ID ITA2B_HUMAN Reviewed; 1039 AA. AC P08514; B2RCY8; O95366; Q14443; Q17R67; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 3. DT 27-MAR-2024, entry version 264. DE RecName: Full=Integrin alpha-IIb; DE AltName: Full=GPalpha IIb; DE Short=GPIIb; DE AltName: Full=Platelet membrane glycoprotein IIb; DE AltName: CD_antigen=CD41; DE Contains: DE RecName: Full=Integrin alpha-IIb heavy chain; DE Contains: DE RecName: Full=Integrin alpha-IIb light chain, form 1; DE Contains: DE RecName: Full=Integrin alpha-IIb light chain, form 2; DE Flags: Precursor; GN Name=ITGA2B; Synonyms=GP2B, ITGAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-313. RX PubMed=2439501; DOI=10.1016/s0021-9258(18)47438-8; RA Poncz M., Eisman R., Heidenreich R., Silver S.M., Vilaire G., Surrey S., RA Schwartz E., Bennett J.S.; RT "Structure of the platelet membrane glycoprotein IIb. Homology to the alpha RT subunits of the vitronectin and fibronectin membrane receptors."; RL J. Biol. Chem. 262:8476-8482(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-313. 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=2322558; DOI=10.1021/bi00457a020; RA Heidenreich R., Eisman R., Surrey S., Delgrosso K., Bennett J.S., RA Schwartz E., Poncz M.; RT "Organization of the gene for platelet glycoprotein IIb."; RL Biochemistry 29:1232-1244(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 1-62 AND 1021-1039. RX PubMed=2845986; DOI=10.1016/s0006-291x(88)80884-2; RA Prandini M.H., Denarier E., Frachet P., Uzan G., Marguerie G.; RT "Isolation of the human platelet glycoprotein IIb gene and characterization RT of the 5' flanking region."; RL Biochem. Biophys. Res. Commun. 156:595-601(1988). RN [8] RP PROTEIN SEQUENCE OF 32-56 AND 903-917. RX PubMed=3534886; DOI=10.1073/pnas.83.21.8351; RA Charo I.F., Fitzgerald L.A., Steiner B., Rall S.C., Bekeart L.S., RA Phillips D.R.; RT "Platelet glycoproteins IIb and IIIa: evidence for a family of RT immunologically and structurally related glycoproteins in mammalian RT cells."; RL Proc. Natl. Acad. Sci. U.S.A. 83:8351-8355(1986). RN [9] RP PROTEIN SEQUENCE OF 32-42. 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 32 AND 872. RX PubMed=8620874; DOI=10.1111/j.1432-1033.1996.0205n.x; RA Makogonenko E.M., Yakubenko V.P., Ingham K.C., Medved L.V.; RT "Thermal stability of individual domains in platelet glycoprotein RT IIbIIIa."; RL Eur. J. Biochem. 237:205-211(1996). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 392-1039 (ISOFORM 1). RX PubMed=3422188; DOI=10.1111/j.1432-1033.1988.tb13762.x; RA Uzan G., Frachet P., Lajmanovich A., Prandini M.-H., Denarier E., RA Duperray A., Loftus J., Ginsberg M., Plow E., Marguerie G.; RT "cDNA clones for human platelet GPIIb corresponding to mRNA from RT megakaryocytes and HEL cells. Evidence for an extensive homology to other RT Arg-Gly-Asp adhesion receptors."; RL Eur. J. Biochem. 171:87-93(1988). RN [12] RP PROTEIN SEQUENCE OF 487-501 AND 1026-1038. 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 [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 753-1039 (ISOFORM 3), AND TISSUE SPECIFICITY. RX PubMed=9809974; RA Trikha M., Cai Y., Grignon D., Honn K.V.; RT "Identification of a novel truncated alphaIIb integrin."; RL Cancer Res. 58:4771-4775(1998). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 868-1039 (ISOFORM 1). RX PubMed=3479442; DOI=10.1172/jci113277; RA Bray P.F., Rosa J.P., Johnston G.I., Shiu D.T., Cook R.G., Lau C., RA Kan Y.W., McEver R.P., Shuman M.A.; RT "Platelet glycoprotein IIb. Chromosomal localization and tissue RT expression."; RL J. Clin. Invest. 80:1812-1817(1987). RN [15] RP PROTEIN SEQUENCE OF 903-922 AND 934-939. RX PubMed=2476117; DOI=10.1042/bj2610551; RA Calvete J.J., Alvarez M.V., Rivas G., Hew C.L., Henschen A., RA Gonzalez-Rodriguez J.; RT "Interchain and intrachain disulphide bonds in human platelet glycoprotein RT IIb. Localization of the epitopes for several monoclonal antibodies."; RL Biochem. J. 261:551-560(1989). RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 938-997 (ISOFORMS 1 AND 2), AND TISSUE RP SPECIFICITY. RC TISSUE=Erythroleukemia; RX PubMed=2351656; DOI=10.1016/s0021-9258(19)38705-8; RA Bray P.F., Leung C.S.-I., Shuman M.A.; RT "Human platelets and megakaryocytes contain alternately spliced RT glycoprotein IIb mRNAs."; RL J. Biol. Chem. 265:9587-9590(1990). RN [17] RP PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-46; RP ASN-280; ASN-601 AND ASN-711. RX PubMed=2775232; DOI=10.1042/bj2610561; RA Calvete J.J., Henschen A., Gonzalez-Rodriguez J.; RT "Complete localization of the intrachain disulphide bonds and the N- RT glycosylation points in the alpha-subunit of human platelet glycoprotein RT IIb."; RL Biochem. J. 261:561-568(1989). RN [18] RP PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT SER-878. RX PubMed=7688323; DOI=10.1016/0014-5793(93)80959-x; RA Calvete J.J., Muniz-Diaz E.; RT "Localization of an O-glycosylation site in the alpha-subunit of the human RT platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen RT expression."; RL FEBS Lett. 328:30-34(1993). RN [19] RP PROTEOLYTIC CLEAVAGE, AND PYROGLUTAMATE FORMATION AT GLN-891. RX PubMed=2226834; DOI=10.1016/0014-5793(90)80443-m; RA Calvete J.J., Schafer W., Henschen A., Gonzalez-Rodriguez J.; RT "Characterization of the beta-chain N-terminus heterogeneity and the alpha- RT chain C-terminus of human platelet GPIIb. Posttranslational cleavage RT sites."; RL FEBS Lett. 272:37-40(1990). RN [20] RP INTERACTION WITH CIB1. RC TISSUE=Fetal liver; RX PubMed=9030514; DOI=10.1074/jbc.272.8.4651; RA Naik U.P., Patel P.M., Parise L.V.; RT "Identification of a novel calcium-binding protein that interacts with the RT integrin alphaIIb cytoplasmic domain."; RL J. Biol. Chem. 272:4651-4654(1997). RN [21] RP INTERACTION WITH CIB1. RX PubMed=10477286; DOI=10.1042/bj3420729; RA Shock D.D., Naik U.P., Brittain J.E., Alahari S.K., Sondek J., Parise L.V.; RT "Calcium-dependent properties of CIB binding to the integrin alphaIIb RT cytoplasmic domain and translocation to the platelet cytoskeleton."; RL Biochem. J. 342:729-735(1999). RN [22] RP MUTAGENESIS OF 1029-PRO-PRO-1030. RX PubMed=10212286; DOI=10.1074/jbc.274.18.12945; RA Leisner T.M., Wencel-Drake J.D., Wang W., Lam S.C.; RT "Bidirectional transmembrane modulation of integrin alphaIIbbeta3 RT conformations."; RL J. Biol. Chem. 274:12945-12949(1999). RN [23] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-601. 