ID ITAV_MOUSE Reviewed; 1044 AA.
AC P43406; A2AKI6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 202.
DE RecName: Full=Integrin alpha-V;
DE AltName: Full=Vitronectin receptor subunit alpha;
DE AltName: CD_antigen=CD51;
DE Contains:
DE RecName: Full=Integrin alpha-V heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-V light chain;
DE Flags: Precursor;
GN Name=Itgav;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Kidney;
RX PubMed=8601592; DOI=10.1083/jcb.132.6.1161;
RA Wada J., Kumar A., Liu Z., Ruoslahti E., Reichardt L., Marvaldi J.,
RA Kanwar Y.S.;
RT "Cloning of mouse integrin alphaV cDNA and role of the alphaV-related
RT matrix receptors in metanephric development.";
RL J. Cell Biol. 132:1161-1176(1996).
RN [2]
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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9827803; DOI=10.1016/s0092-8674(00)81618-9;
RA Bader B.L., Rayburn H., Crowley D., Hynes R.O.;
RT "Extensive vasculogenesis, angiogenesis, and organogenesis precede
RT lethality in mice lacking all alpha v integrins.";
RL Cell 95:507-519(1998).
RN [4]
RP FUNCTION.
RX PubMed=10025398; DOI=10.1016/s0092-8674(00)80545-0;
RA Munger J.S., Huang X., Kawakatsu H., Griffiths M.J., Dalton S.L., Wu J.,
RA Pittet J.F., Kaminski N., Garat C., Matthay M.A., Rifkin D.B., Sheppard D.;
RT "The integrin alpha v beta 6 binds and activates latent TGF beta 1: a
RT mechanism for regulating pulmonary inflammation and fibrosis.";
RL Cell 96:319-328(1999).
RN [5]
RP FUNCTION.
RX PubMed=11323698; DOI=10.1038/87749;
RA Castells M.C., Klickstein L.B., Hassani K., Cumplido J.A., Lacouture M.E.,
RA Austen K.F., Katz H.R.;
RT "gp49B1-alpha(v)beta3 interaction inhibits antigen-induced mast cell
RT activation.";
RL Nat. Immunol. 2:436-442(2001).
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., Minamisawa S.,
RA Cheng C.F., Kobuke K., Dalton N., Takada Y., Tashiro K., Ross J., Honjo T.,
RA Chien K.R.;
RT "Fibulin-5/DANCE is essential for elastogenesis in vivo.";
RL Nature 415:171-175(2002).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-615; ASN-869 AND
RP ASN-941.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-615 AND ASN-869.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION.
RX PubMed=24935931; DOI=10.4049/jimmunol.1302772;
RA Fukao S., Haniuda K., Nojima T., Takai T., Kitamura D.;
RT "gp49B-mediated negative regulation of antibody production by memory and
RT marginal zone B cells.";
RL J. Immunol. 193:635-644(2014).
RN [11]
RP FUNCTION.
RX PubMed=25127859; DOI=10.4049/jimmunol.1401102;
RA Edwards J.P., Thornton A.M., Shevach E.M.;
RT "Release of active TGF-beta1 from the latent TGF-beta1/GARP complex on T
RT regulatory cells is mediated by integrin beta8.";
RL J. Immunol. 193:2843-2849(2014).
CC -!- FUNCTION: The alpha-V (ITGAV) integrins are receptors for vitronectin,
CC cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-
CC 2, osteopontin, osteomodulin, prothrombin, thrombospondin, TGFB1 and
CC vWF (PubMed:9827803, PubMed:10025398). They recognize the sequence R-G-
CC D in a wide array of ligands. Alpha-V integrins may play a role in
CC embryo implantation, angiogenesis and wound healing (PubMed:9827803).
CC ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act as its coreceptor
CC in CX3CR1-dependent fractalkine signaling (By similarity). ITGAV:ITGB3
CC binds to NRG1 (via EGF domain) and this binding is essential for NRG1-
CC ERBB signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential
CC for FGF1 signaling (By similarity). ITGAV:ITGB3 binds to FGF2 and this
CC binding is essential for FGF2 signaling (By similarity). ITGAV:ITGB3
CC binds to IGF1 and this binding is essential for IGF1 signaling (By
CC similarity). ITGAV:ITGB3 binds to IGF2 and this binding is essential
CC for IGF2 signaling (By similarity). ITGAV:ITGB3 binds to IL1B and this
CC binding is essential for IL1B signaling (By similarity). ITGAV:ITGB3
CC binds to PLA2G2A via a site (site 2) which is distinct from the
CC classical ligand-binding site (site 1) and this induces integrin
CC conformational changes and enhanced ligand binding to site 1 (By
CC similarity). ITGAV:ITGB3 and ITGAV:ITGB6 act as a receptor for
CC fibrillin-1 (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1
CC (By similarity). Integrin alpha-V/beta-6 or alpha-V/beta-8 (ITGAV:ITGB6
CC or ITGAV:ITGB8) mediates R-G-D-dependent release of transforming growth
CC factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide
CC (LAP), thereby playing a key role in TGF-beta-1 activation
CC (PubMed:10025398, PubMed:25127859). ITGAV:ITGB3 acts as a receptor for
CC CD40LG (By similarity). ITGAV:ITGB3 binds to the Lilrb4a/Gp49b receptor
CC and enhances the Lilrb4a-mediated inhibition of mast cell activation
CC (PubMed:11323698). ITGAV:ITGB3 also suppresses marginal zone B cell
CC antibody production through its interaction with Lilrb4a
CC (PubMed:24935931). ITGAV:ITGB3 acts as a receptor for IBSP and promotes
CC cell adhesion and migration to IBSP (By similarity).
