[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3A). PubMed=3494014 [NCBI, ExPASy, EBI, Israel, Japan] Fitzgerald L.A., Steiner B., Rall S.C. Jr., Lo S., Phillips D.R.; "Protein sequence of endothelial glycoprotein IIIa derived from a cDNA clone. Identity with platelet glycoprotein IIIa and similarity to 'integrin'."; J. Biol. Chem. 262:3936-3939(1987).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3A). PubMed=2452834 [NCBI, ExPASy, EBI, Israel, Japan] Zimrin A.B., Eisman R., Vilaire G., Schwartz E., Bennett J.S., Poncz M.; "Structure of platelet glycoprotein IIIa. A common subunit for two different membrane receptors."; J. Clin. Invest. 81:1470-1475(1988).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3A). DOI=10.1007/BF00422712; PubMed=2345548 [NCBI, ExPASy, EBI, Israel, Japan] Frachet P., Uzan G., Thevenon D., Denarier E., Prandini M.H., Marguerie G.; "GPIIb and GPIIIa amino acid sequences deduced from human megakaryocyte cDNAs."; Mol. Biol. Rep. 14:27-33(1990).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3C). TISSUE=Osteoclastoma; DOI=10.1074/jbc.272.26.16390; PubMed=9195946 [NCBI, ExPASy, EBI, Israel, Japan] Kumar C.S., James I.E., Wong A., Mwangi V., Feild J.A., Nuthulaganti P., Connor J.R., Eichman C., Ali F., Hwang S.M., Rieman D.J., Drake F.H., Gowen M.; "Cloning and characterization of a novel integrin beta3 subunit."; J. Biol. Chem. 272:16390-16397(1997).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-3A). DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26. TISSUE=Blood; PubMed=8298129 [NCBI, ExPASy, EBI, Israel, Japan] Villa-Garcia M., Li L., Riely G., Bray P.F.; "Isolation and characterization of a TATA-less promoter for the human beta 3 integrin gene."; Blood 83:668-676(1994).
[7]	NUCLEOTIDE SEQUENCE [MRNA] OF 11-788. TISSUE=Erythroleukemia; PubMed=3165296 [NCBI, ExPASy, EBI, Israel, Japan] Rosa J.P., Bray P.F., Gayet O., Johnston G.I., Cook R.G., Jackson K.W., Shuman M.A., McEver R.P.; "Cloning of glycoprotein IIIa cDNA from human erythroleukemia cells and localization of the gene to chromosome 17."; Blood 72:593-600(1988).
[8]	PROTEIN SEQUENCE OF 27-37. TISSUE=Platelet; PubMed=1953640 [NCBI, ExPASy, EBI, Israel, Japan] Catimel B., Parmentier S., Leung L.L., McGregor J.L.; "Separation of important new platelet glycoproteins (GPIa, GPIc, GPIc*, GPIIa and GMP-140) by F.P.L.C. Characterization by monoclonal antibodies and gas-phase sequencing."; Biochem. J. 279:419-425(1991).
[9]	PROTEIN SEQUENCE OF 27-34. TISSUE=Platelet; DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan] Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.; "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."; Nat. Biotechnol. 21:566-569(2003).
[10]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-788. PubMed=2341395 [NCBI, ExPASy, EBI, Israel, Japan] Zimrin A.B., Gidwitz S., Lord S., Schwartz E., Bennett J.S., White G.C. II, Poncz M.; "The genomic organization of platelet glycoprotein IIIa."; J. Biol. Chem. 265:8590-8595(1990).
[11]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-788. PubMed=2145280 [NCBI, ExPASy, EBI, Israel, Japan] Lanza F., Kieffer N., Phillips D.R., Fitzgerald L.A.; "Characterization of the human platelet glycoprotein IIIa gene. Comparison with the fibronectin receptor beta-subunit gene."; J. Biol. Chem. 265:18098-18103(1990).
[12]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-120, AND VARIANTS PRO-59 AND ARG-66. TISSUE=Blood; Pascual C., Balas A., Garcia-Sanchez F., Rodriguez de la Rua A., Vicario J.L.; "A new exon II polymorphism in the platelet glycoprotein IIIa."; Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
[13]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-204. DOI=10.1093/intimm/4.9.1031; PubMed=1382574 [NCBI, ExPASy, EBI, Israel, Japan] Jiang W.-M., Jenkins D., Yuan Q., Leung E., Choo K.H., Watson J.D., Krissansen G.W.; "The gene organization of the human beta 7 subunit, the common beta subunit of the leukocyte integrins HML-1 and LPAM-1."; Int. Immunol. 4:1031-1040(1992).
[14]	PROTEIN SEQUENCE OF 218-234 AND 439-443. PubMed=3801670 [NCBI, ExPASy, EBI, Israel, Japan] Hiraiwa A., Matsukage A., Shiku H., Takahashi T., Naito K., Yamada K.; "Purification and partial amino acid sequence of human platelet membrane glycoproteins IIb and IIIa."; Blood 69:560-564(1987).
[15]	NUCLEOTIDE SEQUENCE [MRNA] OF 707-788 (ISOFORM BETA-3B). TISSUE=Placenta; DOI=10.1073/pnas.86.14.5415; PubMed=2787511 [NCBI, ExPASy, EBI, Israel, Japan] Van Kuppevelt T.H.M.S.M., Languino L.R., Gailit J.O., Suzuki S., Ruoslahti E.; "An alternative cytoplasmic domain of the integrin beta 3 subunit."; Proc. Natl. Acad. Sci. U.S.A. 86:5415-5418(1989).
[16]	PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS. PubMed=2001252 [NCBI, ExPASy, EBI, Israel, Japan] Calvete J.J., Henschen A., Gonzalez-Rodriguez J.; "Assignment of disulphide bonds in human platelet GPIIIa. A disulphide pattern for the beta-subunits of the integrin family."; Biochem. J. 274:63-71(1991).
[17]	INTERACTION WITH HIV-1 TAT. PubMed=10397733 [NCBI, ExPASy, EBI, Israel, Japan] Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S., Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.; "The Tat protein of human immunodeficiency virus type-1 promotes vascular cell growth and locomotion by engaging the alpha5beta1 and alphavbeta3 integrins and by mobilizing sequestered basic fibroblast growth factor."; Blood 94:663-672(1999).
[18]	INTERACTION WITH FLNB. TISSUE=Keratinocyte, and Skeletal muscle; DOI=10.1083/jcb.200103037; PubMed=11807098 [NCBI, ExPASy, EBI, Israel, Japan] van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T., Shapiro S.S., Sonnenberg A.; "Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin (beta) subunits."; J. Cell Biol. 156:361-376(2002).