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 [24] RP INTERACTION WITH RNF181. RX PubMed=18331836; DOI=10.1016/j.bbrc.2008.02.142; RA Brophy T.M., Raab M., Daxecker H., Culligan K.G., Lehmann I., Chubb A.J., RA Treumann A., Moran N.; RT "RN181, a novel ubiquitin E3 ligase that interacts with the KVGFFKR motif RT of platelet integrin alpha(IIb)beta3."; RL Biochem. Biophys. Res. Commun. 369:1088-1093(2008). RN [25] RP INTERACTION WITH CIB1. RX PubMed=21388953; DOI=10.1074/jbc.m110.179028; RA Huang H., Ishida H., Yamniuk A.P., Vogel H.J.; RT "Solution structures of Ca2+-CIB1 and Mg2+-CIB1 and their interactions with RT the platelet integrin alphaIIb cytoplasmic domain."; RL J. Biol. Chem. 286:17181-17192(2011). RN [26] RP INTERACTION WITH CIB1; CIB2; CIB3 AND CIB4. RX PubMed=22779914; DOI=10.1139/o2012-021; RA Huang H., Bogstie J.N., Vogel H.J.; RT "Biophysical and structural studies of the human calcium- and integrin- RT binding protein family: understanding their functional similarities and RT differences."; RL Biochem. Cell Biol. 90:646-656(2012). RN [27] RP INTERACTION WITH CIB1. RX PubMed=22283712; DOI=10.1021/ja2111306; RA Huang H., Vogel H.J.; RT "Structural basis for the activation of platelet integrin alphaIIbbeta3 by RT calcium- and integrin-binding protein 1."; RL J. Am. Chem. Soc. 134:3864-3872(2012). RN [28] {ECO:0007744|PDB:1TYE} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 32-483 IN COMPLEX WITH ITGB3 AND RP CALCIUM, GLYCOSYLATION AT ASN-46, AND DISULFIDE BONDS. RX PubMed=15378069; DOI=10.1038/nature02976; RA Xiao T., Takagi J., Coller B.S., Wang J.H., Springer T.A.; RT "Structural basis for allostery in integrins and binding to fibrinogen- RT mimetic therapeutics."; RL Nature 432:59-67(2004). RN [29] {ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU} RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 32-989 IN COMPLEX WITH ITGB3 AND RP CALCIUM, GLYCOSYLATION AT ASN-46; ASN-280 AND ASN-601, AND DISULFIDE BONDS. RX PubMed=19111664; DOI=10.1016/j.molcel.2008.11.018; RA Zhu J., Luo B.H., Xiao T., Zhang C., Nishida N., Springer T.A.; RT "Structure of a complete integrin ectodomain in a physiologic resting state RT and activation and deactivation by applied forces."; RL Mol. Cell 32:849-861(2008). RN [30] RP REVIEW ON GT1 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 [31] RP VARIANT SER-874, AND POLYMORPHISM. RX PubMed=2350579; RA Lyman S., Aster R.H., Visentin G.P., Newman P.J.; RT "Polymorphism of human platelet membrane glycoprotein IIb associated with RT the Baka/Bakb alloantigen system."; RL Blood 75:2343-2348(1990). RN [32] RP VARIANT GT1 ASP-273. RX PubMed=8282784; DOI=10.1172/jci116942; RA Poncz M., Rifat S., Coller B.S., Newman P.J., Shattil S.J., Parrella T., RA Fortina P., Bennett J.S.; RT "Glanzmann thrombasthenia secondary to a Gly273-->Asp mutation adjacent to RT the first calcium-binding domain of platelet glycoprotein IIb."; RL J. Clin. Invest. 93:172-179(1994). RN [33] RP VARIANT GT1 ASP-449. RX PubMed=7508443; DOI=10.1016/s0021-9258(17)41800-x; RA Wilcox D.A., Wautier J.-L., Pidard D., Newman P.J.; RT "A single amino acid substitution flanking the fourth calcium binding RT domain of alpha IIb prevents maturation of the alpha IIb beta 3 integrin RT complex."; RL J. Biol. Chem. 269:4450-4457(1994). RN [34] RP VARIANT GT1 HIS-358. RX PubMed=7706461; DOI=10.1172/jci117828; RA Wilcox D.A., Paddock C.M., Lyman S., Gill J.C., Newman P.J.; RT "Glanzmann thrombasthenia resulting from a single amino acid substitution RT between the second and third calcium-binding domains of GPIIb. Role of the RT GPIIb amino terminus in integrin subunit association."; RL J. Clin. Invest. 95:1553-1560(1995). RN [35] RP VARIANT GT1 456-VAL-ASP-457 DEL, AND CHARACTERIZATION OF VARIANT GT1 RP 456-VAL-ASP-457 DEL. RX PubMed=8704171; RA Basani R.B., Vilaire G., Shattil S.J., Kolodziej M.A., Bennett J.S., RA Poncz M.; RT "Glanzmann thrombasthenia due to a two amino acid deletion in the fourth RT calcium-binding domain of alpha IIb: demonstration of the importance of RT calcium-binding domains in the conformation of alpha IIb beta 3."; RL Blood 88:167-173(1996). RN [36] RP VARIANTS GT1 ILE-207; THR-596 AND GLN-1026. 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 [37] RP VARIANT GT1 PRO-214, AND CHARACTERIZATION OF VARIANT GT1 PRO-214. RX PubMed=9473221; RA Grimaldi C.M., Chen F., Wu C., Weiss H.J., Coller B.S., French D.L.; RT "Glycoprotein IIb Leu214Pro mutation produces Glanzmann thrombasthenia with RT both quantitative and qualitative abnormalities in GPIIb/IIIa."; RL Blood 91:1562-1571(1998). RN [38] RP VARIANT GT1 PRO-778. RX PubMed=9763559; RA Tadokoro S., Tomiyama Y., Honda S., Arai M., Yamamoto N., Shiraga M., RA Kosugi S., Kanakura Y., Kurata Y., Matsuzawa Y.; RT "A Gln747-->Pro substitution in the IIb subunit is responsible for a RT moderate IIbbeta3 deficiency in Glanzmann thrombasthenia."; RL Blood 92:2750-2758(1998). RN [39] RP VARIANT BDPLT16 GLN-1026, AND CHARACTERIZATION OF VARIANT BDPLT16 GLN-1026. RX PubMed=9834222; RA Peyruchaud O., Nurden A.T., Milet S., Macchi L., Pannochia A., Bray P.F., RA Kieffer N., Bourre F.; RT "R to Q amino acid substitution in the GFFKR sequence of the cytoplasmic RT domain of the integrin IIb subunit in a patient with a Glanzmann's RT thrombasthenia-like syndrome."; RL Blood 92:4178-4187(1998). RN [40] RP VARIANTS GT1 SER-320; LYS-355 AND PRO-778. RX PubMed=9722314; DOI=10.1046/j.1365-2141.1998.00824.x; RA Ambo H., Kamata T., Handa M., Kawai Y., Oda A., Murata M., Takada Y., RA Ikeda Y.; RT "Novel point mutations in the alphaIIb subunit (Phe289-->Ser, Glu324-->Lys RT and Gln747-->Pro) causing thrombasthenic phenotypes in four Japanese RT patients."; RL Br. J. Haematol. 102:829-840(1998). RN [41] RP VARIANTS GT1 LYS-355 AND THR-596. RX PubMed=9734640; DOI=10.1046/j.1365-2141.1998.00852.x; RA Ruan J., Peyruchaud O., Alberio L., Valles G., Clemetson K., Bourre F., RA Nurden A.T.; RT "Double heterozygosity of the GPIIb gene in a Swiss patient with RT Glanzmann's thrombasthenia."; RL Br. J. Haematol. 102:918-925(1998). RN [42] RP VARIANTS ILE-40; SER-874 AND ASN-968, AND POLYMORPHISM. 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 [43] RP VARIANT GT1 ARG-705, AND CHARACTERIZATION OF VARIANT GT1 ARG-705. RX PubMed=9920835; RA Gonzalez-Manchon C., Fernandez-Pinel M., Arias-Salgado E.G., Ferrer M., RA Alvarez M.