ITB3_HUMAN
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 03-AUG-2022, entry version 278.
DE RecName: Full=Integrin beta-3 {ECO:0000305};
DE AltName: Full=Platelet membrane glycoprotein IIIa {ECO:0000305};
DE Short=GPIIIa {ECO:0000305};
DE AltName: CD_antigen=CD61;
DE Flags: Precursor;
GN Name=ITGB3 {ECO:0000312|HGNC:HGNC:6156}; Synonyms=GP3A;
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 BETA-3A).
RX PubMed=3494014; DOI=10.1016/s0021-9258(18)61290-6;
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., 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., Marguerie G.;
RT "GPIIb and GPIIIa amino acid sequences deduced from human megakaryocyte
RT cDNAs.";
RL Mol. Biol. Rep. 14:27-33(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3C), FUNCTION, AND SUBCELLULAR
RP 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., Nuthulaganti P.,
RA Connor J.R., Eichman C., Ali F., Hwang S.M., Rieman D.J., Drake F.H.,
RA 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., 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 [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 project:
RT 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 beta
RT 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., Jackson K.W.,
RA Shuman M.A., McEver R.P.;
RT "Cloning of glycoprotein IIIa cDNA from human erythroleukemia cells and
RT 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, GPIc*,
RT GPIIa and GMP-140) by F.P.L.C. Characterization by monoclonal antibodies
RT 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., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT 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; DOI=10.1016/s0021-9258(19)38928-8;
RA Zimrin A.B., Gidwitz S., Lord S., Schwartz E., Bennett J.S., White G.C. II,
RA 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; DOI=10.1016/s0021-9258(17)44722-3;
RA Lanza F., Kieffer N., Phillips D.R., Fitzgerald L.A.;
RT "Characterization of the human platelet glycoprotein IIIa gene. Comparison
RT 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 subunit
RT 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 membrane
RT 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., Heino J.,
RA Hyypiae T.;
RT "Entry of coxsackievirus A9 into host cells: specific interactions with
RT 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 IIIa)
RT tyrosine phosphorylation induced by platelet aggregation.";
RL J. Biol. Chem. 271:10811-10815(1996).
RN [20]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HANTAAN GLYCOPROTEIN
RP 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 vascular
RT cell growth and locomotion by engaging the alpha5beta1 and alphavbeta3
RT integrins and by mobilizing sequestered basic fibroblast 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 a
RT site recognized by PDK1 and Akt/PKB in vitro, regulates Shc binding.";
RL J. Biol. Chem. 275:30901-30906(2000).
RN [23]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN PARECHOVIRUS 1
RP 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., Brugge J.S.,
RA 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., Takafuta T.,
RA 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., Lau L.F.;
RT "CCN3 (NOV) is a novel angiogenic regulator of the CCN protein 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 by
RT 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 CYTOMEGALOVIRUS/HHV-5
RP 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., Authi K.S.,
RA 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 alphavbeta3
RT 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 chondrocyte
RT 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., Moore R.J.,
RA 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 integrin
RT 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 AND
RP 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., Liu F.T.,
RA Takada Y.K., Takada Y.;
RT "Pro-inflammatory secretory phospholipase A2 type IIA binds to integrins
RT alphavbeta3 and alpha4beta1 and induces proliferation of monocytic cells in
RT an integrin-dependent manner.";
RL J. Biol. Chem. 283:26107-26115(2008).
RN [40]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-773, AND IDENTIFICATION BY
RP 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 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 Kaposi's
RT sarcoma-associated herpesvirus and functions as an RGD-dependent entry
RT receptor.";
RL J. Virol. 82:1570-1580(2008).
RN [42]
RP IDENTIFICATION OF ALLOANTIGEN HPA-1A BY MASS SPECTROMETRY, AND ASSOCIATION
RP 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 INTERACTION WITH PTN, AND PHOSPHORYLATION AT TYR-773.
RX PubMed=19141530; DOI=10.1096/fj.08-117564;
RA Mikelis C., Sfaelou E., Koutsioumpa M., Kieffer N., Papadimitriou E.;
RT "Integrin alpha(v)beta(3) is a pleiotrophin receptor required for
RT pleiotrophin-induced endothelial cell migration through receptor protein
RT tyrosine phosphatase beta/zeta.";
RL FASEB J. 23:1459-1469(2009).
RN [44]
RP FUNCTION, BINDING TO IGF1, AND IDENTIFICATION IN A COMPLEX WITH IGF1 AND
RP 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 integrin
RT alphavbeta3 is involved in IGF-1 signaling.";
RL J. Biol. Chem. 284:24106-24114(2009).
RN [45]
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 multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [46]
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., Plow E.F.,
RA Ma Y.Q.;
RT "Tyrosine phosphorylation of integrin beta3 regulates kindlin-2 binding and
RT integrin activation.";
RL J. Biol. Chem. 285:30370-30374(2010).
RN [47]
RP FUNCTION, BINDING TO NRG1, AND IDENTIFICATION IN A COMPLEX WITH NRG1 AND
RP 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 [48]
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 [49]
RP FUNCTION, BINDING TO CX3CL1, IDENTIFICATION IN A COMPLEX WITH CX3CR1 AND
RP 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 fractalkine,
RT and the integrin-binding defective mutant of fractalkine is an antagonist
RT of CX3CR1.";
RL J. Immunol. 189:5809-5819(2012).
RN [50]
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 [51]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN METAPNEUMOVIRUS
RP 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 metapneumovirus
RT fusion (f) protein in cell-cell fusion, viral infectivity, and
RT pathogenesis.";
RL J. Virol. 88:4338-4352(2014).
RN [52]
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 through
RT direct binding to a ligand-binding site distinct from the classical RGD-
RT binding site.";
RL PLoS ONE 9:E96372-E96372(2014).
RN [53]
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., Takada Y.K.,
RA Takada Y.;
RT "Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces
RT integrin activation through direct binding to a newly identified binding
RT site (site 2) in integrins alphavbeta3, alpha4beta1, and alpha5beta1.";
RL J. Biol. Chem. 290:259-271(2015).
RN [54]
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., Takada Y.;
RT "The CD9, CD81, and CD151 EC2 domains bind to the classical RGD-binding
RT site of integrin alphavbeta3.";
RL Biochem. J. 474:589-596(2017).
