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Database: UniProt
Entry: P05106
LinkDB: P05106
Original site: P05106 
ID   ITB3_HUMAN              Reviewed;         788 AA.
AC   P05106; A0PJW2; D3DXJ8; O15495; Q12806; Q13413; Q14648; Q16499;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   10-APR-2019, entry version 257.
DE   RecName: Full=Integrin beta-3;
DE   AltName: Full=Platelet membrane glycoprotein IIIa;
DE            Short=GPIIIa;
DE   AltName: CD_antigen=CD61;
DE   Flags: Precursor;
GN   Name=ITGB3; Synonyms=GP3A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3A).
RX   PubMed=3494014;
RA   Fitzgerald L.A., Steiner B., Rall S.C. Jr., Lo S., Phillips D.R.;
RT   "Protein sequence of endothelial glycoprotein IIIa derived from a cDNA
RT   clone. Identity with platelet glycoprotein IIIa and similarity to
RT   'integrin'.";
RL   J. Biol. Chem. 262:3936-3939(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3A).
RX   PubMed=2452834; DOI=10.1172/JCI113478;
RA   Zimrin A.B., Eisman R., Vilaire G., Schwartz E., Bennett J.S.,
RA   Poncz M.;
RT   "Structure of platelet glycoprotein IIIa. A common subunit for two
RT   different membrane receptors.";
RL   J. Clin. Invest. 81:1470-1475(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3A).
RX   PubMed=2345548; DOI=10.1007/BF00422712;
RA   Frachet P., Uzan G., Thevenon D., Denarier E., Prandini M.H.,
RA   Marguerie G.;
RT   "GPIIb and GPIIIa amino acid sequences deduced from human
RT   megakaryocyte cDNAs.";
RL   Mol. Biol. Rep. 14:27-33(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3C), FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Osteoclastoma;
RX   PubMed=9195946; DOI=10.1074/jbc.272.26.16390;
RA   Kumar C.S., James I.E., Wong A., Mwangi V., Feild J.A.,
RA   Nuthulaganti P., Connor J.R., Eichman C., Ali F., Hwang S.M.,
RA   Rieman D.J., Drake F.H., Gowen M.;
RT   "Cloning and characterization of a novel integrin beta3 subunit.";
RL   J. Biol. Chem. 272:16390-16397(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-3A).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RC   TISSUE=Blood;
RX   PubMed=8298129;
RA   Villa-Garcia M., Li L., Riely G., Bray P.F.;
RT   "Isolation and characterization of a TATA-less promoter for the human
RT   beta 3 integrin gene.";
RL   Blood 83:668-676(1994).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-788.
RC   TISSUE=Erythroleukemia;
RX   PubMed=3165296;
RA   Rosa J.P., Bray P.F., Gayet O., Johnston G.I., Cook R.G.,
RA   Jackson K.W., Shuman M.A., McEver R.P.;
RT   "Cloning of glycoprotein IIIa cDNA from human erythroleukemia cells
RT   and localization of the gene to chromosome 17.";
RL   Blood 72:593-600(1988).
RN   [9]
RP   PROTEIN SEQUENCE OF 27-37.
RC   TISSUE=Platelet;
RX   PubMed=1953640; DOI=10.1042/bj2790419;
RA   Catimel B., Parmentier S., Leung L.L., McGregor J.L.;
RT   "Separation of important new platelet glycoproteins (GPIa, GPIc,
RT   GPIc*, GPIIa and GMP-140) by F.P.L.C. Characterization by monoclonal
RT   antibodies and gas-phase sequencing.";
RL   Biochem. J. 279:419-425(1991).
RN   [10]
RP   PROTEIN SEQUENCE OF 27-34.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-788.
RX   PubMed=2341395;
RA   Zimrin A.B., Gidwitz S., Lord S., Schwartz E., Bennett J.S.,
RA   White G.C. II, Poncz M.;
RT   "The genomic organization of platelet glycoprotein IIIa.";
RL   J. Biol. Chem. 265:8590-8595(1990).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-788.
RX   PubMed=2145280;
RA   Lanza F., Kieffer N., Phillips D.R., Fitzgerald L.A.;
RT   "Characterization of the human platelet glycoprotein IIIa gene.
RT   Comparison with the fibronectin receptor beta-subunit gene.";
RL   J. Biol. Chem. 265:18098-18103(1990).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-120, AND VARIANTS PRO-59 AND
RP   ARG-66.
RC   TISSUE=Blood;
RA   Pascual C., Balas A., Garcia-Sanchez F., Rodriguez de la Rua A.,
RA   Vicario J.L.;
RT   "A new exon II polymorphism in the platelet glycoprotein IIIa.";
RL   Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-204.
RX   PubMed=1382574; DOI=10.1093/intimm/4.9.1031;
RA   Jiang W.-M., Jenkins D., Yuan Q., Leung E., Choo K.H., Watson J.D.,
RA   Krissansen G.W.;
RT   "The gene organization of the human beta 7 subunit, the common beta
RT   subunit of the leukocyte integrins HML-1 and LPAM-1.";
RL   Int. Immunol. 4:1031-1040(1992).
RN   [15]
RP   PROTEIN SEQUENCE OF 218-234 AND 439-443.
RX   PubMed=3801670;
RA   Hiraiwa A., Matsukage A., Shiku H., Takahashi T., Naito K., Yamada K.;
RT   "Purification and partial amino acid sequence of human platelet
RT   membrane glycoproteins IIb and IIIa.";
RL   Blood 69:560-564(1987).
RN   [16]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 707-788 (ISOFORM BETA-3B).
RC   TISSUE=Placenta;
RX   PubMed=2787511; DOI=10.1073/pnas.86.14.5415;
RA   Van Kuppevelt T.H.M.S.M., Languino L.R., Gailit J.O., Suzuki S.,
RA   Ruoslahti E.;
RT   "An alternative cytoplasmic domain of the integrin beta 3 subunit.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:5415-5418(1989).
RN   [17]
RP   PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RX   PubMed=2001252; DOI=10.1042/bj2740063;
RA   Calvete J.J., Henschen A., Gonzalez-Rodriguez J.;
RT   "Assignment of disulphide bonds in human platelet GPIIIa. A disulphide
RT   pattern for the beta-subunits of the integrin family.";
RL   Biochem. J. 274:63-71(1991).
RN   [18]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS A9
RP   CAPSID PROTEINS.
RX   PubMed=7519807; DOI=10.1006/viro.1994.1494;
RA   Roivainen M., Piirainen L., Hovi T., Virtanen I., Riikonen T.,
RA   Heino J., Hyypiae T.;
RT   "Entry of coxsackievirus A9 into host cells: specific interactions
RT   with alpha v beta 3 integrin, the vitronectin receptor.";
RL   Virology 203:357-365(1994).
RN   [19]
RP   PHOSPHORYLATION AT TYR-773 AND TYR-785 (ISOFORM BETA-3A).
RX   PubMed=8631894; DOI=10.1074/jbc.271.18.10811;
RA   Law D.A., Nannizzi-Alaimo L., Phillips D.R.;
RT   "Outside-in integrin signal transduction. Alpha IIb beta 3-(GP IIb
RT   IIIa) tyrosine phosphorylation induced by platelet aggregation.";
RL   J. Biol. Chem. 271:10811-10815(1996).
RN   [20]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HANTAAN
RP   GLYCOPROTEIN G.
RX   PubMed=9618541; DOI=10.1073/pnas.95.12.7074;
RA   Gavrilovskaya I.N., Shepley M., Shaw R., Ginsberg M.H., Mackow E.R.;
RT   "beta3 Integrins mediate the cellular entry of hantaviruses that cause
RT   respiratory failure.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:7074-7079(1998).
RN   [21]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 TAT.
RX   PubMed=10397733;
RA   Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S.,
RA   Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.;
RT   "The Tat protein of human immunodeficiency virus type-1 promotes
RT   vascular cell growth and locomotion by engaging the alpha5beta1 and
RT   alphavbeta3 integrins and by mobilizing sequestered basic fibroblast
RT   growth factor.";
RL   Blood 94:663-672(1999).
RN   [22]
RP   PHOSPHORYLATION AT THR-779.
RX   PubMed=10896934; DOI=10.1074/jbc.M001908200;
RA   Kirk R.I., Sanderson M.R., Lerea K.M.;
RT   "Threonine phosphorylation of the beta 3 integrin cytoplasmic tail, at
RT   a site recognized by PDK1 and Akt/PKB in vitro, regulates Shc
RT   binding.";
RL   J. Biol. Chem. 275:30901-30906(2000).
RN   [23]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN
RP   PARECHOVIRUS 1 CAPSID PROTEINS.
RX   PubMed=11160695; DOI=10.1128/JVI.75.4.1958-1967.2001;
RA   Joki-Korpela P., Marjomaki V., Krogerus C., Heino J., Hyypia T.;
RT   "Entry of human parechovirus 1.";
RL   J. Virol. 75:1958-1967(2001).
RN   [24]
RP   INTERACTION WITH SYK.
RX   PubMed=11940607; DOI=10.1083/jcb.200112113;
RA   Obergfell A., Eto K., Mocsai A., Buensuceso C., Moores S.L.,
RA   Brugge J.S., Lowell C.A., Shattil S.J.;
RT   "Coordinate interactions of Csk, Src, and Syk kinases with
RT   [alpha]IIb[beta]3 initiate integrin signaling to the cytoskeleton.";
RL   J. Cell Biol. 157:265-275(2002).
RN   [25]
RP   INTERACTION WITH FLNB.
RC   TISSUE=Keratinocyte, and Skeletal muscle;
RX   PubMed=11807098; DOI=10.1083/jcb.200103037;
RA   van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M.,
RA   Takafuta T., Shapiro S.S., Sonnenberg A.;
RT   "Different splice variants of filamin-B affect myogenesis, subcellular
RT   distribution, and determine binding to integrin (beta) subunits.";
RL   J. Cell Biol. 156:361-376(2002).
RN   [26]
RP   INTERACTION WITH CCN3.
RX   PubMed=12695522; DOI=10.1074/jbc.M302028200;
RA   Lin C.G., Leu S.J., Chen N., Tebeau C.M., Lin S.X., Yeung C.Y.,
RA   Lau L.F.;
RT   "CCN3 (NOV) is a novel angiogenic regulator of the CCN protein
RT   family.";
RL   J. Biol. Chem. 278:24200-24208(2003).
RN   [27]
RP   FUNCTION, AND INTERACTION WITH FBN1.
RX   PubMed=12807887; DOI=10.1074/jbc.M303159200;
RA   Bax D.V., Bernard S.E., Lomas A., Morgan A., Humphries J.,
RA   Shuttleworth C.A., Humphries M.J., Kielty C.M.;
RT   "Cell adhesion to fibrillin-1 molecules and microfibrils is mediated
RT   by alpha 5 beta 1 and alpha v beta 3 integrins.";
RL   J. Biol. Chem. 278:34605-34616(2003).
RN   [28]
RP   INTERACTION WITH MYO10.
RX   PubMed=15156152; DOI=10.1038/ncb1136;
RA   Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A.,
RA   Cheney R.E., Stromblad S.;
RT   "Myosin-X provides a motor-based link between integrins and the
RT   cytoskeleton.";
RL   Nat. Cell Biol. 6:523-531(2004).
RN   [29]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH
RP   CYTOMEGALOVIRUS/HHV-5 GH:GL PROTEINS.
RX   PubMed=15834425; DOI=10.1038/nm1236;
RA   Wang X., Huang D.Y., Huong S.M., Huang E.S.;
RT   "Integrin alphavbeta3 is a coreceptor for human cytomegalovirus.";
RL   Nat. Med. 11:515-521(2005).
RN   [30]
RP   INTERACTION WITH PDIA6.
