ITB3_RAT
ID ITB3_RAT Reviewed; 787 AA.
AC Q8R2H2; M0RCF3;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Integrin beta-3 {ECO:0000305};
DE AltName: Full=Platelet membrane glycoprotein IIIa {ECO:0000305};
DE Short=GPIIIa {ECO:0000305};
DE Flags: Precursor;
GN Name=Itgb3 {ECO:0000312|RGD:628868};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:CAD29521.1};
RN [1] {ECO:0000312|EMBL:CAD29521.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar {ECO:0000312|EMBL:CAD29521.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:CAD29521.1};
RA Stephan C., Hamacher M.;
RT "Cloning of the rat integrin beta3 subunit.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18549786; DOI=10.1016/j.neuron.2008.04.011;
RA Cingolani L.A., Thalhammer A., Yu L.M., Catalano M., Ramos T.,
RA Colicos M.A., Goda Y.;
RT "Activity-dependent regulation of synaptic AMPA receptor composition and
RT abundance by beta3 integrins.";
RL Neuron 58:749-762(2008).
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, vitronectin and
CC von Willebrand factor. Integrin alpha-IIB/beta-3 (ITGA2B:ITGB3) is a
CC receptor for fibronectin, fibrinogen, plasminogen, prothrombin,
CC thrombospondin and vitronectin. Integrins alpha-IIB/beta-3 and alpha-
CC V/beta-3 recognize the sequence R-G-D in a wide array of ligands.
CC Integrin alpha-IIB/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-
CC G-D-V in fibrinogen gamma chain. Following activation integrin alpha-
CC IIB/beta-3 brings about platelet/platelet interaction through binding
CC of soluble fibrinogen. This step leads to rapid platelet aggregation
CC which physically plugs ruptured endothelial surfaces. Fibrinogen
CC binding enhances SELP expression in activated platelets (By
CC similarity). ITGAV:ITGB3 binds to fractalkine (CX3CL1) and acts as its
CC coreceptor in CX3CR1-dependent fractalkine signaling. ITGAV:ITGB3 binds
CC to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB
CC signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential for
CC FGF1 signaling. ITGAV:ITGB3 binds to FGF2 and this binding is essential
CC for FGF2 signaling (By similarity). ITGAV:ITGB3 binds to IGF1 and this
CC binding is essential for IGF1 signaling (By similarity). ITGAV:ITGB3
CC binds to IGF2 and this binding is essential for IGF2 signaling (By
CC similarity). ITGAV:ITGB3 binds to IL1B and this binding is essential
CC for IL1B signaling (By similarity). ITGAV:ITGB3 binds to PLA2G2A via a
CC site (site 2) which is distinct from the classical ligand-binding site
CC (site 1) and this induces integrin conformational changes and enhanced
CC ligand binding to site 1 (By similarity). ITGAV:ITGB3 acts as a
CC receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell
CC adhesion to FBN1 (By similarity). In brain, plays a role in synaptic
CC transmission and plasticity. Involved in the regulation of the
CC serotonin neurotransmission, is required to localize to specific
CC compartments within the synapse the serotonin receptor SLC6A4 and for
CC an appropriate reuptake of serotonin (By similarity). Controls
CC excitatory synaptic strength by regulating GRIA2-containing AMPAR
CC endocytosis, which affects AMPAR abundance and composition
CC (PubMed:18549786). ITGAV:ITGB3 acts as a receptor for CD40LG (By
CC similarity). {ECO:0000250|UniProtKB:O54890,
CC ECO:0000250|UniProtKB:P05106, ECO:0000269|PubMed:18549786}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (By similarity).
CC Beta-3 (ITGB3) associates with either alpha-IIB (ITGA2B) or alpha-V
CC (ITGAV). Interacts with FLNB and COMP (By similarity). Interacts with
CC PDIA6 following platelet stimulation (By similarity). Interacts with
CC SYK; upon activation by ITGB3 promotes platelet adhesion (By
CC similarity). Interacts with MYO10 (By similarity). Interacts with DAB2.
CC Interacts with FERMT2. Integrin ITGAV:ITGB3 interacts with FBLN5 (via
CC N-terminus) (By similarity). Interacts with EMP2; regulates the levels
CC of the heterodimer ITGA5:ITGB3 integrin expression on the plasma
CC membrane (By similarity). ITGAV:ITGB3 interacts with CCN3 (By
CC similarity). ITGAV:ITGB3 interacts with AGRA2 (By similarity).
CC ITGAV:ITGB3 is found in a ternary complex with CX3CR1 and CX3CL1.
CC ITGAV:ITGB3 is found in a ternary complex with NRG1 and ERBB3.
CC ITGAV:ITGB3 is found in a ternary complex with FGF1 and FGFR1.
CC ITGAV:ITGB3 interacts with FGF2; it is likely that FGF2 can
CC simultaneously bind ITGAV:ITGB3 and FGF receptors (By similarity).
