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Database: UniProt
Entry: O54890
LinkDB: O54890
Original site: O54890 
ID   ITB3_MOUSE              Reviewed;         787 AA.
AC   O54890; Q3TZC6;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   10-APR-2019, entry version 171.
DE   RecName: Full=Integrin beta-3;
DE   AltName: Full=Platelet membrane glycoprotein IIIa;
DE            Short=GPIIIa;
DE   AltName: CD_antigen=CD61;
DE   Flags: Precursor;
GN   Name=Itgb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H/HeN;
RA   McHugh K.P., Teitelbaum S.L., Kitazawa S., Ross F.P.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH FBLN5.
RX   PubMed=11805835; DOI=10.1038/415171a;
RA   Nakamura T., Lozano P.R., Ikeda Y., Iwanaga Y., Hinek A.,
RA   Minamisawa S., Cheng C.F., Kobuke K., Dalton N., Takada Y.,
RA   Tashiro K., Ross J., Honjo T., Chien K.R.;
RT   "Fibulin-5/DANCE is essential for elastogenesis in vivo.";
RL   Nature 415:171-175(2002).
RN   [7]
RP   INTERACTION WITH DAB2.
RX   PubMed=12606711; DOI=10.1073/pnas.262791999;
RA   Calderwood D.A., Fujioka Y., de Pereda J.M., Garcia-Alvarez B.,
RA   Nakamoto T., Margolis B., McGlade C.J., Liddington R.C.,
RA   Ginsberg M.H.;
RT   "Integrin beta cytoplasmic domain interactions with phosphotyrosine-
RT   binding domains: a structural prototype for diversity in integrin
RT   signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2272-2277(2003).
RN   [8]
RP   INTERACTION WITH FERMT2.
RX   PubMed=18483218; DOI=10.1101/gad.469408;
RA   Montanez E., Ussar S., Schifferer M., Bosl M., Zent R., Moser M.,
RA   Fassler R.;
RT   "Kindlin-2 controls bidirectional signaling of integrins.";
RL   Genes Dev. 22:1325-1330(2008).
RN   [9]
RP   FUNCTION.
RX   PubMed=19332769; DOI=10.1182/blood-2008-03-145821;
RA   Yang H., Lang S., Zhai Z., Li L., Kahr W.H., Chen P., Brkic J.,
RA   Spring C.M., Flick M.J., Degen J.L., Freedman J., Ni H.;
RT   "Fibrinogen is required for maintenance of platelet intracellular and
RT   cell-surface P-selectin expression.";
RL   Blood 114:425-436(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-766, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [11]
RP   INTERACTION WITH MXRA8.
RX   PubMed=22492581; DOI=10.1002/jbmr.1632;
RA   Jung Y.K., Han S.W., Kim G.W., Jeong J.H., Kim H.J., Choi J.Y.;
RT   "DICAM inhibits osteoclast differentiation through attenuation of the
RT   integrin alphaVbeta3 pathway.";
RL   J. Bone Miner. Res. 27:2024-2034(2012).
CC   -!- FUNCTION: Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for
CC       cytotactin, fibronectin, laminin, matrix metalloproteinase-2,
CC       osteopontin, osteomodulin, prothrombin, thrombospondin,
CC       vitronectin and von Willebrand factor. Integrin alpha-IIB/beta-3
CC       (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen,
CC       plasminogen, prothrombin, thrombospondin and vitronectin.
CC       Integrins alpha-IIB/beta-3 and alpha-V/beta-3 recognize the
CC       sequence R-G-D in a wide array of ligands. Integrin alpha-
CC       IIB/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in
CC       fibrinogen gamma chain. Following activation integrin alpha-
CC       IIB/beta-3 brings about platelet/platelet interaction through
CC       binding of soluble fibrinogen. This step leads to rapid platelet
CC       aggregation which physically plugs ruptured endothelial surfaces.
CC       Fibrinogen binding enhances SELP expression in activated platelets
CC       (PubMed:19332769). ITGAV:ITGB3 binds to fractalkine (CX3CL1) and
CC       acts as its coreceptor in CX3CR1-dependent fractalkine signaling.