RX   PubMed=15466936; DOI=10.1182/blood-2004-02-0608;
RA   Jordan P.A., Stevens J.M., Hubbard G.P., Barrett N.E., Sage T.,
RA   Authi K.S., Gibbins J.M.;
RT   "A role for the thiol isomerase protein ERP5 in platelet function.";
RL   Blood 105:1500-1507(2005).
RN   [31]
RP   INTERACTION WITH EMP2.
RX   PubMed=16216233; DOI=10.1016/j.ydbio.2005.09.003;
RA   Wadehra M., Forbes A., Pushkarna N., Goodglick L., Gordon L.K.,
RA   Williams C.J., Braun J.;
RT   "Epithelial membrane protein-2 regulates surface expression of
RT   alphavbeta3 integrin in the endometrium.";
RL   Dev. Biol. 287:336-345(2005).
RN   [32]
RP   INTERACTION WITH COMP.
RX   PubMed=16051604; DOI=10.1074/jbc.M504778200;
RA   Chen F.-H., Thomas A.O., Hecht J.T., Goldring M.B., Lawler J.;
RT   "Cartilage oligomeric matrix protein/thrombospondin 5 supports
RT   chondrocyte attachment through interaction with integrins.";
RL   J. Biol. Chem. 280:32655-32661(2005).
RN   [33]
RP   REVIEW.
RX   PubMed=16322781; DOI=10.1172/JCI26989;
RA   Bennett J.S.;
RT   "Structure and function of the platelet integrin alphaIIbbeta3.";
RL   J. Clin. Invest. 115:3363-3369(2005).
RN   [34]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [35]
RP   INTERACTION WITH ADGRA2.
RX   PubMed=16982628; DOI=10.1074/jbc.M605291200;
RA   Vallon M., Essler M.;
RT   "Proteolytically processed soluble tumor endothelial marker (TEM) 5
RT   mediates endothelial cell survival during angiogenesis by linking
RT   integrin alpha(v)beta3 to glycosaminoglycans.";
RL   J. Biol. Chem. 281:34179-34188(2006).
RN   [36]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125.
RC   TISSUE=Platelet;
RX   PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
RA   Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT   "Elucidation of N-glycosylation sites on human platelet proteins: a
RT   glycoproteomic approach.";
RL   Mol. Cell. Proteomics 5:226-233(2006).
RN   [37]
RP   REVIEW.
RX   PubMed=17635696; DOI=10.1111/j.1538-7836.2007.02537.x;
RA   Ma Y.Q., Qin J., Plow E.F.;
RT   "Platelet integrin alpha(IIb)beta(3): activation mechanisms.";
RL   J. Thromb. Haemost. 5:1345-1352(2007).
RN   [38]
RP   FUNCTION, BINDING TO FGF1, AND IDENTIFICATION IN A COMPLEX WITH FGF1
RP   AND FGFR1.
RX   PubMed=18441324; DOI=10.1074/jbc.M801213200;
RA   Mori S., Wu C.Y., Yamaji S., Saegusa J., Shi B., Ma Z., Kuwabara Y.,
RA   Lam K.S., Isseroff R.R., Takada Y.K., Takada Y.;
RT   "Direct binding of integrin alphavbeta3 to FGF1 plays a role in FGF1
RT   signaling.";
RL   J. Biol. Chem. 283:18066-18075(2008).
RN   [39]
RP   FUNCTION.
RX   PubMed=18635536; DOI=10.1074/jbc.M804835200;
RA   Saegusa J., Akakura N., Wu C.Y., Hoogland C., Ma Z., Lam K.S.,
RA   Liu F.T., Takada Y.K., Takada Y.;
RT   "Pro-inflammatory secretory phospholipase A2 type IIA binds to
RT   integrins alphavbeta3 and alpha4beta1 and induces proliferation of
RT   monocytic cells in an integrin-dependent manner.";
RL   J. Biol. Chem. 283:26107-26115(2008).
RN   [40]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-773, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [41]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HHV-8
RP   GLYCOPROTEIN B.
RX   PubMed=18045938; DOI=10.1128/JVI.01673-07;
RA   Garrigues H.J., Rubinchikova Y.E., Dipersio C.M., Rose T.M.;
RT   "Integrin alphaVbeta3 Binds to the RGD motif of glycoprotein B of
RT   Kaposi's sarcoma-associated herpesvirus and functions as an RGD-
RT   dependent entry receptor.";
RL   J. Virol. 82:1570-1580(2008).
RN   [42]
RP   IDENTIFICATION OF ALLOANTIGEN HPA-1A BY MASS SPECTROMETRY, AND
RP   ASSOCIATION TO ALLELE HLA-DRB3*01:01.
RX   PubMed=19494351; DOI=10.1182/blood-2009-04-211839;
RA   Anani Sarab G., Moss M., Barker R.N., Urbaniak S.J.;
RT   "Naturally processed peptides spanning the HPA-1a polymorphism are
RT   efficiently generated and displayed from platelet glycoprotein by HLA-
RT   DRB3*0101-positive antigen-presenting cells.";
RL   Blood 114:1954-1957(2009).
RN   [43]
RP   FUNCTION, BINDING TO IGF1, AND IDENTIFICATION IN A COMPLEX WITH IGF1
RP   AND IGF1R.
RX   PubMed=19578119; DOI=10.1074/jbc.M109.013201;
RA   Saegusa J., Yamaji S., Ieguchi K., Wu C.Y., Lam K.S., Liu F.T.,
RA   Takada Y.K., Takada Y.;
RT   "The direct binding of insulin-like growth factor-1 (IGF-1) to
RT   integrin alphavbeta3 is involved in IGF-1 signaling.";
RL   J. Biol. Chem. 284:24106-24114(2009).
RN   [44]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-680.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [45]
RP   INTERACTION WITH FERMT2, AND SUBCELLULAR LOCATION.
RX   PubMed=20702409; DOI=10.1074/jbc.C110.134247;
RA   Bledzka K., Bialkowska K., Nie H., Qin J., Byzova T., Wu C.,
RA   Plow E.F., Ma Y.Q.;
RT   "Tyrosine phosphorylation of integrin beta3 regulates kindlin-2
RT   binding and integrin activation.";
RL   J. Biol. Chem. 285:30370-30374(2010).
RN   [46]
RP   FUNCTION, BINDING TO NRG1, AND IDENTIFICATION IN A COMPLEX WITH NRG1
RP   AND ERBB3.
RX   PubMed=20682778; DOI=10.1074/jbc.M110.113878;
RA   Ieguchi K., Fujita M., Ma Z., Davari P., Taniguchi Y., Sekiguchi K.,
RA   Wang B., Takada Y.K., Takada Y.;
RT   "Direct binding of the EGF-like domain of neuregulin-1 to integrins
RT   ({alpha}v{beta}3 and {alpha}6{beta}4) is involved in neuregulin-1/ErbB
RT   signaling.";
RL   J. Biol. Chem. 285:31388-31398(2010).
RN   [47]
RP   INTERACTION WITH MXRA8.
RX   PubMed=22492581; DOI=10.1002/jbmr.1632;
RA   Jung Y.K., Han S.W., Kim G.W., Jeong J.H., Kim H.J., Choi J.Y.;
RT   "DICAM inhibits osteoclast differentiation through attenuation of the
RT   integrin alphaVbeta3 pathway.";
RL   J. Bone Miner. Res. 27:2024-2034(2012).
RN   [48]
RP   FUNCTION, BINDING TO CX3CL1, IDENTIFICATION IN A COMPLEX WITH CX3CR1
RP   AND CX3CL1, AND CX3CL1-BINDING REGION.
RX   PubMed=23125415; DOI=10.4049/jimmunol.1200889;
RA   Fujita M., Takada Y.K., Takada Y.;
RT   "Integrins alphavbeta3 and alpha4beta1 act as coreceptors for
RT   fractalkine, and the integrin-binding defective mutant of fractalkine
RT   is an antagonist of CX3CR1.";
RL   J. Immunol. 189:5809-5819(2012).
RN   [49]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH WEST NILE VIRUS
RP   ENVELOPE PROTEIN E.
RX   PubMed=23658209; DOI=10.1099/vir.0.052613-0;
RA   Schmidt K., Keller M., Bader B.L., Korytar T., Finke S., Ziegler U.,
RA   Groschup M.H.;
RT   "Integrins modulate the infection efficiency of West Nile virus into
RT   cells.";
RL   J. Gen. Virol. 94:1723-1733(2013).
RN   [50]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN
RP   METAPNEUMOVIRUS FUSION PROTEIN.
RX   PubMed=24478423; DOI=10.1128/JVI.03491-13;
RA   Wei Y., Zhang Y., Cai H., Mirza A.M., Iorio R.M., Peeples M.E.,
RA   Niewiesk S., Li J.;
RT   "Roles of the putative integrin-binding motif of the human
RT   metapneumovirus fusion (f) protein in cell-cell fusion, viral
RT   infectivity, and pathogenesis.";
RL   J. Virol. 88:4338-4352(2014).
RN   [51]
RP   BINDING TO CX3CL1, AND CX3CL1-BINDING REGION.
RX   PubMed=24789099; DOI=10.1371/journal.pone.0096372;
RA   Fujita M., Takada Y.K., Takada Y.;
RT   "The chemokine fractalkine can activate integrins without CX3CR1
RT   through direct binding to a ligand-binding site distinct from the
RT   classical RGD-binding site.";
RL   PLoS ONE 9:E96372-E96372(2014).
RN   [52]
RP   FUNCTION.
RX   PubMed=25398877; DOI=10.1074/jbc.M114.579946;
RA   Fujita M., Zhu K., Fujita C.K., Zhao M., Lam K.S., Kurth M.J.,
RA   Takada Y.K., Takada Y.;
RT   "Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces
RT   integrin activation through direct binding to a newly identified
RT   binding site (site 2) in integrins alphavbeta3, alpha4beta1, and
RT   alpha5beta1.";
RL   J. Biol. Chem. 290:259-271(2015).
RN   [53]
RP   INTERACTION WITH CD9; CD81 AND CD151.
RX   PubMed=27993971; DOI=10.1042/BCJ20160998;
RA   Yu J., Lee C.Y., Changou C.A., Cedano-Prieto D.M., Takada Y.K.,
RA   Takada Y.;
RT   "The CD9, CD81, and CD151 EC2 domains bind to the classical RGD-
RT   binding site of integrin alphavbeta3.";
RL   Biochem. J. 474:589-596(2017).
RN   [54]
RP   FUNCTION, AND INTERACTION WITH FGF2.
RX   PubMed=28302677; DOI=10.1042/BSR20170173;
RA   Mori S., Hatori N., Kawaguchi N., Hamada Y., Shih T.C., Wu C.Y.,
RA   Lam K.S., Matsuura N., Yamamoto H., Takada Y.K., Takada Y.;
RT   "The integrin-binding defective FGF2 mutants potently suppress FGF2
RT   signalling and angiogenesis.";
RL   Biosci. Rep. 37:0-0(2017).
RN   [55]
RP   FUNCTION, AND INTERACTION WITH IL1B.
RX   PubMed=29030430; DOI=10.1074/jbc.M117.818302;
RA   Takada Y.K., Yu J., Fujita M., Saegusa J., Wu C.Y., Takada Y.;
RT   "Direct binding to integrins and loss of disulfide linkage in
RT   interleukin-1beta (IL-1beta) are involved in the agonistic action of
RT   IL-1beta.";
RL   J. Biol. Chem. 292:20067-20075(2017).
RN   [56]
RP   FUNCTION, AND INTERACTION WITH IGF2.
RX   PubMed=28873464; DOI=10.1371/journal.pone.0184285;
RA   Cedano Prieto D.M., Cheng Y., Chang C.C., Yu J., Takada Y.K.,
RA   Takada Y.;
RT   "Direct integrin binding to insulin-like growth factor-2 through the
RT   C-domain is required for insulin-like growth factor receptor type 1
RT   (IGF1R) signaling.";
RL   PLoS ONE 12:E0184285-E0184285(2017).