[19]	PHOSPHORYLATION AT TYR-773 AND TYR-785 (ISOFORM BETA-3A). DOI=10.1074/jbc.271.18.10811; PubMed=8631894 [NCBI, ExPASy, EBI, Israel, Japan] Law D.A., Nannizzi-Alaimo L., Phillips D.R.; "Outside-in integrin signal transduction. Alpha IIb beta 3-(GP IIb IIIa) tyrosine phosphorylation induced by platelet aggregation."; J. Biol. Chem. 271:10811-10815(1996).
[20]	PHOSPHORYLATION AT THR-779. DOI=10.1074/jbc.M001908200; PubMed=10896934 [NCBI, ExPASy, EBI, Israel, Japan] Kirk R.I., Sanderson M.R., Lerea K.M.; "Threonine phosphorylation of the beta 3 integrin cytoplasmic tail, at a site recognized by PDK1 and Akt/PKB in vitro, regulates Shc binding."; J. Biol. Chem. 275:30901-30906(2000).
[21]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan] Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.; "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."; J. Proteome Res. 4:2070-2080(2005).
[22]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1074/mcp.M500324-MCP200; PubMed=16263699 [NCBI, ExPASy, EBI, Israel, Japan] Lewandrowski U., Moebius J., Walter U., Sickmann A.; "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."; Mol. Cell. Proteomics 5:226-233(2006).
[23]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-773 AND TYR-785, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan] Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.; "Phosphoproteome of resting human platelets."; J. Proteome Res. 7:526-534(2008).
[24]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-680, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan] Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."; J. Proteome Res. 8:651-661(2009).
[25]	X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 27-718. DOI=10.1126/science.1064535; PubMed=11546839 [NCBI, ExPASy, EBI, Israel, Japan] Xiong J.P., Stehle T., Diefenbach B., Zhang R., Dunker R., Scott D.L., Joachimiak A., Goodman S.L., Arnaout M.A.; "Crystal structure of the extracellular segment of integrin alpha Vbeta3."; Science 294:339-345(2001).
[26]	REVIEW ON GT VARIANTS. PubMed=7878622 [NCBI, ExPASy, EBI, Israel, Japan] Bray P.F.; "Inherited diseases of platelet glycoproteins: considerations for rapid molecular characterization."; Thromb. Haemost. 72:492-502(1994).
[27]	VARIANT HPA-1B PRO-59, AND DESCRIPTION OF ALLOANTIGEN SYSTEM PL(A). PubMed=2565345 [NCBI, ExPASy, EBI, Israel, Japan] Newman P.J., Derbes R.S., Aster R.H.; "The human platelet alloantigens, PlA1 and PlA2, are associated with a leucine33/proline33 amino acid polymorphism in membrane glycoprotein IIIa, and are distinguishable by DNA typing."; J. Clin. Invest. 83:1778-1781(1989).
[28]	VARIANT HPA-4B GLN-169, AND DESCRIPTION OF ALLOANTIGEN SYSTEM PEN. PubMed=1430225 [NCBI, ExPASy, EBI, Israel, Japan] Wang R., Furihata K., McFarland J.G., Friedman K., Aster R.H., Newman P.J.; "An amino acid polymorphism within the RGD binding domain of platelet membrane glycoprotein IIIa is responsible for the formation of the Pena/Penb alloantigen system."; J. Clin. Invest. 90:2038-2043(1992).
[29]	VARIANT MO(+) ALA-433. PubMed=8093349 [NCBI, ExPASy, EBI, Israel, Japan] Kuijpers R.W.A.M., Simsek S., Faber N.M., Goldschmeding R., van Wermerkerken R.K.V., von Dem Borne A.E.G.K.; "Single point mutation in human glycoprotein IIIa is associated with a new platelet-specific alloantigen (Mo) involved in neonatal alloimmune thrombocytopenia."; Blood 81:70-76(1993).
[30]	VARIANT CA(+)/TU(+) GLN-515, AND DESCRIPTION OF ALLOANTIGEN SYSTEM CA/TU. PubMed=7694683 [NCBI, ExPASy, EBI, Israel, Japan] Wang R., McFarland J.G., Kekomaki R., Newman P.J.; "Amino acid 489 is encoded by a mutational 'hot spot' on the beta 3 integrin chain: the CA/TU human platelet alloantigen system."; Blood 82:3386-3391(1993).
[31]	VARIANT SR(A) CYS-662, AND DESCRIPTION OF ALLOANTIGEN SYSTEM SR(A). PubMed=8132570 [NCBI, ExPASy, EBI, Israel, Japan] Santoso S., Kalb R., Kroll H., Walka M., Kiefel V., Mueller-Eckhardt C., Newman P.J.; "A point mutation leads to an unpaired cysteine residue and a molecular weight polymorphism of a functional platelet beta 3 integrin subunit. The Sra alloantigen system of GPIIIa."; J. Biol. Chem. 269:8439-8444(1994).
[32]	VARIANT GT TYR-145. DOI=10.1126/science.2392682; PubMed=2392682 [NCBI, ExPASy, EBI, Israel, Japan] Loftus J.C., O'Toole T.E., Plow E.F., Glass A., Frelinger A.L. III, Ginsberg M.H.; "A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation."; Science 249:915-918(1990).
[33]	VARIANT GT GLN-240. PubMed=1371279 [NCBI, ExPASy, EBI, Israel, Japan] Bajt M.L., Ginsberg M.H., Frelinger A.L. III, Berndt M.C., Loftus J.C.; "A spontaneous mutation of integrin alpha IIb beta 3 (platelet glycoprotein IIb-IIIa) helps define a ligand binding site."; J. Biol. Chem. 267:3789-3794(1992).
[34]	VARIANT GT TRP-240. PubMed=1602006 [NCBI, ExPASy, EBI, Israel, Japan] Lanza F., Stierle A., Fournier D., Morales M., Andre G., Nurden A.T., Cazenave J.-P.; "A new variant of Glanzmann's thrombasthenia (Strasbourg I). Platelets with functionally defective glycoprotein IIb-IIIa complexes and a glycoprotein IIIa 214Arg-->214Trp mutation."; J. Clin. Invest. 89:1995-2004(1992).
[35]	VARIANT GT PRO-778. DOI=10.1073/pnas.89.21.10169; PubMed=1438206 [NCBI, ExPASy, EBI, Israel, Japan] Chen Y.-P., Djaffar I., Pidard D., Steiner B., Cieutat A.-M., Caen J.P., Rosa J.-P.; "Ser-752-->Pro mutation in the cytoplasmic domain of integrin beta 3 subunit and defective activation of platelet integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) in a variant of Glanzmann thrombasthenia."; Proc. Natl. Acad. Sci. U.S.A. 89:10169-10173(1992).
