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Integrin beta-3 (Platelet membrane glycoprotein IIIa) (GPIIIa) (CD antigen CD61)

 ITB3_MOUSE              Reviewed;         787 AA.
O54890; Q3TZC6;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 161.
RecName: Full=Integrin beta-3;
AltName: Full=Platelet membrane glycoprotein IIIa;
Short=GPIIIa;
AltName: CD_antigen=CD61;
Flags: Precursor;
Name=Itgb3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/HeN;
McHugh K.P., Teitelbaum S.L., Kitazawa S., Ross F.P.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Inner ear;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
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]
INTERACTION WITH FBLN5.
PubMed=11805835; DOI=10.1038/415171a;
Nakamura T., Lozano P.R., Ikeda Y., Iwanaga Y., Hinek A.,
Minamisawa S., Cheng C.F., Kobuke K., Dalton N., Takada Y.,
Tashiro K., Ross J., Honjo T., Chien K.R.;
"Fibulin-5/DANCE is essential for elastogenesis in vivo.";
Nature 415:171-175(2002).
[7]
INTERACTION WITH DAB2.
PubMed=12606711; DOI=10.1073/pnas.262791999;
Calderwood D.A., Fujioka Y., de Pereda J.M., Garcia-Alvarez B.,
Nakamoto T., Margolis B., McGlade C.J., Liddington R.C.,
Ginsberg M.H.;
"Integrin beta cytoplasmic domain interactions with phosphotyrosine-
binding domains: a structural prototype for diversity in integrin
signaling.";
Proc. Natl. Acad. Sci. U.S.A. 100:2272-2277(2003).
[8]
INTERACTION WITH FERMT2.
PubMed=18483218; DOI=10.1101/gad.469408;
Montanez E., Ussar S., Schifferer M., Bosl M., Zent R., Moser M.,
Fassler R.;
"Kindlin-2 controls bidirectional signaling of integrins.";
Genes Dev. 22:1325-1330(2008).
[9]
FUNCTION.
PubMed=19332769; DOI=10.1182/blood-2008-03-145821;
Yang H., Lang S., Zhai Z., Li L., Kahr W.H., Chen P., Brkic J.,
Spring C.M., Flick M.J., Degen J.L., Freedman J., Ni H.;
"Fibrinogen is required for maintenance of platelet intracellular and
cell-surface P-selectin expression.";
Blood 114:425-436(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-766, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for
cytotactin, fibronectin, laminin, matrix metalloproteinase-2,
osteopontin, osteomodulin, prothrombin, thrombospondin,
vitronectin and von Willebrand factor. Integrin alpha-IIB/beta-3
(ITGA2B:ITGB3) 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 surfaces.
Fibrinogen binding enhances SELP expression in activated platelets
(PubMed:19332769). ITGAV:ITGB3 binds to fractalkine (CX3CL1) and
acts as its coreceptor in CX3CR1-dependent fractalkine signaling.
ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is
essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and
this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to
IGF1 and this binding is essential for IGF1 signaling (By
similarity). ITGAV:ITGB3 binds to PLA2G2A via a site (site 2)
which is distinct from the classical ligand-binding site (site 1)
and this induces integrin conformational changes and enhanced
ligand binding to site 1 (By similarity). ITGAV:ITGB3 acts as a
receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell
adhesion to FBN1 (By similarity). {ECO:0000250|UniProtKB:P05106,
ECO:0000269|PubMed:19332769}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit (By
similarity). Beta-3 (ITGB3) associates with either alpha-IIB
(ITGA2B) or alpha-V (ITGAV). Interacts with FLNB and COMP (By
similarity). Interacts with PDIA6 following platelet stimulation
(By similarity). Interacts with SYK; upon activation by ITGB3
promotes platelet adhesion (By similarity). Interacts with MYO10
(By similarity). Interacts with DAB2 (PubMed:12606711). Interacts
with FERMT2 (PubMed:18483218). Integrin ITGAV:ITGB3 interacts with
FBLN5 (via N-terminus) (PubMed:11805835). Interacts with EMP2;
regulates the levels of the heterodimer ITGA5:ITGB3 integrin
expression on the plasma membrane (By similarity). ITGAV:ITGB3
interacts with NOV (By similarity). ITGAV:ITGB3 interacts with
AGRA2 (By similarity). ITGAV:ITGB3 is found in a ternary complex
with CX3CR1 and CX3CL1. ITGAV:ITGB3 is found in a ternary complex
with NRG1 and ERBB3. ITGAV:ITGB3 is found in a ternary complex
with FGF1 and FGFR1. ITGAV:ITGB3 is found in a ternary complex
with IGF1 and IGF1R (By similarity). ITGAV:ITGB3 interacts with
FBN1 (By similarity). {ECO:0000250|UniProtKB:P05106,
ECO:0000269|PubMed:11805835, ECO:0000269|PubMed:12606711,
ECO:0000269|PubMed:18483218}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P05106}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P05106}. Cell projection,
lamellipodium membrane {ECO:0000250|UniProtKB:P05106}. Cell
junction, focal adhesion {ECO:0000250|UniProtKB:P05106}.