RN   [57]
RP   INTERACTION WITH CXCL12.
RX   PubMed=29301984; DOI=10.1042/BCJ20170867;
RA   Fujita M., Davari P., Takada Y.K., Takada Y.;
RT   "Stromal cell-derived factor-1 (CXCL12) activates integrins by direct
RT   binding to an allosteric ligand-binding site (site 2) of integrins
RT   without CXCR4.";
RL   Biochem. J. 475:723-732(2018).
RN   [58]
RP   X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 27-718, AND GLYCOSYLATION AT
RP   ASN-346; ASN-397; ASN-585 AND ASN-680.
RX   PubMed=11546839; DOI=10.1126/science.1064535;
RA   Xiong J.P., Stehle T., Diefenbach B., Zhang R., Dunker R., Scott D.L.,
RA   Joachimiak A., Goodman S.L., Arnaout M.A.;
RT   "Crystal structure of the extracellular segment of integrin alpha
RT   Vbeta3.";
RL   Science 294:339-345(2001).
RN   [59]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 50-61 (ALLOANTIGEN HPA-1A)
RP   IN COMPLEX WITH HLA-DRA/HLA-DRB3 HETERODIMER.
RX   PubMed=17583734; DOI=10.1016/j.jmb.2007.05.025;
RA   Parry C.S., Gorski J., Stern L.J.;
RT   "Crystallographic structure of the human leukocyte antigen DRA,
RT   DRB3*0101: models of a directional alloimmune response and
RT   autoimmunity.";
RL   J. Mol. Biol. 371:435-446(2007).
RN   [60]
RP   REVIEW ON GT VARIANTS.
RX   PubMed=7878622;
RA   Bray P.F.;
RT   "Inherited diseases of platelet glycoproteins: considerations for
RT   rapid molecular characterization.";
RL   Thromb. Haemost. 72:492-502(1994).
RN   [61]
RP   VARIANT HPA-1B PRO-59, AND DESCRIPTION OF ALLOANTIGEN SYSTEM PL(A).
RX   PubMed=2565345; DOI=10.1172/JCI114082;
RA   Newman P.J., Derbes R.S., Aster R.H.;
RT   "The human platelet alloantigens, PlA1 and PlA2, are associated with a
RT   leucine33/proline33 amino acid polymorphism in membrane glycoprotein
RT   IIIa, and are distinguishable by DNA typing.";
RL   J. Clin. Invest. 83:1778-1781(1989).
RN   [62]
RP   VARIANT HPA-4B GLN-169, AND DESCRIPTION OF ALLOANTIGEN SYSTEM PEN.
RX   PubMed=1430225; DOI=10.1172/JCI116084;
RA   Wang R., Furihata K., McFarland J.G., Friedman K., Aster R.H.,
RA   Newman P.J.;
RT   "An amino acid polymorphism within the RGD binding domain of platelet
RT   membrane glycoprotein IIIa is responsible for the formation of the
RT   Pena/Penb alloantigen system.";
RL   J. Clin. Invest. 90:2038-2043(1992).
RN   [63]
RP   VARIANT MO(+) ALA-433.
RX   PubMed=8093349;
RA   Kuijpers R.W.A.M., Simsek S., Faber N.M., Goldschmeding R.,
RA   van Wermerkerken R.K.V., von Dem Borne A.E.G.K.;
RT   "Single point mutation in human glycoprotein IIIa is associated with a
RT   new platelet-specific alloantigen (Mo) involved in neonatal alloimmune
RT   thrombocytopenia.";
RL   Blood 81:70-76(1993).
RN   [64]
RP   VARIANT CA(+)/TU(+) GLN-515, AND DESCRIPTION OF ALLOANTIGEN SYSTEM
RP   CA/TU.
RX   PubMed=7694683;
RA   Wang R., McFarland J.G., Kekomaki R., Newman P.J.;
RT   "Amino acid 489 is encoded by a mutational 'hot spot' on the beta 3
RT   integrin chain: the CA/TU human platelet alloantigen system.";
RL   Blood 82:3386-3391(1993).
RN   [65]
RP   VARIANT SR(A) CYS-662, AND DESCRIPTION OF ALLOANTIGEN SYSTEM SR(A).
RX   PubMed=8132570;
RA   Santoso S., Kalb R., Kroll H., Walka M., Kiefel V.,
RA   Mueller-Eckhardt C., Newman P.J.;
RT   "A point mutation leads to an unpaired cysteine residue and a
RT   molecular weight polymorphism of a functional platelet beta 3 integrin
RT   subunit. The Sra alloantigen system of GPIIIa.";
RL   J. Biol. Chem. 269:8439-8444(1994).
RN   [66]
RP   VARIANT GT TYR-145.
RX   PubMed=2392682; DOI=10.1126/science.2392682;
RA   Loftus J.C., O'Toole T.E., Plow E.F., Glass A., Frelinger A.L. III,
RA   Ginsberg M.H.;
RT   "A beta 3 integrin mutation abolishes ligand binding and alters
RT   divalent cation-dependent conformation.";
RL   Science 249:915-918(1990).
RN   [67]
RP   VARIANT GT GLN-240.
RX   PubMed=1371279;
RA   Bajt M.L., Ginsberg M.H., Frelinger A.L. III, Berndt M.C.,
RA   Loftus J.C.;
RT   "A spontaneous mutation of integrin alpha IIb beta 3 (platelet
RT   glycoprotein IIb-IIIa) helps define a ligand binding site.";
RL   J. Biol. Chem. 267:3789-3794(1992).
RN   [68]
RP   VARIANT GT TRP-240.
RX   PubMed=1602006; DOI=10.1172/JCI115808;
RA   Lanza F., Stierle A., Fournier D., Morales M., Andre G., Nurden A.T.,
RA   Cazenave J.-P.;
RT   "A new variant of Glanzmann's thrombasthenia (Strasbourg I). Platelets
RT   with functionally defective glycoprotein IIb-IIIa complexes and a
RT   glycoprotein IIIa 214Arg-->214Trp mutation.";
RL   J. Clin. Invest. 89:1995-2004(1992).
RN   [69]
RP   VARIANT GT PRO-778.
RX   PubMed=1438206; DOI=10.1073/pnas.89.21.10169;
RA   Chen Y.-P., Djaffar I., Pidard D., Steiner B., Cieutat A.-M.,
RA   Caen J.P., Rosa J.-P.;
RT   "Ser-752-->Pro mutation in the cytoplasmic domain of integrin beta 3
RT   subunit and defective activation of platelet integrin alpha IIb beta 3
RT   (glycoprotein IIb-IIIa) in a variant of Glanzmann thrombasthenia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:10169-10173(1992).
RN   [70]
RP   VARIANT GT TYR-400.
RX   PubMed=8781422;
RA   Grimaldi C.M., Chen F., Scudder L.E., Coller B.S., French D.L.;
RT   "A Cys374Tyr homozygous mutation of platelet glycoprotein IIIa (beta
RT   3) in a Chinese patient with Glanzmann's thrombasthenia.";
RL   Blood 88:1666-1675(1996).
RN   [71]
RP   VARIANT GT TRP-143.
RX   PubMed=9376589;
RA   Basani R.B., Brown D.L., Vilaire G., Bennett J.S., Poncz M.;
RT   "A Leu117-->Trp mutation within the RGD-peptide cross-linking region
RT   of beta3 results in Glanzmann thrombasthenia by preventing alphaIIb
RT   beta3 export to the platelet surface.";
RL   Blood 90:3082-3088(1997).
RN   [72]
RP   VARIANTS GT ASN-145; GLN-242 AND PRO-288.
RX   PubMed=9215749; DOI=10.1006/bcmd.1997.0117;
RA   French D.L., Coller B.S.;
RT   "Hematologically important mutations: Glanzmann thrombasthenia.";
RL   Blood Cells Mol. Dis. 23:39-51(1997).
RN   [73]
RP   VARIANTS GT PRO-306; PHE-586; SER-598 AND SER-605.
RX   PubMed=9790984; DOI=10.1006/bbrc.1998.9526;
RA   Ambo H., Kamata T., Handa M., Taki M., Kuwajima M., Kawai Y., Oda A.,
RA   Murata M., Takada Y., Watanabe K., Ikeda Y.;
RT   "Three novel integrin beta3 subunit missense mutations (H280P, C560F,
RT   and G579S) in thrombasthenia, including one (H280P) prevalent in
RT   Japanese patients.";
RL   Biochem. Biophys. Res. Commun. 251:763-768(1998).
RN   [74]
RP   VARIANT GT LEU-188.
RX   PubMed=9684783;
RA   Jackson D.E., White M.M., Jennings L.K., Newman P.J.;
RT   "A Ser162-->Leu mutation within glycoprotein (GP) IIIa (integrin
RT   beta3) results in an unstable alphaIIbbeta3 complex that retains
RT   partial function in a novel form of type II Glanzmann
RT   thrombasthenia.";
RL   Thromb. Haemost. 80:42-48(1998).
RN   [75]
RP   VARIANT GT ARG-568.
RX   PubMed=10233432; DOI=10.1111/j.1365-2141.1999.01376.x;
RA   Ruan J., Schmugge M., Clemetson K.J., Cazes E., Combrie R., Bourre F.,
RA   Nurden A.T.;
RT   "Homozygous Cys542-->Arg substitution in GPIIIa in a Swiss patient
RT   with type I Glanzmann's thrombasthenia.";
RL   Br. J. Haematol. 105:523-531(1999).
RN   [76]
RP   VARIANTS PRO-59; GLN-169 AND ILE-453.
RX   PubMed=10391209; DOI=10.1038/10290;
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RT   "Characterization of single-nucleotide polymorphisms in coding regions
RT   of human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [77]
RP   ERRATUM.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
RN   [78]
RP   VARIANT GT ARG-586, AND CHARACTERIZATION OF VARIANT GT ARG-586.
RX   PubMed=11588040; DOI=10.1182/blood.V98.8.2432;
RA   Ruiz C., Liu C.-Y., Sun Q.-H., Sigaud-Fiks M., Fressinaud E.,
RA   Muller J.-Y., Nurden P., Nurden A.T., Newman P.J., Valentin N.;
RT   "A point mutation in the cysteine-rich domain of glycoprotein (GP)
RT   IIIa results in the expression of a GPIIb-IIIa (alphaIIbbeta3)
RT   integrin receptor locked in a high-affinity state and a Glanzmann
RT   thrombasthenia-like phenotype.";
RL   Blood 98:2432-2441(2001).
RN   [79]
RP   VARIANT ILE-166, AND CHARACTERIZATION OF VARIANT ILE-166.
RX   PubMed=12036875; DOI=10.1182/blood.V99.12.4449;
RA   Jallu V., Meunier M., Brement M., Kaplan C.;
RT   "A new platelet polymorphism Duv(a+), localized within the RGD binding
RT   domain of glycoprotein IIIa, is associated with neonatal
RT   thrombocytopenia.";
RL   Blood 99:4449-4456(2002).
RN   [80]
RP   VARIANT GT PRO-222.
RX   PubMed=11897046; DOI=10.1080/09537100220122466;
RA   Nurden A.T., Ruan J., Pasquet J.-M., Gauthier B., Combrie R.,
RA   Kunicki T., Nurden P.;
RT   "A novel 196Leu to Pro substitution in the beta3 subunit of the
RT   alphaIIbbeta3 integrin in a patient with a variant form of Glanzmann
RT   thrombasthenia.";
RL   Platelets 13:101-111(2002).
RN   [81]
RP   VARIANTS GT TRP-119; VAL-243 AND ARG-601.