[36]	VARIANT GT TYR-400. PubMed=8781422 [NCBI, ExPASy, EBI, Israel, Japan] Grimaldi C.M., Chen F., Scudder L.E., Coller B.S., French D.L.; "A Cys374Tyr homozygous mutation of platelet glycoprotein IIIa (beta 3) in a Chinese patient with Glanzmann's thrombasthenia."; Blood 88:1666-1675(1996).
[37]	VARIANT GT TRP-143. PubMed=9376589 [NCBI, ExPASy, EBI, Israel, Japan] Basani R.B., Brown D.L., Vilaire G., Bennett J.S., Poncz M.; "A Leu117-->Trp mutation within the RGD-peptide cross-linking region of beta3 results in Glanzmann thrombasthenia by preventing alphaIIb beta3 export to the platelet surface."; Blood 90:3082-3088(1997).
[38]	VARIANTS GT ASN-145; GLN-242 AND PRO-288. DOI=10.1006/bcmd.1997.0117; PubMed=9215749 [NCBI, ExPASy, EBI, Israel, Japan] French D.L., Coller B.S.; "Hematologically important mutations: Glanzmann thrombasthenia."; Blood Cells Mol. Dis. 23:39-51(1997).
[39]	VARIANTS GT PRO-306; PHE-586; SER-598 AND SER-605. DOI=10.1006/bbrc.1998.9526; PubMed=9790984 [NCBI, ExPASy, EBI, Israel, Japan] Ambo H., Kamata T., Handa M., Taki M., Kuwajima M., Kawai Y., Oda A., Murata M., Takada Y., Watanabe K., Ikeda Y.; "Three novel integrin beta3 subunit missense mutations (H280P, C560F, and G579S) in thrombasthenia, including one (H280P) prevalent in Japanese patients."; Biochem. Biophys. Res. Commun. 251:763-768(1998).
[40]	VARIANT GT LEU-188. PubMed=9684783 [NCBI, ExPASy, EBI, Israel, Japan] Jackson D.E., White M.M., Jennings L.K., Newman P.J.; "A Ser162-->Leu mutation within glycoprotein (GP) IIIa (integrin beta3) results in an unstable alphaIIbbeta3 complex that retains partial function in a novel form of type II Glanzmann thrombasthenia."; Thromb. Haemost. 80:42-48(1998).
[41]	VARIANT GT ARG-568. DOI=10.1046/j.1365-2141.1999.01376.x; PubMed=10233432 [NCBI, ExPASy, EBI, Israel, Japan] Ruan J., Schmugge M., Clemetson K.J., Cazes E., Combrie R., Bourre F., Nurden A.T.; "Homozygous Cys542-->Arg substitution in GPIIIa in a Swiss patient with type I Glanzmann's thrombasthenia."; Br. J. Haematol. 105:523-531(1999).
[42]	VARIANTS PRO-59; GLN-169 AND ILE-453. DOI=10.1038/10290; PubMed=10391209 [NCBI, ExPASy, EBI, Israel, Japan] Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.; "Characterization of single-nucleotide polymorphisms in coding regions of human genes."; Nat. Genet. 22:231-238(1999).
[43]	ERRATUM. Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.; Nat. Genet. 23:373-373(1999).
[44]	VARIANT GT ARG-586, AND CHARACTERIZATION OF VARIANT GT ARG-586. DOI=10.1182/blood.V98.8.2432; PubMed=11588040 [NCBI, ExPASy, EBI, Israel, Japan] Ruiz C., Liu C.-Y., Sun Q.-H., Sigaud-Fiks M., Fressinaud E., Muller J.-Y., Nurden P., Nurden A.T., Newman P.J., Valentin N.; "A point mutation in the cysteine-rich domain of glycoprotein (GP) IIIa results in the expression of a GPIIb-IIIa (alphaIIbbeta3) integrin receptor locked in a high-affinity state and a Glanzmann thrombasthenia-like phenotype."; Blood 98:2432-2441(2001).
[45]	VARIANT ILE-166, AND CHARACTERIZATION OF VARIANT ILE-166. DOI=10.1182/blood.V99.12.4449; PubMed=12036875 [NCBI, ExPASy, EBI, Israel, Japan] Jallu V., Meunier M., Brement M., Kaplan C.; "A new platelet polymorphism Duv(a+), localized within the RGD binding domain of glycoprotein IIIa, is associated with neonatal thrombocytopenia."; Blood 99:4449-4456(2002).
[46]	VARIANT GT PRO-222. DOI=10.1080/09537100220122466; PubMed=11897046 [NCBI, ExPASy, EBI, Israel, Japan] Nurden A.T., Ruan J., Pasquet J.-M., Gauthier B., Combrie R., Kunicki T., Nurden P.; "A novel 196Leu to Pro substitution in the beta3 subunit of the alphaIIbbeta3 integrin in a patient with a variant form of Glanzmann thrombasthenia."; Platelets 13:101-111(2002).
[47]	VARIANTS GT TRP-119; VAL-243 AND ARG-601. PubMed=12083483 [NCBI, ExPASy, EBI, Israel, Japan] D'Andrea G., Colaizzo D., Vecchione G., Grandone E., Di Minno G., Margaglione M.; "Glanzmann's thrombasthenia: identification of 19 new mutations in 30 patients."; Thromb. Haemost. 87:1034-1042(2002).
[48]	VARIANT GT TYR-532. DOI=10.1267/THRO88030503; PubMed=12353082 [NCBI, ExPASy, EBI, Israel, Japan] Nair S., Li J., Mitchell W.B., Mohanty D., Coller B.S., French D.L.; "Two new beta3 integrin mutations in Indian patients with Glanzmann thrombasthenia: localization of mutations affecting cysteine residues in integrin beta3."; Thromb. Haemost. 88:503-509(2002).
[49]	VARIANT GT VAL-150, AND CHARACTERIZATION OF VARIANT GT VAL-150. DOI=10.1267/THRO04061377; PubMed=15583747 [NCBI, ExPASy, EBI, Israel, Japan] Gonzalez-Manchon C., Butta N., Larrucea S., Arias-Salgado E.G., Alonso S., Lopez A., Parrilla R.; "A variant thrombasthenic phenotype associated with compound heterozygosity of integrin beta3-subunit: (Met124Val)beta3 alters the subunit dimerization rendering a decreased number of constitutive active alphaIIbbeta3 receptors."; Thromb. Haemost. 92:1377-1386(2004).
[50]	VARIANTS GT PRO-306 AND ASN-330, AND CHARACTERIZATION OF VARIANT GT ASN-330. DOI=10.1111/j.1538-7836.2004.00990.x; PubMed=15634267 [NCBI, ExPASy, EBI, Israel, Japan] Tanaka S., Hayashi T., Yoshimura K., Nakayama M., Fujita T., Amano T., Tani Y.; "Double heterozygosity for a novel missense mutation of Ile304 to Asn in addition to the missense mutation His280 to Pro in the integrin beta3 gene as a cause of the absence of platelet alphaIIbbeta3 in Glanzmann's thrombasthenia."; J. Thromb. Haemost. 3:68-73(2005).
[51]	VARIANTS GT CYS-141 AND LEU-321. DOI=10.1111/j.1538-7836.2005.01159.x; PubMed=15748237 [NCBI, ExPASy, EBI, Israel, Japan] Nair S., Ghosh K., Shetty S., Mohanty D.; "Mutations in GPIIIa molecule as a cause for Glanzmann thrombasthenia in Indian patients."; J. Thromb. Haemost. 3:482-488(2005).

