ID Q3YA99_DANRE Unreviewed; 787 AA.
AC Q3YA99;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=itgb1b.1 {ECO:0000313|RefSeq:NP_001030151.1,
GN ECO:0000313|ZFIN:ZDB-GENE-060803-3};
GN Synonyms=itgb1 {ECO:0000313|EMBL:AAZ78242.1};
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|EMBL:AAZ78242.1};
RN [1] {ECO:0000313|EMBL:AAZ78242.1, ECO:0000313|RefSeq:NP_001030151.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16787535; DOI=10.1186/1471-2121-7-24;
RA Mould A.P., McLeish J.A., Huxley-Jones J., Goonesinghe A.C.,
RA Hurlstone A.F., Boot-Handford R.P., Humphries M.J.;
RT "Identification of multiple integrin beta1 homologs in zebrafish (Danio
RT rerio).";
RL BMC Cell Biol. 7:24-24(2006).
RN [2] {ECO:0000313|RefSeq:NP_001030151.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20333216;
RA Braasch I., Brunet F., Volff J.N., Schartl M.;
RT "Pigmentation pathway evolution after whole-genome duplication in fish.";
RL Genome Biol. Evol. 1:479-493(2009).
RN [3] {ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., 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., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA 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).
RN [4] {ECO:0000313|RefSeq:NP_001030151.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25305346;
RA Wang X., Li L., Liu D.;
RT "Expression analysis of integrin beta1 isoforms during zebrafish embryonic
RT development.";
RL Gene Expr. Patterns 16:86-92(2014).
RN [5] {ECO:0000313|RefSeq:NP_001030151.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25931248;
RA Esain V., Kwan W., Carroll K.J., Cortes M., Liu S.Y., Frechette G.M.,
RA Sheward L.M., Nissim S., Goessling W., North T.E.;
RT "Cannabinoid Receptor-2 Regulates Embryonic Hematopoietic Stem Cell
RT Development via Prostaglandin E2 and P-Selectin Activity.";
RL Stem Cells 33:2596-2612(2015).
RN [6] {ECO:0000313|RefSeq:NP_001030151.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27780917;
RA Wang X., Yuan W., Wang X., Qi J., Qin Y., Shi Y., Zhang J., Gong J.,
RA Dong Z., Liu X., Sun C., Chai R., Le Noble F., Liu D.;
RT "The somite-secreted factor Maeg promotes zebrafish embryonic
RT angiogenesis.";
RL Oncotarget 7:77749-77763(2016).
RN [7] {ECO:0000313|RefSeq:NP_001030151.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30635353;
RA Gunawan F., Gentile A., Fukuda R., Tsedeke A.T., Jimenez-Amilburu V.,
RA Ramadass R., Iida A., Sehara-Fujisawa A., Stainier D.Y.R.;
RT "Focal adhesions are essential to drive zebrafish heart valve
RT morphogenesis.";
RL J. Cell Biol. 218:1039-1054(2019).
RN [8] {ECO:0000313|RefSeq:NP_001030151.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}. Cell
CC 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}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR EMBL; DQ149103; AAZ78242.1; -; mRNA.
DR RefSeq; NP_001030151.1; NM_001034979.1.
DR GeneID; 566771; -.
DR KEGG; dre:566771; -.
DR AGR; ZFIN:ZDB-GENE-060803-3; -.
DR CTD; 566771; -.
DR ZFIN; ZDB-GENE-060803-3; itgb1b.1.
DR OrthoDB; 5475862at2759; -.
DR PhylomeDB; Q3YA99; -.
DR Proteomes; UP000000437; Chromosome 2.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR Gene3D; 4.10.1240.30; -; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR033760; Integrin_beta_N.
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; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF28; INTEGRIN BETA-1; 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 Pfam; PF17205; PSI_integrin; 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 SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF53300; vWA-like; 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:Q3YA99};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..787
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001030151.1"
FT /id="PRO_5035034379"
FT TRANSMEM 718..740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..458
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 633..717
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 741..787
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT REGION 80..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 35..45
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 38..69
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 48..58
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 201..206
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 254..294
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 394..408
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 428..680
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 456..460
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 471..483
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 480..519
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 485..494
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 496..510
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 525..530
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 527..562
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 532..547
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 549..554
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 568..573
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 570..601
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 575..584
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 586..593
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 607..612
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 609..654
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 614..623
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 626..629
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 633..642
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 639..712
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 658..688
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 787 AA; 86570 MW; 173496DB545A6D52 CRC64;
MKMKLLLLSA LLGFVFHVGA KTDSNPCISA NAKTCGECIQ IGPQCVWCKD PDFKPSRCDD
IESMAKAGCT ADGVENPRGA VTIDKNKPVT NRKTDGGQNL RPDEITQIQP QKVTLNLRSG
EAQKFTLKFK RAEDYPIDLY FLMDLSHSMV SNLENVKKLG TELANEMKDI TKDLHIGFGS
FLEKLVMPYI LMTPKYLKNP CFPSDCTAPF SYKNVLSLTD NHGLFTQEVS KQKTSGNLDA
PEAGFDAIMQ AAVCTDVIGW RNVTRLLVFS TDAGFHLAGD GKLGGIVRPN DGKCHLDNNM
YTMSNYFDYP TISQLVDTLS GNNIQTIFAV TEEIREIYQE LSALIPKSAV GILSTSSSNV
IKLIIDAYNS LSSEVILENS KLPDGVSISY VSHCKNGVSG TGDNGRKCSN ISIGDEVLFD
IEITAKGCPS KGKPETIKIK PLGFSEEVEI LLNYICECEC HKDGIKNSPK CSGGQGTLEC
GVCRCNEGRL GRLCECSHDE VLADDLDAYC RMNNGTEVCS NNGECVCGTC ECKKRDNPEE
RYSGKFCECD NFSCDRSNNK LCGGHGRCEC KKCICDANYT GSACDCPLDT ATCLASTNEI
CNGRGKCECG VCKCDENYEG PTCEICPTCP RICTERKDCV ECRHFGTGSK QKTCEEDCKS
YSIKKVKTKE DLPPPNINHC KERDVDDCWI FFTSSIEKDG SIQVYVAENR ECPSGPDIIP
IVAGVVAGIV LIGLALLLIW KLLMVIHDRR EFDKFEKEKN NAKWDTGENP IYKSAVTTVV
NPRYEGK
//
