ID A0A0G2JVZ6_RAT Unreviewed; 1007 AA.
AC A0A0G2JVZ6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Integrin subunit alpha V {ECO:0000313|Ensembl:ENSRNOP00000069681.2};
GN Name=Itgav {ECO:0000313|Ensembl:ENSRNOP00000069681.2,
GN ECO:0000313|RGD:1310613};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000069681.2, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000069681.2, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069681.2,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000069681.2}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069681.2};
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; A0A0G2JVZ6; -.
DR STRING; 10116.ENSRNOP00000069681; -.
DR jPOST; A0A0G2JVZ6; -.
DR Ensembl; ENSRNOT00000088549.2; ENSRNOP00000069681.2; ENSRNOG00000004912.8.
DR AGR; RGD:1310613; -.
DR RGD; 1310613; Itgav.
DR VEuPathDB; HostDB:ENSRNOG00000004912; -.
DR GeneTree; ENSGT00940000158361; -.
DR InParanoid; A0A0G2JVZ6; -.
DR Reactome; R-RNO-1566948; Elastic fibre formation.
DR Reactome; R-RNO-210990; PECAM1 interactions.
DR Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-RNO-3000170; Syndecan interactions.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-445144; Signal transduction by L1.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000004912; Expressed in adult mammalian kidney and 18 other cell types or tissues.
DR ExpressionAtlas; A0A0G2JVZ6; baseline and differential.
DR GO; GO:0035868; C:alphav-beta3 integrin-HMGB1 complex; ISO:RGD.
DR GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0031527; C:filopodium membrane; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0034683; C:integrin alphav-beta3 complex; ISO:RGD.
DR GO; GO:0034684; C:integrin alphav-beta5 complex; ISO:RGD.
DR GO; GO:0034685; C:integrin alphav-beta6 complex; ISO:RGD.
DR GO; GO:0034686; C:integrin alphav-beta8 complex; ISO:RGD.
DR GO; GO:0008305; C:integrin complex; ISO:RGD.
DR GO; GO:0031258; C:lamellipodium membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0031528; C:microvillus membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISO:RGD.
DR GO; GO:0050840; F:extracellular matrix binding; ISO:RGD.
DR GO; GO:1990430; F:extracellular matrix protein binding; ISO:RGD.
DR GO; GO:0001968; F:fibronectin binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; IEP:RGD.
DR GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; ISO:RGD.
DR GO; GO:0043277; P:apoptotic cell clearance; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISO:RGD.
DR GO; GO:0016477; P:cell migration; IMP:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0031589; P:cell-substrate adhesion; ISO:RGD.
DR GO; GO:0035987; P:endodermal cell differentiation; ISO:RGD.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0050919; P:negative chemotaxis; ISO:RGD.
DR GO; GO:2000536; P:negative regulation of entry of bacterium into host cell; ISO:RGD.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0010888; P:negative regulation of lipid storage; ISO:RGD.
DR GO; GO:0032369; P:negative regulation of lipid transport; ISO:RGD.
DR GO; GO:0050748; P:negative regulation of lipoprotein metabolic process; ISO:RGD.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISO:RGD.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; ISO:RGD.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISO:RGD.
DR GO; GO:0050764; P:regulation of phagocytosis; ISO:RGD.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; ISO:RGD.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:0071604; P:transforming growth factor beta production; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; IEP:RGD.
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; 2.
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; 5.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2JVZ6};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
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..30
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 31..1007
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5035340141"
FT TRANSMEM 953..975
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 32..98
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 109..170
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 271..336
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 337..394
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 398..461
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 446..553
FT /note="Integrin alpha first immunoglubulin-like"
FT /evidence="ECO:0000259|Pfam:PF08441"
FT DOMAIN 585..723
FT /note="Integrin alpha second immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20805"
FT DOMAIN 731..942
FT /note="Integrin alpha third immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20806"
FT REGION 986..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1007 AA; 111050 MW; D0B5FECF98A7B670 CRC64;
MADPGRLLLR PRPGGLLLLL LGLLLPFAGS FNLDVESPAE YAGPEGSYFG FAVDFFVPST
SSRMFLLVGA PKANTTQPGI IEGGQVLKCD CSSSRRCQPI EFDSTGNRDY AKDDPLEFKS
HQWFGASVRS KQDKILACAP LYHWRTEMKQ EREPVGTCFL QDGTKTVEYA PCRSKNIDAD
GQGFCQGGFS IDFTKVSQLI SDQVAEIISK YDPNVYSIKY NNQLATRTAQ AIFDDSYLGS
FSSSLTDFVS GVPRAARTLG MVYIYDGKNM SSLHNFTGEQ MAAYFGFSVA ATDINGDDYA
DVFIGAPLFM DRGSDGKLQE VGQVSVSLQR ASGDFQTTKL NGFEVFARFG SAIAPLGDLD
QDGFNDIAIA APYGGEDKKG LVYIFNGRST GLNSVPSQIL QGQWAAQSMP PSFGYSMKGA
TDVDRNGYPD LVVGAFGVDR AVLYRARPVV TVNAGLEVYP SILNQDNKIC PLPGTALKVS
CFNVRFCLKA DGKGTLPRKL NFQVELLLDK LKQKGAIRRA LFLHNRSPGH SKDMTVFRGG
QTQCEELVAY LRVRRSALLS LLVVSPSFVY MIFPTCKLAH ILLDCGEDNV CKPKLEVSVD
SDQKKIYIGD DNPLTLTVKA QNQGEGAYEA ELIVSIPPQA DFIGVVRNNE ALARLSCAFK
TENQTRQVVC DLGNPMKAGT QLLAGLRFSV HQQSEMDTSV KFDLKIQSSN SFDNVSPVVS
YKVDLAVLAA VEIRGVSSPD HIFLPIPNWE YKETPETEED VGPVVQHIYE LRNNGPSSFS
KAILNLQWPY KYNNNTLLYI LHYDIDGPMN CTADTEINPL RIKSMSLQTP EKNDTAAEQG
GRNHLITKRD LSLSEGDVHT LGCGTAQCLQ ITCQVGRLDR GKSAILYVKS LLWTETFMNK
ENQNHSYSLK SSASFNIIEF PYKNLPIEDL FNSTLVTTNI TWGIQPAPMP VPVWVIILAV
LAGLLLLAVL VFVMYRMGFF KRVRPPQEEQ EREQLQPHEN GEGNSET
//
