ID F1QG85_DANRE Unreviewed; 798 AA. AC F1QG85; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 25-MAY-2022, entry version 86. 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 Danionidae; Danioninae; 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., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., 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., Clark S., RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., RA Raisen C., 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., Babbage A., RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., RA Ellington A., 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., Bird C., RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. CC Cell projection, invadopodium membrane {ECO:0000256|ARBA:ARBA00004297}; CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004297}. CC Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cell CC projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004199}; Single- CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004199}. CC Melanosome {ECO:0000256|ARBA:ARBA00004223}. Membrane CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000633}; Single- CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, CC ECO:0000256|RuleBase:RU000633}. CC -!- SIMILARITY: Belongs to the integrin beta chain family. CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}. 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_005170612.3. DR STRING; 7955.ENSDARP00000039699; -. DR PaxDb; F1QG85; -. DR PRIDE; F1QG85; -. DR Ensembl; ENSDART00000039700.7; ENSDARP00000039699.4; ENSDARG00000071863.7. DR GeneID; 556734; -. DR CTD; 556734; -. DR ZFIN; ZDB-GENE-060803-2; itgb1a. DR eggNOG; KOG1226; Eukaryota. DR GeneTree; ENSGT01030000234611; -. DR HOGENOM; CLU_011772_2_1_1; -. DR InParanoid; F1QG85; -. DR OMA; QVAVCGX; -. DR PhylomeDB; F1QG85; -. DR TreeFam; TF105392; -. DR Proteomes; UP000000437; Chromosome 24. DR Bgee; ENSDARG00000071863; Expressed in swim bladder and 27 other tissues. DR ExpressionAtlas; F1QG85; baseline. DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central. DR GO; GO:0008305; C:integrin complex; IEA:InterPro. DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IBA:GO_Central. DR GO; GO:0001968; F:fibronectin binding; IGI:ZFIN. DR GO; GO:0005178; F:integrin binding; IBA:GO_Central. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ZFIN. DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro. DR GO; GO:0003181; P:atrioventricular valve morphogenesis; IMP:ZFIN. DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central. DR GO; GO:0016477; P:cell migration; IBA:GO_Central. DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central. DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IMP:ZFIN. DR Gene3D; 3.40.50.410; -; 1. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR040622; I-EGF_1. DR InterPro; IPR027071; Integrin_beta-1. DR InterPro; IPR015812; Integrin_bsu. DR InterPro; IPR014836; Integrin_bsu_cyt_dom. DR InterPro; IPR012896; Integrin_bsu_tail. DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf. DR InterPro; IPR002369; Integrin_bsu_VWA. DR InterPro; IPR032695; Integrin_dom_sf. DR InterPro; IPR016201; PSI. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR10082; PTHR10082; 1. DR PANTHER; PTHR10082:SF28; PTHR10082:SF28; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF18372; I-EGF_1; 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; SSF53300; SSF53300; 1. DR SUPFAM; SSF69179; SSF69179; 1. DR SUPFAM; SSF69687; SSF69687; 1. DR PROSITE; PS00243; INTEGRIN_BETA; 1. PE 1: Evidence at protein level; KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889, KW ECO:0000256|RuleBase:RU000633}; KW Cell junction {ECO:0000256|ARBA:ARBA00022949}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Cell projection {ECO:0000256|ARBA:ARBA00023273}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002512-1}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Myogenesis {ECO:0000256|ARBA:ARBA00022541}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Proteomics identification {ECO:0007829|PeptideAtlas:F1QG85}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000633}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..798 FT /note="Integrin beta" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5009954137" FT TRANSMEM 729..751 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 26..76 FT /note="PSI" FT /evidence="ECO:0000259|SMART:SM00423" FT DOMAIN 34..464 FT /note="INB" FT /evidence="ECO:0000259|SMART:SM00187" FT DOMAIN 640..728 FT /note="Integrin_B_tail" FT /evidence="ECO:0000259|SMART:SM01242" FT DOMAIN 752..798 FT /note="Integrin_b_cyt" FT /evidence="ECO:0000259|SMART:SM01241" FT DISULFID 27..464 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 35..45 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 38..75 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 48..64 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 206..212 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 260..300 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 400..414 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 434..691 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 462..466 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 477..489 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 486..525 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 491..500 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 502..516 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 531..536 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 533..568 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 538..553 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 555..560 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 574..579 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 576..607 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 581..590 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 592..599 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 613..618 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 615..661 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 620..630 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 633..636 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 640..649 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 646..723 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" FT DISULFID 665..699 FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1" 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 //