ITAV_CHICK
ID ITAV_CHICK Reviewed; 1034 AA.
AC P26008;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Integrin alpha-V;
DE AltName: Full=Vitronectin receptor subunit alpha;
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=1703004; DOI=10.1021/bi00496a006;
RA Bossy B., Reichardt L.F.;
RT "Chick integrin alpha V subunit molecular analysis reveals high
RT conservation of structural domains and association with multiple beta
RT subunits in embryo fibroblasts.";
RL Biochemistry 29:10191-10198(1990).
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. They recognize the sequence R-G-D in a wide array of ligands.
CC Alpha-V integrins may play a role in embryo implantation, angiogenesis
CC and wound healing (By similarity). ITGAV:ITGB3 binds to fractalkine
CC (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine
CC signaling. ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding
CC is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and
CC this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to FGF2
CC and this binding is essential for FGF2 signaling. ITGAV:ITGB3 binds to
CC IGF1 and this binding is essential for IGF1 signaling. ITGAV:ITGB3
CC binds to IGF2 and this binding is essential for IGF2 signaling.
CC ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B
CC signaling. ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is
CC distinct from the classical ligand-binding site (site 1) and this
CC induces integrin conformational changes and enhanced ligand binding to
CC site 1. ITGAV:ITGB3 and ITGAV:ITGB6 act as receptors for fibrillin-1
CC (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1 (By
CC similarity). Integrin alpha-V/beta-6 or alpha-V/beta-8 (ITGAV:ITGB6 or
CC 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 (By
CC similarity). ITGAV:ITGB3 acts as a receptor for CD40LG (By similarity).
CC {ECO:0000250|UniProtKB:P06756, ECO:0000250|UniProtKB:P43406}.
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) (By similarity).
CC Interacts with RAB25. Interacts with CIB1 (By similarity). Integrins
CC ITGAV:ITGB3 and ITGAV:ITGB5 interact with FBLN5 (via N-terminus) (By
CC similarity). ITGAV:ITGB3 and ITGAV:ITGB5 interact with CCN3 (By
CC similarity). ITGAV:ITGB3 interacts with ADGRA2 (By similarity).
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 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 is found in a ternary complex with IGF1 and IGF1R (By
CC similarity). ITGAV:ITGB3 interacts with IGF2 (By similarity).
CC ITGAV:ITGB3 and ITGAV:ITGB6 interact with FBN1 (By similarity).
CC ITGAV:ITGB3 interacts with CD9, CD81 and CD151 (via second
CC extracellular domain) (By similarity). ITGAV:ITGB6 interacts with TGFB1
CC (By similarity). {ECO:0000250|UniProtKB:P06756,
CC ECO:0000250|UniProtKB:P43406}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cell junction, focal adhesion {ECO:0000250|UniProtKB:P06756}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; M60517; AAA49138.1; -; mRNA.
DR PIR; A36108; A36108.
DR RefSeq; NP_990770.1; NM_205439.1.
DR AlphaFoldDB; P26008; -.
DR SMR; P26008; -.
DR BioGRID; 676669; 2.
DR STRING; 9031.ENSGALP00000004173; -.
DR PaxDb; P26008; -.
DR PRIDE; P26008; -.
DR GeneID; 396420; -.
DR KEGG; gga:396420; -.
DR CTD; 3685; -.
DR VEuPathDB; HostDB:geneid_396420; -.
DR eggNOG; KOG3637; Eukaryota.
DR InParanoid; P26008; -.
DR OrthoDB; 743479at2759; -.
DR PhylomeDB; P26008; -.
DR PRO; PR:P26008; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0034685; C:integrin alphav-beta6 complex; ISS:UniProtKB.
DR GO; GO:0034686; C:integrin alphav-beta8 complex; ISS:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; ISS:UniProtKB.
DR Gene3D; 2.130.10.130; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 3.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell junction; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; Integrin; Membrane; Metal-binding; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1034
FT /note="Integrin alpha-V"
FT /id="PRO_0000016307"
FT CHAIN 20..875
FT /note="Integrin alpha-V heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016308"
FT CHAIN 877..1034
FT /note="Integrin alpha-V light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016309"
FT TOPO_DOM 20..978
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 979..1002
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1003..1034
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 21..86
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 97..158
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 161..213
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 225..279
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 280..345
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 346..403
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 407..470
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 1013..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1005..1009
FT /note="GFFKR motif"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 310
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 367
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 369
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 373
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 433
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT BINDING 439
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 837
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 951
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 959
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..85
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 126..146
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 160..173
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 479..488
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 494..551
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 612..618
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 684..697
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 838..890
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250|UniProtKB:P06756"
FT DISULFID 895..900
FT /evidence="ECO:0000250|UniProtKB:P06756"
SQ SEQUENCE 1034 AA; 114389 MW; D76B0B8A692DC684 CRC64;
MAALRASLLL SCALTAARAF NLDAERPAVY SGAEGSYFGF AVDFFAPDAS SMFLLVGAPK
ANTSQSNVVE GGQVLQCNWN SNRNCQPIIF DSTGNRDFAP DDPLEFKSHQ WFGASVRSKN
DKILACAPLY HWRTETKQER EPVGTCYLFD GSKSVEYAPC RSTTIDADGQ GFCQGGFSID
FTKGDRVLLG GPGSFYWQGQ LISDRVAEIL AKYDSKVYST KYDDQLATRP ASAAFDDSYL
GYSVAVGDFS GDGIEDFVSG VPRAARTLGM VSIYNGKNMS SMYNFTGEQM AAYFGYSVAT
TDINGDDYTD LFIGAPLFMD RGSDGKLQEV GQVSICLQRA SGGFQIAKLN GFEIFARFGS
AIAPLGDLDQ DGFNDIAVAA PYGGEDKRGL VYIYNGRATG LNAVPSRILE GQWAARTMPP
SFGYSLKGAT DVDKNGYPDL IVGAFGVDTA VLYRARPVIR VNAALEVNPT ILNPENKACS
LADVKVSCFK VKFCLKADGK GKLPNSLNFQ VELLLDKLKQ KGAIRRALFL HSKQPSHSKN
MTITKGGKMN CEELDAFLRD ESEFRDKLTP ITIFMEYRLD YKTAVDATGL HPILNQFIPA
NMSRQAHILL DCGEDNICKP KLEVSVRSDQ KKIYIGDDNP LTLIVTAENQ GEGAYEAELF
VIVPPQADFI GVVRNNEALA RLSCAFKTEN QTRMVVCDLG NPMKAGTKLL AGLRFSVHQQ
SEMDTSVKFD LQIRSSNLFD NLSPVAFYQV DLAISAAVEI RGVSSPDHIF LPIANWQPKE
NPETEDDIGP LVQHIYELRN NGPSAFSKVM MTLQWPYKYK NYTLLYIVQY DIDGPMNCTS
DMEINPLKIK ISAPKEDEKN ETFSREDNRN HRISRRDLTA IEGDVQTLGC GNADCLKIVC
QVGHLERGKS AILYLKSRLW TQTFMNKENQ NHSYSLQSSA SFNVIEFPYK NLSFEDIHNS
TVVTTNITWG IQPQPMPVPV WVIILAVLAG LLLLAVLVLV MYRMGFFKRV RPPQEEQERE
QLQPHENGEG TSEA