CC {ECO:0000250|UniProtKB:P06756, ECO:0000269|PubMed:10025398,
CC ECO:0000269|PubMed:11323698, ECO:0000269|PubMed:24935931,
CC ECO:0000269|PubMed:25127859, ECO:0000269|PubMed:9827803}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit
CC is composed of a heavy and a light chain linked by a disulfide bond.
CC Alpha-V (ITGAV) associates with either beta-1 (ITGB1), beta-3 (ITGB3),
CC beta-5 (ITGB5), beta-6 (ITGB6) or beta-8 (ITGB8) (Probable). Interacts
CC with RAB25. Interacts with CIB1 (By similarity). Integrins ITGAV:ITGB3
CC and ITGAV:ITGB5 interact with FBLN5 (via N-terminus) (PubMed:11805835).
CC ITGAV:ITGB3 and ITGAV:ITGB5 interact with CCN3 (By similarity).
CC ITGAV:ITGB3 interacts with ADGRA2 (By similarity). ITGAV:ITGB3
CC interacts with FGF2; it is likely that FGF2 can simultaneously bind
CC ITGAV:ITGB3 and FGF receptors (By similarity). ITGAV:ITGB3 is found in
CC a ternary complex with CX3CR1 and CX3CL1. ITGAV:ITGB3 is found in a
CC ternary complex with NRG1 and ERBB3. ITGAV:ITGB3 is found in a ternary
CC complex with FGF1 and FGFR1. ITGAV:ITGB3 is found in a ternary complex
CC with IGF1 and IGF1R (By similarity). ITGAV:ITGB3 interacts with IGF2
CC (By similarity). ITGAV:ITGB3 and ITGAV:ITGB6 interact with FBN1 (By
CC similarity). ITGAV:ITGB3 interacts with CD9, CD81 and CD151 (via second
CC extracellular domain) (By similarity). ITGAV:ITGB6 interacts with TGFB1
CC (PubMed:10025398). ITGAV:ITGB3 interacts with PTN. Forms a complex with
CC PTPRZ1 and PTN that stimulates endothelial cell migration through ITGB3
CC 'Tyr-773' phosphorylation (By similarity).
CC {ECO:0000250|UniProtKB:P06756, ECO:0000269|PubMed:10025398,
CC ECO:0000269|PubMed:11805835, ECO:0000305|PubMed:11805835}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P06756}.
CC -!- DISRUPTION PHENOTYPE: Mice expressing a null mutation of the alpha-V
CC subunit gene survive until late in embryonic development and
CC occasionally even to birth. They demonstrate cleft palate, and
CC defective development of CNS and gastrointestinal blood vessels.
CC {ECO:0000269|PubMed:9827803}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; U14135; AAC52497.1; -; mRNA.
DR EMBL; AL772301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS16181.1; -.
DR PIR; T10050; T10050.
DR RefSeq; NP_032428.2; NM_008402.3.
DR AlphaFoldDB; P43406; -.
DR SMR; P43406; -.
DR BioGRID; 200824; 4.
DR ComplexPortal; CPX-3035; Integrin alphav-beta3 complex.
DR ComplexPortal; CPX-3130; Integrin alphav-beta1 complex.
DR ComplexPortal; CPX-3131; Integrin alphav-beta5 complex.
DR ComplexPortal; CPX-3132; Integrin alphav-beta6 complex.
DR ComplexPortal; CPX-3133; Integrin alphav-beta8 complex.
DR CORUM; P43406; -.
DR IntAct; P43406; 3.
DR STRING; 10090.ENSMUSP00000028499; -.
DR BindingDB; P43406; -.
DR ChEMBL; CHEMBL3430891; -.
DR ChEMBL; CHEMBL4523628; -.
DR GlyConnect; 2402; 13 N-Linked glycans (5 sites).
DR GlyCosmos; P43406; 12 sites, 13 glycans.
DR GlyGen; P43406; 13 sites, 13 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P43406; -.