Comments

FUNCTION: Integrin alpha-V/beta-3 is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.
SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-3 associates with either alpha-IIb or alpha-V. Isoform Beta-3C interacts with FLNB. Interacts with HIV-1 Tat.
INTERACTION:
Self; NbExp=3; IntAct=EBI-702847, EBI-702847;
P06935:- (xeno); NbExp=2; IntAct=EBI-702847, EBI-981051;
P06756:ITGAV; NbExp=3; IntAct=EBI-702847, EBI-298282;
P54939:TLN1 (xeno); NbExp=1; IntAct=EBI-702847, EBI-1035421;
P26039:Tln1 (xeno); NbExp=1; IntAct=EBI-702847, EBI-1039593;
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	Beta-3A
Isoform ID	P05106-1
This is the isoform sequence displayed in this entry.

Name	Beta-3B
Isoform ID	P05106-2
Features which should be applied to build the isoform sequence: VSP_002745.

Name	Beta-3C
Isoform ID	P05106-3
Features which should be applied to build the isoform sequence: VSP_002746.

TISSUE SPECIFICITY: Isoform beta-3A and isoform beta-3C are widely expressed. Isoform beta-3A is specifically expressed in osteoblast cells; isoform beta-3C is specifically expressed in prostate and testis.
PTM: Phosphorylated on tyrosine residues in response to thrombin-induced platelet aggregation. Probably involved in outside-in signaling. A peptide (AA 740-762) is capable of binding GRB2 only when both Tyr-773 and Tyr-785 are phosphorylated. Phosphorylation of Thr-779 inhibits SHC binding.
POLYMORPHISM: Position 59 is associated with platelet-specific alloantigen HPA-1 (ZW or PL(A)). HPA-1A/ZW(A)/PL(A1) has Leu-59 and HPA-1B/ZW(B)/PL(A2) has Pro-59.
POLYMORPHISM: Position 169 is associated with platelet-specific alloantigen HPA-4 (PEN or YUK). HPA-4A/PEN(A)/YUK(A) has Arg-169 and HPA-4B/PEN(B)/YUK(B) has Gln-169. HPA-4B is involved in neonatal alloimmune thrombocytopenia (NAIT or NATP).
POLYMORPHISM: Position 433 is associated with platelet-specific alloantigen MO. MO(-) has Pro-433 and MO(+) has Ala-433. MO(+) is involved in NAIT.
POLYMORPHISM: Position 515 is associated with platelet-specific alloantigen CA/TU. CA(-)/TU(-) has Arg-515 and CA(+)/TU(+) has Gln-515. CA(+) is involved in NAIT.
POLYMORPHISM: Position 662 is associated with platelet-specific alloantigen SR(A). SR(A)(-) has Arg-662 and SR(A)(+) has Cys-662.
DISEASE: Defects in ITGB3 are a cause of Glanzmann thrombasthenia (GT) [MIM:273800]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. Its inheritance is autosomal recessive. It is characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb-IIIa complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the GPIIb-IIIa complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT variants have normal or near normal (60-100%) expression of dysfunctional receptors.
SIMILARITY: Belongs to the integrin beta chain family.
SIMILARITY: Contains 1 VWFA domain.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ITGB3";.
WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=ITGB3";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J02703; AAA52589.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M20311; AAA60122.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M35999; AAA35927.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U95204; AAB71380.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC127666; AAI27667.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC127667; AAI27668.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L28832; AAA20880.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32686; AAA67537.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32667; AAA67537.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32672; AAA67537.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32673; AAA67537.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32674; AAA67537.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32675; AAA67537.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32680; AAA67537.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32681; AAA67537.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32682; AAA67537.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32685; AAA67537.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57494; AAA52600.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57481; AAA52600.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57482; AAA52600.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57483; AAA52600.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57484; AAA52600.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57485; AAA52600.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57486; AAA52600.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57487; AAA52600.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57488; AAA52600.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57489; AAA52600.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57490; AAA52600.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57491; AAA52600.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57492; AAA52600.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57493; AAA52600.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03881; AAA16076.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S49379; AAB23689.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M25108; AAA36121.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00220350; -.
IPI00220351; -.
IPI00303283; -.

PIR

A26547; A26547.
A60798; A60798.
B36268; B36268.
I77349; I77349.
S14324; S14324.

RefSeq

NP_000203.2; -.

UniGene

Hs.218040

3D structure databases

PDB

1JV2; X-ray; 3.10 A; B=27-718.	[ExPASy / RCSB / EBI]
1KUP; NMR; -; B=742-766.	[ExPASy / RCSB / EBI]
1KUZ; NMR; -; B=742-766.	[ExPASy / RCSB / EBI]
1L5G; X-ray; 3.20 A; B=27-718.	[ExPASy / RCSB / EBI]
1M1X; X-ray; 3.30 A; B=27-718.	[ExPASy / RCSB / EBI]
1M8O; NMR; -; B=742-788.	[ExPASy / RCSB / EBI]
1MK7; X-ray; 2.20 A; A/C=765-775.	[ExPASy / RCSB / EBI]
1MK9; X-ray; 2.80 A; A/C/E/G=765-776.	[ExPASy / RCSB / EBI]
1RN0; Model; -; B=135-378.	[ExPASy / RCSB / EBI]
1S4X; NMR; -; A=742-788.	[ExPASy / RCSB / EBI]
1TYE; X-ray; 2.90 A; B/D/F=27-466.	[ExPASy / RCSB / EBI]
1U8C; X-ray; 3.10 A; B=27-718.	[ExPASy / RCSB / EBI]
2INI; Model; -; B=81-460, B=558-716.	[ExPASy / RCSB / EBI]
2K9J; NMR; -; B=711-753.	[ExPASy / RCSB / EBI]
2Q6W; X-ray; 2.25 A; C/F=50-61.	[ExPASy / RCSB / EBI]
2RMZ; NMR; -; A=711-753.	[ExPASy / RCSB / EBI]
2RN0; NMR; -; A=711-753.	[ExPASy / RCSB / EBI]
2VC2; X-ray; 3.10 A; B=27-487.	[ExPASy / RCSB / EBI]
2VDK; X-ray; 2.80 A; B=27-487.	[ExPASy / RCSB / EBI]
2VDL; X-ray; 2.75 A; B=27-487.	[ExPASy / RCSB / EBI]
2VDM; X-ray; 2.90 A; B=27-487.	[ExPASy / RCSB / EBI]
2VDN; X-ray; 2.90 A; B=27-487.	[ExPASy / RCSB / EBI]
2VDO; X-ray; 2.51 A; B=27-487.	[ExPASy / RCSB / EBI]
2VDP; X-ray; 2.80 A; B=27-487.	[ExPASy / RCSB / EBI]
2VDQ; X-ray; 2.59 A; B=27-487.	[ExPASy / RCSB / EBI]
2VDR; X-ray; 2.40 A; B=27-487.	[ExPASy / RCSB / EBI]
3FCS; X-ray; 2.55 A; B/D=27-716.	[ExPASy / RCSB / EBI]
3FCU; X-ray; 2.90 A; B/D/F=27-487.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1JV2; -.
1KUP; -.
1KUZ; -.
1L5G; -.
1M1X; -.
1M8O; -.
1MK7; -.
1MK9; -.
1RN0; -.
1S4X; -.
1TYE; -.
1U8C; -.
2INI; -.
2K9J; -.
2Q6W; -.
2RMZ; -.
2RN0; -.
2VC2; -.
2VDK; -.
2VDL; -.
2VDM; -.
2VDN; -.
2VDO; -.
2VDP; -.
2VDQ; -.
2VDR; -.
3FCS; -.
3FCU; -.

ModBase

P05106.