RN [55]
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., Lam K.S.,
RA 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 [56]
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 interleukin-
RT 1beta (IL-1beta) are involved in the agonistic action of IL-1beta.";
RL J. Biol. Chem. 292:20067-20075(2017).
RN [57]
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., Takada Y.;
RT "Direct integrin binding to insulin-like growth factor-2 through the C-
RT domain is required for insulin-like growth factor receptor type 1 (IGF1R)
RT signaling.";
RL PLoS ONE 12:E0184285-E0184285(2017).
RN [58]
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 without
RT CXCR4.";
RL Biochem. J. 475:723-732(2018).
RN [59]
RP FUNCTION.
RX PubMed=31331973; DOI=10.4049/jimmunol.1801630;
RA Takada Y.K., Yu J., Shimoda M., Takada Y.;
RT "Integrin Binding to the Trimeric Interface of CD40L Plays a Critical Role
RT in CD40/CD40L Signaling.";
RL J. Immunol. 203:1383-1391(2019).
RN [60]
RP MOTIF.
RX PubMed=33436497; DOI=10.1126/scisignal.abd0334;
RA Meszaros B., Samano-Sanchez H., Alvarado-Valverde J., Calyseva J.,
RA Martinez-Perez E., Alves R., Shields D.C., Kumar M., Rippmann F.,
RA Chemes L.B., Gibson T.J.;
RT "Short linear motif candidates in the cell entry system used by SARS-CoV-2
RT and their potential therapeutic implications.";
RL Sci. Signal. 14:0-0(2021).
RN [61]
RP MOTIF.
RX PubMed=33436498; DOI=10.1126/scisignal.abf1117;
RA Kliche J., Kuss H., Ali M., Ivarsson Y.;
RT "Cytoplasmic short linear motifs in ACE2 and integrin beta3 link SARS-CoV-2
RT host cell receptors to mediators of endocytosis and autophagy.";
RL Sci. Signal. 14:0-0(2021).
RN [62]
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 Vbeta3.";
RL Science 294:339-345(2001).
RN [63]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 50-61 (ALLOANTIGEN HPA-1A) IN
RP 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, DRB3*0101:
RT models of a directional alloimmune response and autoimmunity.";
RL J. Mol. Biol. 371:435-446(2007).
RN [64]
RP REVIEW ON GT2 VARIANTS.
RX PubMed=7878622;
RA Bray P.F.;
RT "Inherited diseases of platelet glycoproteins: considerations for rapid
RT molecular characterization.";
RL Thromb. Haemost. 72:492-502(1994).
RN [65]
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 IIIa,
RT and are distinguishable by DNA typing.";
RL J. Clin. Invest. 83:1778-1781(1989).
RN [66]
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., 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 [67]
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 new
RT platelet-specific alloantigen (Mo) involved in neonatal alloimmune
RT thrombocytopenia.";
RL Blood 81:70-76(1993).
RN [68]
RP VARIANT CA(+)/TU(+) GLN-515, AND DESCRIPTION OF ALLOANTIGEN SYSTEM 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 [69]
RP VARIANT SR(A) CYS-662, AND DESCRIPTION OF ALLOANTIGEN SYSTEM SR(A).
RX PubMed=8132570; DOI=10.1016/s0021-9258(17)37213-7;
RA Santoso S., Kalb R., Kroll H., Walka M., Kiefel V., Mueller-Eckhardt C.,
RA Newman P.J.;
RT "A point mutation leads to an unpaired cysteine residue and a molecular
RT weight polymorphism of a functional platelet beta 3 integrin subunit. The
RT Sra alloantigen system of GPIIIa.";
RL J. Biol. Chem. 269:8439-8444(1994).
RN [70]
RP VARIANT GT2 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 divalent
RT cation-dependent conformation.";
RL Science 249:915-918(1990).
RN [71]
RP VARIANT GT2 GLN-240.
RX PubMed=1371279; DOI=10.1016/s0021-9258(19)50595-6;
RA Bajt M.L., Ginsberg M.H., Frelinger A.L. III, Berndt M.C., Loftus J.C.;
RT "A spontaneous mutation of integrin alpha IIb beta 3 (platelet glycoprotein
RT IIb-IIIa) helps define a ligand binding site.";
RL J. Biol. Chem. 267:3789-3794(1992).
RN [72]
RP VARIANT GT2 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 with
RT functionally defective glycoprotein IIb-IIIa complexes and a glycoprotein
RT IIIa 214Arg-->214Trp mutation.";
RL J. Clin. Invest. 89:1995-2004(1992).
RN [73]
RP VARIANT GT2 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., Caen J.P.,
RA 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 [74]
RP VARIANT GT2 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 3) in
RT a Chinese patient with Glanzmann's thrombasthenia.";
RL Blood 88:1666-1675(1996).
RN [75]
RP VARIANT GT2 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 of
RT beta3 results in Glanzmann thrombasthenia by preventing alphaIIb beta3
RT export to the platelet surface.";
RL Blood 90:3082-3088(1997).
RN [76]
RP VARIANTS GT2 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 [77]
RP VARIANTS GT2 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, and
RT G579S) in thrombasthenia, including one (H280P) prevalent in Japanese
RT patients.";
RL Biochem. Biophys. Res. Commun. 251:763-768(1998).
RN [78]
RP VARIANT GT2 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 beta3)
RT results in an unstable alphaIIbbeta3 complex that retains partial function
RT in a novel form of type II Glanzmann thrombasthenia.";
RL Thromb. Haemost. 80:42-48(1998).
RN [79]
RP VARIANT GT2 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 with
RT type I Glanzmann's thrombasthenia.";
RL Br. J. Haematol. 105:523-531(1999).
RN [80]
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 of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [81]
RP ERRATUM OF PUBMED:10391209.
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 [82]
RP VARIANT GT2 ARG-586, AND CHARACTERIZATION OF VARIANT GT2 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., Muller J.-Y.,
RA Nurden P., Nurden A.T., Newman P.J., Valentin N.;
RT "A point mutation in the cysteine-rich domain of glycoprotein (GP) IIIa
RT results in the expression of a GPIIb-IIIa (alphaIIbbeta3) integrin receptor
RT locked in a high-affinity state and a Glanzmann thrombasthenia-like
RT phenotype.";
RL Blood 98:2432-2441(2001).
