ITA2B_HUMAN
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 03-AUG-2022, entry version 255.
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]
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 [29]
RP VARIANT HPA-3 (BAK).
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 [30]
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 [31]
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 [32]
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 [33]
RP VARIANT GT1 VAL-456-457-ASP DEL, AND CHARACTERIZATION OF VARIANT GT1
RP VAL-456-457-ASP 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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 [47]
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 [48]
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 [49]
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 [50]
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 [51]
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 [52]
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 [53]
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 -!- 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 ---------------------------------------------------------------------------
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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. [P08514-2]
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; 7LA4; EM; 3.30 A; A=1-1039.
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; 7LA4; -.
DR AlphaFoldDB; P08514; -.
DR BMRB; P08514; -.
DR SMR; P08514; -.
DR BioGRID; 109881; 19.
DR ComplexPortal; CPX-1799; Integrin alphaIIb-beta3 complex.
DR CORUM; P08514; -.
DR DIP; DIP-68N; -.
DR IntAct; P08514; 5.
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 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; P08514; -.
DR PeptideAtlas; P08514; -.
DR PRIDE; 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; 1958 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 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; 743479at2759; -.
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 1087 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 128 other tissues.
DR ExpressionAtlas; P08514; baseline and differential.
DR Genevisible; P08514; HS.
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: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: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 DisProt; DP01841; -.
DR Gene3D; 2.130.10.130; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
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:0000250|UniProtKB:P08648"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 461
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
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:2775232"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2775232"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:2775232"
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:2775232"
FT DISULFID 138..161
FT /evidence="ECO:0000269|PubMed:2775232"
FT DISULFID 177..198
FT /evidence="ECO:0000269|PubMed:2775232"
FT DISULFID 504..515
FT /evidence="ECO:0000269|PubMed:2775232"
FT DISULFID 521..576
FT /evidence="ECO:0000269|PubMed:2775232"
FT DISULFID 633..639
FT /evidence="ECO:0000269|PubMed:2775232"
FT DISULFID 705..718
FT /evidence="ECO:0000269|PubMed:2775232"
FT DISULFID 857..911
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000269|PubMed:2775232"
FT DISULFID 916..921
FT /evidence="ECO:0000269|PubMed:2775232"
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 alpha-
FT IIb/beta-3 and abrogates ligand binding to the activated
FT integrin)"
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 alpha-
FT IIb/beta-3)"
FT /evidence="ECO:0000269|PubMed:10607701"
FT /id="VAR_009886"
FT VARIANT 202
FT /note="F -> C (in GT1; associated with abrogation of alpha-
FT 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 alpha-
FT IIb/bet-3 is 28% of control; mutant pro-alpha-IIb subunit
FT is retained in the endoplasmic reticulum)"
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 alpha-
FT IIb/bet-3 is 11% of control; mutant pro-alpha-IIb subunit
FT 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 IIb/
FT 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 (alloantigen HPA-3B; dbSNP:rs5911)"
FT /evidence="ECO:0000269|PubMed:10391209"
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 pro-
FT 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 (ligand-
FT 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:3T3P"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1TYE"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3FCS"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2VDL"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:3T3P"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:3T3P"
FT TURN 189..193
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:7LA4"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3FCS"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:7LA4"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:3T3P"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:3T3P"
FT TURN 413..416
FT /evidence="ECO:0007829|PDB:6V4P"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:1TYE"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 450..456
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 465..470
FT /evidence="ECO:0007829|PDB:3T3P"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:3T3P"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:3T3P"
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 HELIX 997..1020
FT /evidence="ECO:0007829|PDB:2K1A"
FT STRAND 1022..1024
FT /evidence="ECO:0007829|PDB:1DPK"
FT TURN 1025..1027
FT /evidence="ECO:0007829|PDB:1DPK"
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