Protein-protein interaction databases

DIP

DIP:304N; -.

IntAct

P05106; 7.

PTM databases

PhosphoSite

P05106; -.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6cyclingpathway; Arf6 signaling events.
ephrinbrevpathway; Ephrin B reverse signaling.
il4_2pathway; IL4-mediated signaling events.
avb3_integrin_pathway; Integrins in angiogenesis.
avb3_opn_pathway; Osteopontin-mediated events.
s1p_s1p1_pathway; S1P1 pathway.
s1p_s1p3_pathway; S1P3 pathway.
ptp1bpathway; Signaling events mediated by PTP1B.
vegfr1_2_pathway; Signaling events mediated by VEGFR1 and VEGFR2.

Reactome

REACT_13552; Integrin cell surface interactions.
REACT_604; Hemostasis.
REACT_6900; Signaling in Immune system.

Organism-specific databases

GC17P042686; -.

HIX0039255; -.

HGNC:6156; ITGB3.

CAB002501; -.

173470; gene+phenotype. [NCBI / EBI]
273800; phenotype. [NCBI / EBI]

Orphanet

849; Glanzmann thrombasthenia.
140957; Macrothrombocytopenia with abnormal proplatelet formation, autosomal dominant.

PharmGKB

PA205; -.

Gene expression databases

P05106; -.

P05106; -.

HS_ITGB3; -.

ENSG00000056345; Homo sapiens.

Ontologies

GO:0008305;	Cellular component: integrin complex (inferred from direct assay from UniProtKB).
GO:0031092;	Cellular component: platelet alpha granule membrane (inferred from experiment from Reactome).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0004872;	Molecular function: receptor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0007596;	Biological process: blood coagulation (traceable author statement from ProtInc).
GO:0007160;	Biological process: cell-matrix adhesion (inferred from electronic annotation from InterPro).
GO:0007229;	Biological process: integrin-mediated signaling pathway (inferred from electronic annotation from UniProtKB-KW).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0010745;	Biological process: negative regulation of foam cell differentiation (inferred from mutant phenotype from UniProtKB).
GO:0010888;	Biological process: negative regulation of lipid storage (inferred from mutant phenotype from UniProtKB).
GO:0032369;	Biological process: negative regulation of lipid transport (inferred from mutant phenotype from UniProtKB).
GO:0050748;	Biological process: negative regulation of lipoprotein metabolic process (inferred from mutant phenotype from UniProtKB).
GO:0045715;	Biological process: negative regulation of low-density lipoprotein receptor biosynthetic process (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR013032; EGF-like_reg_CS.
IPR013111; EGF_extracell.
IPR015812; Integrin_bsu.
IPR015435; Integrin_bsu-3_C.
IPR001169; Integrin_bsu_C.
IPR014836; Integrin_bsu_cyt.
IPR002369; Integrin_bsu_N.
IPR012012; Integrin_bsu_subgr.
IPR012896; Integrin_bsu_tail.
IPR003659; Plexin-like.
IPR002035; VWF_A.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.5.630; Integrin_bsu_cyt; 1.

PANTHER

PTHR10082; Integrin_beta_C; 1.
PTHR10082:SF10; Integrin_bsu-3_C; 1.

Pfam

PF07974; EGF_2; 3.
PF08725; Integrin_b_cyt; 1.
PF07965; Integrin_B_tail; 1.
PF00362; Integrin_beta; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF002512; Integrin_B; 1.

PRINTS

PR01186; INTEGRINB.

SMART

SM00187; INB; 1.
SM00423; PSI; 1.
SM00327; VWA; 1.
SMART graphical view of domain structure.

PROSITE

PS00022; EGF_1; UNKNOWN_2.
PS01186; EGF_2; UNKNOWN_1.
PS00243; INTEGRIN_BETA; 3.
PS50234; VWFA; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P05106; -.

Genome annotation databases

Ensembl

ENSG00000056345; Homo sapiens. [Contig view]

GeneID

3690; -.

KEGG

hsa:3690; -.

Phylogenomic databases

HOVERGEN

P05106; -.

OMA

P05106; CGPGWLG.

Other

DrugBank

DB00054; Abciximab.
DB00775; Tirofiban.

14453; -.

P05106; -.