RX   PubMed=12083483;
RA   D'Andrea G., Colaizzo D., Vecchione G., Grandone E., Di Minno G.,
RA   Margaglione M.;
RT   "Glanzmann's thrombasthenia: identification of 19 new mutations in 30
RT   patients.";
RL   Thromb. Haemost. 87:1034-1042(2002).
RN   [82]
RP   VARIANT GT TYR-532.
RX   PubMed=12353082; DOI=10.1267/THRO88030503;
RA   Nair S., Li J., Mitchell W.B., Mohanty D., Coller B.S., French D.L.;
RT   "Two new beta3 integrin mutations in Indian patients with Glanzmann
RT   thrombasthenia: localization of mutations affecting cysteine residues
RT   in integrin beta3.";
RL   Thromb. Haemost. 88:503-509(2002).
RN   [83]
RP   VARIANT GT VAL-150, AND CHARACTERIZATION OF VARIANT GT VAL-150.
RX   PubMed=15583747; DOI=10.1267/THRO04061377;
RA   Gonzalez-Manchon C., Butta N., Larrucea S., Arias-Salgado E.G.,
RA   Alonso S., Lopez A., Parrilla R.;
RT   "A variant thrombasthenic phenotype associated with compound
RT   heterozygosity of integrin beta3-subunit: (Met124Val)beta3 alters the
RT   subunit dimerization rendering a decreased number of constitutive
RT   active alphaIIbbeta3 receptors.";
RL   Thromb. Haemost. 92:1377-1386(2004).
RN   [84]
RP   VARIANTS GT PRO-306 AND ASN-330, AND CHARACTERIZATION OF VARIANT GT
RP   ASN-330.
RX   PubMed=15634267; DOI=10.1111/j.1538-7836.2004.00990.x;
RA   Tanaka S., Hayashi T., Yoshimura K., Nakayama M., Fujita T., Amano T.,
RA   Tani Y.;
RT   "Double heterozygosity for a novel missense mutation of Ile304 to Asn
RT   in addition to the missense mutation His280 to Pro in the integrin
RT   beta3 gene as a cause of the absence of platelet alphaIIbbeta3 in
RT   Glanzmann's thrombasthenia.";
RL   J. Thromb. Haemost. 3:68-73(2005).
RN   [85]
RP   VARIANTS GT CYS-141 AND LEU-321.
RX   PubMed=15748237; DOI=10.1111/j.1538-7836.2005.01159.x;
RA   Nair S., Ghosh K., Shetty S., Mohanty D.;
RT   "Mutations in GPIIIa molecule as a cause for Glanzmann thrombasthenia
RT   in Indian patients.";
RL   J. Thromb. Haemost. 3:482-488(2005).
RN   [86]
RP   VARIANT BDPLT16 HIS-749, AND CHARACTERIZATION OF VARIANT BDPLT16
RP   HIS-749.
RX   PubMed=18065693; DOI=10.1182/blood-2007-09-112615;
RA   Ghevaert C., Salsmann A., Watkins N.A., Schaffner-Reckinger E.,
RA   Rankin A., Garner S.F., Stephens J., Smith G.A., Debili N.,
RA   Vainchenker W., de Groot P.G., Huntington J.A., Laffan M., Kieffer N.,
RA   Ouwehand W.H.;
RT   "A nonsynonymous SNP in the ITGB3 gene disrupts the conserved
RT   membrane-proximal cytoplasmic salt bridge in the alphaIIbbeta3
RT   integrin and cosegregates dominantly with abnormal proplatelet
RT   formation and macrothrombocytopenia.";
RL   Blood 111:3407-3414(2008).
RN   [87]
RP   VARIANTS GT TYR-64; ARG-144; PRO-222; ASP-247 AND MET-279,
RP   CHARACTERIZATION OF VARIANTS TYR-64; PRO-222; ASP-247 AND MET-279, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=20020534; DOI=10.1002/humu.21179;
RA   Jallu V., Dusseaux M., Panzer S., Torchet M.F., Hezard N.,
RA   Goudemand J., de Brevern A.G., Kaplan C.;
RT   "AlphaIIbbeta3 integrin: new allelic variants in Glanzmann
RT   thrombasthenia, effects on ITGA2B and ITGB3 mRNA splicing, expression,
RT   and structure-function.";
RL   Hum. Mutat. 31:237-246(2010).
CC   -!- FUNCTION: Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for
CC       cytotactin, fibronectin, laminin, matrix metalloproteinase-2,
CC       osteopontin, osteomodulin, prothrombin, thrombospondin,
CC       vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3
CC       (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen,
CC       plasminogen, prothrombin, thrombospondin and vitronectin.
CC       Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the
CC       sequence R-G-D in a wide array of ligands. Integrin alpha-
CC       IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in
CC       fibrinogen gamma chain. Following activation integrin alpha-
CC       IIb/beta-3 brings about platelet/platelet interaction through
CC       binding of soluble fibrinogen. This step leads to rapid platelet
CC       aggregation which physically plugs ruptured endothelial surface.
CC       Fibrinogen binding enhances SELP expression in activated platelets
CC       (By similarity). ITGAV:ITGB3 binds to fractalkine (CX3CL1) and
CC       acts as its coreceptor in CX3CR1-dependent fractalkine signaling
CC       (PubMed:23125415, PubMed:24789099). ITGAV:ITGB3 binds to NRG1 (via
CC       EGF domain) and this binding is essential for NRG1-ERBB signaling
CC       (PubMed:20682778). ITGAV:ITGB3 binds to FGF1 and this binding is
CC       essential for FGF1 signaling (PubMed:18441324). ITGAV:ITGB3 binds
CC       to FGF2 and this binding is essential for FGF2 signaling
CC       (PubMed:28302677). ITGAV:ITGB3 binds to IGF1 and this binding is
CC       essential for IGF1 signaling (PubMed:19578119). ITGAV:ITGB3 binds
CC       to IGF2 and this binding is essential for IGF2 signaling
CC       (PubMed:28873464). ITGAV:ITGB3 binds to IL1B and this binding is
CC       essential for IL1B signaling (PubMed:29030430). ITGAV:ITGB3 binds
CC       to PLA2G2A via a site (site 2) which is distinct from the
CC       classical ligand-binding site (site 1) and this induces integrin
CC       conformational changes and enhanced ligand binding to site 1
CC       (PubMed:18635536, PubMed:25398877). ITGAV:ITGB3 acts as a receptor
CC       for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion
CC       to FBN1 (PubMed:12807887). {ECO:0000250|UniProtKB:O54890,
CC       ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:18441324,
CC       ECO:0000269|PubMed:18635536, ECO:0000269|PubMed:19578119,
CC       ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:23125415,
CC       ECO:0000269|PubMed:24789099, ECO:0000269|PubMed:25398877,
CC       ECO:0000269|PubMed:28302677, ECO:0000269|PubMed:28873464,
CC       ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:9195946,
CC       ECO:0000303|PubMed:16322781, ECO:0000303|PubMed:17635696}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a
CC       receptor for Herpes virus 8/HHV-8. {ECO:0000269|PubMed:18045938}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a
CC       receptor for Coxsackievirus A9. {ECO:0000269|PubMed:7519807}.
CC   -!- FUNCTION: (Microbial infection) Acts as a receptor for Hantaan
CC       virus. {ECO:0000269|PubMed:9618541}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a
CC       receptor for Cytomegalovirus/HHV-5. {ECO:0000269|PubMed:15834425}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGA5:ITGB3 acts as a
CC       receptor for Human metapneumovirus. {ECO:0000269|PubMed:24478423}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts aP05556s
CC       a receptor for Human parechovirus 1.
CC       {ECO:0000269|PubMed:11160695}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a
CC       receptor for West nile virus. {ECO:0000269|PubMed:23658209}.
CC   -!- FUNCTION: (Microbial infection) In case of HIV-1 infection, the
CC       interaction with extracellular viral Tat protein seems to enhance
CC       angiogenesis in Kaposi's sarcoma lesions.
CC       {ECO:0000269|PubMed:10397733}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-3
CC       (ITGB3) associates with either alpha-IIb (ITGA2B) or alpha-V
CC       (ITGAV). Isoform Beta-3C interacts with FLNB. Interacts with COMP.
CC       Interacts with PDIA6 following platelet stimulation. Interacts
CC       with SYK; upon activation by ITGB3 promotes platelet adhesion.
CC       Interacts with MYO10. Interacts with DAB2. Interacts with FERMT2.
CC       Interacts with EMP2; regulates the levels of the heterodimer
CC       ITGA5:ITGB3 integrin expression on the plasma membrane
CC       (PubMed:16216233). Integrin ITGAV:ITGB3 interacts with FBLN5 (via
CC       N-terminus) (By similarity). ITGAV:ITGB3 interacts with CCN3
CC       (PubMed:12695522). ITGAV:ITGB3 is found in a ternary complex with
CC       CX3CR1 and CX3CL1 (PubMed:23125415). ITGAV:ITGB3 is found in a
CC       ternary complex with NRG1 and ERBB3 (PubMed:20682778). ITGAV:ITGB3
CC       is found in a ternary complex with FGF1 and FGFR1
CC       (PubMed:18441324). ITGAV:ITGB3 interacts with FGF2; it is likely
CC       that FGF2 can simultaneously bind ITGAV:ITGB3 and FGF receptors
CC       (PubMed:28302677). ITGAV:ITGB3 binds to IL1B (PubMed:29030430).
CC       ITGAV:ITGB3 is found in a ternary complex with IGF1 and IGF1R
CC       (PubMed:19578119). ITGAV:ITGB3 interacts with IGF2
CC       (PubMed:28873464). ITGAV:ITGB3 interacts with FBN1
CC       (PubMed:12807887). ITGAV:ITGB3 interacts with CD9, CD81 and CD151
CC       (via second extracellular domain) (PubMed:27993971). Interacts
CC       (via the allosteric site (site 2)) with CXCL12 in a CXCR4-
CC       independent manner (PubMed:29301984). Interacts with MXRA8/DICAM;
CC       the interaction inhibits ITGAV:ITGB3 heterodimer formation
CC       (PubMed:22492581). {ECO:0000250|UniProtKB:O54890,
CC       ECO:0000269|PubMed:11807098, ECO:0000269|PubMed:11940607,
CC       ECO:0000269|PubMed:12695522, ECO:0000269|PubMed:12807887,
CC       ECO:0000269|PubMed:15156152, ECO:0000269|PubMed:15466936,
CC       ECO:0000269|PubMed:16051604, ECO:0000269|PubMed:16216233,
CC       ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:18441324,
CC       ECO:0000269|PubMed:19578119, ECO:0000269|PubMed:20682778,
CC       ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:22492581,
CC       ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:27993971,
CC       ECO:0000269|PubMed:28302677, ECO:0000269|PubMed:28873464,
CC       ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:29301984}.
CC   -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
CC       herpes virus 8/HHV-8 glycoprotein B.
CC       {ECO:0000269|PubMed:18045938}.
CC   -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
CC       coxsackievirus A9 capsid proteins. {ECO:0000269|PubMed:7519807}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Hantaan virus
CC       glycoprotein G. {ECO:0000269|PubMed:9618541}.
CC   -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
CC       cytomegalovirus/HHV-5 gH:gL proteins.
CC       {ECO:0000269|PubMed:15834425}.
CC   -!- SUBUNIT: (Microbial infection) Integrin ITGA5:ITGB3 interacts with
CC       human metapneumovirus fusion protein.
CC       {ECO:0000269|PubMed:24478423}.
CC   -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
CC       human parechovirus 1 capsid proteins.
CC       {ECO:0000269|PubMed:11160695}.
CC   -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
CC       west nile virus envelope protein E. {ECO:0000269|PubMed:23658209}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat
CC       (PubMed:10397733). ITGAV:ITGB3 interacts with AGRA2
CC       (PubMed:16982628). {ECO:0000269|PubMed:10397733,
CC       ECO:0000269|PubMed:16982628}.
