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 29-MAY-2013, entry version 191. 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). 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; 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; 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 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 [19] RP 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] 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 [26] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125, AND MASS RP SPECTROMETRY. 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 [27] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125, AND MASS RP SPECTROMETRY. 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 [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-773, AND MASS RP SPECTROMETRY. 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 [29] 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 [30] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-680, AND MASS RP SPECTROMETRY. 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 [31] 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 [32] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 27-718. 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 [33] 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 [34] 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 [35] 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 [36] 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 [37] 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 [38] 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 [39] 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 [40] 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 [41] 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 [42] 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 [43] 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 [44] 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 [45] 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 [46] 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 [47] 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 [48] 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 [49] RP VARIANT GT ARG-568. RX PubMed=10233432; DOI=10.1046/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 [50] 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 [51] 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 [52] 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 [53] 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 [54] 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 [55] 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 [56] 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 [57] 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 [58] 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 [59] 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). CC -!- FUNCTION: Integrin alpha-V/beta-3 is a receptor for cytotactin, CC fibronectin, laminin, matrix metalloproteinase-2, osteopontin, CC osteomodulin, prothrombin, thrombospondin, vitronectin and von CC Willebrand factor. Integrin alpha-IIb/beta-3 is a receptor for CC fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin CC and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 CC recognize the sequence R-G-D in a wide array of ligands. Integrin CC alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V CC in 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 In case of HIV-1 infection, the interaction with extracellular CC viral Tat protein seems to enhance angiogenesis in Kaposi's CC sarcoma lesions. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-3 CC associates with either alpha-IIb or alpha-V. Isoform Beta-3C CC interacts with FLNB. Interacts with COMP. Interacts with HIV-1 CC Tat. Interacts with PDIA6 following platelet stimulation. CC Interacts with SYK; upon activation by ITGB3 promotes platelet CC adhesion. Interacts with MYO10. Interacts with DAB2. Interacts CC with FERMT2. CC -!