CC ITGAV:ITGB3 binds to IL1B (By similarity). ITGAV:ITGB3 is found in a
CC ternary complex with IGF1 and IGF1R (By similarity). ITGAV:ITGB3
CC interacts with IGF2 (By similarity). ITGAV:ITGB3 interacts with FBN1
CC (By similarity). ITGAV:ITGB3 interacts with CD9, CD81 and CD151 (via
CC second extracellular domain) (By similarity). Interacts (via the
CC allosteric site (site 2)) with CXCL12 in a CXCR4-independent manner (By
CC similarity). Interacts with MXRA8/DICAM; the interaction inhibits
CC ITGAV:ITGB3 heterodimer formation (By similarity). ITGAV:ITGB3
CC interacts with PTN. Forms a complex with PTPRZ1 and PTN that stimulates
CC endothelial cell migration through ITGB3 Tyr-772 phosphorylation (By
CC similarity). ITGAV:ITGB3 interacts with SLC6A4 (By similarity).
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:O54890,
CC ECO:0000250|UniProtKB:P05106}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05106};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05106}.
CC Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:P05106}.
CC Cell junction, focal adhesion {ECO:0000250|UniProtKB:O54890}.
CC Postsynaptic cell membrane {ECO:0000269|PubMed:18549786}; Single-pass
CC type I membrane protein {ECO:0000305}. Synapse
CC {ECO:0000250|UniProtKB:O54890}.
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. {ECO:0000305}.
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DR EMBL; AJ440952; CAD29521.1; -; mRNA.
DR EMBL; AABR07030536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; PN0509; PN0509.
DR RefSeq; NP_714942.1; NM_153720.1.
DR AlphaFoldDB; Q8R2H2; -.
DR SMR; Q8R2H2; -.
DR CORUM; Q8R2H2; -.
DR STRING; 10116.ENSRNOP00000067271; -.
DR BindingDB; Q8R2H2; -.
DR ChEMBL; CHEMBL4296069; -.
DR GlyGen; Q8R2H2; 5 sites.
DR Ensembl; ENSRNOT00000073350; ENSRNOP00000067271; ENSRNOG00000048449.
DR GeneID; 29302; -.
DR KEGG; rno:29302; -.
DR CTD; 3690; -.
DR RGD; 628868; Itgb3.
DR GeneTree; ENSGT00980000198528; -.
DR HOGENOM; CLU_011772_0_1_1; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; Q8R2H2; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-1566948; Elastic fibre formation.
DR Reactome; R-RNO-210990; PECAM1 interactions.
DR Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-RNO-3000170; Syndecan interactions.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR Reactome; R-RNO-354192; Integrin signaling.
DR Reactome; R-RNO-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-RNO-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-445144; Signal transduction by L1.
DR Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR PRO; PR:Q8R2H2; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Genevisible; Q8R2H2; RN.
DR GO; GO:0071133; C:alpha9-beta1 integrin-ADAM8 complex; ISO:RGD.
DR GO; GO:0035868; C:alphav-beta3 integrin-HMGB1 complex; ISO:RGD.
DR GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; ISO:RGD.
DR GO; GO:0035866; C:alphav-beta3 integrin-PKCalpha complex; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0031527; C:filopodium membrane; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0099699; C:integral component of synaptic membrane; ISO:RGD.
DR GO; GO:0034683; C:integrin alphav-beta3 complex; ISO:RGD.
DR GO; GO:0008305; C:integrin complex; IDA:RGD.
DR GO; GO:0031258; C:lamellipodium membrane; ISO:RGD.
DR GO; GO:0042470; C:melanosome; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0031528; C:microvillus membrane; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0019960; F:C-X3-C chemokine binding; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0050840; F:extracellular matrix binding; ISO:RGD.
DR GO; GO:0017134; F:fibroblast growth factor binding; IEA:Ensembl.
DR GO; GO:0001968; F:fibronectin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0031994; F:insulin-like growth factor I binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0038132; F:neuregulin binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISO:RGD.
DR GO; GO:0005080; F:protein kinase C binding; ISO:RGD.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; ISO:RGD.
DR GO; GO:0032147; P:activation of protein kinase activity; ISO:RGD.
DR GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; ISO:RGD.
DR GO; GO:0043277; P:apoptotic cell clearance; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; TAS:RGD.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISO:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0031589; P:cell-substrate adhesion; ISO:RGD.
DR GO; GO:0007044; P:cell-substrate junction assembly; ISO:RGD.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEP:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISO:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007566; P:embryo implantation; IEP:RGD.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0048333; P:mesodermal cell differentiation; ISO:RGD.
DR GO; GO:0050919; P:negative chemotaxis; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:0010888; P:negative regulation of lipid storage; ISO:RGD.
DR GO; GO:0032369; P:negative regulation of lipid transport; ISO:RGD.
DR GO; GO:0050748; P:negative regulation of lipoprotein metabolic process; ISO:RGD.
DR GO; GO:1905598; P:negative regulation of low-density lipoprotein receptor activity; ISO:RGD.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISO:RGD.
