ID F7D459_MONDO Unreviewed; 1058 AA.
AC F7D459;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Integrin subunit alpha V {ECO:0000313|Ensembl:ENSMODP00000013342.3};
GN Name=ITGAV {ECO:0000313|Ensembl:ENSMODP00000013342.3};
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000013342.3, ECO:0000313|Proteomes:UP000002280};
RN [1] {ECO:0000313|Ensembl:ENSMODP00000013342.3, ECO:0000313|Proteomes:UP000002280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17495919; DOI=10.1038/nature05805;
RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT coding sequences.";
RL Nature 447:167-177(2007).
RN [2] {ECO:0000313|Ensembl:ENSMODP00000013342.3}
RP IDENTIFICATION.
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 RefSeq; XP_007494546.1; XM_007494484.2.
DR AlphaFoldDB; F7D459; -.
DR STRING; 13616.ENSMODP00000013342; -.
DR Ensembl; ENSMODT00000013587.4; ENSMODP00000013342.3; ENSMODG00000010653.4.
DR GeneID; 100028127; -.
DR KEGG; mdo:100028127; -.
DR CTD; 3685; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000158361; -.
DR HOGENOM; CLU_004111_4_0_1; -.
DR InParanoid; F7D459; -.
DR OMA; YILHYEV; -.
DR OrthoDB; 3816176at2759; -.
DR TreeFam; TF105391; -.
DR Proteomes; UP000002280; Chromosome 4.
DR Bgee; ENSMODG00000010653; Expressed in extraembryonic membrane and 19 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:0002020; F:protease 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: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:0008284; P:positive regulation of cell population 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: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; 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 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:UP000002280};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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..41
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 42..1058
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003355901"
FT TRANSMEM 1004..1026
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 43..108
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 119..180
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 183..235
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 247..301
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 302..367
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 368..425
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 429..492
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 477..635
FT /note="Integrin alpha first immunoglubulin-like"
FT /evidence="ECO:0000259|Pfam:PF08441"
FT DOMAIN 636..774
FT /note="Integrin alpha second immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20805"
FT DOMAIN 782..993
FT /note="Integrin alpha third immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20806"
FT REGION 1037..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 117465 MW; 7CD0D4F1CB5DE7EF CRC64;
MAPWLGRKRR RQLQLLHLQR RCLHLLLPGL LLLLLPPPGS AFNLDVDSPA EYSGPEGSYF
GFAVDFFAPD PSSMFLLVGA PKANTTQPGI VEGGQVLKCS WSSNRFCQPV EFDSTGNRDY
AKNDPLEFKS HQWFGASVRS KQDKILACAP LYHWRTELKQ EREPVGTCFL QDGTKTVEYA
PCRSKNIDAD GQGFCQGGFS IDFTKADRVL LGGPGSFYWQ GQLISDQVAE IVSKYDPHVY
SIKYNNQLAT RTAQAVFDDS YLGYSVAVGD FNDDGIEDFV SGVPRAARTL GMVYIYDGKN
MSSLYNFTGE QMAAYFGFSV ASTDINGDDY ADVFIGAPLF MDRGSDGKLQ EVGQVSMCLQ
QASGGFQIIK LNGFEIFARF GSAIAPLGDL DQDGFNDVAI AAPYGGEDKR GIVYIYNGRA
TGLNSAPSQI LEGKWAARAM PPSFGYSLKG ATDIDQNGYP DLIVGAFGVD RAVLYRARPV
ITVNAVLEVY PTILNQDNKT CPLPGTDVKV SCFNVRFCLK ADGKGRLPEK LNFQVELLLD
KLKQKGAIRR ALFLHNKSPG HSKNMSISKG GQMQCEELTA YLRDESEFRD KLTPITIFME
YWLDYKTAAD VTGLQPILNQ FTPANISRQA HILLDCGEDN ICKPKLEVSV HSDQKKIYIG
DDNPLTLIVN AQNLGEGAYE AELIVSIPPQ ADFIGGVRNS ETLSRLSCAF KTENQTRQVV
CDLGNPMKAG TKLLAGLRFS VHQQSEIDTS VKFDLQIQSS NLYDKVSPMI SYKVDLAISA
AVEIRGVSSP DHVFLPIPNW EYKENPQTEE DVGPVVQHIY ELRNNGPSSF SKAMLNLQWP
YKYKNNTLLY ILHYEVDGPM NCTSDMEINP LKIKISSPKI DEKNETILGQ GDRNHHVSKR
NLPPSEGDVH TLGCGIAECL KIVCQVGRLD RGKSVILYVK SLLWTETFMN KENQNHSYSL
KSSASFNVIE FPYKNLPIDD IHNSTLVTTN ITWGIQPSTM PVPLWVIILA VLAGLLLLAV
LVFVMYRMGF FKRVRPPQEE QEREQLQPHE NGEGTSDA
//