-V., Garcia-Munoz S., Ayuso M.S., Parrilla R.; RT "Molecular genetic analysis of a compound heterozygote for the glycoprotein RT (GP) IIb gene associated with Glanzmann's thrombasthenia: disruption of the RT 674-687 disulfide bridge in GPIIb prevents surface exposure of GPIIb-IIIa RT complexes."; RL Blood 93:866-875(1999). RN [44] RP ERRATUM OF PUBMED:9920835. 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 [45] RP VARIANTS GT1 ALA-176 AND LEU-176. RX PubMed=10607701; RA Basani R.B., French D.L., Vilaire G., Brown D.L., Chen F., Coller B.S., RA Derrick J.M., Gartner T.K., Bennett J.S., Poncz M.; RT "A naturally occurring mutation near the amino terminus of alphaIIb defines RT a new region involved in ligand binding to alphaIIbbeta3."; RL Blood 95:180-188(2000). RN [46] RP VARIANTS GT1 TRP-161; LEU-222; ARG-412 AND PRO-847. RX PubMed=11798398; DOI=10.1080/095371001317126383; RA Vinciguerra C., Bordet J.C., Beaune G., Grenier C., Dechavanne M., RA Negrier C.; RT "Description of 10 new mutations in platelet glycoprotein IIb (alphaIIb) RT and glycoprotein IIIa (beta3) genes."; RL Platelets 12:486-495(2001). RN [47] RP VARIANT GT1 PRO-86, AND CHARACTERIZATION OF VARIANT GT1 PRO-86. RX PubMed=12181054; DOI=10.1046/j.1365-2141.2002.03678.x; RA Tanaka S., Hayashi T., Hori Y., Terada C., Han K.S., Ahn H.S., Bourre F., RA Tani Y.; RT "A Leu55 to Pro substitution in the integrin alphaIIb is responsible for a RT case of Glanzmann's thrombasthenia."; RL Br. J. Haematol. 118:833-835(2002). RN [48] RP VARIANTS GT1 VAL-139; ALA-176; GLU-267; ASP-380; THR-405; ASP-581; ARG-705; RP VAL-752 AND PRO-755. 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 [49] RP VARIANTS GT1 PHE-329 AND THR-405, AND CHARACTERIZATION OF VARIANTS GT1 RP PHE-329 AND THR-405. RX PubMed=12424194; DOI=10.1182/blood-2002-07-2266; RA Mitchell W.B., Li J.H., Singh F., Michelson A.D., Bussel J., Coller B.S., RA French D.L.; RT "Two novel mutations in the alpha IIb calcium-binding domains identify RT hydrophobic regions essential for alpha IIbbeta 3 biogenesis."; RL Blood 101:2268-2276(2003). RN [50] RP VARIANT GT1 HIS-174, AND CHARACTERIZATION OF VARIANT GT1 HIS-174. RX PubMed=12506038; DOI=10.1182/blood-2002-07-2144; RA Kiyoi T., Tomiyama Y., Honda S., Tadokoro S., Arai M., Kashiwagi H., RA Kosugi S., Kato H., Kurata Y., Matsuzawa Y.; RT "A naturally occurring Tyr143His alpha IIb mutation abolishes alpha IIb RT beta 3 function for soluble ligands but retains its ability for mediating RT cell adhesion and clot retraction: comparison with other mutations causing RT ligand-binding defects."; RL Blood 101:3485-3491(2003). RN [51] RP VARIANT GT1 MET-982, CHARACTERIZATION OF VARIANT GT1 MET-982, AND VARIANT RP THR-989. RX PubMed=15099289; DOI=10.1046/j.1538-7836.2004.00711.x; RA Nurden A.T., Breillat C., Jacquelin B., Combrie R., Freedman J., RA Blanchette V.S., Schmugge M., Rand M.L.; RT "Triple heterozygosity in the integrin alphaIIb subunit in a patient with RT Glanzmann's thrombasthenia."; RL J. Thromb. Haemost. 2:813-819(2004). RN [52] RP VARIANT GT1 CYS-202, AND CHARACTERIZATION OF VARIANT GT1 CYS-202. RX PubMed=15219201; DOI=10.1111/j.1538-7836.2004.00758.x; RA Rosenberg N., Landau M., Luboshitz J., Rechavi G., Seligsohn U.; RT "A novel Phe171Cys mutation in integrin alpha causes Glanzmann RT thrombasthenia by abrogating alphaIIbbeta3 complex formation."; RL J. Thromb. Haemost. 2:1167-1175(2004). RN [53] RP VARIANT GT1 LEU-943, AND CHARACTERIZATION OF VARIANT GT1 LEU-943. RX PubMed=17018384; RA Jayo A., Pabon D., Lastres P., Jimenez-Yuste V., Gonzalez-Manchon C.; RT "Type II Glanzmann thrombasthenia in a compound heterozygote for the alpha RT IIb gene. A novel missense mutation in exon 27."; RL Haematologica 91:1352-1359(2006). RN [54] RP VARIANTS GT1 THR-405; THR-596; ARG-705; PRO-778; PHE-934; LEU-957; MET-982 RP AND THR-989, AND CHARACTERIZATION OF VARIANTS GT1 PHE-934 AND LEU-957. 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 [55] RP VARIANT BDPLT16 TRP-1026, AND CHARACTERIZATION OF VARIANT BDPLT16 TRP-1026. RX PubMed=21454453; DOI=10.1182/blood-2010-12-323691; RA Kunishima S., Kashiwagi H., Otsu M., Takayama N., Eto K., Onodera M., RA Miyajima Y., Takamatsu Y., Suzumiya J., Matsubara K., Tomiyama Y., RA Saito H.; RT "Heterozygous ITGA2B R995W mutation inducing constitutive activation of the RT alphaIIbbeta3 receptor affects proplatelet formation and causes congenital RT macrothrombocytopenia."; RL Blood 117:5479-5484(2011). CC -!- FUNCTION: Integrin alpha-IIb/beta-3 is a receptor for fibronectin, CC fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. CC It recognizes the sequence R-G-D in a wide array of ligands. It CC recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma CC chain. Following activation integrin alpha-IIb/beta-3 brings about CC platelet/platelet interaction through binding of soluble fibrinogen. CC This step leads to rapid platelet aggregation which physically plugs CC ruptured endothelial cell surface. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit CC is composed of a heavy and a light chain linked by a disulfide bond. CC Alpha-IIb associates with beta-3. Directly interacts with RNF181. CC Interacts (via C-terminus cytoplasmic tail region) with CIB1; the CC interaction is direct and calcium-dependent. Interacts (via C-terminus CC cytoplasmic tail region) with CIB2, CIB3 and CIB4; the interactions are CC stabilized/increased in a calcium and magnesium-dependent manner. CC ITGA2B:ITGB3 interacts with PPIA/CYPA; the interaction is ROS and CC PPIase activity-dependent and is increased in the presence of thrombin CC (By similarity). {ECO:0000250|UniProtKB:Q9QUM0, CC ECO:0000269|PubMed:10477286, ECO:0000269|PubMed:18331836, CC ECO:0000269|PubMed:21388953, ECO:0000269|PubMed:22283712, CC ECO:0000269|PubMed:22779914, ECO:0000269|PubMed:9030514}. CC -!- INTERACTION: CC P08514; P08514: ITGA2B; NbExp=7; IntAct=EBI-702693, EBI-702693; CC P08514; P05106: ITGB3; NbExp=12; IntAct=EBI-702693, EBI-702847; CC P08514-1; P21333: FLNA; NbExp=3; IntAct=EBI-15805658, EBI-350432; CC P08514-1; P05106: ITGB3; NbExp=4; IntAct=EBI-15805658, EBI-702847; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P08514-1; Sequence=Displayed; CC Name=2; CC IsoId=P08514-2; Sequence=VSP_002737; CC Name=3; Synonyms=tr-alpha-IIb {ECO:0000303|PubMed:9809974}; CC IsoId=P08514-3; Sequence=VSP_002736; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in platelets CC and megakaryocytes, but not in reticulocytes. Not detected in Jurkat, CC nor in U937 cell lines (PubMed:2351656). Isoform 3 is expressed in CC prostate adenocarcinoma, as well as in several erythroleukemia, CC prostate adenocarcinoma and melanoma cell lines, including PC-3, DU- CC 145, HEL, WM983A, WM983B and WM35. Not detected in platelets, nor in CC normal prostate (at protein level) (PubMed:9809974). CC {ECO:0000269|PubMed:2351656, ECO:0000269|PubMed:9809974}. CC -!