- INTERACTION: CC Self; NbExp=4; 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 P08514:ITGA2B; NbExp=3; IntAct=EBI-702847, EBI-702693; CC P06756:ITGAV; NbExp=9; IntAct=EBI-702847, EBI-298282; CC P05480:Src (xeno); NbExp=5; IntAct=EBI-702847, EBI-298680; CC P54939:TLN1 (xeno); NbExp=2; IntAct=EBI-702847, EBI-1035421; CC P26039:Tln1 (xeno); NbExp=3; IntAct=EBI-702847, EBI-1039593; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Cell projection, lamellipodium membrane. Cell junction, CC focal adhesion. 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. 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. 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 -!- SIMILARITY: Contains 1 VWFA domain. CC -!- WEB RESOURCE: Name=GeneReviews; CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/ITGB3"; 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"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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 IPI; IPI00220350; -. DR IPI; IPI00220351; -. DR IPI; IPI00303283; -. 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. 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; 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; 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; 4G1E; X-ray; 3.00 A; B=27-717. DR PDB; 4G1M; X-ray; 2.90 A; B=27-718. DR PDBsum; 1JV2; -. DR PDBsum; 1KUP; -. DR PDBsum; 1KUZ; -. DR PDBsum; 1L5G; -. DR PDBsum; 1M1X; -. DR PDBsum; 1M8O; -. 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; 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; 4G1E; -. DR PDBsum; 4G1M; -. DR ProteinModelPortal; P05106; -. DR DIP; DIP-304N; -. DR IntAct; P05106; 12. DR MINT; MINT-209501; -. DR STRING; 9606.ENSP00000262017; -. DR PhosphoSite; P05106; -. DR DMDM; 125987835; -. DR PaxDb; P05106; -. DR PRIDE; P05106; -. DR Ensembl; ENST00000262017; ENSP00000262017; ENSG00000259207. DR Ensembl; ENST00000559488; ENSP00000452786; ENSG00000259207. DR GeneID; 3690; -. DR KEGG; hsa:3690; -. DR UCSC; uc002ilj.3; human. DR CTD; 3690; -. DR GeneCards; GC17P045331; -. DR HGNC; HGNC:6156; ITGB3. DR HPA; CAB002501; -. DR HPA; HPA027852; -. DR MIM; 173470; gene+phenotype. DR MIM; 273800; phenotype. DR neXtProt; NX_P05106; -. DR Orphanet; 140957; Autosomal dominant macrothrombocytopenia. DR Orphanet; 853; Fetal and neonatal alloimmune thrombocytopenia. DR Orphanet; 849; Glanzmann thrombasthenia. DR PharmGKB; PA205; -. DR eggNOG; NOG287997; -. DR HOVERGEN; HBG006190; -. DR InParanoid; P05106; -. DR KO; K06493; -. DR OMA; GHGQCSC; -. DR OrthoDB; EOG428210; -. DR PhylomeDB; P05106; -. DR Pathway_Interaction_DB; arf6cyclingpathway; Arf6 signaling events. DR Pathway_Interaction_DB; ephrinbrevpathway; Ephrin B reverse signaling. DR Pathway_Interaction_DB; il4_2pathway; IL4-mediated signaling events. DR Pathway_Interaction_DB; avb3_integrin_pathway; Integrins in angiogenesis. DR Pathway_Interaction_DB; avb3_opn_pathway; Osteopontin-mediated events. DR Pathway_Interaction_DB; s1p_s1p1_pathway; S1P1 pathway. DR Pathway_Interaction_DB; s1p_s1p3_pathway; S1P3 pathway. DR Pathway_Interaction_DB; ptp1bpathway; Signaling events mediated by PTP1B. DR Pathway_Interaction_DB; vegfr1_2_pathway; Signaling events mediated by VEGFR1 and VEGFR2. DR Reactome; REACT_111045; Developmental Biology. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_118779; Extracellular matrix organization. DR Reactome; REACT_604; Hemostasis. DR SignaLink; P05106; -. DR BindingDB; P05106; -. DR ChEMBL; CHEMBL207; -. DR ChiTaRS; ITGB3; human. DR DrugBank; DB00054; Abciximab. DR DrugBank; DB00775; Tirofiban. DR EvolutionaryTrace; P05106; -. DR GenomeRNAi; 3690; -. DR NextBio; 14453; -. DR PMAP-CutDB; P05106; -. DR ArrayExpress; P05106; -. DR Bgee; P05106; -. DR CleanEx; HS_ITGB3; -. DR Genevestigator; P05106; -. DR GermOnline; ENSG00000056345; Homo sapiens. DR GO; GO:0071062; C:alphav-beta3 integrin-vitronectin complex; TAS:BHF-UCL. DR GO; GO:0008305; C:integrin complex; IDA:BHF-UCL. DR GO; GO:0042470; C:melanosome; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome. DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; TAS:BHF-UCL. DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:UniProtKB. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; TAS:BHF-UCL. 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:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro. DR GO; GO:0007044; P:cell-substrate junction assembly; IEA:InterPro. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:BHF-UCL. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. 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: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: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:0014909; P:smooth muscle cell migration; IMP:BHF-UCL. DR GO; GO:0035295; P:tube development; TAS:BHF-UCL. DR GO; GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. DR Gene3D; 1.20.5.630; -; 1. DR Gene3D; 3.40.50.410; -; 1. DR InterPro; IPR027068; Integrin_beta-3. DR InterPro; IPR015812; Integrin_bsu. DR InterPro; IPR014836; Integrin_bsu_cyt_dom. DR InterPro; IPR002369; Integrin_bsu_N. DR InterPro; IPR012896; Integrin_bsu_tail. DR InterPro; IPR003659; Plexin-like. DR InterPro; IPR016201; Plexin-like_fold. DR InterPro; IPR002035; VWF_A. DR PANTHER; PTHR10082; PTHR10082; 1. DR PANTHER; PTHR10082:SF25; PTHR10082:SF25; 1. DR Pfam; PF08725; Integrin_b_cyt; 1. DR Pfam; PF07965; Integrin_B_tail; 1. DR Pfam; PF00362; Integrin_beta; 1. DR PIRSF; PIRSF002512; Integrin_B; 1. DR PRINTS; PR01186; INTEGRINB. DR SMART; SM00187; INB; 1. DR SMART; SM00423; PSI; 1. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF69687; Integrin_bsu_tail; 1. DR SUPFAM; SSF103575; Plexin-like_fold; 1. DR PROSITE; PS00022; EGF_1; UNKNOWN_2. DR PROSITE; PS01186; EGF_2; UNKNOWN_1. DR PROSITE; PS00243; INTEGRIN_BETA; 3. DR PROSITE; PS50234; VWFA; FALSE_NEG. 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-virus interaction; Integrin; Membrane; KW Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 26 Potential. FT CHAIN 27 788 Integrin beta-3. FT /FTId=PRO_0000016344. FT TOPO_DOM 27 718 Extracellular (Potential). FT TRANSMEM 719 741 Helical; (Potential). FT TOPO_DOM 742 788 Cytoplasmic (Potential). 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 463 629 Cysteine-rich tandem repeats. FT MOD_RES 773 773 Phosphotyrosine. FT MOD_RES 779 779 Phosphothreonine; by PDPK1 and PKB/AKT1; FT in vitro. FT CARBOHYD 125 125 N-linked (GlcNAc...). FT CARBOHYD 346 346 N-linked (GlcNAc...) (Potential). FT CARBOHYD 397 397 N-linked (GlcNAc...) (Potential). FT CARBOHYD 478 478 N-linked (GlcNAc...). FT CARBOHYD 585 585 N-linked (GlcNAc...) (Potential). FT CARBOHYD 680 680 N-linked (GlcNAc...). FT DISULFID 31 461 FT DISULFID 39 49 FT DISULFID 42 75 FT DISULFID 52 64 FT DISULFID 203 210 FT DISULFID 258 299 FT DISULFID 400 412 FT DISULFID 432 681 FT DISULFID 459 463 FT DISULFID 474 486 Probable. FT DISULFID 483 521 Probable. FT DISULFID 488 497 Probable. FT DISULFID 499 512 Probable. FT DISULFID 527 532 Probable. FT DISULFID 529 562 Probable. FT DISULFID 534 547 Probable. FT DISULFID 549 554 FT DISULFID 568 573 Probable. FT DISULFID 570 601 Probable. FT DISULFID 575 584 Probable. FT DISULFID 586 593 Probable. FT DISULFID 607 612 Probable. FT DISULFID 609 657 Probable. FT DISULFID 614 624 Probable. FT DISULFID 627 630 Probable. FT DISULFID 634 643 Probable. FT DISULFID 640 713 Probable. FT DISULFID 661 689 FT VAR_SEQ 768 788 ANNPLYKEATSTFTNITYRGT -> VRDGAGRFLKSLV FT (in isoform Beta-3B). FT /FTId=VSP_002745. FT VAR_SEQ 768 788 ANNPLYKEATSTFTNITYRGT -> HYAQSLRKWNQPVSID FT G (in isoform Beta-3C). FT /FTId=VSP_002746. FT VARIANT 59 59 L -> P (in alloantigen HPA-1B; FT dbSNP:rs5918). FT /FTId=VAR_003993. FT VARIANT 66 66 L -> R (in dbSNP:rs36080296). FT /FTId=VAR_049633. FT VARIANT 119 119 R -> W (in GT). FT /FTId=VAR_030473. FT VARIANT 141 141 Y -> C (in GT). FT /FTId=VAR_030474. FT VARIANT 143 143 L -> W (in GT). FT /FTId=VAR_010649. FT VARIANT 145 145 D -> N (in GT). FT /FTId=VAR_030475. FT VARIANT 145 145 D -> Y (in GT; type B). 