ITGAV

The product of this gene belongs to the integrin alpha chain family. Integrins are heterodimeric integral membrane proteins composed of an alpha subunit and a beta subunit that function in cell surface adhesion and signaling. The encoded preproprotein is proteolytically processed to generate light and heavy chains that comprise the alpha V subunit. This subunit associates with beta 1, beta 3, beta 5, beta 6 and beta 8 subunits. The heterodimer consisting of alpha V and beta 3 subunits is also known as the vitronectin receptor. This integrin may regulate angiogenesis and cancer progression. Alternative splicing results in multiple transcript variants. Note that the integrin alpha 5 and integrin alpha V subunits are encoded by distinct genes. [provided by RefSeq, Oct 2015]

Integrin Subunit Alpha V

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 a receptor 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 act as a receptor for CD40LG (PubMed:31331973).
(Microbial infection) Integrin ITGAV:ITGB5 acts as a receptor for Adenovirus type C.
(Microbial infection) Integrin ITGAV:ITGB5 and ITGAV:ITGB3 act as receptors for Coxsackievirus A9 and B1.
(Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Herpes virus 8/HHV-8.
(Microbial infection) Integrin ITGAV:ITGB6 acts as a receptor for herpes simplex 1/HHV-1.
(Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Human parechovirus 1.
(Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for West nile virus.
(Microbial infection) In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.

AngiogenesisManual Assertion Based On ExperimentIEP:UniProtKB
Apolipoprotein A-I-mediated signaling pathwayManual Assertion Based On ExperimentIMP:UniProtKB
Apoptotic cell clearanceManual Assertion Based On ExperimentIGI:BHF-UCL
Calcium ion transmembrane transportManual Assertion Based On ExperimentIDA:UniProtKB
Cell adhesionManual Assertion Based On ExperimentIDA:BHF-UCL
Cell adhesion mediated by integrinManual Assertion Based On ExperimentIDA:UniProtKB
Cell migrationManual Assertion Based On ExperimentIMP:BHF-UCL
Cell-matrix adhesionManual Assertion Based On ExperimentIMP:UniProtKB
Cell-substrate adhesionManual Assertion Based On ExperimentIMP:UniProtKB
Endodermal cell differentiationManual Assertion Based On ExperimentIMP:UniProtKB
Entry into host cell by a symbiont-containing vacuole1 PublicationNAS:BHF-UCL
ERK1 and ERK2 cascadeISS:BHF-UCL
Extrinsic apoptotic signaling pathway in absence of ligandISS:BHF-UCL
Heterotypic cell-cell adhesionManual Assertion Based On ExperimentIMP:UniProtKB
Integrin-mediated signaling pathwayManual Assertion Based On ExperimentIDA:ComplexPortal
Negative chemotaxisManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of entry of bacterium into host cellManual Assertion Based On ExperimentIDA:BHF-UCL
Negative regulation of extrinsic apoptotic signaling pathwayManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of lipid storageManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of lipid transportManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of lipoprotein metabolic processManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of low-density lipoprotein receptor activityManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of macrophage derived foam cell differentiationManual Assertion Based On ExperimentIMP:BHF-UCL
Positive regulation of cell adhesionManual Assertion Based On ExperimentIDA:BHF-UCL
Positive regulation of cell migrationIEA:Ensembl
Positive regulation of cell population proliferationManual Assertion Based On ExperimentIDA:BHF-UCL
Positive regulation of cytosolic calcium ion concentrationIEA:Ensembl
Positive regulation of intracellular signal transductionManual Assertion Based On ExperimentIMP:BHF-UCL
Positive regulation of osteoblast proliferationIEA:Ensembl
Positive regulation of small GTPase mediated signal transductionManual Assertion Based On ExperimentIMP:BHF-UCL
Regulation of phagocytosisManual Assertion Based On ExperimentIDA:BHF-UCL
Regulation of transforming growth factor beta activationManual Assertion Based On ExperimentIDA:UniProtKB
Substrate adhesion-dependent cell spreadingManual Assertion Based On ExperimentIDA:UniProtKB
Transforming growth factor beta productionIEA:Ensembl
VasculogenesisIEA:Ensembl
Viral entry into host cellManual Assertion Based On ExperimentIMP:UniProtKB

Cell membrane; Cell junction, focal adhesion

Extracellular: 31-992
Helical: 993-1016
Cytoplasmic: 1017-1048