- POLYMORPHISM: Position 874 is associated with platelet-specific CC alloantigen HPA-3/BAK/LEK. HPA-3A/BAK(A)/LEK(A) has Ile-874 and HPA- CC 3B/BAK(B)/LEK(B) has Ser-874. HPA-3B is involved in neonatal alloimmune CC thrombocytopenia (NAIT or NATP). {ECO:0000269|PubMed:10391209, CC ECO:0000269|PubMed:2350579}. CC -!- DISEASE: Glanzmann thrombasthenia 1 (GT1) [MIM:273800]: 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. GT1 inheritance is autosomal CC recessive. {ECO:0000269|PubMed:10607701, ECO:0000269|PubMed:11798398, CC ECO:0000269|PubMed:12083483, ECO:0000269|PubMed:12181054, CC ECO:0000269|PubMed:12424194, ECO:0000269|PubMed:12506038, CC ECO:0000269|PubMed:15099289, ECO:0000269|PubMed:15219201, CC ECO:0000269|PubMed:17018384, ECO:0000269|PubMed:20020534, CC ECO:0000269|PubMed:7508443, ECO:0000269|PubMed:7706461, CC ECO:0000269|PubMed:8282784, ECO:0000269|PubMed:8704171, CC ECO:0000269|PubMed:9215749, ECO:0000269|PubMed:9473221, CC ECO:0000269|PubMed:9722314, ECO:0000269|PubMed:9734640, CC ECO:0000269|PubMed:9763559, ECO:0000269|PubMed:9920835}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Bleeding disorder, platelet-type, 16 (BDPLT16) [MIM:187800]: CC An autosomal dominant form of congenital macrothrombocytopenia CC associated with platelet anisocytosis. It is a disorder of platelet CC production. Affected individuals may have no or only mildly increased CC bleeding tendency. In vitro studies show mild platelet functional CC abnormalities. {ECO:0000269|PubMed:21454453, CC ECO:0000269|PubMed:9834222}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J02764; AAA60114.1; -; mRNA. DR EMBL; M34480; AAA35926.1; -; mRNA. DR EMBL; M34344; AAA53150.1; -; Genomic_DNA. DR EMBL; M33319; AAA53150.1; JOINED; Genomic_DNA. DR EMBL; M33320; AAA53150.1; JOINED; Genomic_DNA. DR EMBL; AK315335; BAG37735.1; -; mRNA. DR EMBL; AC003043; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC117443; AAI17444.1; -; mRNA. DR EMBL; BC126442; AAI26443.1; -; mRNA. DR EMBL; M22568; AAA52587.1; -; Genomic_DNA. DR EMBL; M22569; AAA52588.1; -; Genomic_DNA. DR EMBL; X06831; CAA29987.1; -; mRNA. DR EMBL; AF098114; AAC98507.1; -; mRNA. DR EMBL; M18085; AAA52597.1; -; mRNA. DR EMBL; M54799; AAA52599.1; -; Genomic_DNA. DR CCDS; CCDS32665.1; -. [P08514-1] DR PIR; A34269; A34269. DR RefSeq; NP_000410.2; NM_000419.4. [P08514-1] DR RefSeq; XP_011523051.1; XM_011524749.1. DR PDB; 1DPK; NMR; -; A=1020-1039. DR PDB; 1DPQ; NMR; -; A=1020-1039. DR PDB; 1KUP; NMR; -; A=1018-1028. DR PDB; 1KUZ; NMR; -; A=1018-1028. DR PDB; 1M8O; NMR; -; A=1020-1039. DR PDB; 1S4W; NMR; -; A=1020-1039. DR PDB; 1TYE; X-ray; 2.90 A; A/C/E=32-483. DR PDB; 2K1A; NMR; -; A=989-1029. DR PDB; 2K9J; NMR; -; A=989-1029. DR PDB; 2KNC; NMR; -; A=991-1039. DR PDB; 2MTP; NMR; -; B=1019-1039. DR PDB; 2N9Y; NMR; -; A=989-1029. DR PDB; 2VC2; X-ray; 3.10 A; A=32-483. DR PDB; 2VDK; X-ray; 2.80 A; A=32-483. DR PDB; 2VDL; X-ray; 2.75 A; A=32-483. DR PDB; 2VDM; X-ray; 2.90 A; A=32-483. DR PDB; 2VDN; X-ray; 2.90 A; A=32-483. DR PDB; 2VDO; X-ray; 2.51 A; A=32-483. DR PDB; 2VDP; X-ray; 2.80 A; A=32-483. DR PDB; 2VDQ; X-ray; 2.59 A; A=32-483. DR PDB; 2VDR; X-ray; 2.40 A; A=32-483. DR PDB; 3FCS; X-ray; 2.55 A; A/C=32-989. DR PDB; 3FCU; X-ray; 2.90 A; A/C/E=32-488. DR PDB; 3NID; X-ray; 2.30 A; A/C=32-488. DR PDB; 3NIF; X-ray; 2.40 A; A/C=32-488. DR PDB; 3NIG; X-ray; 2.25 A; A/C=32-488. DR PDB; 3T3M; X-ray; 2.60 A; A/C=32-488. DR PDB; 3T3P; X-ray; 2.20 A; A/C=32-488. DR PDB; 3ZDX; X-ray; 2.45 A; A/C=32-488. DR PDB; 3ZDY; X-ray; 2.45 A; A/C=32-488. DR PDB; 3ZDZ; X-ray; 2.75 A; A/C=32-488. DR PDB; 3ZE0; X-ray; 2.95 A; A/C=32-488. DR PDB; 3ZE1; X-ray; 3.00 A; A/C=32-488. DR PDB; 3ZE2; X-ray; 2.35 A; A/C=32-488. DR PDB; 4CAK; EM; 20.50 A; A=32-989. DR PDB; 4Z7N; X-ray; 2.60 A; A/C=32-486. DR PDB; 4Z7O; X-ray; 2.85 A; A/C=32-486. DR PDB; 4Z7Q; X-ray; 2.70 A; A/C=32-485. DR PDB; 5HDB; X-ray; 2.70 A; A/C=32-485. DR PDB; 6V4P; EM; 2.80 A; A=1-963. DR PDB; 7KN0; NMR; -; A=989-1029. DR PDB; 7L8P; X-ray; 2.35 A; A/C=32-488. DR PDB; 7LA4; EM; 3.30 A; A=1-1039. DR PDB; 7SC4; X-ray; 1.85 A; A/B=1019-1039. DR PDB; 7SFT; NMR; -; B=1019-1039. DR PDB; 7TCT; X-ray; 2.50 A; A/C=32-488. DR PDB; 7TD8; X-ray; 2.60 A; A/C=32-484. DR PDB; 7THO; X-ray; 2.75 A; A/C=32-485. DR PDB; 7TMZ; X-ray; 2.20 A; A/C=32-485. DR PDB; 7TPD; X-ray; 2.60 A; A/C=32-488. DR PDB; 7U60; X-ray; 2.55 A; A/C=32-486. DR PDB; 7U9F; X-ray; 2.70 A; A/C=32-485. DR PDB; 7U9V; X-ray; 2.25 A; A/C=32-485. DR PDB; 7UBR; X-ray; 2.05 A; A/C=32-485. DR PDB; 7UCY; X-ray; 2.35 A; A/C=32-488. DR PDB; 7UDG; X-ray; 2.80 A; A/C=32-488. DR PDB; 7UDH; X-ray; 2.00 A; A/C=32-488. DR PDB; 7UE0; X-ray; 2.74 A; A/C=32-488. DR PDB; 7UFH; X-ray; 3.00 A; A/C=32-488. DR PDB; 7UH8; X-ray; 2.75 A; A/C=32-488. DR PDB; 7UJE; X-ray; 2.50 A; A/C=32-485. DR PDB; 7UJK; X-ray; 2.43 A; A/C=32-488. DR PDB; 7UK9; X-ray; 2.60 A; A/C=32-488. DR PDB; 7UKO; X-ray; 2.60 A; A/C=32-488. DR PDB; 7UKP; X-ray; 2.80 A; A/C=32-488. DR PDB; 7UKT; X-ray; 2.37 A; A/C=32-488. DR PDB; 8T2U; EM; 3.10 A; A=32-1039. DR PDB; 8T2V; EM; 3.40 A; A=32-1039. DR PDBsum; 1DPK; -. DR PDBsum; 1DPQ; -. DR PDBsum; 1KUP; -. DR PDBsum; 1KUZ; -. DR PDBsum; 1M8O; -. DR PDBsum; 1S4W; -. DR PDBsum; 1TYE; -. DR PDBsum; 2K1A; -. DR PDBsum; 2K9J; -. DR PDBsum; 2KNC; -. DR PDBsum; 2MTP; -. DR PDBsum; 2N9Y; -. 