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Integrin alpha-V (Vitronectin receptor subunit alpha) (CD antigen CD51) [Cleaved into: Integrin alpha-V heavy chain; Integrin alpha-V light chain]

 ITAV_BOVIN              Reviewed;        1048 AA.
P80746; Q0PDN6; Q9GK48; Q9MZD6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
07-NOV-2018, entry version 118.
RecName: Full=Integrin alpha-V;
AltName: Full=Vitronectin receptor subunit alpha;
AltName: CD_antigen=CD51;
Contains:
RecName: Full=Integrin alpha-V heavy chain;
Contains:
RecName: Full=Integrin alpha-V light chain;
Flags: Precursor;
Name=ITGAV;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH FMDV CAPSID PROTEINS
(MICROBIAL INFECTION).
TISSUE=Lung;
PubMed=10906183; DOI=10.1128/JVI.74.16.7298-7306.2000;
Neff S., Mason P.W., Baxt B.;
"High-efficiency utilization of the bovine integrin alpha(v)beta(3) as
a receptor for foot-and-mouth disease virus is dependent on the bovine
beta(3) subunit.";
J. Virol. 74:7298-7306(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
Du J., Chang H., Cong G., Shao J., Lin T., Liu Z., Liu X., Cai X.,
Xie Q.;
"Molecular cloning and characteristics of bovine alpha V cDNA.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 42-1048.
TISSUE=Mammary gland;
Andersen M.H., Rasmussen J.T., Berglund L., Petersen T.E.;
"Bovine alpha-V integrin subunit (fragment).";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 31-50 AND 891-910.
TISSUE=Mammary gland;
PubMed=9154926; DOI=10.1021/bi963119m;
Andersen M.H., Berglund L., Rasmussen J.T., Petersen T.E.;
"Bovine PAS-6/7 binds alpha v beta 5 integrins and anionic
phospholipids through two domains.";
Biochemistry 36:5441-5446(1997).
[5]
INTERACTION WITH HOST FMDV VP1 (MICROBIAL INFECTION).
PubMed=12551988; DOI=10.1128/JVI.77.4.2500-2511.2003;
Duque H., Baxt B.;
"Foot-and-mouth disease virus receptors: comparison of bovine alpha(V)
integrin utilization by type A and O viruses.";
J. Virol. 77:2500-2511(2003).
-!- FUNCTION: The alpha-V (ITGAV) integrins are receptors for
vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix
metalloproteinase-2, osteopontin, osteomodulin, prothrombin,
thrombospondin, TGFB1 and vWF. They recognize the sequence R-G-D
in a wide array of ligands. Alpha-V integrins may play a role in
embryo implantation, angiogenesis and wound healing (By
similarity). ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act
as its coreceptor in CX3CR1-dependent fractalkine signaling.
ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is
essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and
this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to
FGF2 and this binding is essential for FGF2 signaling. ITGAV:ITGB3
binds to IGF1 and this binding is essential for IGF1 signaling.
ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2
signaling. ITGAV:ITGB3 binds to IL1B and this binding is essential
for IL1B signaling. 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. ITGAV:ITGB3 and ITGAV:ITGB6 act as a
receptor for fibrillin-1 (FBN1) and mediate R-G-D-dependent cell
adhesion to FBN1 (By similarity). 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 (By similarity).
{ECO:0000250|UniProtKB:P06756, ECO:0000250|UniProtKB:P43406}.
-!- SUBUNIT: 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) (By similarity). Interacts with RAB25. Interacts with CIB1
(By similarity). Integrins ITGAV:ITGB3 and ITGAV:ITGB5 interact
with FBLN5 (via N-terminus) (By similarity). ITGAV:ITGB3 and
ITGAV:ITGB5 interact with NOV (By similarity). ITGAV:ITGB3
interacts with ADGRA2 (By similarity). ITGAV:ITGB3 interacts with
FGF2; it is likely that FGF2 can simultaneously bind ITGAV:ITGB3
and FGF receptors (By similarity). ITGAV:ITGB3 is found in a
ternary complex with CX3CR1 and CX3CL1. ITGAV:ITGB3 is found in a
ternary complex with NRG1 and ERBB3. ITGAV:ITGB3 is found in a
ternary complex with FGF1 and FGFR1. ITGAV:ITGB3 is found in a
ternary complex with IGF1 and IGF1R (By similarity). ITGAV:ITGB3
interacts with IGF2 (By similarity). ITGAV:ITGB3 and ITGAV:ITGB6
interact with FBN1 (By similarity). ITGAV:ITGB3 interacts with
CD9, CD81 and CD151 (via second extracellular domain) (By
similarity). ITGAV:ITGB6 interacts with TGFB1 (By similarity).