RN [83]
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 [84]
RP VARIANT GT2 PRO-222.
RX PubMed=11897046; DOI=10.1080/09537100220122466;
RA Nurden A.T., Ruan J., Pasquet J.-M., Gauthier B., Combrie R., Kunicki T.,
RA 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 [85]
RP VARIANTS GT2 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 [86]
RP VARIANT GT2 TYR-532.
RX PubMed=12353082; DOI=10.1055/s-0037-1613244;
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 in
RT integrin beta3.";
RL Thromb. Haemost. 88:503-509(2002).
RN [87]
RP VARIANT GT2 VAL-150, AND CHARACTERIZATION OF VARIANT GT2 VAL-150.
RX PubMed=15583747; DOI=10.1160/th04-06-0380;
RA Gonzalez-Manchon C., Butta N., Larrucea S., Arias-Salgado E.G., Alonso S.,
RA Lopez A., Parrilla R.;
RT "A variant thrombasthenic phenotype associated with compound heterozygosity
RT of integrin beta3-subunit: (Met124Val)beta3 alters the subunit dimerization
RT rendering a decreased number of constitutive active alphaIIbbeta3
RT receptors.";
RL Thromb. Haemost. 92:1377-1386(2004).
RN [88]
RP VARIANTS GT2 PRO-306 AND ASN-330, AND CHARACTERIZATION OF VARIANT GT2
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 in
RT addition to the missense mutation His280 to Pro in the integrin beta3 gene
RT as a cause of the absence of platelet alphaIIbbeta3 in Glanzmann's
RT thrombasthenia.";
RL J. Thromb. Haemost. 3:68-73(2005).
RN [89]
RP VARIANTS GT2 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 in
RT Indian patients.";
RL J. Thromb. Haemost. 3:482-488(2005).
RN [90]
RP VARIANT BDPLT24 HIS-749, AND CHARACTERIZATION OF VARIANT BDPLT24 HIS-749.
RX PubMed=18065693; DOI=10.1182/blood-2007-09-112615;
RA Ghevaert C., Salsmann A., Watkins N.A., Schaffner-Reckinger E., Rankin A.,
RA Garner S.F., Stephens J., Smith G.A., Debili N., Vainchenker W.,
RA de Groot P.G., Huntington J.A., Laffan M., Kieffer N., Ouwehand W.H.;
RT "A nonsynonymous SNP in the ITGB3 gene disrupts the conserved membrane-
RT proximal cytoplasmic salt bridge in the alphaIIbbeta3 integrin and
RT cosegregates dominantly with abnormal proplatelet formation and
RT macrothrombocytopenia.";
RL Blood 111:3407-3414(2008).
RN [91]
RP VARIANTS GT2 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., Goudemand J.,
RA de Brevern A.G., Kaplan C.;
RT "AlphaIIbbeta3 integrin: new allelic variants in Glanzmann thrombasthenia,
RT effects on ITGA2B and ITGB3 mRNA splicing, expression, and structure-
RT function.";
RL Hum. Mutat. 31:237-246(2010).
RN [92]
RP VARIANT GT2 GLN-240, AND VARIANT PRO-59.
RX PubMed=29084015; DOI=10.1097/mbc.0000000000000673;
RA Kazemi A., Abolghasemi H., Kazemzadeh S., Vahidi R., Faranoush M.,
RA Farsinejad A., Ala F.;
RT "Molecular characterization of Glanzmann's thrombasthenia in Iran:
RT identification of three novel mutations.";
RL Blood Coagul. Fibrinolysis 28:681-686(2017).
RN [93]
RP VARIANT BDPLT24 THR-746 DEL, AND CHARACTERIZATION OF VARIANTS BDPLT24
RP THR-746 DEL AND HIS-749.
RX PubMed=29380037; DOI=10.1007/s00277-017-3214-4;
RA Miyashita N., Onozawa M., Hayasaka K., Yamada T., Migita O., Hata K.,
RA Okada K., Goto H., Nakagawa M., Hashimoto D., Kahata K., Kondo T.,
RA Kunishima S., Teshima T.;
RT "A novel heterozygous ITGB3 p.T720del inducing spontaneous activation of
RT integrin alphaIIbbeta3 in autosomal dominant macrothrombocytopenia with
RT aggregation dysfunction.";
RL Ann. Hematol. 97:629-640(2018).
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, vitronectin and
CC von Willebrand factor. Integrin alpha-IIb/beta-3 (ITGA2B:ITGB3) is a
CC receptor for fibronectin, fibrinogen, plasminogen, prothrombin,
CC thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-
CC V/beta-3 recognize the sequence R-G-D in a wide array of ligands.
CC Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-
CC G-D-V in fibrinogen gamma chain. Following activation integrin alpha-
CC IIb/beta-3 brings about platelet/platelet interaction through binding
CC of soluble fibrinogen. This step leads to rapid platelet aggregation
CC which physically plugs ruptured endothelial surface. Fibrinogen binding
CC enhances SELP expression in activated platelets (By similarity).
CC ITGAV:ITGB3 binds to fractalkine (CX3CL1) and acts as its coreceptor in
CC CX3CR1-dependent fractalkine signaling (PubMed:23125415,
CC PubMed:24789099). ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this
CC binding is essential for NRG1-ERBB signaling (PubMed:20682778).
CC ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1
CC signaling (PubMed:18441324). ITGAV:ITGB3 binds to FGF2 and this binding
CC is essential for FGF2 signaling (PubMed:28302677). ITGAV:ITGB3 binds to
CC IGF1 and this binding is essential for IGF1 signaling
CC (PubMed:19578119). ITGAV:ITGB3 binds to IGF2 and this binding is
CC essential for IGF2 signaling (PubMed:28873464). ITGAV:ITGB3 binds to
CC IL1B and this binding is essential for IL1B signaling
CC (PubMed:29030430). ITGAV:ITGB3 binds to PLA2G2A via a site (site 2)
CC which is distinct from the classical ligand-binding site (site 1) and
CC this induces integrin conformational changes and enhanced ligand
CC binding to site 1 (PubMed:18635536, PubMed:25398877). ITGAV:ITGB3 acts
CC as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell
CC adhesion to FBN1 (PubMed:12807887). In brain, plays a role in synaptic
CC transmission and plasticity. Involved in the regulation of the
CC serotonin neurotransmission, is required to localize to specific
CC compartments within the synapse the serotonin receptor SLC6A4 and for
CC an appropriate reuptake of serotonin. Controls excitatory synaptic
CC strength by regulating GRIA2-containing AMPAR endocytosis, which
CC affects AMPAR abundance and composition (By similarity). ITGAV:ITGB3
CC act as a receptor for CD40LG (PubMed:31331973).