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; 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; 4Z7N; -. DR PDBsum; 4Z7O; -. DR PDBsum; 4Z7Q; -. DR PDBsum; 5HDB; -. DR PDBsum; 6V4P; -. DR PDBsum; 7KN0; -. DR PDBsum; 7L8P; -. DR PDBsum; 7LA4; -. DR PDBsum; 7SC4; -. DR PDBsum; 7SFT; -. DR PDBsum; 7TCT; -. DR PDBsum; 7TD8; -. DR PDBsum; 7THO; -. DR PDBsum; 7TMZ; -. DR PDBsum; 7TPD; -. DR PDBsum; 7U60; -. DR PDBsum; 7U9F; -. DR PDBsum; 7U9V; -. DR PDBsum; 7UBR; -. DR PDBsum; 7UCY; -. DR PDBsum; 7UDG; -. DR PDBsum; 7UDH; -. DR PDBsum; 7UE0; -. DR PDBsum; 7UFH; -. DR PDBsum; 7UH8; -. DR PDBsum; 7UJE; -. DR PDBsum; 7UJK; -. DR PDBsum; 7UK9; -. DR PDBsum; 7UKO; -. DR PDBsum; 7UKP; -. DR PDBsum; 7UKT; -. DR PDBsum; 8T2U; -. DR PDBsum; 8T2V; -. DR AlphaFoldDB; P08514; -. DR BMRB; P08514; -. DR EMDB; EMD-21044; -. DR EMDB; EMD-2281; -. DR EMDB; EMD-23245; -. DR EMDB; EMD-40988; -. DR EMDB; EMD-40989; -. DR SMR; P08514; -. DR BioGRID; 109881; 21. DR ComplexPortal; CPX-1799; Integrin alphaIIb-beta3 complex. DR CORUM; P08514; -. DR DIP; DIP-68N; -. DR IntAct; P08514; 6. DR MINT; P08514; -. DR STRING; 9606.ENSP00000262407; -. DR BindingDB; P08514; -. DR ChEMBL; CHEMBL212; -. DR DrugBank; DB00054; Abciximab. DR DrugBank; DB06472; Fradafiban. DR DrugBank; DB04863; Lefradafiban. DR DrugBank; DB00775; Tirofiban. DR DrugCentral; P08514; -. DR GuidetoPHARMACOLOGY; 2441; -. DR GlyCosmos; P08514; 8 sites, 4 glycans. DR GlyGen; P08514; 8 sites, 4 O-linked glycans (2 sites). DR iPTMnet; P08514; -. DR PhosphoSitePlus; P08514; -. DR BioMuta; ITGA2B; -. DR DMDM; 226694183; -. DR OGP; P08514; -. DR jPOST; P08514; -. DR MassIVE; P08514; -. DR PaxDb; 9606-ENSP00000262407; -. DR PeptideAtlas; P08514; -. DR ProteomicsDB; 52113; -. [P08514-1] DR ProteomicsDB; 52114; -. [P08514-2] DR ProteomicsDB; 52115; -. [P08514-3] DR TopDownProteomics; P08514-1; -. [P08514-1] DR ABCD; P08514; 23 sequenced antibodies. DR Antibodypedia; 4350; 2170 antibodies from 51 providers. DR DNASU; 3674; -. DR Ensembl; ENST00000262407.6; ENSP00000262407.5; ENSG00000005961.19. [P08514-1] DR GeneID; 3674; -. DR KEGG; hsa:3674; -. DR MANE-Select; ENST00000262407.6; ENSP00000262407.5; NM_000419.5; NP_000410.2. DR UCSC; uc002igt.2; human. [P08514-1] DR AGR; HGNC:6138; -. DR CTD; 3674; -. DR DisGeNET; 3674; -. DR GeneCards; ITGA2B; -. DR HGNC; HGNC:6138; ITGA2B. DR HPA; ENSG00000005961; Tissue enhanced (bone marrow, epididymis, lymphoid tissue). DR MalaCards; ITGA2B; -. DR MIM; 187800; phenotype. DR MIM; 273800; phenotype. DR MIM; 607759; gene. DR neXtProt; NX_P08514; -. DR OpenTargets; ENSG00000005961; -. DR Orphanet; 140957; Autosomal dominant macrothrombocytopenia. DR Orphanet; 853; Fetal and neonatal alloimmune thrombocytopenia. DR Orphanet; 849; Glanzmann thrombasthenia. DR PharmGKB; PA29938; -. DR VEuPathDB; HostDB:ENSG00000005961; -. DR eggNOG; KOG3637; Eukaryota. DR GeneTree; ENSGT00940000160724; -. DR HOGENOM; CLU_004111_4_1_1; -. DR InParanoid; P08514; -. DR OMA; LQMDTAN; -. DR OrthoDB; 3816176at2759; -. DR PhylomeDB; P08514; -. DR TreeFam; TF105391; -. DR PathwayCommons; P08514; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-216083; Integrin cell surface 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-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-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function. DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants. DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants. DR SignaLink; P08514; -. DR SIGNOR; P08514; -. DR BioGRID-ORCS; 3674; 20 hits in 1173 CRISPR screens. DR ChiTaRS; ITGA2B; human. DR EvolutionaryTrace; P08514; -. DR GeneWiki; ITGA2B; -. DR GenomeRNAi; 3674; -. DR Pharos; P08514; Tclin. DR PRO; PR:P08514; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P08514; Protein. DR Bgee; ENSG00000005961; Expressed in monocyte and 130 other cell types or tissues. DR ExpressionAtlas; P08514; baseline and differential. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0009986; C:cell surface; HDA:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl. DR GO; GO:0008305; C:integrin complex; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome. DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl. DR GO; GO:0070051; F:fibrinogen binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005178; F:integrin binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt. DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central. DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central. DR GO; GO:0007229; P:integrin-mediated signaling pathway; HDA:UniProtKB. DR GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl. DR DisProt; DP01841; -. DR Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1. DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1. DR Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1. DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1. DR Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1. DR InterPro; IPR013517; FG-GAP. DR InterPro; IPR013519; Int_alpha_beta-p. DR InterPro; IPR000413; Integrin_alpha. DR InterPro; IPR018184; Integrin_alpha_C_CS. DR InterPro; IPR013649; Integrin_alpha_Ig-like_1. DR InterPro; IPR048285; Integrin_alpha_Ig-like_2. DR InterPro; IPR048286; Integrin_alpha_Ig-like_3. DR InterPro; IPR028994; Integrin_alpha_N. DR InterPro; IPR032695; Integrin_dom_sf. DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1. DR PANTHER; PTHR23220:SF73; INTEGRIN ALPHA-IIB; 1. DR Pfam; PF01839; FG-GAP; 2. DR Pfam; PF08441; Integrin_A_Ig_1; 1. DR Pfam; PF20805; Integrin_A_Ig_2; 1. DR Pfam; PF20806; Integrin_A_Ig_3; 1. DR Pfam; PF00357; Integrin_alpha; 1. DR PRINTS; PR01185; INTEGRINA. DR SMART; SM00191; Int_alpha; 5. DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1. DR SUPFAM; SSF69179; Integrin domains; 3. DR PROSITE; PS51470; FG_GAP; 7. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. DR Genevisible; P08514; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; KW Cleavage on pair of basic residues; Direct protein sequencing; KW Disease variant; Disulfide bond; Glycoprotein; Integrin; Membrane; KW Metal-binding; Pyrrolidone carboxylic acid; Receptor; Reference proteome; KW Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..31 FT /evidence="ECO:0000269|PubMed:1953640, FT ECO:0000269|PubMed:3534886, ECO:0000269|PubMed:8620874" FT CHAIN 32..1039 FT /note="Integrin alpha-IIb" FT /id="PRO_0000016275" FT CHAIN 32..887 FT /note="Integrin alpha-IIb heavy chain" FT /id="PRO_0000016276" FT CHAIN 891..1039 FT /note="Integrin alpha-IIb light chain, form 1" FT /id="PRO_0000292348" FT CHAIN 903..1039 FT /note="Integrin alpha-IIb light chain, form 2" FT /id="PRO_0000016277" FT TOPO_DOM 32..993 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 994..1019 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1020..1039 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 35..96 FT /note="FG-GAP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 110..173 FT /note="FG-GAP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 