ID B5DEG1_RAT Unreviewed; 1062 AA. AC B5DEG1; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 24-JAN-2024, entry version 120. DE SubName: Full=RGD1564327 protein {ECO:0000313|EMBL:AAI68655.1}; GN Name=Itga8 {ECO:0000313|RGD:621634}; GN Synonyms=RGD1564327 {ECO:0000313|EMBL:AAI68655.1}; 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|EMBL:AAI68655.1}; RN [1] {ECO:0000313|EMBL:AAI68655.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung {ECO:0000313|EMBL:AAI68655.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC168655; AAI68655.1; -; mRNA. DR RefSeq; NP_001167443.1; NM_001173972.1. DR AlphaFoldDB; B5DEG1; -. DR SMR; B5DEG1; -. DR STRING; 10116.ENSRNOP00000022713; -. DR iPTMnet; B5DEG1; -. DR PhosphoSitePlus; B5DEG1; -. DR PaxDb; 10116-ENSRNOP00000022713; -. DR PeptideAtlas; B5DEG1; -. DR GeneID; 364786; -. DR KEGG; rno:364786; -. DR AGR; RGD:621634; -. DR CTD; 8516; -. DR RGD; 621634; Itga8. DR VEuPathDB; HostDB:ENSRNOG00000016538; -. DR eggNOG; KOG3637; Eukaryota. DR HOGENOM; CLU_004111_4_0_1; -. DR InParanoid; B5DEG1; -. DR OrthoDB; 3816176at2759; -. DR TreeFam; TF105391; -. 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-3000178; ECM proteoglycans. DR Bgee; ENSRNOG00000016538; Expressed in lung and 17 other cell types or tissues. DR GO; GO:0045177; C:apical part of cell; ISO:RGD. DR GO; GO:0009986; C:cell surface; ISO:RGD. DR GO; GO:0032591; C:dendritic spine membrane; IDA:RGD. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0008305; C:integrin complex; IBA:GO_Central. DR GO; GO:0043204; C:perikaryon; IDA:RGD. DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO. DR GO; GO:0005178; F:integrin binding; IBA:GO_Central. DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central. DR GO; GO:0030030; P:cell projection organization; ISO: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:0045184; P:establishment of protein localization; ISO:RGD. DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD. DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0001822; P:kidney development; ISO:RGD. DR GO; GO:0007613; P:memory; ISO:RGD. DR GO; GO:0048333; P:mesodermal cell differentiation; ISO:RGD. DR GO; GO:0001656; P:metanephros development; ISO:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD. DR GO; GO:0051145; P:smooth muscle cell differentiation; ISO:RGD. DR GO; GO:0048745; P:smooth muscle tissue development; ISO:RGD. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO: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:SF5; INTEGRIN ALPHA-8; 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; 6. DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1. DR SUPFAM; SSF69179; Integrin domains; 3. DR PROSITE; PS51470; FG_GAP; 6. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. PE 2: Evidence at transcript 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}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}. FT DOMAIN 482..638 FT /note="Integrin alpha first immunoglubulin-like" FT /evidence="ECO:0000259|Pfam:PF08441" FT DOMAIN 640..780 FT /note="Integrin alpha second immunoglobulin-like" FT /evidence="ECO:0000259|Pfam:PF20805" FT DOMAIN 786..1000 FT /note="Integrin alpha third immunoglobulin-like" FT /evidence="ECO:0000259|Pfam:PF20806" SQ SEQUENCE 1062 AA; 117575 MW; 24F33BC97E4B670C CRC64; MSARTHRGPP ENWAPPFACL CCVSAVLGML WSPVSLAFNL DVDKLTVYSG PEGSYFGYSL DFYIPDARTA SVLVGAPKAN TSQPDIVEGG AVYYCPWPAE RSAQCKQIPF DTTNNRKIRV NGTKEPIEFK SNQWFGATVR AHKGKVVACA PLYHWRTLKP NPAKDPVGTC YVAIQNFSAY AEHSPCRNSN VDPEGQGYCQ AGFSLDFYKN GDLIVGGPGS FYWQGQVITV SVADIIANYS FKDILRKLAA EKQTDVAPAS YDDSYLGYSV AAGEFTGDSL QELVAGIPRG AQNFGYVSII NSTDMTFIQN FTGEQMASYF GYTVVVSDVN NDGMDDILVG APLFMEREFE SNPREVGQVY LYLQVSALLF QDPQVLTGTE TFGRFGSSVA HLGDLNQDGY NDIAIGVPFA GKDQRGKVLI YNGNARGLHS KPSQVLQGIW GSQTIPSGFG FSLRGDADID KNDYPDLLVG AFGEGKVAVY RARPVVTVDA QLLLHPMIIN LENKTCQIPE FPTPVACFSL RVCASIAGQS ISNTVALMAE VQLDFLKQKG AIKRTLFLHN HQSHLIFPFV MRQQKSLHCQ DFMVYLRDET EFRDKLSPIN VSLNYSLDDS TFEDGLEVKP ILNHYRENVV TEQAHILVDC GEDNLCVPDL RLSARPDKQE IIIGDENHLM LIINARNEGE GAYEAELFVM IPEEADYVGI ERNNKGLRLL SCEYKMENVT RMVVCDLGNP MVTGTNFSLG LRFAVPRLEK TNMSINFDLQ IRSSNKDNPD SNFVSVQINV TAVAQVEIRG VSHPPQIVLP IHNWEPAEEP HKEEEVGPLV EHIYELHNIG PSTISDSILE VGWPFSAREE FLLYVFHLQT LGPLQCQTNP EINPQDIKPA ASPEDTPELS AFLRNATIPH LVRKRDVPVV QPHRQSPAKI LNCTNIDCLQ ISCAVGRLGG GESAVLKVRS RLWAHTFLQR KNDPYALASL VSFEVKKIPY KEQPAKLPAG STAIKTSVIW ATPNVSFSIP LWVIILAILL GLLVLAILTL ALWKCGFFDR ARPPQDEMTD REQLTSDKTP EA //