DR PhosphoSitePlus; P43406; -.
DR SwissPalm; P43406; -.
DR EPD; P43406; -.
DR jPOST; P43406; -.
DR MaxQB; P43406; -.
DR PaxDb; 10090-ENSMUSP00000028499; -.
DR PeptideAtlas; P43406; -.
DR ProteomicsDB; 268896; -.
DR Pumba; P43406; -.
DR ABCD; P43406; 12 sequenced antibodies.
DR Antibodypedia; 1498; 1722 antibodies from 47 providers.
DR DNASU; 16410; -.
DR Ensembl; ENSMUST00000028499.11; ENSMUSP00000028499.5; ENSMUSG00000027087.12.
DR GeneID; 16410; -.
DR KEGG; mmu:16410; -.
DR UCSC; uc008kid.2; mouse.
DR AGR; MGI:96608; -.
DR CTD; 3685; -.
DR MGI; MGI:96608; Itgav.
DR VEuPathDB; HostDB:ENSMUSG00000027087; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000158361; -.
DR HOGENOM; CLU_004111_4_0_1; -.
DR InParanoid; P43406; -.
DR OMA; YILHYEV; -.
DR OrthoDB; 3816176at2759; -.
DR PhylomeDB; P43406; -.
DR TreeFam; TF105391; -.
DR Reactome; R-MMU-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
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-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-MMU-3000170; Syndecan interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-445144; Signal transduction by L1.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 16410; 18 hits in 82 CRISPR screens.
DR ChiTaRS; Itgav; mouse.
DR PRO; PR:P43406; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P43406; Protein.
DR Bgee; ENSMUSG00000027087; Expressed in cumulus cell and 282 other cell types or tissues.
DR ExpressionAtlas; P43406; baseline and differential.
DR Genevisible; P43406; MM.
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:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0034682; C:integrin alphav-beta1 complex; IEA:Ensembl.
DR GO; GO:0034683; C:integrin alphav-beta3 complex; ISO:MGI.
DR GO; GO:0034684; C:integrin alphav-beta5 complex; IDA:BHF-UCL.
DR GO; GO:0034685; C:integrin alphav-beta6 complex; IDA:CAFA.
DR GO; GO:0034686; C:integrin alphav-beta8 complex; ISS:UniProtKB.
DR GO; GO:0008305; C:integrin complex; ISS:BHF-UCL.
DR GO; GO:0031258; C:lamellipodium membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0031528; C:microvillus membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0019960; F:C-X3-C chemokine binding; IEA:Ensembl.
DR GO; GO:0050840; F:extracellular matrix binding; ISO:MGI.
DR GO; GO:1990430; F:extracellular matrix protein binding; ISO:MGI.
DR GO; GO:0017134; F:fibroblast growth factor binding; IEA:Ensembl.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0031994; F:insulin-like growth factor I binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IPI:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038132; F:neuregulin binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISS:BHF-UCL.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; ISO:MGI.
DR GO; GO:0043277; P:apoptotic cell clearance; IDA:BHF-UCL.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; ISS:BHF-UCL.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:CAFA.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0031589; P:cell-substrate adhesion; ISO:MGI.
DR GO; GO:0032490; P:detection of molecule of bacterial origin; TAS:BHF-UCL.
DR GO; GO:0035987; P:endodermal cell differentiation; ISO:MGI.
DR GO; GO:0043542; P:endothelial cell migration; TAS:BHF-UCL.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:BHF-UCL.
DR GO; GO:0009566; P:fertilization; NAS:BHF-UCL.
DR GO; GO:0048041; P:focal adhesion assembly; NAS:BHF-UCL.
DR GO; GO:0035262; P:gonad morphogenesis; NAS:BHF-UCL.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; TAS:BHF-UCL.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0050919; P:negative chemotaxis; ISO:MGI.
DR GO; GO:2000536; P:negative regulation of entry of bacterium into host cell; ISS:BHF-UCL.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0010888; P:negative regulation of lipid storage; ISS:BHF-UCL.
DR GO; GO:0032369; P:negative regulation of lipid transport; ISS:BHF-UCL.
DR GO; GO:0050748; P:negative regulation of lipoprotein metabolic process; ISS:BHF-UCL.
DR GO; GO:1905598; P:negative regulation of low-density lipoprotein receptor activity; ISS:BHF-UCL.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISS:BHF-UCL.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISO:MGI.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IMP:BHF-UCL.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISO:MGI.
DR GO; GO:0045124; P:regulation of bone resorption; TAS:BHF-UCL.
DR GO; GO:0050764; P:regulation of phagocytosis; ISS:BHF-UCL.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; ISS:UniProtKB.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; TAS:BHF-UCL.
DR GO; GO:0071731; P:response to nitric oxide; TAS:BHF-UCL.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0042110; P:T cell activation; TAS:BHF-UCL.
