{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P06756","secondaryAccessions":["A0AV67","B0LPF4","B7Z883","B7ZLX0","D3DPG8","E7EWZ6","Q53SK4","Q59EB7","Q6LD15"],"uniProtkbId":"ITAV_HUMAN","entryAudit":{"firstPublicDate":"1988-01-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-04-03","entryVersion":268,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Integrin alpha-V"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:6150"}],"value":"Vitronectin receptor"}},{"fullName":{"value":"Vitronectin receptor subunit alpha"}}],"cdAntigenNames":[{"value":"CD51"}],"contains":[{"recommendedName":{"fullName":{"value":"Integrin alpha-V heavy chain"}}},{"recommendedName":{"fullName":{"value":"Integrin alpha-V light chain"}}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:6150"}],"value":"ITGAV"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:6150"}],"value":"MSK8"},{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:6150"}],"value":"VNRA"},{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:6150"}],"value":"VTNR"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10640428"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12807887"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15184403"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17158881"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18441324"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18635536"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19578119"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20682778"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22278742"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23125415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25398877"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28117447"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28302677"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28873464"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29030430"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31331973"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39713860"}],"value":"The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415). ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling (PubMed:18441324). ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling (PubMed:28302677). ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:19578119). ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464). ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling (PubMed:29030430). 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 (PubMed:18635536, PubMed:25398877). ITGAV:ITGB3 and ITGAV:ITGB6 act as receptors for fibrillin-1 (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881). Integrin alpha-V/beta-6 or alpha-V/beta-8 (ITGAV:ITGB6 or ITGAV:ITGB8) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation (PubMed:15184403, PubMed:22278742, PubMed:28117447). ITGAV:ITGB3 acts as a receptor for CD40LG (PubMed:31331973). ITGAV:ITGB3 acts as a receptor for IBSP and promotes cell adhesion and migration to IBSP (PubMed:10640428). ITGAV:ITGB3 acts as a receptor for SNED1 and mediates R-G-D-dependent cell adhesion to SNED1 (PubMed:39713860)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20615244"}],"value":"(Microbial infection) Integrin ITGAV:ITGB5 acts as a receptor for Adenovirus type C"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15194773"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7519807"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9426447"}],"value":"(Microbial infection) Integrin ITGAV:ITGB5 and ITGAV:ITGB3 act as receptors for Coxsackievirus A9 and B1"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18045938"}],"value":"(Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Herpes virus 8/HHV-8"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24367260"}],"value":"(Microbial infection) Integrin ITGAV:ITGB6 acts as a receptor for herpes simplex 1/HHV-1"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11160695"}],"value":"(Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Human parechovirus 1"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23658209"}],"value":"(Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for West nile virus"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10397733"}],"value":"(Microbial infection) In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P43406"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P80746"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12695522"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12807887"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16982628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17158881"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17925226"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18441324"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19141530"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19578119"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20615244"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20682778"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22278742"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23125415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23658209"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24011356"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27993971"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28117447"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28302677"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28873464"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29030430"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37184585"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38016540"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39197621"}],"value":"Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-V (ITGAV) associates with either beta-1 (ITGB1), beta-3 (ITGB3), beta-5 (ITGB5), beta-6 (ITGB6) or beta-8 (ITGB8). Interacts with CIB1 (PubMed:24011356). Interacts with RAB25 (PubMed:17925226). Integrins ITGAV:ITGB3 and ITGAV:ITGB5 interact with FBLN5 (via N-terminus) (By similarity). ITGAV:ITGB3 and ITGAV:ITGB5 interact with CCN3 (PubMed:12695522). ITGAV:ITGB3 interacts with ADGRA2 (PubMed:16982628). ITGAV:ITGB3 interacts with FGF2; it is likely that FGF2 can simultaneously bind ITGAV:ITGB3 and FGF receptors (PubMed:28302677). ITGAV:ITGB3 interacts with IL1B (PubMed:29030430). ITGAV:ITGB3 interacts with SELP (via C-type lectin domain); the interaction mediates cell-cell interaction and adhesion (PubMed:37184585). ITGAV:ITGB3 is found in a ternary complex with CX3CR1 and CX3CL1 (PubMed:23125415). ITGAV:ITGB3 is found in a ternary complex with NRG1 and ERBB3 (PubMed:20682778). ITGAV:ITGB3 is found in a ternary complex with FGF1 and FGFR1 (PubMed:18441324). ITGAV:ITGB3 is found in a ternary complex with IGF1 and IGF1R (PubMed:19578119). ITGAV:ITGB3 interacts with IGF2 (PubMed:28873464). ITGAV:ITGB3 and ITGAV:ITGB6 interact with FBN1 (PubMed:12807887, PubMed:17158881). ITGAV:ITGB3 interacts with CD9, CD81 and CD151 (via second extracellular domain) (PubMed:27993971). ITGAV:ITGB6 interacts with TGFB1 (PubMed:22278742, PubMed:28117447). ITGAV:ITGB3 interacts with PTN (PubMed:19141530). Forms a complex with PTPRZ1 and PTN that stimulates endothelial cell migration through ITGB3 'Tyr-773' phosphorylation (PubMed:19141530). Interacts with TM4SF19 (PubMed:38016540). ITGAV:ITGB3 interacts with Bothrops moojeni disintegrin Moojecin; the interaction may inhibit ADP-induced platelet aggregation in human plasma (PubMed:39197621)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18045938"}],"value":"(Microbial infection) Integrin ITGAV:ITGB3 interacts with herpes virus 8/HHV-8 envelope glycoprotein B"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15194773"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7519807"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9426447"}],"value":"(Microbial infection) Integrin ITGAV:ITGB3 and ITGAV:ITGB6 bind to coxsackievirus A9 and coxsackievirus B1 capsid proteins (PubMed:15194773, PubMed:7519807, PubMed:9426447)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24367260"}],"value":"(Microbial infection) Integrin ITGAV:ITGB6 interacts 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