187..238 FT /note="FG-GAP 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 251..305 FT /note="FG-GAP 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 306..371 FT /note="FG-GAP 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 373..432 FT /note="FG-GAP 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 435..496 FT /note="FG-GAP 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT MOTIF 1022..1026 FT /note="GFFKR motif" FT BINDING 274 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 276 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 278 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 281 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 283 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 328 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 330 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 332 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 334 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 336 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 396 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 398 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 400 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 402 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 404 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 457 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 459 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 461 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 463 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT BINDING 465 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, FT ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU" FT MOD_RES 891 FT /note="Pyrrolidone carboxylic acid; in light chain form 1" FT /evidence="ECO:0000269|PubMed:2226834" FT CARBOHYD 46 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:2775232, FT ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, FT ECO:0007744|PDB:3FCU" FT CARBOHYD 280 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19111664, FT ECO:0000269|PubMed:2775232, ECO:0007744|PDB:3FCS" FT CARBOHYD 601 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:2775232, FT ECO:0007744|PDB:3FCS" FT CARBOHYD 711 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:2775232" FT CARBOHYD 874 FT /note="O-linked (GalNAc...) serine; in variant S-874" FT CARBOHYD 878 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:7688323" FT CARBOHYD 962 FT /note="N-linked (GlcNAc...) asparagine" FT DISULFID 87..96 FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:2775232, FT ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, FT ECO:0007744|PDB:3FCU" FT DISULFID 138..161 FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:2775232, FT ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, FT ECO:0007744|PDB:3FCU" FT DISULFID 177..198 FT /evidence="ECO:0000269|PubMed:15378069, FT ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:2775232, FT ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, FT ECO:0007744|PDB:3FCU" FT DISULFID 504..515 FT /evidence="ECO:0000269|PubMed:19111664, FT ECO:0000269|PubMed:2775232, ECO:0007744|PDB:3FCS" FT DISULFID 521..576 FT /evidence="ECO:0000269|PubMed:19111664, FT ECO:0000269|PubMed:2775232, ECO:0007744|PDB:3FCS" FT DISULFID 633..639 FT /evidence="ECO:0000269|PubMed:19111664, FT ECO:0000269|PubMed:2775232, ECO:0007744|PDB:3FCS" FT DISULFID 705..718 FT /evidence="ECO:0000269|PubMed:19111664, FT ECO:0000269|PubMed:2775232, ECO:0007744|PDB:3FCS" FT DISULFID 857..921 FT /note="Interchain (between heavy and light chains)" FT /evidence="ECO:0000269|PubMed:19111664, FT ECO:0007744|PDB:3FCS" FT DISULFID 911..916 FT /evidence="ECO:0000269|PubMed:19111664, FT ECO:0007744|PDB:3FCS" FT VAR_SEQ 910..1039 FT /note="SCDSAPCTVVQCDLQEMARGQRAMVTVLAFLWLPSLYQRPLDQFVLQSHAWF FT NVSSLPYAVPPLSLPRGEAQVWTQLLRALEERAIPIWWVLVGVLGGLLLLTILVLAMWK FT VGFFKRNRPPLEEDDEEGE -> VSRLSGLWPGLPGTHGAEGMGGGRGVRVCCGPLWAT FT LGPWEHFK (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_002736" FT VAR_SEQ 948..981 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_002737" FT VARIANT 40 FT /note="T -> I (in dbSNP:rs5915)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_014176" FT VARIANT 86 FT /note="L -> P (in GT1; cells co-transfected with mutated FT alpha-IIb and wild-type beta-3 scarcely expressed the FT alpha-IIb/beta-3 complex; dbSNP:rs1052533574)" FT /evidence="ECO:0000269|PubMed:12181054" FT /id="VAR_030445" FT VARIANT 139 FT /note="A -> V (in GT1)" FT /evidence="ECO:0000269|PubMed:12083483" FT /id="VAR_030446" FT VARIANT 161 FT /note="C -> W (in GT1)" FT /evidence="ECO:0000269|PubMed:11798398" FT /id="VAR_030447" FT VARIANT 174 FT /note="Y -> H (in GT1; abolishes the binding function of FT alpha-IIb/beta-3 for soluble ligands without disturbing FT alpha-IIb/beta-3 expression; functional defect is likely FT caused by its allosteric effect rather than by a defect in FT the ligand-binding site itself)" FT /evidence="ECO:0000269|PubMed:12506038" FT /id="VAR_030448" FT VARIANT 176 FT /note="P -> A (in GT1; impairs surface expression of FT alpha-IIb/beta-3 and abrogates ligand binding to the FT activated integrin; dbSNP:rs2048640485)" FT /evidence="ECO:0000269|PubMed:10607701, FT ECO:0000269|PubMed:12083483" FT /id="VAR_009885" FT VARIANT 176 FT /note="P -> L (in GT1; impairs surface expression of FT alpha-IIb/beta-3)" FT /evidence="ECO:0000269|PubMed:10607701" FT /id="VAR_009886" FT VARIANT 202 FT /note="F -> C (in GT1; results in abrogation of FT alpha-IIb/beta-3 complex formation)" FT /evidence="ECO:0000269|PubMed:15219201" FT /id="VAR_030449" FT VARIANT 207 FT /note="T -> I (in GT1)" FT /evidence="ECO:0000269|PubMed:9215749" FT /id="VAR_030450" FT VARIANT 214 FT /note="L -> P (in GT1; disrupts the structural conformation FT and the ligand binding properties of the heterodimeric FT complex; in addition the mutation appears to confer FT susceptibility to proteolysis; dbSNP:rs137852911)" FT /evidence="ECO:0000269|PubMed:9473221" FT /id="VAR_030451" FT VARIANT 222 FT /note="F -> L (in GT1)" FT /evidence="ECO:0000269|PubMed:11798398" FT /id="VAR_030452" FT VARIANT 267 FT /note="G -> E (in GT1)" FT /evidence="ECO:0000269|PubMed:12083483" FT /id="VAR_030453" FT VARIANT 273 FT /note="G -> D (in GT1; alters the heterodimer conformation FT thus impairing their intracellular transport; FT dbSNP:rs137852907)" FT /evidence="ECO:0000269|PubMed:8282784" FT /id="VAR_003979" FT VARIANT 313 FT /note="G -> A (in dbSNP:rs1126554)" FT /evidence="ECO:0000269|PubMed:2345548, FT ECO:0000269|PubMed:2439501" FT /id="VAR_054820" FT VARIANT 320 FT /note="F -> S (in GT1; type I; impairs surface expression FT of alpha-IIb/beta-3)" FT /evidence="ECO:0000269|PubMed:9722314" FT /id="VAR_009887" FT VARIANT 329 FT /note="V -> F (in GT1; expression of mutant subunit FT alpha-IIb/bet-3 is 28% of control; mutant pro-alpha-IIb FT subunit is retained in the endoplasmic reticulum; FT dbSNP:rs2048619428)" FT /evidence="ECO:0000269|PubMed:12424194" FT /id="VAR_030454" FT VARIANT 355 FT /note="E -> K (in GT1; type I; impairs surface expression FT of alpha-IIb/beta-3; dbSNP:rs137852910)" FT /evidence="ECO:0000269|PubMed:9722314, FT ECO:0000269|PubMed:9734640" FT /id="VAR_009888" FT VARIANT 358 FT /note="R -> H (in GT1; type II; dbSNP:rs137852908)" FT /evidence="ECO:0000269|PubMed:7706461" FT /id="VAR_003980" FT VARIANT 380 FT /note="G -> D (in GT1; dbSNP:rs766006685)" FT /evidence="ECO:0000269|PubMed:12083483" FT /id="VAR_030455" FT VARIANT 405 FT /note="I -> T (in GT1; expression of mutant subunit FT alpha-IIb/bet-3 is 11% of control; mutant pro-alpha-IIb FT subunit is retained in the endoplasmic reticulum; FT dbSNP:rs75622274)" FT /evidence="ECO:0000269|PubMed:12083483, FT ECO:0000269|PubMed:12424194, ECO:0000269|PubMed:20020534" FT /id="VAR_030456" FT VARIANT 412 FT /note="G -> R (in GT1; dbSNP:rs780786843)" FT /evidence="ECO:0000269|PubMed:11798398" FT /id="VAR_030457" FT VARIANT 449 FT /note="G -> D (in GT1; type I; dbSNP:rs1598380253)" FT /evidence="ECO:0000269|PubMed:7508443" FT /id="VAR_003981" FT VARIANT 456..457 FT /note="Missing (in GT1; alteres the conformation of FT heterodimers such that they were neither recognized by the FT heterodimer-specific antibody A2A9 nor able to undergo FT further intracellular processing or transport to the cell FT surface)" FT /id="VAR_030458" FT VARIANT 581 FT /note="A -> D (in GT1)" FT /evidence="ECO:0000269|PubMed:12083483" FT /id="VAR_030459" FT VARIANT 596 FT /note="I -> T (in GT1; type I; dbSNP:rs76811038)" FT /evidence="ECO:0000269|PubMed:20020534, FT ECO:0000269|PubMed:9215749, ECO:0000269|PubMed:9734640" FT /id="VAR_030460" FT VARIANT 649 FT /note="V -> L (in dbSNP:rs7207402)" FT /id="VAR_054821" FT VARIANT 705 FT /note="C -> R (in GT1; type II; the rate of subunit FT maturation and the surface exposure of glycoprotein FT IIb/beta-3 are strongly reduced; dbSNP:rs77961246)" FT /evidence="ECO:0000269|PubMed:12083483, FT ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:9920835" FT /id="VAR_030461" FT VARIANT 752 FT /note="L -> V (in GT1; dbSNP:rs761174160)" FT /evidence="ECO:0000269|PubMed:12083483" FT /id="VAR_030462" FT VARIANT 755 FT /note="R -> P (in GT1; dbSNP:rs763762304)" FT /evidence="ECO:0000269|PubMed:12083483" FT /id="VAR_030463" FT VARIANT 778 FT /note="Q -> P (in GT1; type II; dbSNP:rs74475415)" FT /evidence="ECO:0000269|PubMed:20020534, FT ECO:0000269|PubMed:9722314, ECO:0000269|PubMed:9763559" FT /id="VAR_003982" FT VARIANT 847 FT /note="L -> P (in GT1; dbSNP:rs1344532070)" FT /evidence="ECO:0000269|PubMed:11798398" FT /id="VAR_030464" FT VARIANT 874 FT /note="I -> S (in alloantigen HPA-3B; dbSNP:rs5911)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:2350579" FT /id="VAR_003983" FT VARIANT 934 FT /note="V -> F (in GT1; severe type 1 phenotype; the FT mutation prevented normal ITGA2B/ITGB3 complex expression FT on the cell surface; dbSNP:rs77458039)" FT /evidence="ECO:0000269|PubMed:20020534" FT /id="VAR_069917" FT VARIANT 943 FT /note="P -> L (in GT1; marked reduction in the rate of FT surface expression)" FT /evidence="ECO:0000269|PubMed:17018384" FT /id="VAR_030465" FT VARIANT 957 FT /note="S -> L (in GT1; severe type 1 phenotype; the FT mutation prevented normal ITGA2B/ITGB3 complex expression FT on the cell surface; the mutation may interfere with FT correct folding of the protein; dbSNP:rs80002943)" FT /evidence="ECO:0000269|PubMed:20020534" FT /id="VAR_069918" FT VARIANT 968 FT /note="Y -> N (in dbSNP:rs5914)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_014177" FT VARIANT 982 FT /note="V -> M (in GT1; much reduced surface expression of FT alpha-IIb/beta-3 and a block in the maturation of FT pro-alpha-IIb; dbSNP:rs78657866)" FT /evidence="ECO:0000269|PubMed:15099289, FT ECO:0000269|PubMed:20020534" FT /id="VAR_030466" FT VARIANT 989 FT /note="A -> T (in dbSNP:rs78165611)" FT /evidence="ECO:0000269|PubMed:15099289, FT ECO:0000269|PubMed:20020534" FT /id="VAR_030467" FT VARIANT 1026 FT /note="R -> Q (in GT1 and BDPLT16; results in low surface FT expression of the mutant protein; dbSNP:rs879255514)" FT /evidence="ECO:0000269|PubMed:9215749, FT ECO:0000269|PubMed:9834222" FT /id="VAR_030468" FT VARIANT 1026 FT /note="R -> W (in BDPLT16; results in abnormal membrane FT ruffling and cytoplasmic protrusions as well as defective FT proplatelet formation; dbSNP:rs766503255)" FT /evidence="ECO:0000269|PubMed:21454453" FT /id="VAR_069919" FT MUTAGEN 1029..1030 FT /note="PP->AA: Imparts constitutive activity FT (ligand-binding) to alpha-IIb/beta-3." FT /evidence="ECO:0000269|PubMed:10212286" FT CONFLICT 23 FT /note="P -> A (in Ref. 2; AAA35926)" FT /evidence="ECO:0000305" FT CONFLICT 120 FT /note="A -> S (in Ref. 4; BAG37735)" FT /evidence="ECO:0000305" FT CONFLICT 287..288 FT /note="GA -> VP (in Ref. 3; AAA53150)" FT /evidence="ECO:0000305" FT CONFLICT 346 FT /note="E -> D (in Ref. 2; AAA35926)" FT /evidence="ECO:0000305" FT CONFLICT 565 FT /note="N -> D (in Ref. 2; AAA35926)" FT /evidence="ECO:0000305" FT CONFLICT 566 FT /note="L -> V (in Ref. 11; CAA29987)" FT /evidence="ECO:0000305" FT CONFLICT 633 FT /note="C -> S (in Ref. 1; AAA60114)" FT /evidence="ECO:0000305" FT CONFLICT 729 FT /note="Q -> E (in Ref. 11; CAA29987)" FT /evidence="ECO:0000305" FT CONFLICT 971 FT /note="P -> A (in Ref. 3; AAA53150)" FT /evidence="ECO:0000305" FT CONFLICT 1029 FT /note="P -> H (in Ref. 2; AAA35926 and 7; AAA52588)" FT /evidence="ECO:0000305" FT CONFLICT 1030 FT /note="P -> T (in Ref. 7; AAA52588)" FT /evidence="ECO:0000305" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 52..58 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:1TYE" FT STRAND 64..70 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 82..88 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 91..94 FT /evidence="ECO:0007829|PDB:7UCY" FT