CC {ECO:0000250|UniProtKB:O54890, ECO:0000269|PubMed:12807887,
CC ECO:0000269|PubMed:18441324, ECO:0000269|PubMed:18635536,
CC ECO:0000269|PubMed:19578119, ECO:0000269|PubMed:20682778,
CC ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:24789099,
CC ECO:0000269|PubMed:25398877, ECO:0000269|PubMed:28302677,
CC ECO:0000269|PubMed:28873464, ECO:0000269|PubMed:29030430,
CC ECO:0000269|PubMed:31331973, ECO:0000269|PubMed:9195946,
CC ECO:0000303|PubMed:16322781, ECO:0000303|PubMed:17635696}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor
CC for Herpes virus 8/HHV-8. {ECO:0000269|PubMed:18045938}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor
CC for Coxsackievirus A9. {ECO:0000269|PubMed:7519807}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Hantaan virus.
CC {ECO:0000269|PubMed:9618541}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor
CC for Cytomegalovirus/HHV-5. {ECO:0000269|PubMed:15834425}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGA5:ITGB3 acts as a receptor
CC for Human metapneumovirus. {ECO:0000269|PubMed:24478423}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts aP05556s a
CC receptor for Human parechovirus 1. {ECO:0000269|PubMed:11160695}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor
CC 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 (ITGB3)
CC associates with either alpha-IIb (ITGA2B) or alpha-V (ITGAV). Isoform
CC Beta-3C interacts with FLNB. Interacts with COMP. Interacts with PDIA6
CC following platelet stimulation. Interacts with SYK; upon activation by
CC ITGB3 promotes platelet adhesion. Interacts with MYO10. Interacts with
CC DAB2. Interacts with FERMT2. Interacts with EMP2; regulates the levels
CC of the heterodimer ITGA5:ITGB3 integrin expression on the plasma
CC membrane (PubMed:16216233). Integrin ITGAV:ITGB3 interacts with FBLN5
CC (via 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 ternary
CC complex with NRG1 and ERBB3 (PubMed:20682778). ITGAV:ITGB3 is found in
CC a ternary complex with FGF1 and FGFR1 (PubMed:18441324). ITGAV:ITGB3
CC interacts with FGF2; it is likely that FGF2 can simultaneously bind
CC ITGAV:ITGB3 and FGF receptors (PubMed:28302677). ITGAV:ITGB3 binds to
CC IL1B (PubMed:29030430). ITGAV:ITGB3 is found in a ternary complex with
CC IGF1 and IGF1R (PubMed:19578119). ITGAV:ITGB3 interacts with IGF2
CC (PubMed:28873464). ITGAV:ITGB3 interacts with FBN1 (PubMed:12807887).
CC ITGAV:ITGB3 interacts with CD9, CD81 and CD151 (via second
CC extracellular domain) (PubMed:27993971). Interacts (via the allosteric
CC site (site 2)) with CXCL12 in a CXCR4-independent manner
CC (PubMed:29301984). Interacts with MXRA8/DICAM; the interaction inhibits
CC ITGAV:ITGB3 heterodimer formation (PubMed:22492581). ITGAV:ITGB3
CC interacts with PTN (PubMed:19141530). Forms a complex with PTPRZ1 and
CC PTN that stimulates endothelial cell migration through ITGB3 Tyr-773
CC phosphorylation (PubMed:19141530). ITGAV:ITGB3 interacts with SLC6A4
CC (By similarity). ITGA2B:ITGB3 interacts with PPIA/CYPA; the interaction
CC is ROS and PPIase activity-dependent and is increased in the presence
CC of thrombin (By similarity). {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:19141530, ECO:0000269|PubMed:19578119,
CC ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:20702409,
CC ECO:0000269|PubMed:22492581, ECO:0000269|PubMed:23125415,
CC ECO:0000269|PubMed:27993971, ECO:0000269|PubMed:28302677,
CC ECO:0000269|PubMed:28873464, ECO:0000269|PubMed:29030430,
CC ECO:0000269|PubMed:29301984}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
CC herpes virus 8/HHV-8 glycoprotein B. {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. {ECO:0000269|PubMed:15834425}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGA5:ITGB3 interacts with
CC human metapneumovirus fusion protein. {ECO:0000269|PubMed:24478423}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
CC human parechovirus 1 capsid proteins. {ECO:0000269|PubMed:11160695}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with west
CC 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 (PubMed:16982628).
CC {ECO:0000269|PubMed:10397733, ECO:0000269|PubMed:16982628}.
CC -!- INTERACTION:
CC P05106; P78423: CX3CL1; NbExp=7; IntAct=EBI-702847, EBI-15188013;
CC P05106; P21333: FLNA; NbExp=3; IntAct=EBI-702847, EBI-350432;
CC P05106; P08514: ITGA2B; NbExp=12; IntAct=EBI-702847, EBI-702693;
CC P05106; P08514-1: ITGA2B; NbExp=4; IntAct=EBI-702847, EBI-15805658;
CC P05106; P06756: ITGAV; NbExp=13; IntAct=EBI-702847, EBI-298282;
CC P05106; P05106: ITGB3; NbExp=6; IntAct=EBI-702847, EBI-702847;
CC P05106; PRO_0000022750 [P14555]: PLA2G2A; NbExp=3; IntAct=EBI-702847, EBI-16414951;
CC P05106; P18031: PTPN1; NbExp=4; IntAct=EBI-702847, EBI-968788;
CC P05106; Q9Y490: TLN1; NbExp=6; IntAct=EBI-702847, EBI-2462036;
CC P05106; P05094: ACTN1; Xeno; NbExp=2; IntAct=EBI-702847, EBI-5847257;
CC P05106; F5HB81: gB; Xeno; NbExp=2; IntAct=EBI-702847, EBI-9027696;
CC P05106; Q62101: Prkd1; Xeno; NbExp=2; IntAct=EBI-702847, EBI-6903636;
CC P05106; P05480-2: Src; Xeno; NbExp=4; IntAct=EBI-702847, EBI-26656723;
CC P05106; P26039: Tln1; Xeno; NbExp=7; IntAct=EBI-702847, EBI-1039593;
CC P05106; P54939: TLN1; Xeno; NbExp=2; IntAct=EBI-702847, EBI-1035421;
CC P05106; P06935; Xeno; NbExp=4; IntAct=EBI-702847, EBI-981051;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20020534,
CC ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:9195946}; Single-pass
CC 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}. Cell
CC junction, focal adhesion {ECO:0000269|PubMed:20702409}. Postsynaptic
CC cell membrane {ECO:0000250|UniProtKB:O54890}; Single-pass type I
CC membrane protein {ECO:0000250|UniProtKB:O54890}. Synapse
CC {ECO:0000250|UniProtKB:O54890}.