CC   -!- INTERACTION:
CC       Self; NbExp=5; IntAct=EBI-702847, EBI-702847;
CC       P06935:- (xeno); NbExp=4; IntAct=EBI-702847, EBI-981051;
CC       P05094:ACTN1 (xeno); NbExp=2; IntAct=EBI-702847, EBI-5847257;
CC       P78423:CX3CL1; NbExp=7; IntAct=EBI-702847, EBI-15188013;
CC       P21333:FLNA; NbExp=3; IntAct=EBI-702847, EBI-350432;
CC       F5HB81:gB (xeno); NbExp=2; IntAct=EBI-702847, EBI-9027696;
CC       P08514:ITGA2B; NbExp=11; IntAct=EBI-702847, EBI-702693;
CC       P08514-1:ITGA2B; NbExp=4; IntAct=EBI-702847, EBI-15805658;
CC       P06756:ITGAV; NbExp=13; IntAct=EBI-702847, EBI-298282;
CC       P14555:PLA2G2A; NbExp=3; IntAct=EBI-702847, EBI-16414951;
CC       Q62101:Prkd1 (xeno); NbExp=2; IntAct=EBI-702847, EBI-6903636;
CC       P18031:PTPN1; NbExp=4; IntAct=EBI-702847, EBI-968788;
CC       P05480:Src (xeno); NbExp=5; IntAct=EBI-702847, EBI-298680;
CC       P54939:TLN1 (xeno); NbExp=2; IntAct=EBI-702847, EBI-1035421;
CC       Q9Y490:TLN1; NbExp=4; IntAct=EBI-702847, EBI-2462036;
CC       P26039:Tln1 (xeno); NbExp=7; IntAct=EBI-702847, EBI-1039593;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20020534,
CC       ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:9195946}; Single-
CC       pass type I membrane protein {ECO:0000269|PubMed:20020534,
CC       ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:9195946}. Cell
CC       projection, lamellipodium membrane {ECO:0000269|PubMed:20702409}.
CC       Cell junction, focal adhesion {ECO:0000269|PubMed:20702409}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Beta-3A;
CC         IsoId=P05106-1; Sequence=Displayed;
CC       Name=Beta-3B;
CC         IsoId=P05106-2; Sequence=VSP_002745;
CC       Name=Beta-3C;
CC         IsoId=P05106-3; Sequence=VSP_002746;
CC   -!- TISSUE SPECIFICITY: Isoform beta-3A and isoform beta-3C are widely
CC       expressed. Isoform beta-3A is specifically expressed in osteoblast
CC       cells; isoform beta-3C is specifically expressed in prostate and
CC       testis.
CC   -!- PTM: Phosphorylated on tyrosine residues in response to thrombin-
CC       induced platelet aggregation. Probably involved in outside-in
CC       signaling. A peptide (AA 740-762) is capable of binding GRB2 only
CC       when both Tyr-773 and Tyr-785 are phosphorylated. Phosphorylation
CC       of Thr-779 inhibits SHC binding. {ECO:0000269|PubMed:10896934}.
CC   -!- POLYMORPHISM: Position 59 is associated with platelet-specific
CC       alloantigen HPA-1 (ZW or PL(A)). HPA-1A/ZW(A)/PL(A1) has Leu-59
CC       and HPA-1B/ZW(B)/PL(A2) has Pro-59. HPA-1A is involved in fetal-
CC       maternal alloimmune thromobocytopenia (FMAIT) as well as in
CC       neonatal alloimmune thrombocytopenia (NAIT).
CC   -!- POLYMORPHISM: Position 169 is associated with platelet-specific
CC       alloantigen HPA-4 (PEN or YUK). HPA-4A/PEN(A)/YUK(A) has Arg-169
CC       and HPA-4B/PEN(B)/YUK(B) has Gln-169. HPA-4B is involved in
CC       neonatal alloimmune thrombocytopenia (NAIT or NATP).
CC   -!- POLYMORPHISM: Position 433 is associated with platelet-specific
CC       alloantigen MO. MO(-) has Pro-433 and MO(+) has Ala-433. MO(+) is
CC       involved in NAIT.
CC   -!- POLYMORPHISM: Position 515 is associated with platelet-specific
CC       alloantigen CA/TU. CA(-)/TU(-) has Arg-515 and CA(+)/TU(+) has
CC       Gln-515. CA(+) is involved in NAIT.
CC   -!- POLYMORPHISM: Position 662 is associated with platelet-specific
CC       alloantigen SR(A). SR(A)(-) has Arg-662 and SR(A)(+) has Cys-662.
CC   -!- DISEASE: Glanzmann thrombasthenia (GT) [MIM:273800]: A common
CC       inherited disease of platelet aggregation. It is characterized by
CC       mucocutaneous bleeding of mild-to-moderate severity. GT has been
CC       classified clinically into types I and II. In type I, platelets
CC       show absence of the glycoprotein IIb-IIIa complexes at their
CC       surface and lack fibrinogen and clot retraction capability. In
CC       type II, the platelets express the GPIIb-IIIa complex at reduced
CC       levels, have detectable amounts of fibrinogen, and have low or
CC       moderate clot retraction capability. {ECO:0000269|PubMed:10233432,
CC       ECO:0000269|PubMed:11588040, ECO:0000269|PubMed:11897046,
CC       ECO:0000269|PubMed:12083483, ECO:0000269|PubMed:12353082,
CC       ECO:0000269|PubMed:1371279, ECO:0000269|PubMed:1438206,
CC       ECO:0000269|PubMed:15583747, ECO:0000269|PubMed:15634267,
CC       ECO:0000269|PubMed:15748237, ECO:0000269|PubMed:1602006,
CC       ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:2392682,
CC       ECO:0000269|PubMed:8781422, ECO:0000269|PubMed:9215749,
CC       ECO:0000269|PubMed:9376589, ECO:0000269|PubMed:9684783,
CC       ECO:0000269|PubMed:9790984}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Bleeding disorder, platelet-type 16 (BDPLT16)
CC       [MIM:187800]: An autosomal dominant form of congenital
CC       macrothrombocytopenia associated with platelet anisocytosis. It is
CC       a disorder of platelet production. Affected individuals may have
CC       no or only mildly increased bleeding tendency. In vitro studies
CC       show mild platelet functional abnormalities.
CC       {ECO:0000269|PubMed:18065693}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=ITGB3";
DR   EMBL; J02703; AAA52589.1; -; mRNA.
DR   EMBL; M20311; AAA60122.1; -; mRNA.
DR   EMBL; M35999; AAA35927.1; -; mRNA.
DR   EMBL; U95204; AAB71380.1; -; mRNA.
DR   EMBL; CH471231; EAW57682.1; -; Genomic_DNA.
DR   EMBL; BC127666; AAI27667.1; -; mRNA.
DR   EMBL; BC127667; AAI27668.1; -; mRNA.
DR   EMBL; L28832; AAA20880.2; -; Genomic_DNA.
DR   EMBL; M32686; AAA67537.1; -; Genomic_DNA.
DR   EMBL; M32667; AAA67537.1; JOINED; Genomic_DNA.
DR   EMBL; M32672; AAA67537.1; JOINED; Genomic_DNA.
DR   EMBL; M32673; AAA67537.1; JOINED; Genomic_DNA.
DR   EMBL; M32674; AAA67537.1; JOINED; Genomic_DNA.
DR   EMBL; M32675; AAA67537.1; JOINED; Genomic_DNA.
DR   EMBL; M32680; AAA67537.1; JOINED; Genomic_DNA.
DR   EMBL; M32681; AAA67537.1; JOINED; Genomic_DNA.
DR   EMBL; M32682; AAA67537.1; JOINED; Genomic_DNA.
DR   EMBL; M32685; AAA67537.1; JOINED; Genomic_DNA.
DR   EMBL; M57494; AAA52600.1; -; Genomic_DNA.
DR   EMBL; M57481; AAA52600.1; JOINED; Genomic_DNA.
DR   EMBL; M57482; AAA52600.1; JOINED; Genomic_DNA.
DR   EMBL; M57483; AAA52600.1; JOINED; Genomic_DNA.
DR   EMBL; M57484; AAA52600.1; JOINED; Genomic_DNA.
DR   EMBL; M57485; AAA52600.1; JOINED; Genomic_DNA.
DR   EMBL; M57486; AAA52600.1; JOINED; Genomic_DNA.
DR   EMBL; M57487; AAA52600.1; JOINED; Genomic_DNA.
DR   EMBL; M57488; AAA52600.1; JOINED; Genomic_DNA.
DR   EMBL; M57489; AAA52600.1; JOINED; Genomic_DNA.
DR   EMBL; M57490; AAA52600.1; JOINED; Genomic_DNA.
DR   EMBL; M57491; AAA52600.1; JOINED; Genomic_DNA.
DR   EMBL; M57492; AAA52600.1; JOINED; Genomic_DNA.
DR   EMBL; M57493; AAA52600.1; JOINED; Genomic_DNA.
DR   EMBL; U03881; AAA16076.1; -; Genomic_DNA.
DR   EMBL; S49379; AAB23689.2; -; Genomic_DNA.
DR   EMBL; M25108; AAA36121.1; -; mRNA.
DR   CCDS; CCDS11511.1; -. [P05106-1]
DR   PIR; A26547; A26547.
DR   PIR; A60798; A60798.
DR   PIR; B36268; B36268.
DR   PIR; I77349; I77349.
DR   PIR; S14324; S14324.
DR   RefSeq; NP_000203.2; NM_000212.2. [P05106-1]
DR   UniGene; Hs.218040; -.
DR   PDB; 1JV2; X-ray; 3.10 A; B=27-718.
DR   PDB; 1KUP; NMR; -; B=742-766.
DR   PDB; 1KUZ; NMR; -; B=742-766.
DR   PDB; 1L5G; X-ray; 3.20 A; B=27-718.
DR   PDB; 1M1X; X-ray; 3.30 A; B=27-718.
DR   PDB; 1M8O; NMR; -; B=742-788.
DR   PDB; 1MIZ; X-ray; 1.90 A; A=765-769.
DR   PDB; 1MK7; X-ray; 2.20 A; A/C=765-775.
DR   PDB; 1MK9; X-ray; 2.80 A; A/C/E/G=765-776.
DR   PDB; 1RN0; Model; -; B=135-378.
DR   PDB; 1S4X; NMR; -; A=742-788.
DR   PDB; 1TYE; X-ray; 2.90 A; B/D/F=27-466.
DR   PDB; 1U8C; X-ray; 3.10 A; B=27-718.
DR   PDB; 2INI; Model; -; B=81-460, B=558-716.
DR   PDB; 2K9J; NMR; -; B=711-753.
DR   PDB; 2KNC; NMR; -; B=715-788.
DR   PDB; 2KV9; NMR; -; B=739-788.
DR   PDB; 2L1C; NMR; -; B=762-788.
DR   PDB; 2L91; NMR; -; A=711-753.
DR   PDB; 2LJD; NMR; -; A=742-788.
DR   PDB; 2LJE; NMR; -; A=742-788.
DR   PDB; 2LJF; NMR; -; A=742-788.
DR   PDB; 2MTP; NMR; -; C=742-788.
DR   PDB; 2N9Y; NMR; -; B=712-753.
DR   PDB; 2Q6W; X-ray; 2.25 A; C/F=50-61.
DR   PDB; 2RMZ; NMR; -; A=711-753.
DR   PDB; 2RN0; NMR; -; A=711-753.
DR   PDB; 2VC2; X-ray; 3.10 A; B=27-487.
DR   PDB; 2VDK; X-ray; 2.80 A; B=27-487.
DR   PDB; 2VDL; X-ray; 2.75 A; B=27-487.
DR   PDB; 2VDM; X-ray; 2.90 A; B=27-487.
DR   PDB; 2VDN; X-ray; 2.90 A; B=27-487.