CC       ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is
CC       essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and
CC       this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to
CC       FGF2 and this binding is essential for FGF2 signaling (By
CC       similarity). ITGAV:ITGB3 binds to IGF1 and this binding is
CC       essential for IGF1 signaling (By similarity). ITGAV:ITGB3 binds to
CC       IGF2 and this binding is essential for IGF2 signaling (By
CC       similarity). ITGAV:ITGB3 binds to IL1B and this binding is
CC       essential for IL1B signaling (By similarity). ITGAV:ITGB3 binds to
CC       PLA2G2A via a site (site 2) which is distinct from the classical
CC       ligand-binding site (site 1) and this induces integrin
CC       conformational changes and enhanced ligand binding to site 1 (By
CC       similarity). ITGAV:ITGB3 acts as a receptor for fibrillin-1 (FBN1)
CC       and mediates R-G-D-dependent cell adhesion to FBN1 (By
CC       similarity). {ECO:0000250|UniProtKB:P05106,
CC       ECO:0000269|PubMed:19332769}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (By
CC       similarity). Beta-3 (ITGB3) associates with either alpha-IIB
CC       (ITGA2B) or alpha-V (ITGAV). Interacts with FLNB and COMP (By
CC       similarity). Interacts with PDIA6 following platelet stimulation
CC       (By similarity). Interacts with SYK; upon activation by ITGB3
CC       promotes platelet adhesion (By similarity). Interacts with MYO10
CC       (By similarity). Interacts with DAB2 (PubMed:12606711). Interacts
CC       with FERMT2 (PubMed:18483218). Integrin ITGAV:ITGB3 interacts with
CC       FBLN5 (via N-terminus) (PubMed:11805835). Interacts with EMP2;
CC       regulates the levels of the heterodimer ITGA5:ITGB3 integrin
CC       expression on the plasma membrane (By similarity). ITGAV:ITGB3
CC       interacts with CCN3 (By similarity). ITGAV:ITGB3 interacts with
CC       AGRA2 (By similarity). ITGAV:ITGB3 is found in a ternary complex
CC       with CX3CR1 and CX3CL1. ITGAV:ITGB3 is found in a ternary complex
CC       with NRG1 and ERBB3. ITGAV:ITGB3 is found in a ternary complex
CC       with FGF1 and FGFR1. ITGAV:ITGB3 interacts with FGF2; it is likely
CC       that FGF2 can simultaneously bind ITGAV:ITGB3 and FGF receptors
CC       (By similarity). ITGAV:ITGB3 binds to IL1B (By similarity).
CC       ITGAV:ITGB3 is found in a ternary complex with IGF1 and IGF1R (By
CC       similarity). ITGAV:ITGB3 interacts with IGF2 (By similarity).
CC       ITGAV:ITGB3 interacts with FBN1 (By similarity). ITGAV:ITGB3
CC       interacts with CD9, CD81 and CD151 (via second extracellular
CC       domain) (By similarity). Interacts (via the allosteric site (site
CC       2)) with CXCL12 in a CXCR4-independent manner (By similarity).
CC       Interacts with MXRA8/DICAM; the interaction inhibits ITGAV:ITGB3
CC       heterodimer formation (PubMed:22492581).
CC       {ECO:0000250|UniProtKB:P05106, ECO:0000269|PubMed:11805835,
CC       ECO:0000269|PubMed:12606711, ECO:0000269|PubMed:18483218,
CC       ECO:0000269|PubMed:22492581}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P05106}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P05106}. Cell projection,
CC       lamellipodium membrane {ECO:0000250|UniProtKB:P05106}. Cell
CC       junction, focal adhesion {ECO:0000250|UniProtKB:P05106}.
CC   -!- PTM: Phosphorylated on tyrosine residues in response to thrombin-
CC       induced platelet aggregation. Probably involved in outside-in
CC       signaling. {ECO:0000250|UniProtKB:P05106}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
DR   EMBL; AF026509; AAB94086.1; -; mRNA.
DR   EMBL; AK157958; BAE34283.1; -; mRNA.
DR   EMBL; AL603709; CAM22629.1; -; Genomic_DNA.
DR   EMBL; BX000996; CAM22629.1; JOINED; Genomic_DNA.
DR   EMBL; BX000996; CAM27926.1; -; Genomic_DNA.
DR   EMBL; AL603709; CAM27926.1; JOINED; Genomic_DNA.
DR   EMBL; CH466558; EDL34227.1; -; Genomic_DNA.
DR   EMBL; BC125518; AAI25519.1; -; mRNA.
DR   EMBL; BC125520; AAI25521.1; -; mRNA.
DR   CCDS; CCDS25536.1; -.
DR   PIR; PN0510; PN0510.
DR   RefSeq; NP_058060.2; NM_016780.2.
DR   UniGene; Mm.87150; -.
DR   PDB; 5XQ1; X-ray; 2.95 A; A/B=773-787.
DR   PDBsum; 5XQ1; -.
DR   ProteinModelPortal; O54890; -.
DR   SMR; O54890; -.
DR   BioGrid; 200830; 5.
DR   ComplexPortal; CPX-3035; Integrin alphav-beta3 complex.