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 when
CC both Tyr-773 and Tyr-785 are phosphorylated. Phosphorylation of Thr-779
CC 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 and
CC HPA-1B/ZW(B)/PL(A2) has Pro-59. HPA-1A is involved in fetal-maternal
CC alloimmune thromobocytopenia (FMAIT) as well as in neonatal alloimmune
CC 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 and
CC HPA-4B/PEN(B)/YUK(B) has Gln-169. HPA-4B is involved in neonatal
CC 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 Gln-515.
CC 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 2 (GT2) [MIM:619267]: A form of
CC Glanzmann thrombasthenia, a disorder characterized by failure of
CC platelet aggregation, absent or diminished clot retraction, and
CC mucocutaneous bleeding of mild-to-moderate severity. Glanzmann
CC thrombasthenia has been classified into clinical types I and II. In
CC type I, platelets show absence of glycoprotein IIb-IIIa complexes at
CC their surface and lack fibrinogen and clot retraction capability. In
CC type II, the platelets express glycoprotein IIb-IIIa complexes at
CC reduced 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:29084015, ECO:0000269|PubMed:8781422,
CC ECO:0000269|PubMed:9215749, ECO:0000269|PubMed:9376589,
CC ECO:0000269|PubMed:9684783, ECO:0000269|PubMed:9790984}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Bleeding disorder, platelet-type, 24 (BDPLT24) [MIM:619271]:
CC An autosomal dominant disorder of platelet production characterized by
CC congenital macrothrombocytopenia and platelet anisocytosis. Affected
CC individuals may have no or only mildly increased bleeding tendency.
CC {ECO:0000269|PubMed:18065693, ECO:0000269|PubMed:29380037}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {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=C&genename=ITGB3";
CC ---------------------------------------------------------------------------
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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 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; 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; 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 PDB; 6MK0; X-ray; 3.00 A; B=30-716.
DR PDB; 6MSL; X-ray; 3.10 A; B=27-721.
DR PDB; 6MSU; X-ray; 3.11 A; B=27-721.
DR PDB; 6NAJ; X-ray; 3.10 A; B=27-716.
DR PDB; 6V4P; EM; 2.80 A; B=1-690.
DR PDB; 7KN0; NMR; -; B=712-753.
DR PDB; 7LA4; EM; 3.30 A; B=1-788.
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; 1S4X; -.
DR PDBsum; 1TYE; -.
DR PDBsum; 1U8C; -.
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 PDBsum; 6MK0; -.
DR PDBsum; 6MSL; -.
DR PDBsum; 6MSU; -.
DR PDBsum; 6NAJ; -.
DR PDBsum; 6V4P; -.
DR PDBsum; 7KN0; -.
DR PDBsum; 7LA4; -.
DR AlphaFoldDB; P05106; -.
DR BMRB; P05106; -.
DR SMR; P05106; -.
DR BioGRID; 109896; 49.
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; 36.
DR MINT; P05106; -.
DR STRING; 9606.ENSP00000452786; -.
DR BindingDB; P05106; -.
DR ChEMBL; CHEMBL1907598; -.
DR ChEMBL; CHEMBL2093869; -.
DR ChEMBL; CHEMBL2111461; -.
DR ChEMBL; CHEMBL3883284; -.
DR ChEMBL; CHEMBL4106150; -.
DR DrugBank; DB00054; Abciximab.
DR DrugBank; DB00098; Antithymocyte immunoglobulin (rabbit).
DR DrugBank; DB00063; Eptifibatide.
DR DrugBank; DB13949; Ferric cation.
DR DrugBank; DB15598; Ferric maltol.
DR DrugBank; DB06472; Fradafiban.
DR DrugBank; DB04863; Lefradafiban.
DR DrugBank; DB00451; Levothyroxine.
DR DrugBank; DB05787; LM-609.
DR DrugBank; DB02709; Resveratrol.
DR DrugBank; DB14520; Tetraferric tricitrate decahydrate.
DR DrugBank; DB00775; Tirofiban.
DR DrugCentral; P05106; -.
DR GuidetoPHARMACOLOGY; 2457; -.
DR GlyConnect; 1416; 5 N-Linked glycans (2 sites).
DR GlyGen; P05106; 6 sites, 7 N-linked glycans (2 sites).
DR iPTMnet; P05106; -.
DR PhosphoSitePlus; P05106; -.
DR BioMuta; ITGB3; -.
DR DMDM; 125987835; -.
DR EPD; P05106; -.
DR jPOST; P05106; -.
DR MassIVE; P05106; -.
DR MaxQB; P05106; -.
DR PaxDb; P05106; -.
DR PeptideAtlas; P05106; -.
DR PRIDE; P05106; -.
DR ProteomicsDB; 51790; -. [P05106-1]
DR ProteomicsDB; 51791; -. [P05106-2]
DR ProteomicsDB; 51792; -. [P05106-3]
DR ABCD; P05106; 29 sequenced antibodies.
DR Antibodypedia; 55106; 2374 antibodies from 51 providers.
DR DNASU; 3690; -.
DR Ensembl; ENST00000559488.7; ENSP00000452786.2; ENSG00000259207.9. [P05106-1]
DR GeneID; 3690; -.
DR KEGG; hsa:3690; -.
DR MANE-Select; ENST00000559488.7; ENSP00000452786.2; NM_000212.3; NP_000203.2.
DR UCSC; uc002ilj.4; human. [P05106-1]
DR CTD; 3690; -.
