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Database: UniProt
Entry: F7G9T4_ORNAN
LinkDB: F7G9T4_ORNAN
Original site: F7G9T4_ORNAN 
ID   F7G9T4_ORNAN            Unreviewed;      1041 AA.
AC   F7G9T4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 3.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Integrin subunit alpha V {ECO:0000313|Ensembl:ENSOANP00000024807.3};
GN   Name=ITGAV {ECO:0000313|Ensembl:ENSOANP00000024807.3};
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000024807.3, ECO:0000313|Proteomes:UP000002279};
RN   [1] {ECO:0000313|Ensembl:ENSOANP00000024807.3}
RP   IDENTIFICATION.
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000024807.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC       ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC       {ECO:0000256|ARBA:ARBA00008054, ECO:0000256|RuleBase:RU003762}.
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DR   AlphaFoldDB; F7G9T4; -.
DR   STRING; 9258.ENSOANP00000024807; -.
DR   Ensembl; ENSOANT00000024811.3; ENSOANP00000024807.3; ENSOANG00000015741.3.
DR   eggNOG; KOG3637; Eukaryota.
DR   GeneTree; ENSGT00940000158361; -.
DR   InParanoid; F7G9T4; -.
DR   OMA; YILHYEV; -.
DR   TreeFam; TF105391; -.
DR   Proteomes; UP000002279; Unplaced.
DR   Bgee; ENSOANG00000015741; Expressed in endometrium and 8 other cell types or tissues.
DR   GO; GO:0035868; C:alphav-beta3 integrin-HMGB1 complex; IEA:Ensembl.
DR   GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0031527; C:filopodium membrane; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0034682; C:integrin alphav-beta1 complex; IEA:Ensembl.
DR   GO; GO:0034683; C:integrin alphav-beta3 complex; IEA:Ensembl.
DR   GO; GO:0034684; C:integrin alphav-beta5 complex; IEA:Ensembl.
DR   GO; GO:0034685; C:integrin alphav-beta6 complex; IEA:Ensembl.
DR   GO; GO:0034686; C:integrin alphav-beta8 complex; IEA:Ensembl.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0031258; C:lamellipodium membrane; IEA:Ensembl.
DR   GO; GO:0031528; C:microvillus membrane; IEA:Ensembl.
DR   GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0019960; F:C-X3-C chemokine binding; IEA:Ensembl.
DR   GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR   GO; GO:1990430; F:extracellular matrix protein binding; IEA:Ensembl.
DR   GO; GO:0017134; F:fibroblast growth factor binding; IEA:Ensembl.
DR   GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR   GO; GO:0031994; F:insulin-like growth factor I binding; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0038132; F:neuregulin binding; IEA:Ensembl.
DR   GO; GO:0001846; F:opsonin binding; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:Ensembl.
DR   GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR   GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0043277; P:apoptotic cell clearance; IEA:Ensembl.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IEA:Ensembl.
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:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR   GO; GO:0034113; P:heterotypic cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0050919; P:negative chemotaxis; IEA:Ensembl.
DR   GO; GO:2000536; P:negative regulation of entry of bacterium into host cell; IEA:Ensembl.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0010888; P:negative regulation of lipid storage; IEA:Ensembl.
DR   GO; GO:0032369; P:negative regulation of lipid transport; IEA:Ensembl.
DR   GO; GO:0050748; P:negative regulation of lipoprotein metabolic process; IEA:Ensembl.
DR   GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl.
DR   GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IEA:Ensembl.
DR   GO; GO:0050764; P:regulation of phagocytosis; IEA:Ensembl.
DR   GO; GO:1901388; P:regulation of transforming growth factor beta activation; IEA:Ensembl.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0071604; P:transforming growth factor beta production; IEA:Ensembl.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:Ensembl.
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; 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   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.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW   ECO:0000256|RuleBase:RU003762};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU003762};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU003762};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003762};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU003762}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   CHAIN           18..1041
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT                   /id="PRO_5028521026"
FT   TRANSMEM        980..1001
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   REPEAT          19..84
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          95..156
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          159..211
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          223..277
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          278..343
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          344..401
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          405..468
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   DOMAIN          453..611
FT                   /note="Integrin alpha first immunoglubulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF08441"
FT   DOMAIN          612..741
FT                   /note="Integrin alpha second immunoglobulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF20805"
FT   DOMAIN          758..969
FT                   /note="Integrin alpha third immunoglobulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF20806"
FT   REGION          853..878
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        862..878
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1041 AA;  115203 MW;  3EE55295A5989603 CRC64;
     MVPGRVPVLV LLPLAAAFNL DVSRPAEYSG PRGSYFGFAV DFFAPDSSSM SLLVGAPKAN
     TSQPGIVEGG QVLKCHWPSG HTCQPVTFDS TGNRDYAKND PLEFKSHQWF GASVRSKKDK
     ILACAPLYHW RTEQKQEREP VGTCFLQDGT KTVEYAPCRS RSIDADGQGF CQGGFSIDFT
     KADRVLLGGP GSFYWQGQLI SDQVAEIVSK YDPKVYSIKY NNQLATRAAQ AFFDDSYLGY
     SVAVGDFNGD GIEDFVSGVP RAARTLGMVY IYNGKNMSSL YNFTGEQMAA YFGFSVAATD
     INGDDYADVF IGAPLFMDRG SDGKLQEVGQ VSICLQEASG GFRTLKLNGF EVFARFGSAV
     APLGDLDQDG FNDIAVAAPY GGEDKSGIVY IYNGRATGLN SMPSQILQGH WVSRTMPPSF
     GYSLKGATDI DQNGYPDLIV GAFGVDRAVL YRARPVITVN AVLEVDPTIL NPENKTCSLT
     GTDIKVSCFS VRFCLKADGK GNLPKKLNFQ VELLLDKLKQ KGAIRRALFL HNRSPGHSKN
     MTISKGGQMQ CEELQAYLRD ESEFRDKLTP ITVFMEYRLD YQTAADATGL QPILNQFTPA
     NISRQAHILL DCGEDNVCRP KLEVSVHSDQ KKIYIGDDNP LTLMVNAQNQ GEGAYEAELI
     VTLPPQADFI GVIRNNEALS RLSCAFKTEN QTRQVVCDLG NPMKDGTKLL AGLRFSVHQQ
     SELDTSVRFD LQIHSSNQYD KVSPIASYTV DLAVLAAVEI RGVSSPDHVF LPIPNWEPKD
     YPETEEDVGP VVQHIYELRN SGPSSFSKAM LRLQWPHRYN NNTLLYILHY EIDGPMNCTS
     DMEINPLKIK ISASPTDDRN ETSLGQGDHS NHISKRDLTS TEQDIHTLGC GTAECLKIDC
     QIGRLERGKS AILFVKSLLW TETFMNKENQ NQSYSLKSSA SFNVIEFPYK NLPIDDIHNS
     TVVTTDVNWG IQPSSMPVPV WVIILAVLAG LLLLAVLVLV MHKARSCTFR RWNQMRRSSQ
     GYWRWKNFFL NCHCGSQILA I
//
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