ID   TSP3_HUMAN              Reviewed;         956 AA.
AC   P49746; B1AVR8; B4DQ20; Q8WV34;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 205.
DE   RecName: Full=Thrombospondin-3;
DE   Flags: Precursor;
GN   Name=THBS3; Synonyms=TSP3;
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).
RC   TISSUE=Lung;
RX   PubMed=7558000; DOI=10.1006/geno.1995.1050;
RA   Adolph K.W., Long G.L., Winfield S., Ginns E.I., Bornstein P.;
RT   "Structure and organization of the human thrombospondin 3 gene (THBS3).";
RL   Genomics 27:329-336(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-736.
RX   PubMed=9331372; DOI=10.1101/gr.7.10.1020;
RA   Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E.;
RT   "Identification of three additional genes contiguous to the
RT   glucocerebrosidase locus on chromosome 1q21: implications for Gaucher
RT   disease.";
RL   Genome Res. 7:1020-1026(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 365-956.
RC   TISSUE=Retina;
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] GLY-955.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC       matrix interactions. Can bind to fibrinogen, fibronectin, laminin and
CC       type V collagen.
CC   -!- SUBUNIT: Oligomer; disulfide-linked.
CC   -!- INTERACTION:
CC       P49746; P27797: CALR; NbExp=3; IntAct=EBI-2530931, EBI-1049597;
CC       P49746; P36957: DLST; NbExp=3; IntAct=EBI-2530931, EBI-351007;
CC       P49746; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-2530931, EBI-1055945;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P49746-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P49746-2; Sequence=VSP_045328;
CC   -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
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DR   EMBL; L38969; AAC41762.1; -; mRNA.
DR   EMBL; AL713999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF023268; AAC51818.1; -; Genomic_DNA.
DR   EMBL; AK298592; BAG60782.1; -; mRNA.
DR   EMBL; CH471121; EAW53110.1; -; Genomic_DNA.
DR   EMBL; BC018786; AAH18786.1; -; mRNA.
DR   CCDS; CCDS1099.1; -. [P49746-1]
DR   CCDS; CCDS58034.1; -. [P49746-2]
DR   PIR; A57121; A57121.
DR   RefSeq; NP_001239536.1; NM_001252607.1.
DR   RefSeq; NP_001239537.1; NM_001252608.1. [P49746-2]
DR   RefSeq; NP_009043.1; NM_007112.4. [P49746-1]
DR   AlphaFoldDB; P49746; -.
DR   SMR; P49746; -.
DR   BioGRID; 112917; 92.
DR   ComplexPortal; CPX-1789; Thrombospondin 3 complex.
DR   IntAct; P49746; 43.
DR   MINT; P49746; -.
DR   STRING; 9606.ENSP00000357362; -.
DR   GlyConnect; 1806; 18 N-Linked glycans (2 sites).
DR   GlyCosmos; P49746; 4 sites, 18 glycans.
DR   GlyGen; P49746; 6 sites, 18 N-linked glycans (2 sites), 2 O-linked glycans (2 sites).
DR   iPTMnet; P49746; -.
DR   PhosphoSitePlus; P49746; -.
DR   BioMuta; THBS3; -.
DR   DMDM; 1717814; -.
DR   EPD; P49746; -.
DR   jPOST; P49746; -.
DR   MassIVE; P49746; -.
DR   PaxDb; 9606-ENSP00000357362; -.
DR   PeptideAtlas; P49746; -.
DR   ProteomicsDB; 4837; -.
DR   ProteomicsDB; 56059; -. [P49746-1]
DR   Antibodypedia; 34176; 220 antibodies from 30 providers.
DR   DNASU; 7059; -.
DR   Ensembl; ENST00000368378.7; ENSP00000357362.3; ENSG00000169231.13. [P49746-1]
DR   Ensembl; ENST00000457183.6; ENSP00000392207.2; ENSG00000169231.13. [P49746-2]
DR   GeneID; 7059; -.
DR   KEGG; hsa:7059; -.
DR   MANE-Select; ENST00000368378.7; ENSP00000357362.3; NM_007112.5; NP_009043.1.
DR   UCSC; uc001fix.4; human. [P49746-1]
DR   AGR; HGNC:11787; -.
DR   CTD; 7059; -.
DR   DisGeNET; 7059; -.
DR   GeneCards; THBS3; -.
DR   HGNC; HGNC:11787; THBS3.
DR   HPA; ENSG00000169231; Low tissue specificity.
DR   MIM; 188062; gene.
DR   neXtProt; NX_P49746; -.
DR   OpenTargets; ENSG00000169231; -.
DR   PharmGKB; PA36499; -.
DR   VEuPathDB; HostDB:ENSG00000169231; -.
DR   eggNOG; ENOG502QRK8; Eukaryota.
DR   GeneTree; ENSGT00940000159283; -.
DR   HOGENOM; CLU_009257_1_1_1; -.
DR   InParanoid; P49746; -.
DR   OMA; NSMIHRT; -.
DR   OrthoDB; 5345349at2759; -.
DR   PhylomeDB; P49746; -.
DR   TreeFam; TF324917; -.
DR   PathwayCommons; P49746; -.
DR   Reactome; R-HSA-186797; Signaling by PDGF.
DR   SignaLink; P49746; -.
DR   BioGRID-ORCS; 7059; 24 hits in 1158 CRISPR screens.
DR   ChiTaRS; THBS3; human.
DR   GeneWiki; THBS3; -.
DR   GenomeRNAi; 7059; -.
DR   Pharos; P49746; Tbio.
DR   PRO; PR:P49746; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P49746; Protein.