DR DisGeNET; 3690; -.
DR GeneCards; ITGB3; -.
DR HGNC; HGNC:6156; ITGB3.
DR HPA; ENSG00000259207; Tissue enhanced (thyroid).
DR MalaCards; ITGB3; -.
DR MIM; 173470; gene.
DR MIM; 619267; phenotype.
DR MIM; 619271; 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 VEuPathDB; HostDB:ENSG00000259207; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT00980000198528; -.
DR HOGENOM; CLU_011772_0_1_1; -.
DR InParanoid; P05106; -.
DR OMA; PRCNNGN; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; P05106; -.
DR TreeFam; TF105392; -.
DR PathwayCommons; P05106; -.
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-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-HSA-3000170; Syndecan interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-354192; Integrin 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-6802952; Signaling by BRAF and RAF1 fusions.
DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants.
DR SignaLink; P05106; -.
DR SIGNOR; P05106; -.
DR BioGRID-ORCS; 3690; 30 hits in 1081 CRISPR screens.
DR ChiTaRS; ITGB3; human.
DR EvolutionaryTrace; P05106; -.
DR GeneWiki; CD61; -.
DR GenomeRNAi; 3690; -.
DR Pharos; P05106; Tclin.
DR PRO; PR:P05106; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P05106; protein.
DR Bgee; ENSG00000259207; Expressed in monocyte and 139 other tissues.
DR ExpressionAtlas; P05106; baseline and differential.
DR Genevisible; P05106; HS.
DR GO; GO:0071133; C:alpha9-beta1 integrin-ADAM8 complex; IEA:Ensembl.
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:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
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:0099699; C:integral component of synaptic membrane; IEA:Ensembl.
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:0005654; C:nucleoplasm; IDA:HPA.
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:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:ARUK-UCL.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS: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:0070051; F:fibrinogen binding; IEA:Ensembl.
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:0005080; F:protein kinase C binding; IEA:Ensembl.
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:0007044; P:cell-substrate junction assembly; IEA:Ensembl.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
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:0048333; P:mesodermal cell differentiation; IEP:UniProtKB.
DR GO; GO:0050919; P:negative chemotaxis; IMP:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
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:1905598; P:negative regulation of low-density lipoprotein receptor activity; 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:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1900731; P:positive regulation of adenylate cyclase-inhibiting opioid receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IEA:Ensembl.
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:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IEA:Ensembl.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl.
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:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:2000406; P:positive regulation of T cell migration; IEA:Ensembl.
DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; TAS:BHF-UCL.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0045124; P:regulation of bone resorption; TAS:BHF-UCL.
DR GO; GO:1903053; P:regulation of extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR GO; GO:0061097; P:regulation of protein tyrosine kinase activity; IEA:Ensembl.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:0051611; P:regulation of serotonin uptake; ISS:UniProtKB.
DR GO; GO:1901163; P:regulation of trophoblast cell migration; IEA:Ensembl.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0009314; P:response to radiation; IEA:Ensembl.
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:0046718; P:viral entry into host cell; IMP:UniProtKB.
DR GO; GO:0042060; P:wound healing; IC:BHF-UCL.
DR DisProt; DP01842; -.
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; Direct protein sequencing; Disease variant;
KW Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
KW Host-virus interaction; Integrin; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Repeat; Signal;
KW Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..788
FT /note="Integrin beta-3"
FT /id="PRO_0000016344"
FT TOPO_DOM 27..718
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..741
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 742..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 135..377
FT /note="VWFA"
FT REPEAT 463..511
FT /note="I"
FT REPEAT 512..553
FT /note="II"
FT REPEAT 554..592
FT /note="III"
FT REPEAT 593..629
FT /note="IV"
FT REGION 203..210
FT /note="Involved in CX3CL1-, NRG1-, FGF1- and IGF1-binding"
FT /evidence="ECO:0000269|PubMed:18441324,
FT ECO:0000269|PubMed:19578119, ECO:0000269|PubMed:20682778,
FT ECO:0000269|PubMed:23125415"
FT REGION 293..313
FT /note="CX3CL1-binding"
FT /evidence="ECO:0000269|PubMed:24789099"
FT REGION 463..629
FT /note="Cysteine-rich tandem repeats"
FT MOTIF 777..783
FT /note="LIR"
FT /evidence="ECO:0000305|PubMed:33436497,
FT ECO:0000305|PubMed:33436498"
FT MOD_RES 767
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O54890"
FT MOD_RES 773
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:19141530,
FT ECO:0007744|PubMed:18088087"
FT MOD_RES 779
FT /note="Phosphothreonine; by PDPK1 and PKB/AKT1; in vitro"
FT /evidence="ECO:0000269|PubMed:10896934"
FT MOD_RES 785
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:8631894"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16263699,
FT ECO:0000269|PubMed:16335952"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:11546839"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:11546839"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:11546839"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11546839,
FT ECO:0000269|PubMed:19159218"
FT DISULFID 31..461
FT /evidence="ECO:0000269|PubMed:2001252"
FT DISULFID 39..49