ITGB3; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Cell adhesion; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Host-virus interaction; Integrin; Membrane; Phosphoprotein; Polymorphism; Receptor; Repeat; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 26`	`26`	`Potential.`
`CHAIN`	`27 788`	`762`	`Integrin beta-3.`	`PRO_0000016344`
`TOPO_DOM`	`27 718`	`692`	`Extracellular (Potential).`
`TRANSMEM`	`719 741`	`23`	`Potential.`
`TOPO_DOM`	`742 788`	`47`	`Cytoplasmic (Potential).`
`DOMAIN`	`135 377`	`243`	`VWFA.`
`REPEAT`	`463 511`	`49`	`I.`
`REPEAT`	`512 553`	`42`	`II.`
`REPEAT`	`554 592`	`39`	`III.`
`REPEAT`	`593 629`	`37`	`IV.`
`REGION`	`463 629`	`167`	`Cysteine-rich tandem repeats.`
`MOD_RES`	`773 773`		`Phosphotyrosine.`
`MOD_RES`	`779 779`		`Phosphothreonine; by PDPK1 and PKB/AKT1; in vitro.`
`MOD_RES`	`785 785`		`Phosphotyrosine.`
`CARBOHYD`	`125 125`		`N-linked (GlcNAc...).`
`CARBOHYD`	`346 346`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`397 397`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`478 478`		`N-linked (GlcNAc...).`
`CARBOHYD`	`585 585`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`680 680`		`N-linked (GlcNAc...).`
`DISULFID`	`31 461`
`DISULFID`	`39 49`
`DISULFID`	`42 75`
`DISULFID`	`52 64`
`DISULFID`	`203 210`
`DISULFID`	`258 299`
`DISULFID`	`400 412`
`DISULFID`	`432 681`
`DISULFID`	`459 463`
`DISULFID`	`474 486`		`Probable.`
`DISULFID`	`483 521`		`Probable.`
`DISULFID`	`488 497`		`Probable.`
`DISULFID`	`499 512`		`Probable.`
`DISULFID`	`527 532`		`Probable.`
`DISULFID`	`529 562`		`Probable.`
`DISULFID`	`534 547`		`Probable.`
`DISULFID`	`549 554`
`DISULFID`	`568 573`		`Probable.`
`DISULFID`	`570 601`		`Probable.`
`DISULFID`	`575 584`		`Probable.`
`DISULFID`	`586 593`		`Probable.`
`DISULFID`	`607 612`		`Probable.`
`DISULFID`	`609 657`		`Probable.`
`DISULFID`	`614 624`		`Probable.`
`DISULFID`	`627 630`		`Probable.`
`DISULFID`	`634 643`		`Probable.`
`DISULFID`	`640 713`		`Probable.`
`DISULFID`	`661 689`
`VAR_SEQ`	`768 788`		`ANNPLYKEATSTFTNITYRGT -> VRDGAGRFLKSLV (in isoform Beta-3B).`	`VSP_002745`
`VAR_SEQ`	`768 788`		`ANNPLYKEATSTFTNITYRGT -> HYAQSLRKWNQPVSIDG (in isoform Beta-3C).`	`VSP_002746`
`VARIANT`	`59 59`	`1`	`L -> P (in alloantigen HPA-1B; dbSNP:rs5918 [NCBI]).`	`VAR_003993`
`VARIANT`	`66 66`	`1`	`L -> R (in dbSNP:rs36080296 [NCBI]).`	`VAR_049633`
`VARIANT`	`119 119`	`1`	`R -> W (in GT).`	`VAR_030473`
`VARIANT`	`141 141`	`1`	`Y -> C (in GT).`	`VAR_030474`
`VARIANT`	`143 143`	`1`	`L -> W (in GT).`	`VAR_010649`
`VARIANT`	`145 145`	`1`	`D -> N (in GT).`	`VAR_030475`
`VARIANT`	`145 145`	`1`	`D -> Y (in GT; type B).`	`VAR_003998`
`VARIANT`	`150 150`	`1`	`M -> V (in GT; may confer constitutive activity to the alpha-IIb/(mutated)beta-3 receptor).`	`VAR_030476`
`VARIANT`	`166 166`	`1`	`T -> I (associated with neonatal thrombocytopenia; alloantigen Duv(a+); does not affect significantly the integrin function).`	`VAR_030477`
`VARIANT`	`169 169`	`1`	`R -> Q (in alloantigen HPA-4B; dbSNP:rs5917 [NCBI]).`	`VAR_003994`
`VARIANT`	`188 188`	`1`	`S -> L (in GT; type II).`	`VAR_010651`
`VARIANT`	`222 222`	`1`	`L -> P (in GT; variant form).`	`VAR_030478`
`VARIANT`	`240 240`	`1`	`R -> Q (in GT; type B).`	`VAR_003999`