DR   ComplexPortal; CPX-3116; Integrin alphaIIb-beta3 complex.
DR   CORUM; O54890; -.
DR   DIP; DIP-46416N; -.
DR   IntAct; O54890; 6.
DR   MINT; O54890; -.
DR   STRING; 10090.ENSMUSP00000021028; -.
DR   ChEMBL; CHEMBL3430894; -.
DR   iPTMnet; O54890; -.
DR   PhosphoSitePlus; O54890; -.
DR   EPD; O54890; -.
DR   MaxQB; O54890; -.
DR   PaxDb; O54890; -.
DR   PeptideAtlas; O54890; -.
DR   PRIDE; O54890; -.
DR   Ensembl; ENSMUST00000021028; ENSMUSP00000021028; ENSMUSG00000020689.
DR   GeneID; 16416; -.
DR   KEGG; mmu:16416; -.
DR   UCSC; uc007lwx.2; mouse.
DR   CTD; 3690; -.
DR   MGI; MGI:96612; Itgb3.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; O54890; -.
DR   KO; K06493; -.
DR   OMA; PRCNLKE; -.
DR   OrthoDB; 473040at2759; -.
DR   TreeFam; TF105392; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   Reactome; R-MMU-1566948; Elastic fibre formation.
DR   Reactome; R-MMU-210990; PECAM1 interactions.
DR   Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR   Reactome; R-MMU-216083; Integrin cell surface interactions.
DR   Reactome; R-MMU-3000170; Syndecan interactions.
DR   Reactome; R-MMU-3000178; ECM proteoglycans.
DR   Reactome; R-MMU-354192; Integrin alphaIIb beta3 signaling.
DR   Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR   Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
DR   Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-MMU-445144; Signal transduction by L1.
DR   Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR   ChiTaRS; Itgb3; mouse.
DR   PRO; PR:O54890; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000020689; Expressed in 132 organ(s), highest expression level in blood.
DR   Genevisible; O54890; MM.
DR   GO; GO:0071133; C:alpha9-beta1 integrin-ADAM8 complex; IDA:BHF-UCL.
DR   GO; GO:0035868; C:alphav-beta3 integrin-HMGB1 complex; ISO:MGI.
DR   GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; ISO:MGI.
DR   GO; GO:0035866; C:alphav-beta3 integrin-PKCalpha complex; IDA:BHF-UCL.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0031527; C:filopodium membrane; ISO:MGI.
DR   GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0099699; C:integral component of synaptic membrane; IDA:SynGO.
DR   GO; GO:0034679; C:integrin alpha9-beta1 complex; TAS:BHF-UCL.
DR   GO; GO:0034683; C:integrin alphav-beta3 complex; ISO:MGI.
DR   GO; GO:0008305; C:integrin complex; ISO:MGI.
DR   GO; GO:0031258; C:lamellipodium membrane; ISO:MGI.
DR   GO; GO:0042470; C:melanosome; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0031528; C:microvillus membrane; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR   GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0050840; F:extracellular matrix binding; ISO:MGI.
DR   GO; GO:0070051; F:fibrinogen binding; IEA:Ensembl.
DR   GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0005178; F:integrin binding; IPI:MGI.
DR   GO; GO:0002020; F:protease binding; ISO:MGI.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; ISO:MGI.
DR   GO; GO:0005080; F:protein kinase C binding; IPI:BHF-UCL.
DR   GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; ISO:MGI.
DR   GO; GO:0032147; P:activation of protein kinase activity; ISO:MGI.
DR   GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0043277; P:apoptotic cell clearance; IGI:BHF-UCL.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0048858; P:cell projection morphogenesis; IC:BHF-UCL.
DR   GO; GO:0007160; P:cell-matrix adhesion; IGI:MGI.
DR   GO; GO:0031589; P:cell-substrate adhesion; ISO:MGI.
DR   GO; GO:0007044; P:cell-substrate junction assembly; IDA:MGI.
DR   GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
DR   GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IMP:MGI.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0050919; P:negative chemotaxis; ISO:MGI.
DR   GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR   GO; GO:0010888; P:negative regulation of lipid storage; ISO:MGI.
DR   GO; GO:0032369; P:negative regulation of lipid transport; ISO:MGI.
DR   GO; GO:0050748; P:negative regulation of lipoprotein metabolic process; ISO:MGI.
DR   GO; GO:0045715; P:negative regulation of low-density lipoprotein particle receptor biosynthetic process; ISO:MGI.
DR   GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISO:MGI.
DR   GO; GO:0030168; P:platelet activation; ISO:MGI.
DR   GO; GO:0070527; P:platelet aggregation; ISO:MGI.