FT /evidence="ECO:0000269|PubMed:2001252"
FT DISULFID 42..75
FT /evidence="ECO:0000269|PubMed:2001252"
FT DISULFID 52..64
FT /evidence="ECO:0000269|PubMed:2001252"
FT DISULFID 203..210
FT /evidence="ECO:0000269|PubMed:2001252"
FT DISULFID 258..299
FT /evidence="ECO:0000269|PubMed:2001252"
FT DISULFID 400..412
FT /evidence="ECO:0000269|PubMed:2001252"
FT DISULFID 432..681
FT /evidence="ECO:0000269|PubMed:2001252"
FT DISULFID 459..463
FT /evidence="ECO:0000269|PubMed:2001252"
FT DISULFID 474..486
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 483..521
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 488..497
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 499..512
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 527..532
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 529..562
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 534..547
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 549..554
FT /evidence="ECO:0000269|PubMed:2001252"
FT DISULFID 568..573
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 570..601
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 575..584
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 586..593
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 607..612
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 609..657
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 614..624
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 627..630
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 634..643
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 640..713
FT /evidence="ECO:0000305|PubMed:2001252"
FT DISULFID 661..689
FT /evidence="ECO:0000269|PubMed:2001252"
FT VAR_SEQ 768..788
FT /note="ANNPLYKEATSTFTNITYRGT -> VRDGAGRFLKSLV (in isoform
FT Beta-3B)"
FT /evidence="ECO:0000303|PubMed:2787511"
FT /id="VSP_002745"
FT VAR_SEQ 768..788
FT /note="ANNPLYKEATSTFTNITYRGT -> HYAQSLRKWNQPVSIDG (in
FT isoform Beta-3C)"
FT /evidence="ECO:0000303|PubMed:9195946"
FT /id="VSP_002746"
FT VARIANT 59
FT /note="L -> P (in alloantigen HPA-1B; dbSNP:rs5918)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:2565345, ECO:0000269|PubMed:29084015,
FT ECO:0000269|Ref.13"
FT /id="VAR_003993"
FT VARIANT 64
FT /note="C -> Y (in GT2; severe type 1 phenotype; the
FT mutation prevents normal ITGA2B/ITGB3 complex expression;
FT dbSNP:rs74554539)"
FT /evidence="ECO:0000269|PubMed:20020534"
FT /id="VAR_069920"
FT VARIANT 66
FT /note="L -> R (in dbSNP:rs36080296)"
FT /evidence="ECO:0000269|Ref.13"
FT /id="VAR_049633"
FT VARIANT 119
FT /note="R -> W (in GT2; dbSNP:rs781062792)"
FT /evidence="ECO:0000269|PubMed:12083483"
FT /id="VAR_030473"
FT VARIANT 141
FT /note="Y -> C (in GT2)"
FT /evidence="ECO:0000269|PubMed:15748237"
FT /id="VAR_030474"
FT VARIANT 143
FT /note="L -> W (in GT2; dbSNP:rs121918452)"
FT /evidence="ECO:0000269|PubMed:9376589"
FT /id="VAR_010649"
FT VARIANT 144
FT /note="M -> R (in GT2; severe type 1 phenotype; the
FT mutation prevented normal ITGA2B/ITGB3 complex expression
FT on the cell surface; dbSNP:rs77963874)"
FT /evidence="ECO:0000269|PubMed:20020534"
FT /id="VAR_069921"
FT VARIANT 145
FT /note="D -> N (in GT2; dbSNP:rs121918445)"
FT /evidence="ECO:0000269|PubMed:9215749"
FT /id="VAR_030475"
FT VARIANT 145
FT /note="D -> Y (in GT2; type B; dbSNP:rs121918445)"
FT /evidence="ECO:0000269|PubMed:2392682"
FT /id="VAR_003998"
FT VARIANT 150
FT /note="M -> V (in GT2; may confer constitutive activity to
FT the alpha-IIb/(mutated)beta-3 receptor; dbSNP:rs767548512)"
FT /evidence="ECO:0000269|PubMed:15583747"
FT /id="VAR_030476"
FT VARIANT 166
FT /note="T -> I (associated with neonatal thrombocytopenia;
FT alloantigen Duv(a+); does not affect significantly the
FT integrin function; dbSNP:rs74708909)"
FT /evidence="ECO:0000269|PubMed:12036875"
FT /id="VAR_030477"
FT VARIANT 169
FT /note="R -> Q (in alloantigen HPA-4B; dbSNP:rs5917)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:1430225"
FT /id="VAR_003994"
FT VARIANT 188
FT /note="S -> L (in GT2; type II; dbSNP:rs143146734)"
FT /evidence="ECO:0000269|PubMed:9684783"
FT /id="VAR_010651"
FT VARIANT 222
FT /note="L -> P (in GT2; variant form; dbSNP:rs79208797)"
FT /evidence="ECO:0000269|PubMed:11897046,
FT ECO:0000269|PubMed:20020534"
FT /id="VAR_030478"
FT VARIANT 240
FT /note="R -> Q (in GT2; type B; dbSNP:rs121918444)"
FT /evidence="ECO:0000269|PubMed:1371279,
FT ECO:0000269|PubMed:29084015"
FT /id="VAR_003999"
FT VARIANT 240
FT /note="R -> W (in GT2; variant Strasbourg-1;
FT dbSNP:rs121918446)"
FT /evidence="ECO:0000269|PubMed:1602006"
FT /id="VAR_004000"
FT VARIANT 242
FT /note="R -> Q (in GT2; dbSNP:rs377162158)"
FT /evidence="ECO:0000269|PubMed:9215749"
FT /id="VAR_030479"
FT VARIANT 243
FT /note="D -> V (in GT2)"
FT /evidence="ECO:0000269|PubMed:12083483"
FT /id="VAR_030480"
FT VARIANT 247
FT /note="G -> D (in GT2; severe type 1 phenotype; the
FT mutation prevents normal ITGA2B/ITGB3 complex expression on
FT the cell surface; the mutation may interfere with correct
FT folding of the protein; dbSNP:rs79560904)"
FT /evidence="ECO:0000269|PubMed:20020534"
FT /id="VAR_069922"
FT VARIANT 279
FT /note="K -> M (in GT2; severe type 1 phenotype; the
FT mutation prevents normal ITGA2B/ITGB3 complex expression on
FT the cell surface; the mutation interupts the interaction of
FT the ITGA2B/ITGB3 complex; dbSNP:rs79775494)"
FT /evidence="ECO:0000269|PubMed:20020534"
FT /id="VAR_069923"
FT VARIANT 288
FT /note="L -> P (in GT2)"
FT /evidence="ECO:0000269|PubMed:9215749"
FT /id="VAR_030481"
FT VARIANT 306
FT /note="H -> P (in GT2; dbSNP:rs13306476)"
FT /evidence="ECO:0000269|PubMed:15634267,
FT ECO:0000269|PubMed:9790984"
FT /id="VAR_004001"
FT VARIANT 321
FT /note="M -> L (in GT2)"
FT /evidence="ECO:0000269|PubMed:15748237"
FT /id="VAR_030482"
FT VARIANT 330
FT /note="I -> N (in GT2; not expressed on the surface and
FT absent inside the transfected cells)"
FT /evidence="ECO:0000269|PubMed:15634267"
FT /id="VAR_030483"
FT VARIANT 400
FT /note="C -> Y (in GT2; dbSNP:rs121918449)"
FT /evidence="ECO:0000269|PubMed:8781422"
FT /id="VAR_004002"
FT VARIANT 433
FT /note="P -> A (in alloantigen MO(+); in a case of neonatal
