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-NOV-2015, entry version 40. 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:ENSDARP00000126425} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000126425}; RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. RN [3] {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., Eliott D., Threadgold G., RA Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., RA Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., RA Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., RA Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., RA Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., RA Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., RA Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., RA Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., RA Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., RA Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., RA Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., RA Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., RA Langford C., Yang F., 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 -!- 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 Ensembl; ENSDART00000152023; ENSDARP00000126425; 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-416700; Other semaphorin interactions. 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 Reactome; R-DRE-447041; CHL1 interactions. DR Reactome; R-DRE-75892; Platelet Adhesion to exposed collagen. DR PRO; PR:F1QG85; -. DR Proteomes; UP000000437; Chromosome 24. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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; 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; SM00423; PSI; 1. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF103575; SSF103575; 1. DR SUPFAM; SSF53300; SSF53300; 1. DR SUPFAM; SSF69687; SSF69687; 1. DR PROSITE; PS00243; INTEGRIN_BETA; 3. PE 1: Evidence at protein level; KW Cell adhesion {ECO:0000256|RuleBase:RU000633}; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Integrin {ECO:0000256|RuleBase:RU000633}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0000213|PeptideAtlas:F1QG85}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|RuleBase:RU000633, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 798 Integrin beta. {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005346239. FT TRANSMEM 729 751 Helical. {ECO:0000256|SAM:Phobius}. 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 //