DR   PDB; 2VDO; X-ray; 2.51 A; B=27-487.
DR   PDB; 2VDP; X-ray; 2.80 A; B=27-487.
DR   PDB; 2VDQ; X-ray; 2.59 A; B=27-487.
DR   PDB; 2VDR; X-ray; 2.40 A; B=27-487.
DR   PDB; 3FCS; X-ray; 2.55 A; B/D=27-716.
DR   PDB; 3FCU; X-ray; 2.90 A; B/D/F=27-487.
DR   PDB; 3IJE; X-ray; 2.90 A; B=27-721.
DR   PDB; 3NID; X-ray; 2.30 A; B/D=27-497.
DR   PDB; 3NIF; X-ray; 2.40 A; B/D=27-497.
DR   PDB; 3NIG; X-ray; 2.25 A; B/D=27-497.
DR   PDB; 3T3M; X-ray; 2.60 A; B/D=27-498.
DR   PDB; 3T3P; X-ray; 2.20 A; B/D=27-498.
DR   PDB; 3ZDX; X-ray; 2.45 A; B/D=27-498.
DR   PDB; 3ZDY; X-ray; 2.45 A; B/D=27-498.
DR   PDB; 3ZDZ; X-ray; 2.75 A; B/D=27-498.
DR   PDB; 3ZE0; X-ray; 2.95 A; B/D=27-498.
DR   PDB; 3ZE1; X-ray; 3.00 A; B/D=27-498.
DR   PDB; 3ZE2; X-ray; 2.35 A; B/D=27-498.
DR   PDB; 4CAK; EM; 20.50 A; B=27-716.
DR   PDB; 4G1E; X-ray; 3.00 A; B=27-717.
DR   PDB; 4G1M; X-ray; 2.90 A; B=27-718.
DR   PDB; 4MMX; X-ray; 3.32 A; B=27-718.
DR   PDB; 4MMY; X-ray; 3.18 A; B=27-718.
DR   PDB; 4MMZ; X-ray; 3.10 A; B=27-718.
DR   PDB; 4O02; X-ray; 3.60 A; B=27-718.
DR   PDB; 4Z7N; X-ray; 2.60 A; B/D=29-497.
DR   PDB; 4Z7O; X-ray; 2.85 A; B/D=29-497.
DR   PDB; 4Z7Q; X-ray; 2.70 A; B/D=27-497.
DR   PDB; 5HDB; X-ray; 2.70 A; B/D=27-497.
DR   PDB; 6AVQ; EM; 35.00 A; B=27-718.
DR   PDB; 6AVR; EM; 35.00 A; B=27-718.
DR   PDB; 6AVU; EM; 35.00 A; B=27-718.
DR   PDB; 6BXB; X-ray; 2.39 A; A/B=27-135, A/B=378-548.
DR   PDB; 6BXF; X-ray; 3.20 A; A/B=27-135, A/B=378-548.
DR   PDB; 6BXJ; X-ray; 2.09 A; A=27-135, A=378-714.
DR   PDB; 6CKB; X-ray; 2.80 A; A/B=27-135, A/B=378-548.
DR   PDBsum; 1JV2; -.
DR   PDBsum; 1KUP; -.
DR   PDBsum; 1KUZ; -.
DR   PDBsum; 1L5G; -.
DR   PDBsum; 1M1X; -.
DR   PDBsum; 1M8O; -.
DR   PDBsum; 1MIZ; -.
DR   PDBsum; 1MK7; -.
DR   PDBsum; 1MK9; -.
DR   PDBsum; 1RN0; -.
DR   PDBsum; 1S4X; -.
DR   PDBsum; 1TYE; -.
DR   PDBsum; 1U8C; -.
DR   PDBsum; 2INI; -.
DR   PDBsum; 2K9J; -.
DR   PDBsum; 2KNC; -.
DR   PDBsum; 2KV9; -.
DR   PDBsum; 2L1C; -.
DR   PDBsum; 2L91; -.
DR   PDBsum; 2LJD; -.
DR   PDBsum; 2LJE; -.
DR   PDBsum; 2LJF; -.
DR   PDBsum; 2MTP; -.
DR   PDBsum; 2N9Y; -.
DR   PDBsum; 2Q6W; -.
DR   PDBsum; 2RMZ; -.
DR   PDBsum; 2RN0; -.
DR   PDBsum; 2VC2; -.
DR   PDBsum; 2VDK; -.
DR   PDBsum; 2VDL; -.
DR   PDBsum; 2VDM; -.
DR   PDBsum; 2VDN; -.
DR   PDBsum; 2VDO; -.
DR   PDBsum; 2VDP; -.
DR   PDBsum; 2VDQ; -.
DR   PDBsum; 2VDR; -.
DR   PDBsum; 3FCS; -.
DR   PDBsum; 3FCU; -.
DR   PDBsum; 3IJE; -.
DR   PDBsum; 3NID; -.
DR   PDBsum; 3NIF; -.
DR   PDBsum; 3NIG; -.
DR   PDBsum; 3T3M; -.
DR   PDBsum; 3T3P; -.
DR   PDBsum; 3ZDX; -.
DR   PDBsum; 3ZDY; -.
DR   PDBsum; 3ZDZ; -.
DR   PDBsum; 3ZE0; -.
DR   PDBsum; 3ZE1; -.
DR   PDBsum; 3ZE2; -.
DR   PDBsum; 4CAK; -.
DR   PDBsum; 4G1E; -.
DR   PDBsum; 4G1M; -.
DR   PDBsum; 4MMX; -.
DR   PDBsum; 4MMY; -.
DR   PDBsum; 4MMZ; -.
DR   PDBsum; 4O02; -.
DR   PDBsum; 4Z7N; -.
DR   PDBsum; 4Z7O; -.
DR   PDBsum; 4Z7Q; -.
DR   PDBsum; 5HDB; -.
DR   PDBsum; 6AVQ; -.
DR   PDBsum; 6AVR; -.
DR   PDBsum; 6AVU; -.
DR   PDBsum; 6BXB; -.
DR   PDBsum; 6BXF; -.
DR   PDBsum; 6BXJ; -.
DR   PDBsum; 6CKB; -.
DR   ProteinModelPortal; P05106; -.
DR   SMR; P05106; -.
DR   BioGrid; 109896; 41.
DR   ComplexPortal; CPX-1795; Integrin alphav-beta3 complex.
DR   ComplexPortal; CPX-1799; Integrin alphaIIb-beta3 complex.
DR   CORUM; P05106; -.
DR   DIP; DIP-304N; -.
DR   ELM; P05106; -.
DR   IntAct; P05106; 29.
DR   MINT; P05106; -.
DR   STRING; 9606.ENSP00000452786; -.
DR   BindingDB; P05106; -.
DR   ChEMBL; CHEMBL3883284; -.
DR   DrugBank; DB00054; Abciximab.
DR   DrugBank; DB00098; Anti-thymocyte Globulin (Rabbit).
DR   DrugBank; DB00063; Eptifibatide.
DR   DrugBank; DB04863; Lefradafiban.
DR   DrugBank; DB05787; LM-609.
DR   DrugBank; DB00775; Tirofiban.
DR   GuidetoPHARMACOLOGY; 2457; -.
DR   GlyConnect; 1416; -.
DR   iPTMnet; P05106; -.
DR   PhosphoSitePlus; P05106; -.
DR   BioMuta; ITGB3; -.
DR   DMDM; 125987835; -.
DR   EPD; P05106; -.
DR   jPOST; P05106; -.
DR   MaxQB; P05106; -.
DR   PaxDb; P05106; -.
DR   PeptideAtlas; P05106; -.
DR   PRIDE; P05106; -.
DR   ProteomicsDB; 51790; -.
DR   ProteomicsDB; 51791; -. [P05106-2]
DR   ProteomicsDB; 51792; -. [P05106-3]
DR   Ensembl; ENST00000559488; ENSP00000452786; ENSG00000259207. [P05106-1]
DR   GeneID; 3690; -.
DR   KEGG; hsa:3690; -.
DR   UCSC; uc002ilj.4; human. [P05106-1]
DR   CTD; 3690; -.
DR   DisGeNET; 3690; -.
DR   EuPathDB; HostDB:ENSG00000259207.7; -.
DR   GeneCards; ITGB3; -.
DR   HGNC; HGNC:6156; ITGB3.
DR   HPA; HPA027852; -.
DR   MalaCards; ITGB3; -.
DR   MIM; 173470; gene+phenotype.
DR   MIM; 187800; phenotype.
DR   MIM; 273800; phenotype.
DR   neXtProt; NX_P05106; -.
DR   OpenTargets; ENSG00000259207; -.
DR   Orphanet; 140957; Autosomal dominant macrothrombocytopenia.
DR   Orphanet; 853; Fetal and neonatal alloimmune thrombocytopenia.
DR   Orphanet; 849; Glanzmann thrombasthenia.
DR   PharmGKB; PA205; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P05106; -.
DR   KO; K06493; -.
DR   OMA; PRCNLKE; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; P05106; -.
DR   TreeFam; TF105392; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   Reactome; R-HSA-1566948; Elastic fibre formation.
DR   Reactome; R-HSA-210990; PECAM1 interactions.
DR   Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-3000170; Syndecan interactions.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   Reactome; R-HSA-354192; Integrin alphaIIb beta3 signaling.
DR   Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR   Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
DR   Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-HSA-445144; Signal transduction by L1.
DR   Reactome; R-HSA-5674135; MAP2K and MAPK activation.
DR   Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
DR   Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
DR   Reactome; R-HSA-6802949; Signaling by RAS mutants.
DR   Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
DR   Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR   SignaLink; P05106; -.
DR   SIGNOR; P05106; -.
DR   ChiTaRS; ITGB3; human.
DR   EvolutionaryTrace; P05106; -.
DR   GeneWiki; CD61; -.
DR   GenomeRNAi; 3690; -.
DR   PMAP-CutDB; P05106; -.
DR   PRO; PR:P05106; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000259207; Expressed in 157 organ(s), highest expression level in left coronary artery.
DR   ExpressionAtlas; P05106; baseline and differential.
DR   Genevisible; P05106; HS.
DR   GO; GO:0035868; C:alphav-beta3 integrin-HMGB1 complex; IDA:BHF-UCL.
DR   GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; IDA:UniProtKB.
DR   GO; GO:0035866; C:alphav-beta3 integrin-PKCalpha complex; IDA:BHF-UCL.
DR   GO; GO:0071062; C:alphav-beta3 integrin-vitronectin complex; TAS:BHF-UCL.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0034683; C:integrin alphav-beta3 complex; IDA:UniProtKB.
DR   GO; GO:0008305; C:integrin complex; IDA:BHF-UCL.
DR   GO; GO:0031258; C:lamellipodium membrane; IDA:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR   GO; GO:0031528; C:microvillus membrane; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR   GO; GO:0015026; F:coreceptor activity; TAS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0050840; F:extracellular matrix binding; IDA:UniProtKB.
DR   GO; GO:0001968; F:fibronectin binding; IMP:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005178; F:integrin binding; IPI:BHF-UCL.
DR   GO; GO:0005161; F:platelet-derived growth factor receptor binding; TAS:BHF-UCL.
DR   GO; GO:0002020; F:protease binding; IDA:UniProtKB.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IDA:UniProtKB.
DR   GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IPI:BHF-UCL.
DR   GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0032147; P:activation of protein kinase activity; IMP:BHF-UCL.
DR   GO; GO:0060055; P:angiogenesis involved in wound healing; TAS:BHF-UCL.
DR   GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0043277; P:apoptotic cell clearance; IGI:BHF-UCL.
DR   GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR   GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; HDA:UniProtKB.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB.
DR   GO; GO:0050919; P:negative chemotaxis; IMP:UniProtKB.
DR   GO; GO:0010888; P:negative regulation of lipid storage; IMP:BHF-UCL.