FT alloimmune thrombocytopenia; dbSNP:rs121918448)"
FT /evidence="ECO:0000269|PubMed:8093349"
FT /id="VAR_003995"
FT VARIANT 453
FT /note="V -> I (in dbSNP:rs5921)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_014178"
FT VARIANT 515
FT /note="R -> Q (in alloantigen CA(+)/TU(+);
FT dbSNP:rs13306487)"
FT /evidence="ECO:0000269|PubMed:7694683"
FT /id="VAR_003996"
FT VARIANT 532
FT /note="C -> Y (in GT2)"
FT /evidence="ECO:0000269|PubMed:12353082"
FT /id="VAR_030484"
FT VARIANT 568
FT /note="C -> R (in GT2; type I)"
FT /evidence="ECO:0000269|PubMed:10233432"
FT /id="VAR_010671"
FT VARIANT 586
FT /note="C -> F (in GT2)"
FT /evidence="ECO:0000269|PubMed:9790984"
FT /id="VAR_004003"
FT VARIANT 586
FT /note="C -> R (in GT2; gain-of-function mutation;
FT constitutively binds ligand-induced binding sites
FT antibodies and the fibrinogen-mimetic antibody PAC-1)"
FT /evidence="ECO:0000269|PubMed:11588040"
FT /id="VAR_030485"
FT VARIANT 598
FT /note="G -> S (in GT2)"
FT /evidence="ECO:0000269|PubMed:9790984"
FT /id="VAR_004004"
FT VARIANT 601
FT /note="C -> R (in GT2; dbSNP:rs747534508)"
FT /evidence="ECO:0000269|PubMed:12083483"
FT /id="VAR_030486"
FT VARIANT 605
FT /note="G -> S (in GT2; type II; dbSNP:rs144884023)"
FT /evidence="ECO:0000269|PubMed:9790984"
FT /id="VAR_010672"
FT VARIANT 662
FT /note="R -> C (in alloantigen SR(A); dbSNP:rs151219882)"
FT /evidence="ECO:0000269|PubMed:8132570"
FT /id="VAR_003997"
FT VARIANT 746
FT /note="Missing (in BDPLT24; the mutant protein is
FT constitutively active; decreased platelet surface
FT expression; spontaneous FAK phosphosphorylation; abnormal
FT cell shape)"
FT /evidence="ECO:0000269|PubMed:29380037"
FT /id="VAR_081732"
FT VARIANT 749
FT /note="D -> H (in BDPLT24; the mutant protein is
FT constitutively active; spontaneous FAK phosphosphorylation;
FT abnormal cell shape; dbSNP:rs398122372)"
FT /evidence="ECO:0000269|PubMed:18065693,
FT ECO:0000269|PubMed:29380037"
FT /id="VAR_069924"
FT VARIANT 778
FT /note="S -> P (in GT2; variant Strasbourg-1;
FT dbSNP:rs121918447)"
FT /evidence="ECO:0000269|PubMed:1438206"
FT /id="VAR_004005"
FT CONFLICT 12
FT /note="A -> V (in Ref. 1; AAA52589 and 3; AAA35927)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="K -> P (in Ref. 11; AAA67537 and 14; AAB23689)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="D -> EY (in Ref. 11; AAA67537)"
FT /evidence="ECO:0000305"
FT CONFLICT 649..653
FT /note="GALHD -> EPYMT (in Ref. 1; AAA52589, 2; AAA60122 and
FT 4; AAB71380)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="G -> H (in Ref. 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 737..741
FT /note="ALLIW -> PCSSG (in Ref. 11; AAA67537)"
FT /evidence="ECO:0000305"
FT TURN 30..34
FT /evidence="ECO:0007829|PDB:6BXJ"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:4MMX"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:6BXB"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2VDO"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6BXJ"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:6BXJ"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3ZE2"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3NID"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:3T3P"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:3T3P"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:3T3P"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:3T3P"
FT TURN 202..207
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 266..278
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5HDB"
FT TURN 308..312
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:3T3P"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:3ZE2"
FT HELIX 366..377
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 381..387
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 392..399
FT /evidence="ECO:0007829|PDB:6BXJ"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:6BXB"
FT STRAND 420..429
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:7LA4"
FT STRAND 438..444
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:6BXJ"
FT HELIX 462..466
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:6BXJ"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:3ZE2"
FT TURN 475..477
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:3IJE"
FT TURN 494..498
FT /evidence="ECO:0007829|PDB:6BXB"
FT STRAND 500..504
FT /evidence="ECO:0007829|PDB:3IJE"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:6MK0"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:6BXB"
FT STRAND 512..518
FT /evidence="ECO:0007829|PDB:6BXJ"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 524..528
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 556..561
FT /evidence="ECO:0007829|PDB:3FCS"
FT HELIX 562..564
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 572..575
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:6BXJ"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:6BXJ"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 604..608
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 611..614
FT /evidence="ECO:0007829|PDB:6BXJ"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:3IJE"
FT STRAND 620..624
FT /evidence="ECO:0007829|PDB:1U8C"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:4G1E"
FT HELIX 633..645
FT /evidence="ECO:0007829|PDB:6BXJ"
FT HELIX 650..653
FT /evidence="ECO:0007829|PDB:6BXJ"
FT HELIX 657..660
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 663..670
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 676..684
FT /evidence="ECO:0007829|PDB:6BXJ"
FT TURN 686..688
FT /evidence="ECO:0007829|PDB:1M1X"
FT STRAND 690..697
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:3FCS"
FT STRAND 703..710
FT /evidence="ECO:0007829|PDB:6BXJ"
FT STRAND 715..717
FT /evidence="ECO:0007829|PDB:2KNC"
FT TURN 743..759
FT /evidence="ECO:0007829|PDB:1KUP"
FT TURN 761..765
FT /evidence="ECO:0007829|PDB:1KUP"
FT STRAND 767..770
FT /evidence="ECO:0007829|PDB:1S4X"
FT HELIX 771..774
FT /evidence="ECO:0007829|PDB:1MK7"
FT HELIX 776..779
FT /evidence="ECO:0007829|PDB:2LJD"
FT TURN 782..786
FT /evidence="ECO:0007829|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