DR GO; GO:0030168; P:platelet activation; ISO:RGD.
DR GO; GO:0070527; P:platelet aggregation; IMP:RGD.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:1900731; P:positive regulation of adenylate cyclase-inhibiting opioid receptor signaling pathway; IMP:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
DR GO; GO:0045780; P:positive regulation of bone resorption; IMP:RGD.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IMP:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IMP:RGD.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IMP:RGD.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:2000406; P:positive regulation of T cell migration; ISO:RGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:1903053; P:regulation of extracellular matrix organization; ISO:RGD.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR GO; GO:0061097; P:regulation of protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IDA:RGD.
DR GO; GO:0051611; P:regulation of serotonin uptake; ISS:UniProtKB.
DR GO; GO:1901163; P:regulation of trophoblast cell migration; IEA:Ensembl.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0036119; P:response to platelet-derived growth factor; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR GO; GO:0014909; P:smooth muscle cell migration; ISO:RGD.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:0046718; P:viral entry into host cell; ISO:RGD.
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; PS00243; INTEGRIN_BETA; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell junction; Cell membrane; Cell projection;
KW Disulfide bond; Glycoprotein; Integrin; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..787
FT /note="Integrin beta-3"
FT /evidence="ECO:0000255"
FT /id="PRO_5004312362"
FT TOPO_DOM 27..717
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..738
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 739..787
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..75
FT /note="PSI"
FT /evidence="ECO:0000255"
FT DOMAIN 134..376
FT /note="VWFA"
FT /evidence="ECO:0000255"
FT REPEAT 462..510
FT /note="I"
FT /evidence="ECO:0000255"
FT REPEAT 511..552
FT /note="II"
FT /evidence="ECO:0000255"
FT REPEAT 553..591
FT /note="III"
FT /evidence="ECO:0000255"
FT REPEAT 592..628
FT /note="IV"
FT /evidence="ECO:0000255"
FT REGION 202..209
FT /note="CX3CL1-binding"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT REGION 202..209
FT /note="Involved in CX3CL1-, NRG1-, FGF1- and IGF1-binding"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT REGION 292..312
FT /note="CX3CL1-binding"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT REGION 462..628
FT /note="Cysteine-rich tandem repeats"
FT /evidence="ECO:0000250|UniProtKB:O54890"
FT MOTIF 776..782
FT /note="LIR"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT MOD_RES 766
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O54890"
FT MOD_RES 772
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT MOD_RES 778
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT MOD_RES 784
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..460
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 38..48
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 41..74
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 51..63
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 202..209
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 257..298
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 399..411
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 431..680
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 458..462
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 473..485
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 482..520
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 487..496
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 498..511
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 526..531
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 528..561
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 533..546
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 548..553
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 567..572
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 569..600
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 574..583
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 585..592
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 606..611
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 608..656
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 613..623
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 626..629
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 633..642
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 639..712
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 660..688
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
SQ SEQUENCE 787 AA; 86930 MW; C67826118411FE95 CRC64;
MRTRRPGQLW ATLLALGALA GVVVGESNIC TTRGVNSCQQ CLAVSPVCAW CSDESLPQNS
PRCNLKKNLL KDKCSPESIE FPVSEAQILE ALPLSSKGSG DSAQITQVSP QRIALRLRPD
DSKIFSLQVR QVEDYPVDIY YLMDLSFSMK DDLSSIQTLG TKLASQMRKL TSNLRIGFGA
FVDKPVSPYM FISPPQAIKN PCYTMKSTCL PMFGYKHVLT LTDQVTRFND EVKKQSVSRN
RDAPEGGFDA IMQATVCDEK IGWRNDASHL LVFTTDAKTH IALDGRLAGI VLPNDGRCHI
GPDNHYSAST TMDYPSLGLM TEKLSQKNIN LIFAVTENVV SLYQNYSELI PGTTVGVLSD
DSSNVLQLIV DAYGKIRSKV ELEVRDLPEE LSLSFNATCL NNEVIPGLKS CVGLKIGDTV
SFSIEAKVRG CPQQKEQSFT IKPVGFKDSL TVQVTFDCDC DCQAFAQPLS PRCNNGNGTF
ECGVCRCDQG WLGSMCECSE EDYRPSQQEE CSPKEGQPIC SQRGECLCGQ CVCHSSDFGK
ITGKYCECDD FSCVRYKGEM CSGHGQCNCG DCVCDSDWTG YYCNCTTRTD TCMSTNGLLC
SGRGNCECGS CVCVQPGSYG DTCEKCPTCP DACSFKKDCV ECKKFNRGKL HEENNCNRFC
RDDIELVKEL TDTGKNAVNC TYKNEDDCVV RFQYYEDSSG RAVLYVVEEP ECPKGPDILV
VLLSVMGAIL LIGLATLLIW KLLITIHDRK EFAKFEEERA RAKWDTANNP LYKEATSTFT
NITYRGT