DR   GO; GO:0032369; P:negative regulation of lipid transport; IMP:BHF-UCL.
DR   GO; GO:0050748; P:negative regulation of lipoprotein metabolic process; IMP:BHF-UCL.
DR   GO; GO:0045715; P:negative regulation of low-density lipoprotein particle receptor biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0030168; P:platelet activation; IMP:UniProtKB.
DR   GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
DR   GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:BHF-UCL.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; TAS:BHF-UCL.
DR   GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; TAS:BHF-UCL.
DR   GO; GO:0045124; P:regulation of bone resorption; TAS:BHF-UCL.
DR   GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR   GO; GO:0014909; P:smooth muscle cell migration; IMP:BHF-UCL.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR   GO; GO:0035295; P:tube development; TAS:BHF-UCL.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0046718; P:viral entry into host cell; IMP:UniProtKB.
DR   GO; GO:0042060; P:wound healing; IC:BHF-UCL.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR040622; I-EGF_1.
DR   InterPro; IPR027068; Integrin_beta-3.
DR   InterPro; IPR033760; Integrin_beta_N.
DR   InterPro; IPR015812; Integrin_bsu.
DR   InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR   InterPro; IPR012896; Integrin_bsu_tail.
DR   InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR   InterPro; IPR002369; Integrin_bsu_VWA.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; PTHR10082; 1.
DR   PANTHER; PTHR10082:SF25; PTHR10082:SF25; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF18372; I-EGF_1; 1.
DR   Pfam; PF08725; Integrin_b_cyt; 1.
DR   Pfam; PF07965; Integrin_B_tail; 1.
DR   Pfam; PF00362; Integrin_beta; 1.
DR   Pfam; PF17205; PSI_integrin; 1.
DR   PIRSF; PIRSF002512; Integrin_B; 1.
DR   PRINTS; PR01186; INTEGRINB.
DR   SMART; SM00187; INB; 1.
DR   SMART; SM01241; Integrin_b_cyt; 1.
DR   SMART; SM01242; Integrin_B_tail; 1.
DR   SMART; SM00423; PSI; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF69179; SSF69179; 1.
DR   SUPFAM; SSF69687; SSF69687; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS00243; INTEGRIN_BETA; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW   Cell membrane; Cell projection; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   Glycoprotein; Host cell receptor for virus entry;
KW   Host-virus interaction; Integrin; Membrane; Phosphoprotein;
KW   Polymorphism; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27    788       Integrin beta-3.
FT                                /FTId=PRO_0000016344.
FT   TOPO_DOM     27    718       Extracellular. {ECO:0000255}.
FT   TRANSMEM    719    741       Helical. {ECO:0000255}.
FT   TOPO_DOM    742    788       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      135    377       VWFA.
FT   REPEAT      463    511       I.
FT   REPEAT      512    553       II.
FT   REPEAT      554    592       III.
FT   REPEAT      593    629       IV.
FT   REGION      203    210       Involved in CX3CL1-, NRG1-, FGF1- and
FT                                IGF1-binding.
FT                                {ECO:0000269|PubMed:18441324,
FT                                ECO:0000269|PubMed:19578119,
FT                                ECO:0000269|PubMed:20682778,
FT                                ECO:0000269|PubMed:23125415}.
FT   REGION      293    313       CX3CL1-binding.
FT                                {ECO:0000269|PubMed:24789099}.
FT   REGION      463    629       Cysteine-rich tandem repeats.
FT   MOD_RES     767    767       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O54890}.
FT   MOD_RES     773    773       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:18088087}.
FT   MOD_RES     779    779       Phosphothreonine; by PDPK1 and PKB/AKT1;
FT                                in vitro. {ECO:0000269|PubMed:10896934}.
FT   MOD_RES     785    785       Phosphotyrosine.
FT                                {ECO:0000269|PubMed:8631894}.
FT   CARBOHYD    125    125       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16263699,
FT                                ECO:0000269|PubMed:16335952}.
FT   CARBOHYD    346    346       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255,
FT                                ECO:0000269|PubMed:11546839}.
FT   CARBOHYD    397    397       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255,
FT                                ECO:0000269|PubMed:11546839}.
FT   CARBOHYD    478    478       N-linked (GlcNAc...) asparagine.
FT   CARBOHYD    585    585       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255,
FT                                ECO:0000269|PubMed:11546839}.
FT   CARBOHYD    680    680       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:11546839,
FT                                ECO:0000269|PubMed:19159218}.
FT   DISULFID     31    461       {ECO:0000269|PubMed:2001252}.
FT   DISULFID     39     49       {ECO:0000269|PubMed:2001252}.
FT   DISULFID     42     75       {ECO:0000269|PubMed:2001252}.
FT   DISULFID     52     64       {ECO:0000269|PubMed:2001252}.
FT   DISULFID    203    210       {ECO:0000269|PubMed:2001252}.
FT   DISULFID    258    299       {ECO:0000269|PubMed:2001252}.
FT   DISULFID    400    412       {ECO:0000269|PubMed:2001252}.
FT   DISULFID    432    681       {ECO:0000269|PubMed:2001252}.
FT   DISULFID    459    463       {ECO:0000269|PubMed:2001252}.
FT   DISULFID    474    486       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    483    521       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    488    497       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    499    512       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    527    532       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    529    562       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    534    547       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    549    554       {ECO:0000269|PubMed:2001252}.
FT   DISULFID    568    573       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    570    601       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    575    584       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    586    593       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    607    612       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    609    657       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    614    624       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    627    630       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    634    643       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    640    713       {ECO:0000305|PubMed:2001252}.
FT   DISULFID    661    689       {ECO:0000269|PubMed:2001252}.
FT   VAR_SEQ     768    788       ANNPLYKEATSTFTNITYRGT -> VRDGAGRFLKSLV
FT                                (in isoform Beta-3B).
FT                                {ECO:0000303|PubMed:2787511}.
FT                                /FTId=VSP_002745.
FT   VAR_SEQ     768    788       ANNPLYKEATSTFTNITYRGT -> HYAQSLRKWNQPVSID
FT                                G (in isoform Beta-3C).
FT                                {ECO:0000303|PubMed:9195946}.
FT                                /FTId=VSP_002746.
FT   VARIANT      59     59       L -> P (in alloantigen HPA-1B;
FT                                dbSNP:rs5918).
FT                                {ECO:0000269|PubMed:10391209,
FT                                ECO:0000269|PubMed:2565345,
FT                                ECO:0000269|Ref.13}.
FT                                /FTId=VAR_003993.
FT   VARIANT      64     64       C -> Y (in GT; severe type 1 phenotype;
FT                                the mutation prevents normal ITGA2B/ITGB3
FT                                complex expression; dbSNP:rs74554539).
FT                                {ECO:0000269|PubMed:20020534}.
FT                                /FTId=VAR_069920.
FT   VARIANT      66     66       L -> R (in dbSNP:rs36080296).
FT                                {ECO:0000269|Ref.13}.
FT                                /FTId=VAR_049633.
FT   VARIANT     119    119       R -> W (in GT; dbSNP:rs781062792).
FT                                {ECO:0000269|PubMed:12083483}.
FT                                /FTId=VAR_030473.
FT   VARIANT     141    141       Y -> C (in GT).
FT                                {ECO:0000269|PubMed:15748237}.
FT                                /FTId=VAR_030474.
FT   VARIANT     143    143       L -> W (in GT; dbSNP:rs121918452).
FT                                {ECO:0000269|PubMed:9376589}.
FT                                /FTId=VAR_010649.
FT   VARIANT     144    144       M -> R (in GT; severe type 1 phenotype;
FT                                the mutation prevented normal ITGA2B/
FT                                ITGB3 complex expression on the cell
FT                                surface; dbSNP:rs77963874).
FT                                {ECO:0000269|PubMed:20020534}.
FT                                /FTId=VAR_069921.
FT   VARIANT     145    145       D -> N (in GT).
FT                                {ECO:0000269|PubMed:9215749}.
FT                                /FTId=VAR_030475.
FT   VARIANT     145    145       D -> Y (in GT; type B;
FT                                dbSNP:rs121918445).
FT                                {ECO:0000269|PubMed:2392682}.
FT                                /FTId=VAR_003998.
FT   VARIANT     150    150       M -> V (in GT; may confer constitutive
FT                                activity to the alpha-IIb/(mutated)beta-3
FT                                receptor; dbSNP:rs767548512).
FT                                {ECO:0000269|PubMed:15583747}.
FT                                /FTId=VAR_030476.
FT   VARIANT     166    166       T -> I (associated with neonatal
FT                                thrombocytopenia; alloantigen Duv(a+);
FT                                does not affect significantly the
FT                                integrin function; dbSNP:rs74708909).
FT                                {ECO:0000269|PubMed:12036875}.
FT                                /FTId=VAR_030477.
FT   VARIANT     169    169       R -> Q (in alloantigen HPA-4B;
FT                                dbSNP:rs5917).
FT                                {ECO:0000269|PubMed:10391209,
FT                                ECO:0000269|PubMed:1430225}.
FT                                /FTId=VAR_003994.
FT   VARIANT     188    188       S -> L (in GT; type II;
FT                                dbSNP:rs143146734).
FT                                {ECO:0000269|PubMed:9684783}.
FT                                /FTId=VAR_010651.
FT   VARIANT     222    222       L -> P (in GT; variant form;
FT                                dbSNP:rs79208797).
FT                                {ECO:0000269|PubMed:11897046,
FT                                ECO:0000269|PubMed:20020534}.
FT                                /FTId=VAR_030478.
FT   VARIANT     240    240       R -> Q (in GT; type B;
FT                                dbSNP:rs121918444).
FT                                {ECO:0000269|PubMed:1371279}.
FT                                /FTId=VAR_003999.
FT   VARIANT     240    240       R -> W (in GT; variant Strasbourg-1;
FT                                dbSNP:rs121918446).
FT                                {ECO:0000269|PubMed:1602006}.
FT                                /FTId=VAR_004000.
FT   VARIANT     242    242       R -> Q (in GT; dbSNP:rs377162158).
FT                                {ECO:0000269|PubMed:9215749}.
FT                                /FTId=VAR_030479.
FT   VARIANT     243    243       D -> V (in GT).
FT                                {ECO:0000269|PubMed:12083483}.
FT                                /FTId=VAR_030480.
FT   VARIANT     247    247       G -> D (in GT; severe type 1 phenotype;
FT                                the mutation prevents normal ITGA2B/ITGB3
FT                                complex expression on the cell surface;
FT                                the mutation may interfere with correct
FT                                folding of the protein;
FT                                dbSNP:rs79560904).
FT                                {ECO:0000269|PubMed:20020534}.
FT                                /FTId=VAR_069922.
FT   VARIANT     279    279       K -> M (in GT; severe type 1 phenotype;
FT                                the mutation prevents normal ITGA2B/ITGB3
FT                                complex expression on the cell surface;
FT                                the mutation interupts the interaction of
FT                                the ITGA2B/ITGB3 complex;
FT                                dbSNP:rs79775494).
FT                                {ECO:0000269|PubMed:20020534}.
FT                                /FTId=VAR_069923.
FT   VARIANT     288    288       L -> P (in GT).
FT                                {ECO:0000269|PubMed:9215749}.
FT                                /FTId=VAR_030481.
FT   VARIANT     306    306       H -> P (in GT; dbSNP:rs13306476).
FT                                {ECO:0000269|PubMed:15634267,
FT                                ECO:0000269|PubMed:9790984}.
FT                                /FTId=VAR_004001.
FT   VARIANT     321    321       M -> L (in GT).
FT                                {ECO:0000269|PubMed:15748237}.
FT                                /FTId=VAR_030482.
FT   VARIANT     330    330       I -> N (in GT; not expressed on the
FT                                surface and absent inside the transfected
FT                                cells). {ECO:0000269|PubMed:15634267}.
