ID F1QG85_DANRE Unreviewed; 798 AA. AC F1QG85; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 11-MAY-2016, entry version 46. DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633}; GN Name=itgb1a {ECO:0000313|Ensembl:ENSDARP00000039699, GN ECO:0000313|ZFIN:ZDB-GENE-060803-2}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000039699, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000039699} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000039699}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSDARP00000039699, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000039699, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU000633}; CC Single-pass type I membrane protein CC {ECO:0000256|RuleBase:RU000633}. CC -!- SIMILARITY: Belongs to the integrin beta chain family. CC {ECO:0000256|RuleBase:RU000633}. CC -!- SIMILARITY: Contains VWFA domain. {ECO:0000256|SAAS:SAAS00494662}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSDARP00000039699}. 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; BX322549; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005170669.1; XM_005170612.2. DR RefSeq; XP_009295475.1; XM_009297200.1. DR RefSeq; XP_009295476.1; XM_009297201.1. DR UniGene; Dr.134213; -. DR STRING; 7955.ENSDARP00000039699; -. DR Ensembl; ENSDART00000039700; ENSDARP00000039699; ENSDARG00000071863. DR GeneID; 556734; -. DR CTD; 556734; -. DR ZFIN; ZDB-GENE-060803-2; itgb1a. DR eggNOG; KOG1226; Eukaryota. DR eggNOG; ENOG410XP60; LUCA. DR GeneTree; ENSGT00760000119064; -. DR OMA; LVGQQQI; -. DR OrthoDB; EOG7T7GSB; -. DR TreeFam; TF105392; -. DR Reactome; R-DRE-1566948; Elastic fibre formation. DR Reactome; R-DRE-1566977; Fibronectin matrix formation. DR Reactome; R-DRE-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-DRE-202733; Cell surface interactions at the vascular wall. DR Reactome; R-DRE-210991; Basigin interactions. DR Reactome; R-DRE-2129379; Molecules associated with elastic fibres. DR Reactome; R-DRE-216083; Integrin cell surface interactions. DR Reactome; R-DRE-3000157; Laminin interactions. DR Reactome; R-DRE-3000178; ECM proteoglycans. DR Reactome; R-DRE-445144; Signal transduction by L1. DR Reactome; R-DRE-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions. DR Proteomes; UP000000437; Chromosome 24. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0001968; F:fibronectin binding; IGI:ZFIN. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ZFIN. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 1.20.5.630; -; 1. DR Gene3D; 3.40.50.410; -; 1. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR015812; Integrin_bsu. DR InterPro; IPR014836; Integrin_bsu_cyt_dom. DR InterPro; IPR002369; Integrin_bsu_N. DR InterPro; IPR012896; Integrin_bsu_tail. DR InterPro; IPR032695; Integrin_dom. DR InterPro; IPR016201; Plexin-like_fold. DR InterPro; IPR002035; VWF_A. DR PANTHER; PTHR10082; PTHR10082; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF08725; Integrin_b_cyt; 1. DR Pfam; PF07965; Integrin_B_tail; 1. DR Pfam; PF00362; Integrin_beta; 1. DR PIRSF; PIRSF002512; Integrin_B; 1. DR PRINTS; PR01186; INTEGRINB. DR SMART; SM00187; INB; 1. DR SMART; SM01241; Integrin_b_cyt; 1. DR SMART; SM01242; Integrin_B_tail; 1. DR SMART; SM00423; PSI; 1. DR SUPFAM; SSF103575; SSF103575; 1. DR SUPFAM; SSF53300; SSF53300; 1. DR SUPFAM; SSF69179; SSF69179; 1. DR SUPFAM; SSF69687; SSF69687; 1. DR PROSITE; PS00243; INTEGRIN_BETA; 3. PE 3: Inferred from homology; KW Cell adhesion {ECO:0000256|RuleBase:RU000633}; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Integrin {ECO:0000256|RuleBase:RU000633, KW ECO:0000256|SAAS:SAAS00478940}; KW Membrane {ECO:0000256|SAAS:SAAS00478635}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transmembrane {ECO:0000256|RuleBase:RU000633, KW ECO:0000256|SAAS:SAAS00479639}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00478542}. FT DOMAIN 34 464 INB. {ECO:0000259|SMART:SM00187}. SQ SEQUENCE 798 AA; 88617 MW; E94A2A9448E66394 CRC64; MDLKLLFISA LLGIISCSHA QQEGNECIKA NALSCGECIQ VGDKCGWCTD AEFLKQGEPT SARCDELESL KKRGCAEDKI ENPHGSQRIL KNTPVTNRKK GAEKLRPEDI TQIQPQKLSL QLRSGEPQNI KLKFKRAEDY PIDLYYLMDL SYSMKDDLEN VKNLGTSLMK EMSKITSDFR IGFGSFVEKT VMPYISTTPA KLLNPCTGDQ NCTSPFSYKN VLKLTSNGQR FNSLVGQQQI SGNLDSPEGG FDAIMQVAVC GEHIGWRNVT RLLVFSTDAG FHFAGDGKLG GIVLPNDGRC HLENDMYTMS HYYDYPSIAH LVQKLSENNI QTIFAVTEEF QPVYKELKNL IPKSAVGTLS ANSSNVINLI VDAYNSLSSE VILENSKLPE GVTITYQSRC KNGVVNEGES GRKCSNISIG DEVSFNINIT AQGCPKQGKT ETIKIKPLGF TEEVEITLSF ICECECHKHA MKNSPLCHNG NGSFECGACR CNKGRVGRQC ECRKDEVSTE DLDKNCRKDN GTDICSNNGE CVCGTCECKK RENPEERYSG KYCECDNFNC DRSNNKLCGG HGRCECRVCV CDANYTGSAC DCSLDTSTCL ASNKQICNGR GICECGTCRC TDPKFQGPTC EICPTCPGVC TEHKECVQCR AFGTGEKKDT CKRDCSYFNL IEVEDRDKLP QPVQAFPLMH CKERDARDCW FYYTYAVNNN TEKEVHVVKT MECPPGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN PIYKSAVTTV INPKYEGK //