{ECO:0000250|UniProtKB:P06756, ECO:0000250|UniProtKB:P43406}.
-!- SUBUNIT: (Microbial infection) Alpha-V/beta-6 and alpha-V/beta-3
bind to foot-and-mouth disease virus (FMDV) VP1 protein and acts
as a receptor for this virus. {ECO:0000269|PubMed:10906183,
ECO:0000269|PubMed:12551988}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein. Cell junction, focal adhesion
{ECO:0000250|UniProtKB:P06756}.
-!- SIMILARITY: Belongs to the integrin alpha chain family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF239958; AAF44691.2; -; mRNA.
EMBL; DQ871215; ABH07896.1; -; mRNA.
EMBL; AF317199; AAG38595.1; -; mRNA.
RefSeq; NP_776792.1; NM_174367.1.
UniGene; Bt.5273; -.
ProteinModelPortal; P80746; -.
SMR; P80746; -.
IntAct; P80746; 1.
STRING; 9913.ENSBTAP00000026553; -.
PaxDb; P80746; -.
PeptideAtlas; P80746; -.
PRIDE; P80746; -.
GeneID; 281875; -.
KEGG; bta:281875; -.
CTD; 3685; -.
eggNOG; ENOG410IPB5; Eukaryota.
eggNOG; ENOG410YR19; LUCA.
HOGENOM; HOG000231603; -.
HOVERGEN; HBG006186; -.
InParanoid; P80746; -.
KO; K06487; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
GO; GO:0034685; C:integrin alphav-beta6 complex; ISS:UniProtKB.
GO; GO:0034686; C:integrin alphav-beta8 complex; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0001568; P:blood vessel development; ISS:AgBase.
GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:1901388; P:regulation of transforming growth factor beta activation; ISS:UniProtKB.
Gene3D; 2.130.10.130; -; 1.
InterPro; IPR013517; FG-GAP.
InterPro; IPR013519; Int_alpha_beta-p.
InterPro; IPR000413; Integrin_alpha.
InterPro; IPR013649; Integrin_alpha-2.
InterPro; IPR018184; Integrin_alpha_C_CS.
InterPro; IPR028994; Integrin_alpha_N.
InterPro; IPR032695; Integrin_dom_sf.
Pfam; PF01839; FG-GAP; 3.
Pfam; PF00357; Integrin_alpha; 1.
Pfam; PF08441; Integrin_alpha2; 1.
PRINTS; PR01185; INTEGRINA.
SMART; SM00191; Int_alpha; 5.
SUPFAM; SSF69179; SSF69179; 3.
PROSITE; PS51470; FG_GAP; 7.
PROSITE; PS00242; INTEGRIN_ALPHA; 1.
1: Evidence at protein level;
Calcium; Cell adhesion; Cell junction;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction; Integrin;
Membrane; Metal-binding; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 30 {ECO:0000269|PubMed:9154926}.
CHAIN 31 1048 Integrin alpha-V.
/FTId=PRO_0000016298.
CHAIN 31 889 Integrin alpha-V heavy chain.
/FTId=PRO_0000016299.
CHAIN 891 1048 Integrin alpha-V light chain.
/FTId=PRO_0000016300.
TOPO_DOM 31 992 Extracellular. {ECO:0000255}.
TRANSMEM 993 1016 Helical. {ECO:0000255}.
TOPO_DOM 1017 1048 Cytoplasmic. {ECO:0000255}.
REPEAT 32 98 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 109 170 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 173 225 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 237 291 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 292 357 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 358 415 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 419 482 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CA_BIND 260 268 {ECO:0000255}.
CA_BIND 314 322 {ECO:0000255}.
CA_BIND 379 387 {ECO:0000255}.
CA_BIND 443 451 {ECO:0000255}.
MOTIF 1019 1023 GFFKR motif.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 488 488 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 554 554 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 615 615 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 704 704 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 835 835 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 851 851 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 874 874 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 945 945 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 973 973 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 980 980 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 89 97 {ECO:0000250|UniProtKB:P06756}.
DISULFID 138 158 {ECO:0000250|UniProtKB:P06756}.
DISULFID 172 185 {ECO:0000250|UniProtKB:P06756}.
DISULFID 491 502 {ECO:0000250|UniProtKB:P06756}.
DISULFID 508 565 {ECO:0000250|UniProtKB:P06756}.
DISULFID 626 632 {ECO:0000250|UniProtKB:P06756}.
DISULFID 698 711 {ECO:0000250|UniProtKB:P06756}.