DR   GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:1900731; P:positive regulation of adenylate cyclase-inhibiting opioid receptor signaling pathway; ISO:MGI.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR   GO; GO:0045780; P:positive regulation of bone resorption; ISO:MGI.
DR   GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISO:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR   GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:MGI.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR   GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:MGI.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; ISO:MGI.
DR   GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:MGI.
DR   GO; GO:0033690; P:positive regulation of osteoblast proliferation; IMP:BHF-UCL.
DR   GO; GO:0045672; P:positive regulation of osteoclast differentiation; IC:BHF-UCL.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:MGI.
DR   GO; GO:2000406; P:positive regulation of T cell migration; IDA:UniProtKB.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR   GO; GO:1903053; P:regulation of extracellular matrix organization; IMP:MGI.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:MGI.
DR   GO; GO:0061097; P:regulation of protein tyrosine kinase activity; IMP:MGI.
DR   GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR   GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR   GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR   GO; GO:0014909; P:smooth muscle cell migration; ISO:MGI.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
DR   GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR040622; I-EGF_1.
DR   InterPro; IPR027068; Integrin_beta-3.
DR   InterPro; IPR033760; Integrin_beta_N.
DR   InterPro; IPR015812; Integrin_bsu.
DR   InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR   InterPro; IPR012896; Integrin_bsu_tail.
DR   InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR   InterPro; IPR002369; Integrin_bsu_VWA.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; PTHR10082; 1.
DR   PANTHER; PTHR10082:SF25; PTHR10082:SF25; 1.
DR   Pfam; PF07974; EGF_2; 2.
DR   Pfam; PF18372; I-EGF_1; 1.
DR   Pfam; PF08725; Integrin_b_cyt; 1.
DR   Pfam; PF07965; Integrin_B_tail; 1.
DR   Pfam; PF00362; Integrin_beta; 1.
DR   Pfam; PF17205; PSI_integrin; 1.
DR   PIRSF; PIRSF002512; Integrin_B; 1.
DR   PRINTS; PR01186; INTEGRINB.
DR   SMART; SM00187; INB; 1.
DR   SMART; SM01241; Integrin_b_cyt; 1.
DR   SMART; SM01242; Integrin_B_tail; 1.
DR   SMART; SM00423; PSI; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF69179; SSF69179; 1.
DR   SUPFAM; SSF69687; SSF69687; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS00243; INTEGRIN_BETA; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Cell adhesion; Cell junction; Cell membrane;
KW   Cell projection; Complete proteome; Disulfide bond; Glycoprotein;
KW   Integrin; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26    787       Integrin beta-3.
FT                                /FTId=PRO_0000016345.
FT   TOPO_DOM     26    717       Extracellular. {ECO:0000255}.
FT   TRANSMEM    718    740       Helical. {ECO:0000255}.
FT   TOPO_DOM    741    787       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      134    376       VWFA.
FT   REPEAT      462    510       I.
FT   REPEAT      511    552       II.
FT   REPEAT      553    591       III.
FT   REPEAT      592    628       IV.
FT   REGION      202    209       CX3CL1-binding.
FT                                {ECO:0000250|UniProtKB:P05106}.
FT   REGION      202    209       Involved in CX3CL1-, NRG1-, FGF1- and
FT                                IGF1-binding.
FT                                {ECO:0000250|UniProtKB:P05106}.
FT   REGION      292    312       CX3CL1-binding.
FT                                {ECO:0000250|UniProtKB:P05106}.
FT   REGION      462    628       Cysteine-rich tandem repeats.
FT   MOD_RES     766    766       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     772    772       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P05106}.
FT   MOD_RES     778    778       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P05106}.
FT   MOD_RES     784    784       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P05106}.
FT   CARBOHYD    345    345       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    396    396       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    477    477       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    584    584       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    679    679       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     30    460       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID     38     48       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID     41     74       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID     51     63       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    202    209       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    257    298       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    399    411       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    431    680       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    458    462       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    473    485       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    482    520       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    487    496       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    498    511       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    526    531       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    528    561       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    533    546       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    548    553       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    567    572       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    569    600       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    574    583       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    585    592       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    606    611       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    608    656       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    613    623       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    626    629       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    633    642       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    639    712       {ECO:0000250|UniProtKB:P05106}.
FT   DISULFID    660    688       {ECO:0000250|UniProtKB:P05106}.
FT   CONFLICT    114    114       A -> V (in Ref. 1; AAB94086).
FT                                {ECO:0000305}.
FT   CONFLICT    389    389       E -> G (in Ref. 1; AAB94086).
FT                                {ECO:0000305}.
FT   STRAND      777    780       {ECO:0000244|PDB:5XQ1}.
SQ   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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