STRAND 107..110 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 113..118 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 126..131 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 134..139 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:2VDL" FT STRAND 159..165 FT /evidence="ECO:0007829|PDB:7UDH" FT TURN 166..169 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:7UDH" FT HELIX 183..188 FT /evidence="ECO:0007829|PDB:7UDH" FT TURN 189..193 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 202..206 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:7LA4" FT STRAND 211..216 FT /evidence="ECO:0007829|PDB:7UDH" FT HELIX 219..222 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 225..230 FT /evidence="ECO:0007829|PDB:7UDH" FT HELIX 231..237 FT /evidence="ECO:0007829|PDB:7UDH" FT HELIX 259..261 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 268..273 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 279..281 FT /evidence="ECO:0007829|PDB:7UJE" FT STRAND 283..288 FT /evidence="ECO:0007829|PDB:7UDH" FT HELIX 291..294 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 297..301 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 307..312 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 314..318 FT /evidence="ECO:0007829|PDB:7LA4" FT STRAND 324..327 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 330..333 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 336..341 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 345..348 FT /evidence="ECO:0007829|PDB:7UDH" FT TURN 349..351 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 352..355 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 358..362 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 366..368 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 375..379 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 391..398 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 400..402 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 404..409 FT /evidence="ECO:0007829|PDB:7UDH" FT TURN 413..416 FT /evidence="ECO:0007829|PDB:6V4P" FT STRAND 419..423 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 427..430 FT /evidence="ECO:0007829|PDB:1TYE" FT STRAND 435..439 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 450..456 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 465..470 FT /evidence="ECO:0007829|PDB:7UDH" FT HELIX 471..473 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 475..479 FT /evidence="ECO:0007829|PDB:7UDH" FT STRAND 484..493 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 507..509 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 512..525 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 534..541 FT /evidence="ECO:0007829|PDB:3FCS" FT TURN 542..544 FT /evidence="ECO:0007829|PDB:3FCS" FT HELIX 547..549 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 551..554 FT /evidence="ECO:0007829|PDB:3FCS" FT TURN 555..557 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 559..567 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 575..583 FT /evidence="ECO:0007829|PDB:3FCS" FT HELIX 586..588 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 596..603 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 616..619 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 622..627 FT /evidence="ECO:0007829|PDB:3FCS" FT TURN 634..637 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 643..651 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 653..655 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 662..670 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 678..683 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 688..695 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 705..708 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 710..713 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 715..721 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 728..738 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 746..755 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 759..761 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 767..774 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 779..792 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 810..819 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 821..823 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 825..836 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 842..854 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 856..861 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 906..909 FT /evidence="ECO:0007829|PDB:3FCS" FT TURN 911..913 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 916..926 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 931..940 FT /evidence="ECO:0007829|PDB:3FCS" FT HELIX 942..945 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 952..965 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 967..969 FT /evidence="ECO:0007829|PDB:3FCS" FT STRAND 977..988 FT /evidence="ECO:0007829|PDB:3FCS" FT TURN 991..994 FT /evidence="ECO:0007829|PDB:2KNC" FT STRAND 1019..1027 FT /evidence="ECO:0007829|PDB:7SC4" FT HELIX 1028..1031 FT /evidence="ECO:0007829|PDB:1DPK" FT TURN 1035..1038 FT /evidence="ECO:0007829|PDB:1DPQ" SQ SEQUENCE 1039 AA; 113377 MW; 063EE298E026F116 CRC64; MARALCPLQA LWLLEWVLLL LGPCAAPPAW ALNLDPVQLT FYAGPNGSQF GFSLDFHKDS HGRVAIVVGA PRTLGPSQEE TGGVFLCPWR AEGGQCPSLL FDLRDETRNV GSQTLQTFKA RQGLGASVVS WSDVIVACAP WQHWNVLEKT EEAEKTPVGS CFLAQPESGR RAEYSPCRGN TLSRIYVEND FSWDKRYCEA GFSSVVTQAG ELVLGAPGGY YFLGLLAQAP VADIFSSYRP GILLWHVSSQ SLSFDSSNPE YFDGYWGYSV AVGEFDGDLN TTEYVVGAPT WSWTLGAVEI LDSYYQRLHR LRGEQMASYF GHSVAVTDVN GDGRHDLLVG APLYMESRAD RKLAEVGRVY LFLQPRGPHA LGAPSLLLTG TQLYGRFGSA IAPLGDLDRD GYNDIAVAAP YGGPSGRGQV LVFLGQSEGL RSRPSQVLDS PFPTGSAFGF SLRGAVDIDD NGYPDLIVGA YGANQVAVYR AQPVVKASVQ LLVQDSLNPA VKSCVLPQTK TPVSCFNIQM CVGATGHNIP QKLSLNAELQ LDRQKPRQGR RVLLLGSQQA GTTLNLDLGG KHSPICHTTM AFLRDEADFR DKLSPIVLSL NVSLPPTEAG MAPAVVLHGD THVQEQTRIV LDCGEDDVCV PQLQLTASVT GSPLLVGADN VLELQMDAAN EGEGAYEAEL AVHLPQGAHY MRALSNVEGF ERLICNQKKE NETRVVLCEL GNPMKKNAQI GIAMLVSVGN LEEAGESVSF QLQIRSKNSQ NPNSKIVLLD VPVRAEAQVE LRGNSFPASL VVAAEEGERE QNSLDSWGPK VEHTYELHNN GPGTVNGLHL SIHLPGQSQP SDLLYILDIQ PQGGLQCFPQ PPVNPLKVDW GLPIPSPSPI HPAHHKRDRR QIFLPEPEQP SRLQDPVLVS CDSAPCTVVQ CDLQEMARGQ RAMVTVLAFL WLPSLYQRPL DQFVLQSHAW FNVSSLPYAV PPLSLPRGEA QVWTQLLRAL EERAIPIWWV LVGVLGGLLL LTILVLAMWK VGFFKRNRPP LEEDDEEGE //