`VARIANT`	`240 240`	`1`	`R -> W (in GT; variant Strasbourg-1).`	`VAR_004000`
`VARIANT`	`242 242`	`1`	`R -> Q (in GT).`	`VAR_030479`
`VARIANT`	`243 243`	`1`	`D -> V (in GT).`	`VAR_030480`
`VARIANT`	`288 288`	`1`	`L -> P (in GT).`	`VAR_030481`
`VARIANT`	`306 306`	`1`	`H -> P (in GT; dbSNP:rs13306476 [NCBI]).`	`VAR_004001`
`VARIANT`	`321 321`	`1`	`M -> L (in GT).`	`VAR_030482`
`VARIANT`	`330 330`	`1`	`I -> N (in GT; not expressed on the surface and absent inside the transfected cells).`	`VAR_030483`
`VARIANT`	`400 400`	`1`	`C -> Y (in GT).`	`VAR_004002`
`VARIANT`	`433 433`	`1`	`P -> A (in alloantigen MO(+); in a case of neonatal alloimmune thrombocytopenia).`	`VAR_003995`
`VARIANT`	`453 453`	`1`	`V -> I (in dbSNP:rs5921 [NCBI]).`	`VAR_014178`
`VARIANT`	`515 515`	`1`	`R -> Q (in alloantigen CA(+)/TU(+); dbSNP:rs13306487 [NCBI]).`	`VAR_003996`
`VARIANT`	`532 532`	`1`	`C -> Y (in GT).`	`VAR_030484`
`VARIANT`	`568 568`	`1`	`C -> R (in GT; type I).`	`VAR_010671`
`VARIANT`	`586 586`	`1`	`C -> F (in GT).`	`VAR_004003`
`VARIANT`	`586 586`	`1`	`C -> R (in GT; gain-of-function mutation; constitutively binds ligand-induced binding sites antibodies and the fibrinogen-mimetic antibody PAC-1).`	`VAR_030485`
`VARIANT`	`598 598`	`1`	`G -> S (in GT).`	`VAR_004004`
`VARIANT`	`601 601`	`1`	`C -> R (in GT).`	`VAR_030486`
`VARIANT`	`605 605`	`1`	`G -> S (in GT; type II).`	`VAR_010672`
`VARIANT`	`662 662`	`1`	`R -> C (in alloantigen SR(A)).`	`VAR_003997`
`VARIANT`	`778 778`	`1`	`S -> P (in GT; variant Strasbourg-1).`	`VAR_004005`
`CONFLICT`	`12 12`		`A -> V (in Ref. 1; AAA52589 and 3; AAA35927).`
`CONFLICT`	`151 151`		`K -> P (in Ref. 10; AAA67537 and 13; AAB23689).`
`CONFLICT`	`205 205`		`D -> EY (in Ref. 10; AAA67537).`
`CONFLICT`	`649 653`		`GALHD -> EPYMT (in Ref. 1; AAA52589, 2; AAA60122 and 4; AAB71380).`
`CONFLICT`	`716 716`		`G -> H (in Ref. 7).`
`CONFLICT`	`737 741`		`ALLIW -> PCSSG (in Ref. 10; AAA67537).`
`TURN`	`30 34`	`5`
`HELIX`	`39 43`	`5`
`STRAND`	`49 52`	`4`
`STRAND`	`55 57`	`3`
`STRAND`	`63 66`	`4`
`HELIX`	`67 72`	`6`
`HELIX`	`77 79`	`3`
`STRAND`	`102 104`	`3`
`STRAND`	`112 118`	`7`
`STRAND`	`123 126`	`4`
`STRAND`	`129 131`	`3`
`STRAND`	`138 145`	`8`
`HELIX`	`148 150`	`3`
`TURN`	`151 157`	`7`
`HELIX`	`162 169`	`8`
`STRAND`	`173 182`	`10`
`TURN`	`188 192`	`5`
`STRAND`	`194 196`	`3`
`HELIX`	`197 199`	`3`
`STRAND`	`205 207`	`3`
`STRAND`	`215 217`	`3`
`STRAND`	`222 224`	`3`
`HELIX`	`228 234`	`7`
`STRAND`	`242 246`	`5`
`HELIX`	`249 257`	`9`
`HELIX`	`259 262`	`4`
`STRAND`	`266 278`	`13`
`HELIX`	`285 287`	`3`
`TURN`	`288 290`	`3`
`HELIX`	`308 311`	`4`
`HELIX`	`318 327`	`10`
`STRAND`	`330 337`	`8`
`HELIX`	`338 340`	`3`
`HELIX`	`341 348`	`8`
`STRAND`	`355 359`	`5`
`HELIX`	`364 366`	`3`
`HELIX`	`367 377`	`11`
`STRAND`	`383 386`	`4`
`STRAND`	`390 392`	`3`
`STRAND`	`420 422`	`3`
`STRAND`	`425 431`	`7`
`STRAND`	`439 444`	`6`
`STRAND`	`452 457`	`6`
`STRAND`	`579 584`	`6`
`HELIX`	`600 603`	`4`
`STRAND`	`605 608`	`4`
`STRAND`	`611 614`	`4`
`HELIX`	`633 635`	`3`
`HELIX`	`638 641`	`4`
`TURN`	`642 646`	`5`
`TURN`	`650 652`	`3`
`STRAND`	`653 655`	`3`
`TURN`	`658 660`	`3`
`STRAND`	`665 671`	`7`
`STRAND`	`676 680`	`5`
`STRAND`	`693 695`	`3`
`TURN`	`699 701`	`3`
`STRAND`	`705 710`	`6`
`TURN`	`743 759`	`17`
`HELIX`	`771 774`	`4`