-!- PTM: Phosphorylated on tyrosine residues in response to thrombin-
induced platelet aggregation. Probably involved in outside-in
signaling. {ECO:0000250|UniProtKB:P05106}.
-!- SIMILARITY: Belongs to the integrin beta chain family.
{ECO:0000305}.
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EMBL; AF026509; AAB94086.1; -; mRNA.
EMBL; AK157958; BAE34283.1; -; mRNA.
EMBL; AL603709; CAM22629.1; -; Genomic_DNA.
EMBL; BX000996; CAM22629.1; JOINED; Genomic_DNA.
EMBL; BX000996; CAM27926.1; -; Genomic_DNA.
EMBL; AL603709; CAM27926.1; JOINED; Genomic_DNA.
EMBL; CH466558; EDL34227.1; -; Genomic_DNA.
EMBL; BC125518; AAI25519.1; -; mRNA.
EMBL; BC125520; AAI25521.1; -; mRNA.
CCDS; CCDS25536.1; -.
PIR; PN0510; PN0510.
RefSeq; NP_058060.2; NM_016780.2.
UniGene; Mm.87150; -.
PDB; 5XQ1; X-ray; 2.95 A; A/B=773-787.
PDBsum; 5XQ1; -.
ProteinModelPortal; O54890; -.
SMR; O54890; -.
BioGrid; 200830; 5.
CORUM; O54890; -.
DIP; DIP-46416N; -.
IntAct; O54890; 6.
MINT; MINT-4099028; -.
STRING; 10090.ENSMUSP00000021028; -.
iPTMnet; O54890; -.
PhosphoSitePlus; O54890; -.
EPD; O54890; -.
MaxQB; O54890; -.
PaxDb; O54890; -.
PeptideAtlas; O54890; -.
PRIDE; O54890; -.
Ensembl; ENSMUST00000021028; ENSMUSP00000021028; ENSMUSG00000020689.
GeneID; 16416; -.
KEGG; mmu:16416; -.
UCSC; uc007lwx.2; mouse.
CTD; 3690; -.
MGI; MGI:96612; Itgb3.
eggNOG; KOG1226; Eukaryota.
eggNOG; ENOG410XP60; LUCA.
GeneTree; ENSGT00760000119064; -.
HOGENOM; HOG000252936; -.
HOVERGEN; HBG006190; -.
InParanoid; O54890; -.
KO; K06493; -.
OMA; CHSSDFG; -.
OrthoDB; EOG091G029W; -.
TreeFam; TF105392; -.
Reactome; R-MMU-114608; Platelet degranulation.
Reactome; R-MMU-1566948; Elastic fibre formation.
Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
Reactome; R-MMU-216083; Integrin cell surface interactions.
Reactome; R-MMU-3000170; Syndecan interactions.
Reactome; R-MMU-3000178; ECM proteoglycans.
Reactome; R-MMU-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-445144; Signal transduction by L1.
ChiTaRS; Itgb3; mouse.
PRO; PR:O54890; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020689; -.
CleanEx; MM_ITGB3; -.
Genevisible; O54890; MM.
GO; GO:0071133; C:alpha9-beta1 integrin-ADAM8 complex; IDA:BHF-UCL.
GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; ISO:MGI.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031527; C:filopodium membrane; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0034679; C:integrin alpha9-beta1 complex; TAS:BHF-UCL.
GO; GO:0034683; C:integrin alphav-beta3 complex; ISO:MGI.
GO; GO:0008305; C:integrin complex; ISO:MGI.
GO; GO:0031258; C:lamellipodium membrane; ISO:MGI.
GO; GO:0042470; C:melanosome; ISO:MGI.
GO; GO:0031528; C:microvillus membrane; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0032587; C:ruffle membrane; ISO:MGI.
GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0050840; F:extracellular matrix binding; ISO:MGI.
GO; GO:0070051; F:fibrinogen binding; IEA:Ensembl.
GO; GO:0001968; F:fibronectin binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0005178; F:integrin binding; IPI:MGI.
GO; GO:0042277; F:peptide binding; IEA:Ensembl.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0003756; F:protein disulfide isomerase activity; ISO:MGI.
GO; GO:0004872; F:receptor activity; IEA:InterPro.
GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; ISO:MGI.
GO; GO:0032147; P:activation of protein kinase activity; ISO:MGI.
GO; GO:0060055; P:angiogenesis involved in wound healing; IEA:InterPro.
GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; ISO:MGI.
GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0016049; P:cell growth; ISO:MGI.
GO; GO:0016477; P:cell migration; ISO:MGI.
GO; GO:0048858; P:cell projection morphogenesis; IC:BHF-UCL.
GO; GO:0007160; P:cell-matrix adhesion; IGI:MGI.
GO; GO:0031589; P:cell-substrate adhesion; ISO:MGI.
GO; GO:0007044; P:cell-substrate junction assembly; IDA:MGI.
GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IMP:MGI.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
GO; GO:0050919; P:negative chemotaxis; ISO:MGI.
GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
GO; GO:0010888; P:negative regulation of lipid storage; ISO:MGI.
GO; GO:0032369; P:negative regulation of lipid transport; ISO:MGI.
GO; GO:0050748; P:negative regulation of lipoprotein metabolic process; ISO:MGI.
GO; GO:0045715; P:negative regulation of low-density lipoprotein particle receptor biosynthetic process; ISO:MGI.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISO:MGI.
GO; GO:0030168; P:platelet activation; ISO:MGI.
GO; GO:0070527; P:platelet aggregation; ISO:MGI.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
GO; GO:1900731; P:positive regulation of adenylate cyclase-inhibiting opioid receptor signaling pathway; IEA:Ensembl.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0045780; P:positive regulation of bone resorption; IC:BHF-UCL.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:MGI.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:MGI.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IEA:Ensembl.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; IMP:BHF-UCL.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IC:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:MGI.
GO; GO:2000406; P:positive regulation of T cell migration; IDA:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
GO; GO:1903053; P:regulation of extracellular matrix organization; IMP:MGI.
GO; GO:0061097; P:regulation of protein tyrosine kinase activity; IMP:MGI.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IEA:Ensembl.
GO; GO:0014909; P:smooth muscle cell migration; ISO:MGI.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 1.20.5.630; -; 1.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR013111; EGF_extracell.
InterPro; IPR027068; Integrin_beta-3.
InterPro; IPR033760; Integrin_beta_N.
InterPro; IPR015812; Integrin_bsu.
InterPro; IPR014836; Integrin_bsu_cyt_dom.
InterPro; IPR037076; Integrin_bsu_cyt_dom_sf.
InterPro; IPR012896; Integrin_bsu_tail.
InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
InterPro; IPR002369; Integrin_bsu_VWA.
InterPro; IPR032695; Integrin_dom_sf.
InterPro; IPR016201; PSI.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR10082; PTHR10082; 1.
PANTHER; PTHR10082:SF25; PTHR10082:SF25; 1.
Pfam; PF07974; EGF_2; 2.
Pfam; PF08725; Integrin_b_cyt; 1.
Pfam; PF07965; Integrin_B_tail; 1.
Pfam; PF00362; Integrin_beta; 1.
Pfam; PF17205; PSI_integrin; 1.
PIRSF; PIRSF002512; Integrin_B; 1.
PRINTS; PR01186; INTEGRINB.
SMART; SM00187; INB; 1.
SMART; SM01241; Integrin_b_cyt; 1.
SMART; SM01242; Integrin_B_tail; 1.
SMART; SM00423; PSI; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 1.
SUPFAM; SSF69687; SSF69687; 1.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS00243; INTEGRIN_BETA; 3.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell junction; Cell membrane;
Cell projection; Complete proteome; Disulfide bond; Glycoprotein;
Integrin; Membrane; Phosphoprotein; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 787 Integrin beta-3.
/FTId=PRO_0000016345.
TOPO_DOM 26 717 Extracellular. {ECO:0000255}.
TRANSMEM 718 740 Helical. {ECO:0000255}.
TOPO_DOM 741 787 Cytoplasmic. {ECO:0000255}.
DOMAIN 134 376 VWFA.
REPEAT 462 510 I.
REPEAT 511 552 II.
REPEAT 553 591 III.
REPEAT 592 628 IV.
REGION 202 209 CX3CL1-binding.
{ECO:0000250|UniProtKB:P05106}.
REGION 202 209 Involved in CX3CL1-, NRG1-, FGF1- and
IGF1-binding.
{ECO:0000250|UniProtKB:P05106}.
REGION 292 312 CX3CL1-binding.
{ECO:0000250|UniProtKB:P05106}.
REGION 462 628 Cysteine-rich tandem repeats.
MOD_RES 766 766 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 772 772 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05106}.
MOD_RES 778 778 Phosphothreonine.