DR   Bgee; ENSG00000169231; Expressed in right uterine tube and 152 other cell types or tissues.
DR   ExpressionAtlas; P49746; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; IDA:MGI.
DR   GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl.
DR   GO; GO:0007160; P:cell-matrix adhesion; NAS:UniProtKB.
DR   GO; GO:0003417; P:growth plate cartilage development; IEA:Ensembl.
DR   GO; GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd16079; TSP-3cc; 1.
DR   Gene3D; 1.20.5.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   Gene3D; 4.10.1080.10; TSP type-3 repeat; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR   InterPro; IPR017897; Thrombospondin_3_rpt.
DR   InterPro; IPR008859; Thrombospondin_C.
DR   InterPro; IPR024665; TSP/COMP_coiled-coil.
DR   InterPro; IPR046970; TSP/COMP_coiled-coil_sf.
DR   InterPro; IPR028507; TSP3_coiled-coil.
DR   InterPro; IPR028974; TSP_type-3_rpt.
DR   InterPro; IPR048287; TSPN-like_N.
DR   PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR   PANTHER; PTHR10199:SF89; THROMBOSPONDIN-3; 1.
DR   Pfam; PF11598; COMP; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF02412; TSP_3; 5.
DR   Pfam; PF05735; TSP_C; 1.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF58006; Assembly domain of cartilage oligomeric matrix protein; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS51234; TSP3; 8.
DR   PROSITE; PS51236; TSP_CTER; 1.
DR   Genevisible; P49746; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..956
FT                   /note="Thrombospondin-3"
FT                   /id="PRO_0000035849"
FT   DOMAIN          23..193
FT                   /note="Laminin G-like"
FT   DOMAIN          316..354
FT                   /note="EGF-like 1; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          370..410
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          414..456
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REPEAT          457..491
FT                   /note="TSP type-3 1"
FT   REPEAT          492..527
FT                   /note="TSP type-3 2"
FT   REPEAT          528..550
FT                   /note="TSP type-3 3"
FT   REPEAT          551..586
FT                   /note="TSP type-3 4"
FT   REPEAT          587..609
FT                   /note="TSP type-3 5"
FT   REPEAT          610..647
FT                   /note="TSP type-3 6"
FT   REPEAT          648..687
FT                   /note="TSP type-3 7"
FT   REPEAT          688..723
FT                   /note="TSP type-3 8"
FT   DOMAIN          727..941
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT   REGION          518..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..667
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        644
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        937
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        266
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        269
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        278..289
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        283..300
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        303..314
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        320..332
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        326..341
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        344..368
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        374..388
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        382..397
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        400..412
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        418..432
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        426..442
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        444..455
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        471..478
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        483..503
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        519..539
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        542..562
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        578..598
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        601..621
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        639..659
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        679..699
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        715..936
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   VAR_SEQ         96..215
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045328"
FT   VARIANT         279
FT                   /note="S -> G (in dbSNP:rs35154152)"
FT                   /id="VAR_052658"
FT   VARIANT         955
FT                   /note="R -> G (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035808"
SQ   SEQUENCE   956 AA;  104201 MW;  AE9B136DF0FFE5B8 CRC64;
     METQELRGAL ALLLLCFFTS ASQDLQVIDL LTVGESRQMV AVAEKIRTAL LTAGDIYLLS
     TFRLPPKQGG VLFGLYSRQD NTRWLEASVV GKINKVLVRY QREDGKVHAV NLQQAGLADG
     RTHTVLLRLR GPSRPSPALH LYVDCKLGDQ HAGLPALAPI PPAEVDGLEI RTGQKAYLRM
     QGFVESMKII LGGSMARVGA LSECPFQGDE SIHSAVTNAL HSILGEQTKA LVTQLTLFNQ
     ILVELRDDIR DQVKEMSLIR NTIMECQVCG FHEQRSHCSP NPCFRGVDCM EVYEYPGYRC
     GPCPPGLQGN GTHCSDINEC AHADPCFPGS SCINTMPGFH CEACPRGYKG TQVSGVGIDY
     ARASKQVCND IDECNDGNNG GCDPNSICTN TVGSFKCGPC RLGFLGNQSQ GCLPARTCHS
     PAHSPCHIHA HCLFERNGAV SCQCNVGWAG NGNVCGTDTD IDGYPDQALP CMDNNKHCKQ
     DNCLLTPNSG QEDADNDGVG DQCDDDADGD GIKNVEDNCR LFPNKDQQNS DTDSFGDACD
     NCPNVPNNDQ KDTDGNGEGD ACDNDVDGDG IPNGLDNCPK VPNPLQTDRD EDGVGDACDS
     CPEMSNPTQT DADSDLVGDV CDTNEDSDGD GHQDTKDNCP QLPNSSQLDS DNDGLGDECD
     GDDDNDGIPD YVPPGPDNCR LVPNPNQKDS DGNGVGDVCE DDFDNDAVVD PLDVCPESAE
     VTLTDFRAYQ TVVLDPEGDA QIDPNWVVLN QGMEIVQTMN SDPGLAVGYT AFNGVDFEGT
     FHVNTVTDDD YAGFLFSYQD SGRFYVVMWK QTEQTYWQAT PFRAVAQPGL QLKAVTSVSG
     PGEHLRNALW HTGHTPDQVR LLWTDPRNVG WRDKTSYRWQ LLHRPQVGYI RVKLYEGPQL
     VADSGVIIDT SMRGGRLGVF CFSQENIIWS NLQYRCNDTV PEDFEPFRRQ LLQGRV
//