DR GO; GO:0071604; P:transforming growth factor beta production; IDA:CAFA.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; TAS:BHF-UCL.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
DR Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR013649; Integrin_alpha_Ig-like_1.
DR InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR InterPro; IPR048286; Integrin_alpha_Ig-like_3.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR PANTHER; PTHR23220:SF4; INTEGRIN ALPHA-V; 1.
DR Pfam; PF01839; FG-GAP; 3.
DR Pfam; PF08441; Integrin_A_Ig_1; 1.
DR Pfam; PF20805; Integrin_A_Ig_2; 1.
DR Pfam; PF20806; Integrin_A_Ig_3; 1.
DR Pfam; PF00357; Integrin_alpha; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 3.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cleavage on pair of basic residues; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Integrin; Membrane; Metal-binding; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000250"
FT CHAIN 31..1044
FT /note="Integrin alpha-V"
FT /id="PRO_0000016304"
FT CHAIN 31..885
FT /note="Integrin alpha-V heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016305"
FT CHAIN 887..1044
FT /note="Integrin alpha-V light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016306"
FT TOPO_DOM 31..988
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 989..1012
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1013..1044
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 32..98
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 109..170
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 173..225
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 237..291
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 292..357
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 358..415
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 419..482
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 1023..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1015..1019
FT /note="GFFKR motif"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 851
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 869
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 969
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 976
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 89..97
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 138..158
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 172..185
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 491..502
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 508..565
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 626..632
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 698..711
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 852..910
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 900..905
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT CONFLICT 526..527
FT /note="EL -> DV (in Ref. 1; AAC52497)"
FT /evidence="ECO:0000305"
FT CONFLICT 768..769
FT /note="VL -> EK (in Ref. 1; AAC52497)"
FT /evidence="ECO:0000305"
FT CONFLICT 872
FT /note="A -> G (in Ref. 1; AAC52497)"
FT /evidence="ECO:0000305"
FT CONFLICT 880
FT /note="N -> S (in Ref. 1; AAC52497)"
FT /evidence="ECO:0000305"
FT CONFLICT 887
FT /note="D -> G (in Ref. 1; AAC52497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1044 AA; 115360 MW; 417FD73D776B5918 CRC64;
MAAPGRLLLR PRPGGLLLLL PGLLLPLADA FNLDVESPAE YAGPEGSYFG FAVDFFEPST
SSRMFLLVGA PKANTTQPGI VEGGQVLKCE CSSSRRCQPI EFDSTGNRDY AKDDPLEFKS
HQWFGASVRS KQDKILACAP LYHWRTEMKQ EREPVGTCFL QDGTKTVEYA PCRSKNIDAD
GQGFCQGGFS IDFTKADRVL LGGPGSFYWQ GQLISDQVAE IISKYDPNVY SIKYNNQLAT
RTAQAIFDDS YLGYSVAVGD FNGDGIEDFV SGVPRAARTL GMVYIYDGKN MSSLHNFTGE
QMAAYFGFSV AATDINGDDY ADVFIGAPLF MDRGSDGKLQ EVGQVSVSLQ RAVGDFQTTK
LNGFEVFARF GSAIAPLGDL DQDGFNDIAI AAPYGGEDKK GLVYIFNGRS TGLNSVPSQI
LEGQWAAQSM PPSFGYSMKG ATDVDRNGYP DLVVGAFGVD RAVLYRARPV VTVNAGLEVY
PSILNQDNKI CPLPGTALKV SCFNVRFCLK ADGKGTLPRK LHFQVELLLD KLKQKGAIRR
ALFLHNRSPV HSKTMTVFRG GQMQCEELVA YLRDESEFRD KLTPITIFME YRLDQRTAAD
ATGLQPILNQ FTPANVSRQA HILLDCGEDN VCKPKLEVSV NSDQKKIYIG DDNPLTLTVK
AQNQGEGAYE AELIVSIPPQ ADFIGVVRNN EALARLSCAF KTENQTRQVV CDLGNPMKAG
TQLLAGLRFS VHQQSEMDTS VKFDLKIQSS NSFDNVSPVV SYKVDLAVLA AVEIRGVSSP
DHIFLPIPNW EYKENPETEE DVGPIVQHIY ELRNNGPSSF SKAILNLQWP YKYNNNTLLY
ILHYDIDGPM NCTADTEINP LRIKTPEKND TAAAGQGERN HLITKRDLTL REGDVHTLGC
GIAKCLQITC QVGRLDRGKS AILYVKSLLW TETFMNKENQ NHSYSLKSSA SFNIIEFPYK
NLPIEDLFNS TLVTTNITWG IQPAPMPVPV WVIILAVLAG LLLLAVLVFV MYRMGFFKRV
RPPQEEQERE QLQPHENGEG NSET
//