FT                                /FTId=VAR_030483.
FT   VARIANT     400    400       C -> Y (in GT; dbSNP:rs121918449).
FT                                {ECO:0000269|PubMed:8781422}.
FT                                /FTId=VAR_004002.
FT   VARIANT     433    433       P -> A (in alloantigen MO(+); in a case
FT                                of neonatal alloimmune thrombocytopenia;
FT                                dbSNP:rs121918448).
FT                                {ECO:0000269|PubMed:8093349}.
FT                                /FTId=VAR_003995.
FT   VARIANT     453    453       V -> I (in dbSNP:rs5921).
FT                                {ECO:0000269|PubMed:10391209}.
FT                                /FTId=VAR_014178.
FT   VARIANT     515    515       R -> Q (in alloantigen CA(+)/TU(+);
FT                                dbSNP:rs13306487).
FT                                {ECO:0000269|PubMed:7694683}.
FT                                /FTId=VAR_003996.
FT   VARIANT     532    532       C -> Y (in GT).
FT                                {ECO:0000269|PubMed:12353082}.
FT                                /FTId=VAR_030484.
FT   VARIANT     568    568       C -> R (in GT; type I).
FT                                {ECO:0000269|PubMed:10233432}.
FT                                /FTId=VAR_010671.
FT   VARIANT     586    586       C -> F (in GT).
FT                                {ECO:0000269|PubMed:9790984}.
FT                                /FTId=VAR_004003.
FT   VARIANT     586    586       C -> R (in GT; gain-of-function mutation;
FT                                constitutively binds ligand-induced
FT                                binding sites antibodies and the
FT                                fibrinogen-mimetic antibody PAC-1).
FT                                {ECO:0000269|PubMed:11588040}.
FT                                /FTId=VAR_030485.
FT   VARIANT     598    598       G -> S (in GT).
FT                                {ECO:0000269|PubMed:9790984}.
FT                                /FTId=VAR_004004.
FT   VARIANT     601    601       C -> R (in GT; dbSNP:rs747534508).
FT                                {ECO:0000269|PubMed:12083483}.
FT                                /FTId=VAR_030486.
FT   VARIANT     605    605       G -> S (in GT; type II;
FT                                dbSNP:rs144884023).
FT                                {ECO:0000269|PubMed:9790984}.
FT                                /FTId=VAR_010672.
FT   VARIANT     662    662       R -> C (in alloantigen SR(A);
FT                                dbSNP:rs151219882).
FT                                {ECO:0000269|PubMed:8132570}.
FT                                /FTId=VAR_003997.
FT   VARIANT     749    749       D -> H (in BDPLT16; the mutant protein is
FT                                constitutively active;
FT                                dbSNP:rs398122372).
FT                                {ECO:0000269|PubMed:18065693}.
FT                                /FTId=VAR_069924.
FT   VARIANT     778    778       S -> P (in GT; variant Strasbourg-1;
FT                                dbSNP:rs121918447).
FT                                {ECO:0000269|PubMed:1438206}.
FT                                /FTId=VAR_004005.
FT   CONFLICT     12     12       A -> V (in Ref. 1; AAA52589 and 3;
FT                                AAA35927). {ECO:0000305}.
FT   CONFLICT    151    151       K -> P (in Ref. 11; AAA67537 and 14;
FT                                AAB23689). {ECO:0000305}.
FT   CONFLICT    205    205       D -> EY (in Ref. 11; AAA67537).
FT                                {ECO:0000305}.
FT   CONFLICT    649    653       GALHD -> EPYMT (in Ref. 1; AAA52589, 2;
FT                                AAA60122 and 4; AAB71380). {ECO:0000305}.
FT   CONFLICT    716    716       G -> H (in Ref. 8). {ECO:0000305}.
FT   CONFLICT    737    741       ALLIW -> PCSSG (in Ref. 11; AAA67537).
FT                                {ECO:0000305}.
FT   TURN         30     34       {ECO:0000244|PDB:6BXJ}.
FT   HELIX        35     37       {ECO:0000244|PDB:4MMX}.
FT   HELIX        39     45       {ECO:0000244|PDB:6BXJ}.
FT   STRAND       50     52       {ECO:0000244|PDB:3T3P}.
FT   STRAND       55     57       {ECO:0000244|PDB:6BXB}.
FT   STRAND       59     61       {ECO:0000244|PDB:2VDO}.
FT   STRAND       63     65       {ECO:0000244|PDB:6BXJ}.
FT   HELIX        67     72       {ECO:0000244|PDB:6BXJ}.
FT   TURN         77     79       {ECO:0000244|PDB:6BXJ}.
FT   STRAND       86     91       {ECO:0000244|PDB:6BXJ}.
FT   STRAND       99    101       {ECO:0000244|PDB:3T3P}.
FT   HELIX       103    105       {ECO:0000244|PDB:3ZE2}.
FT   STRAND      109    111       {ECO:0000244|PDB:3NID}.
FT   STRAND      113    118       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      123    131       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      138    145       {ECO:0000244|PDB:3T3P}.
FT   HELIX       148    150       {ECO:0000244|PDB:3T3P}.
FT   HELIX       151    156       {ECO:0000244|PDB:3T3P}.
FT   TURN        157    159       {ECO:0000244|PDB:3T3P}.
FT   HELIX       160    168       {ECO:0000244|PDB:3T3P}.
FT   TURN        169    171       {ECO:0000244|PDB:3T3P}.
FT   STRAND      175    182       {ECO:0000244|PDB:3T3P}.
FT   TURN        188    190       {ECO:0000244|PDB:3T3P}.
FT   HELIX       196    200       {ECO:0000244|PDB:3T3P}.
FT   TURN        202    207       {ECO:0000244|PDB:3T3P}.
FT   STRAND      215    224       {ECO:0000244|PDB:3T3P}.
FT   HELIX       226    235       {ECO:0000244|PDB:3T3P}.
FT   STRAND      242    246       {ECO:0000244|PDB:3T3P}.
FT   HELIX       248    257       {ECO:0000244|PDB:3T3P}.
FT   HELIX       259    262       {ECO:0000244|PDB:3T3P}.
FT   STRAND      266    278       {ECO:0000244|PDB:3T3P}.
FT   HELIX       285    289       {ECO:0000244|PDB:3T3P}.
FT   STRAND      305    307       {ECO:0000244|PDB:5HDB}.
FT   TURN        308    312       {ECO:0000244|PDB:3T3P}.
FT   HELIX       318    327       {ECO:0000244|PDB:3T3P}.
FT   STRAND      331    336       {ECO:0000244|PDB:3T3P}.
FT   HELIX       338    340       {ECO:0000244|PDB:3T3P}.
FT   HELIX       341    349       {ECO:0000244|PDB:3T3P}.
FT   STRAND      355    358       {ECO:0000244|PDB:3T3P}.
FT   TURN        361    363       {ECO:0000244|PDB:3ZE2}.
FT   HELIX       366    377       {ECO:0000244|PDB:3T3P}.
FT   STRAND      381    387       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      392    399       {ECO:0000244|PDB:6BXJ}.
FT   TURN        401    403       {ECO:0000244|PDB:3T3P}.
FT   STRAND      405    407       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      410    414       {ECO:0000244|PDB:6BXB}.
FT   STRAND      420    429       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      438    444       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      451    457       {ECO:0000244|PDB:6BXJ}.
FT   HELIX       462    466       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      468    470       {ECO:0000244|PDB:6BXJ}.
FT   TURN        472    474       {ECO:0000244|PDB:3ZE2}.
FT   TURN        475    477       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      479    482       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      485    487       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      489    491       {ECO:0000244|PDB:3IJE}.
FT   TURN        494    498       {ECO:0000244|PDB:6BXB}.
FT   STRAND      500    504       {ECO:0000244|PDB:3IJE}.
FT   HELIX       509    511       {ECO:0000244|PDB:6BXB}.
FT   STRAND      512    518       {ECO:0000244|PDB:6BXJ}.
FT   HELIX       520    523       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      524    528       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      531    534       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      538    540       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      542    544       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      549    552       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      556    561       {ECO:0000244|PDB:3FCS}.
FT   HELIX       562    564       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      565    569       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      572    575       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      579    581       {ECO:0000244|PDB:6BXJ}.
FT   HELIX       591    593       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      598    600       {ECO:0000244|PDB:6BXJ}.
FT   HELIX       601    603       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      604    608       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      611    614       {ECO:0000244|PDB:6BXJ}.
FT   TURN        616    618       {ECO:0000244|PDB:3IJE}.
FT   STRAND      620    624       {ECO:0000244|PDB:1U8C}.
FT   STRAND      628    630       {ECO:0000244|PDB:4G1E}.
FT   HELIX       633    645       {ECO:0000244|PDB:6BXJ}.
FT   HELIX       650    653       {ECO:0000244|PDB:6BXJ}.
FT   HELIX       657    660       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      663    670       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      676    684       {ECO:0000244|PDB:6BXJ}.
FT   TURN        686    688       {ECO:0000244|PDB:1M1X}.
FT   STRAND      690    697       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      698    700       {ECO:0000244|PDB:3FCS}.
FT   STRAND      703    710       {ECO:0000244|PDB:6BXJ}.
FT   STRAND      715    717       {ECO:0000244|PDB:2KNC}.
FT   TURN        743    759       {ECO:0000244|PDB:1KUP}.
FT   TURN        761    765       {ECO:0000244|PDB:1KUP}.
FT   STRAND      767    770       {ECO:0000244|PDB:1S4X}.
FT   HELIX       771    774       {ECO:0000244|PDB:1MK7}.
FT   HELIX       776    779       {ECO:0000244|PDB:2LJD}.
FT   TURN        782    786       {ECO:0000244|PDB:1S4X}.
SQ   SEQUENCE   788 AA;  87058 MW;  F246623608E05F9E CRC64;
     MRARPRPRPL WATVLALGAL AGVGVGGPNI CTTRGVSSCQ QCLAVSPMCA WCSDEALPLG
     SPRCDLKENL LKDNCAPESI EFPVSEARVL EDRPLSDKGS GDSSQVTQVS PQRIALRLRP
     DDSKNFSIQV RQVEDYPVDI YYLMDLSYSM KDDLWSIQNL GTKLATQMRK LTSNLRIGFG
     AFVDKPVSPY MYISPPEALE NPCYDMKTTC LPMFGYKHVL TLTDQVTRFN EEVKKQSVSR
     NRDAPEGGFD AIMQATVCDE KIGWRNDASH LLVFTTDAKT HIALDGRLAG IVQPNDGQCH
     VGSDNHYSAS TTMDYPSLGL MTEKLSQKNI NLIFAVTENV VNLYQNYSEL IPGTTVGVLS
     MDSSNVLQLI VDAYGKIRSK VELEVRDLPE ELSLSFNATC LNNEVIPGLK SCMGLKIGDT
     VSFSIEAKVR GCPQEKEKSF TIKPVGFKDS LIVQVTFDCD CACQAQAEPN SHRCNNGNGT
     FECGVCRCGP GWLGSQCECS EEDYRPSQQD ECSPREGQPV CSQRGECLCG QCVCHSSDFG
     KITGKYCECD DFSCVRYKGE MCSGHGQCSC GDCLCDSDWT GYYCNCTTRT DTCMSSNGLL
     CSGRGKCECG SCVCIQPGSY GDTCEKCPTC PDACTFKKEC VECKKFDRGA LHDENTCNRY
     CRDEIESVKE LKDTGKDAVN CTYKNEDDCV VRFQYYEDSS GKSILYVVEE PECPKGPDIL
     VVLLSVMGAI LLIGLAALLI WKLLITIHDR KEFAKFEEER ARAKWDTANN PLYKEATSTF
     TNITYRGT
//
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