DISULFID 852 914 Interchain (between heavy and light
chains). {ECO:0000250|UniProtKB:P06756}.
DISULFID 904 909 {ECO:0000250|UniProtKB:P06756}.
CONFLICT 12 12 G -> R (in Ref. 2; ABH07896).
{ECO:0000305}.
CONFLICT 15 17 GLP -> RLL (in Ref. 2; ABH07896).
{ECO:0000305}.
CONFLICT 21 23 SGL -> PGI (in Ref. 2; ABH07896).
{ECO:0000305}.
CONFLICT 29 29 R -> G (in Ref. 2; ABH07896).
{ECO:0000305}.
CONFLICT 63 63 Missing (in Ref. 1; AAF44691).
{ECO:0000305}.
CONFLICT 152 152 R -> G (in Ref. 3; AAG38595).
{ECO:0000305}.
CONFLICT 189 189 F -> S (in Ref. 2; ABH07896).
{ECO:0000305}.
CONFLICT 242 242 T -> I (in Ref. 2; ABH07896).
{ECO:0000305}.
CONFLICT 354 354 G -> R (in Ref. 1; AAF44691).
{ECO:0000305}.
CONFLICT 415 415 A -> T (in Ref. 1; AAF44691).
{ECO:0000305}.
CONFLICT 621 621 H -> R (in Ref. 1; AAF44691).
{ECO:0000305}.
CONFLICT 629 629 D -> G (in Ref. 1; AAF44691).
{ECO:0000305}.
CONFLICT 860 860 P -> R (in Ref. 3; AAG38595).
{ECO:0000305}.
CONFLICT 870 870 T -> A (in Ref. 3; AAG38595).
{ECO:0000305}.
CONFLICT 873 873 K -> R (in Ref. 1; AAF44691).
{ECO:0000305}.
CONFLICT 894 894 L -> V (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 977 977 V -> I (in Ref. 2; ABH07896).
{ECO:0000305}.
SEQUENCE 1048 AA; 116132 MW; A6A5620EB3144502 CRC64;
MAFPPRRRLR LGPRGLPLLL SGLLLPLCRA FNLDVESPAE YSGPEGSYFG FAVDFFVPSA
SSRMFLLVGA PKANTTQPGI VEGGQVLKCD WSSHRRCQPI EFDATGNRDY AKDDPLEFKS
HQWFGASVRS KQDKILACAP LYHWRTEMKQ EREPVGTCFL QDGTKTVEYA PCRSKNIDAD
GQGFCQGGFS IDFTKADRVL LGGPGSFYWQ GQLISDQVAE IVSKYDPKVY SIKYNNQLAT
RTAQAIFDDS YLGYSVAVGD FNGDGIDDFV SGVPRAARTL GMVYIYDGKN MSSLHNFTGE
QMAAYFGFSV AATDINGDDY ADVFIGAPLF MDRGSDGKLQ EVGQVSVSLQ KASGDFQTIK
LNGFEVFARF GSAIAPLGDL DQDGFNDIAI AAPYGGEDKK GIVYIFNGRP TGLNAVPSQI
LEGKWAARSM PPSFGYSMKG ATDIDKNGYP DLIVGAFGVD RAVLYRARPV ITVNAGLEVY
PSILNQENKT CPLPGTDLKV SCFNVRFCLK ADGKGALPTK LDFQVELLLD KLKQKGAIRR
ALFLHNRSPG HSKNMTISRG GQMQCEELIA YLRDESEFRD KLTPITIFME YWLDYRTAAD
ATGLQPILNQ FTPANVSRQA HILLDCGEDN VCKPKLEVSV DSDQKKIYIG DDNPLTLIVK
AQNQGEGAYE AELIVSIPLQ ADFIGVVRNS EALARLSCAF KTENQTRQVV CDLGNPMKAG
TQLLAGLRFS VHQQSEMDTS VKFDLQIQSS NLFDKVSPVV SYKVDLAVLA AVEIRGVSSP
DHIFLPIPNW KYKENPETEE DVGPVVQHIY ELRNNGPSSF SKAMLHLQWP YKYNNNTLLY
ILQYDIDGPM NCTSDMEINP LRIKISNSQT SEKNDTVGGQ GDRNHLITKR DLTLNEGDVH
TLGCGIAECL KIVCQVGRLD RGKSAILYVR SLLWTETFMN KENQNHSYSL KSSASFNVIE
FPYKNLPIED IFNSTLVTTN VTWGIQPAPM PVPVWVIILA VLAGLLLLAV LVFVMYRMGF
FKRVRPPQEE QEREQLQPHE NGEGNSET


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