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). 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). FT /FTId=VAR_030477. FT VARIANT 169 169 R -> Q (in alloantigen HPA-4B; FT dbSNP:rs5917). FT /FTId=VAR_003994. FT VARIANT 188 188 S -> L (in GT; type II). FT /FTId=VAR_010651. FT VARIANT 222 222 L -> P (in GT; variant form). FT /FTId=VAR_030478. FT VARIANT 240 240 R -> Q (in GT; type B). FT /FTId=VAR_003999. FT VARIANT 240 240 R -> W (in GT; variant Strasbourg-1). FT /FTId=VAR_004000. FT VARIANT 242 242 R -> Q (in GT). FT /FTId=VAR_030479. FT VARIANT 243 243 D -> V (in GT). FT /FTId=VAR_030480. FT VARIANT 288 288 L -> P (in GT). FT /FTId=VAR_030481. FT VARIANT 306 306 H -> P (in GT; dbSNP:rs13306476). FT /FTId=VAR_004001. FT VARIANT 321 321 M -> L (in GT). 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). FT /FTId=VAR_030483. FT VARIANT 400 400 C -> Y (in GT). FT /FTId=VAR_004002. FT VARIANT 433 433 P -> A (in alloantigen MO(+); in a case FT of neonatal alloimmune thrombocytopenia). FT /FTId=VAR_003995. FT VARIANT 453 453 V -> I (in dbSNP:rs5921). FT /FTId=VAR_014178. FT VARIANT 515 515 R -> Q (in alloantigen CA(+)/TU(+); FT dbSNP:rs13306487). FT /FTId=VAR_003996. FT VARIANT 532 532 C -> Y (in GT). FT /FTId=VAR_030484. FT VARIANT 568 568 C -> R (in GT; type I). FT /FTId=VAR_010671. FT VARIANT 586 586 C -> F (in GT). 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 /FTId=VAR_030485. FT VARIANT 598 598 G -> S (in GT). FT /FTId=VAR_004004. FT VARIANT 601 601 C -> R (in GT). FT /FTId=VAR_030486. FT VARIANT 605 605 G -> S (in GT; type II). FT /FTId=VAR_010672. FT VARIANT 662 662 R -> C (in alloantigen SR(A)). FT /FTId=VAR_003997. FT VARIANT 778 778 S -> P (in GT; variant Strasbourg-1). FT /FTId=VAR_004005. FT CONFLICT 12 12 A -> V (in Ref. 1; AAA52589 and 3; FT AAA35927). FT CONFLICT 151 151 K -> P (in Ref. 11; AAA67537 and 14; FT AAB23689). FT CONFLICT 205 205 D -> EY (in Ref. 11; AAA67537). FT CONFLICT 649 653 GALHD -> EPYMT (in Ref. 1; AAA52589, 2; FT AAA60122 and 4; AAB71380). FT CONFLICT 716 716 G -> H (in Ref. 8). FT CONFLICT 737 741 ALLIW -> PCSSG (in Ref. 11; AAA67537). FT HELIX 30 33 FT HELIX 39 45 FT STRAND 50 52 FT STRAND 54 57 FT STRAND 59 61 FT STRAND 63 65 FT HELIX 67 72 FT HELIX 77 79 FT STRAND 86 91 FT STRAND 99 101 FT STRAND 102 104 FT STRAND 109 111 FT STRAND 113 118 FT STRAND 123 131 FT STRAND 138 145 FT HELIX 148 150 FT HELIX 151 156 FT TURN 157 159 FT HELIX 160 168 FT TURN 169 171 FT STRAND 175 182 FT TURN 188 190 FT HELIX 196 200 FT TURN 202 207 FT STRAND 215 224 FT HELIX 226 235 FT STRAND 242 246 FT HELIX 248 257 FT HELIX 259 262 FT STRAND 266 278 FT HELIX 285 289 FT STRAND 305 307 FT TURN 308 312 FT HELIX 318 327 FT STRAND 331 336 FT HELIX 338 340 FT HELIX 341 349 FT STRAND 355 358 FT STRAND 361 364 FT HELIX 366 377 FT STRAND 381 387 FT STRAND 392 400 FT TURN 401 403 FT STRAND 404 407 FT STRAND 411 415 FT STRAND 420 429 FT STRAND 434 444 FT STRAND 451 457 FT HELIX 462 466 FT STRAND 468 470 FT TURN 472 478 FT STRAND 479 482 FT STRAND 485 488 FT STRAND 489 491 FT TURN 494 497 FT STRAND 500 504 FT STRAND 513 518 FT HELIX 520 523 FT STRAND 524 527 FT STRAND 529 534 FT STRAND 538 540 FT STRAND 542 544 FT STRAND 549 552 FT STRAND 556 561 FT HELIX 562 564 FT STRAND 565 569 FT STRAND 572 575 FT STRAND 579 584 FT TURN 591 593 FT STRAND 598 600 FT STRAND 602 604 FT STRAND 606 608 FT STRAND 611 613 FT TURN 616 618 FT STRAND 620 624 FT STRAND 628 630 FT TURN 633 635 FT HELIX 639 641 FT TURN 642 646 FT STRAND 649 655 FT TURN 658 660 FT STRAND 664 666 FT STRAND 669 671 FT STRAND 674 678 FT STRAND 680 684 FT STRAND 688 694 FT STRAND 698 700 FT STRAND 704 706 FT STRAND 707 710 FT STRAND 715 717 FT TURN 743 759 FT TURN 761 765 FT STRAND 767 770 FT HELIX 771 774 FT HELIX 776 779 FT TURN 782 786 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 //