{ECO:0000250|UniProtKB:P05106}.
MOD_RES 784 784 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05106}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 477 477 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 584 584 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 679 679 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 30 460 {ECO:0000250|UniProtKB:P05106}.
DISULFID 38 48 {ECO:0000250|UniProtKB:P05106}.
DISULFID 41 74 {ECO:0000250|UniProtKB:P05106}.
DISULFID 51 63 {ECO:0000250|UniProtKB:P05106}.
DISULFID 202 209 {ECO:0000250|UniProtKB:P05106}.
DISULFID 257 298 {ECO:0000250|UniProtKB:P05106}.
DISULFID 399 411 {ECO:0000250|UniProtKB:P05106}.
DISULFID 431 680 {ECO:0000250|UniProtKB:P05106}.
DISULFID 458 462 {ECO:0000250|UniProtKB:P05106}.
DISULFID 473 485 {ECO:0000250|UniProtKB:P05106}.
DISULFID 482 520 {ECO:0000250|UniProtKB:P05106}.
DISULFID 487 496 {ECO:0000250|UniProtKB:P05106}.
DISULFID 498 511 {ECO:0000250|UniProtKB:P05106}.
DISULFID 526 531 {ECO:0000250|UniProtKB:P05106}.
DISULFID 528 561 {ECO:0000250|UniProtKB:P05106}.
DISULFID 533 546 {ECO:0000250|UniProtKB:P05106}.
DISULFID 548 553 {ECO:0000250|UniProtKB:P05106}.
DISULFID 567 572 {ECO:0000250|UniProtKB:P05106}.
DISULFID 569 600 {ECO:0000250|UniProtKB:P05106}.
DISULFID 574 583 {ECO:0000250|UniProtKB:P05106}.
DISULFID 585 592 {ECO:0000250|UniProtKB:P05106}.
DISULFID 606 611 {ECO:0000250|UniProtKB:P05106}.
DISULFID 608 656 {ECO:0000250|UniProtKB:P05106}.
DISULFID 613 623 {ECO:0000250|UniProtKB:P05106}.
DISULFID 626 629 {ECO:0000250|UniProtKB:P05106}.
DISULFID 633 642 {ECO:0000250|UniProtKB:P05106}.
DISULFID 639 712 {ECO:0000250|UniProtKB:P05106}.
DISULFID 660 688 {ECO:0000250|UniProtKB:P05106}.
CONFLICT 114 114 A -> V (in Ref. 1; AAB94086).
{ECO:0000305}.
CONFLICT 389 389 E -> G (in Ref. 1; AAB94086).
{ECO:0000305}.
STRAND 777 780 {ECO:0000244|PDB:5XQ1}.
SEQUENCE 787 AA; 86738 MW; 4F2E606969788794 CRC64;
MRAQWPGQLW AALLALGALA GVVVGESNIC TTRGVNSCQQ CLAVSPVCAW CSDETLSQGS
PRCNLKENLL KDNCAPESIE FPVSEAQILE ARPLSSKGSG SSAQITQVSP QRIALRLRPD
DSKIFSLQVR QVEDYPVDIY YLMDLSFSMK DDLSSIQTLG TKLASQMRKL TSNLRIGFGA
FVDKPVSPYM YISPPQAIKN PCYNMKNACL PMFGYKHVLT LTDQVSRFNE EVKKQSVSRN
RDAPEGGFDA IMQATVCDEK IGWRNDASHL LVFTTDAKTH IALDGRLAGI VLPNDGHCHI
GTDNHYSAST TMDYPSLGLM TEKLSQKNIN LIFAVTENVV SLYQNYSELI PGTTVGVLSD
DSSNVLQLIV DAYGKIRSKV ELEVRDLPEE LSLSFNATCL NNEVIPGLKS CVGLKIGDTV
SFSIEAKVRG CPQEKEQSFT IKPVGFKDSL TVQVTFDCDC ACQAFAQPSS PRCNNGNGTF
ECGVCRCDQG WLGSMCECSE EDYRPSQQEE CSPKEGQPIC SQRGECLCGQ CVCHSSDFGK
ITGKYCECDD FSCVRYKGEM CSGHGQCNCG DCVCDSDWTG YYCNCTTRTD TCMSTNGLLC
SGRGNCECGS CVCVQPGSYG DTCEKCPTCP DACSFKKECV ECKKFNRGTL HEENTCSRYC
RDDIEQVKEL TDTGKNAVNC TYKNEDDCVV RFQYYEDTSG RAVLYVVEEP ECPKGPDILV
VLLSVMGAIL LIGLATLLIW KLLITIHDRK EFAKFEEERA RAKWDTANNP LYKEATSTFT
NITYRGT


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