Sequence information

Length: 788 AA [This is the length of the unprocessed precursor]

Molecular weight: 87058 Da [This is the MW of the unprocessed precursor]

CRC64: F246623608E05F9E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRARPRPRPL WATVLALGAL AGVGVGGPNI CTTRGVSSCQ QCLAVSPMCA WCSDEALPLG 

        70         80         90        100        110        120 
SPRCDLKENL LKDNCAPESI EFPVSEARVL EDRPLSDKGS GDSSQVTQVS PQRIALRLRP 

       130        140        150        160        170        180 
DDSKNFSIQV RQVEDYPVDI YYLMDLSYSM KDDLWSIQNL GTKLATQMRK LTSNLRIGFG 

       190        200        210        220        230        240 
AFVDKPVSPY MYISPPEALE NPCYDMKTTC LPMFGYKHVL TLTDQVTRFN EEVKKQSVSR 

       250        260        270        280        290        300 
NRDAPEGGFD AIMQATVCDE KIGWRNDASH LLVFTTDAKT HIALDGRLAG IVQPNDGQCH 

       310        320        330        340        350        360 
VGSDNHYSAS TTMDYPSLGL MTEKLSQKNI NLIFAVTENV VNLYQNYSEL IPGTTVGVLS 

       370        380        390        400        410        420 
MDSSNVLQLI VDAYGKIRSK VELEVRDLPE ELSLSFNATC LNNEVIPGLK SCMGLKIGDT 

       430        440        450        460        470        480 
VSFSIEAKVR GCPQEKEKSF TIKPVGFKDS LIVQVTFDCD CACQAQAEPN SHRCNNGNGT 

       490        500        510        520        530        540 
FECGVCRCGP GWLGSQCECS EEDYRPSQQD ECSPREGQPV CSQRGECLCG QCVCHSSDFG 

       550        560        570        580        590        600 
KITGKYCECD DFSCVRYKGE MCSGHGQCSC GDCLCDSDWT GYYCNCTTRT DTCMSSNGLL 

       610        620        630        640        650        660 
CSGRGKCECG SCVCIQPGSY GDTCEKCPTC PDACTFKKEC VECKKFDRGA LHDENTCNRY 

       670        680        690        700        710        720 
CRDEIESVKE LKDTGKDAVN CTYKNEDDCV VRFQYYEDSS GKSILYVVEE PECPKGPDIL 

       730        740        750        760        770        780 
VVLLSVMGAI LLIGLAALLI WKLLITIHDR KEFAKFEEER ARAKWDTANN PLYKEATSTF 


TNITYRGT

P05106 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools