASHAS HFLYGTMVSY SCEPGYELLG IPVLICQEDG
TWNGTAPSCI SIECDLPVAP ENGFLHFTQT TMGSAAQYSC KPGHILEGSH LRLCLQNKQW
SGTVPRCEAI SCSKPNPLWN GSIKGDDYSY LGVLYYECDS GYILNGSKKR TCQENRDWDG
HEPMCIPVDC GSPPVPTNGR VKGEEYTFQK EITYSCREGF ILEGARSRIC LTNGSWSGAT
PSCMPVRCPA PPQVPNGVAD GLDYGFKKEV AFHCLEGYVL QGAPRLTCQS NGTWDAEVPV
CKPATCGPPA DLPQGFPNGF SFYHGGHIQY QCFTGYKLHG NPSRRCLPNG SWSGSSPSCL
PCRCSTPIIQ QGTINATDLG CGKTVQIECF KGFKLLGLSE ITCDANGQWS DVPLCEHAQC
GPLPTIPNAI VLEGSLSEDN VVTYSCRPGY TMQGSSDLIC TEKAIWSQPY PTCEPLSCGP
PPTVANAVAT GEAHTYESKV KLRCLEGYVM DSDTDTFTCQ QDGHWVPERI TCSPKKCPVP
SNMTRIRFHG DDFQVNRQVS VSCAEGFTHE GVNWSTCQPD GTWEPPFSDE SCIPVVCGHP
ESPAHGSVVG NKHSFGSTIV YQCDPGYKLE GNRERICQEN RQWSGEVAVC RENRCETPAE
FPNGKAVLEN TTSGPSLLFS CHRGYTLEGS PEAHCTANGT WNHLTPLCKP NPCPVPFVIP
ENAVLSEKEF YVDQNVSIKC REGFLLKGNG VITCSPDETW THTNARCEKI SCGPPSHVEN
AIARGVYYQY GDMITYSCYS GYMLEGSLRS VCLENGTWTP SPVCRAVCRF PCQNGGVCQR
PNACSCPDGW MGRLCEEPIC ILPCLNGGRC VAPYQCDCPT GWTGSRCHTA TCQSPCLNGG
KCIRPNRCHC LSAWTGHDCS RKRRAGL
