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Database: UniProt
Entry: Q8AW81_DANRE
LinkDB: Q8AW81_DANRE
Original site: Q8AW81_DANRE 
ID   Q8AW81_DANRE            Unreviewed;      1305 AA.
AC   Q8AW81;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR000619};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR000619};
GN   Name=erbb3a {ECO:0000313|RefSeq:NP_001005320.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-030916-3};
GN   Synonyms=ERBB {ECO:0000313|RefSeq:NP_001005320.1}, erbb3
GN   {ECO:0000313|RefSeq:NP_001005320.1}, im:7148890
GN   {ECO:0000313|RefSeq:NP_001005320.1}, si:dz150i12.1
GN   {ECO:0000313|RefSeq:NP_001005320.1};
GN   ORFNames=dZ150I12.1-001 {ECO:0000313|EMBL:CAD58760.1};
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:CAD58760.1};
RN   [1] {ECO:0000313|RefSeq:NP_001005320.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15797019; DOI=10.1016/j.cub.2005.02.030;
RA   Lyons D.A., Pogoda H.M., Voas M.G., Woods I.G., Diamond B., Nix R.,
RA   Arana N., Jacobs J., Talbot W.S.;
RT   "erbb3 and erbb2 are essential for schwann cell migration and myelination
RT   in zebrafish.";
RL   Curr. Biol. 15:513-524(2005).
RN   [2] {ECO:0000313|RefSeq:NP_001005320.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15886089;
RA   Lai C.;
RT   "Peripheral glia: Schwann cells in motion.";
RL   Curr. Biol. 15:R332-R334(2005).
RN   [3] {ECO:0000313|RefSeq:NP_001005320.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16109975;
RA   Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R.,
RA   Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.;
RT   "The zebrafish gene map defines ancestral vertebrate chromosomes.";
RL   Genome Res. 15:1307-1314(2005).
RN   [4] {ECO:0000313|RefSeq:NP_001005320.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18508863;
RA   Budi E.H., Patterson L.B., Parichy D.M.;
RT   "Embryonic requirements for ErbB signaling in neural crest development and
RT   adult pigment pattern formation.";
RL   Development 135:2603-2614(2008).
RN   [5] {ECO:0000313|RefSeq:NP_001005320.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19133254;
RA   Rojas-Munoz A., Rajadhyksha S., Gilmour D., van Bebber F., Antos C.,
RA   Rodriguez Esteban C., Nusslein-Volhard C., Izpisua Belmonte J.C.;
RT   "ErbB2 and ErbB3 regulate amputation-induced proliferation and migration
RT   during vertebrate regeneration.";
RL   Dev. Biol. 327:177-190(2009).
RN   [6] {ECO:0000313|EMBL:CAD58760.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Sehra H.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|RefSeq:NP_001005320.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23364329;
RA   Dooley C.M., Mongera A., Walderich B., Nusslein-Volhard C.;
RT   "On the embryonic origin of adult melanophores: the role of ErbB and Kit
RT   signalling in establishing melanophore stem cells in zebrafish.";
RL   Development 140:1003-1013(2013).
RN   [8] {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   [9] {ECO:0000313|RefSeq:NP_001005320.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23234507;
RA   Challa A.K., Chatti K.;
RT   "Conservation and early expression of zebrafish tyrosine kinases support
RT   the utility of zebrafish as a model for tyrosine kinase biology.";
RL   Zebrafish 10:264-274(2013).
RN   [10] {ECO:0000313|RefSeq:NP_001005320.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26469318;
RA   Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA   Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA   Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA   Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA   Reith W., Hertzano R.;
RT   "RFX transcription factors are essential for hearing in mice.";
RL   Nat. Commun. 6:8549-8549(2015).
RN   [11] {ECO:0000313|RefSeq:NP_001005320.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26110643;
RA   Westcot S.E., Hatzold J., Urban M.D., Richetti S.K., Skuster K.J.,
RA   Harm R.M., Lopez Cervera R., Umemoto N., McNulty M.S., Clark K.J.,
RA   Hammerschmidt M., Ekker S.C.;
RT   "Protein-Trap Insertional Mutagenesis Uncovers New Genes Involved in
RT   Zebrafish Skin Development, Including a Neuregulin 2a-Based ErbB Signaling
RT   Pathway Required during Median Fin Fold Morphogenesis.";
RL   PLoS ONE 10:e0130688-e0130688(2015).
RN   [12] {ECO:0000313|RefSeq:NP_001005320.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=27846271;
RA   Samsa L.A., Ito C.E., Brown D.R., Qian L., Liu J.;
RT   "IgG-Containing Isoforms of Neuregulin-1 Are Dispensable for Cardiac
RT   Trabeculation in Zebrafish.";
RL   PLoS ONE 11:e0166734-e0166734(2016).
RN   [13] {ECO:0000313|RefSeq:NP_001005320.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001171};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. EGF receptor subfamily. {ECO:0000256|PIRNR:PIRNR000619}.
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DR   EMBL; AL591365; CAD58760.1; -; Genomic_DNA.
DR   RefSeq; NP_001005320.1; NM_001005320.1.
DR   GeneID; 386635; -.
DR   KEGG; dre:386635; -.
DR   AGR; ZFIN:ZDB-GENE-030916-3; -.
DR   CTD; 386635; -.
DR   ZFIN; ZDB-GENE-030916-3; erbb3a.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; Q8AW81; -.
DR   SignaLink; Q8AW81; -.
DR   Proteomes; UP000000437; Chromosome 6.
DR   GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0038132; F:neuregulin binding; IBA:GO_Central.
DR   GO; GO:0038131; F:neuregulin receptor activity; IBA:GO_Central.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd00064; FU; 1.
DR   CDD; cd05111; PTK_HER3; 1.
DR   CDD; cd12095; TM_ErbB3; 1.
DR   Gene3D; 6.10.250.2930; -; 1.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR044912; Egfr_JX_dom.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR032778; GF_recep_IV.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000494; Rcpt_L-dom.
DR   InterPro; IPR036941; Rcpt_L-dom_sf.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR   PANTHER; PTHR24416:SF88; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-3; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000619; TyrPK_EGF-R; 2.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000619};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000619};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000619, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000619};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000619};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001005320.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000619};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000619}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1305
FT                   /note="Receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP,
FT                   ECO:0000313|RefSeq:NP_001005320.1"
FT                   /id="PRO_5035034087"
FT   TRANSMEM        593..615
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          659..926
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          991..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1057..1096
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1107..1126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1157..1290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1064..1085
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1157..1208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         665..673
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT   BINDING         692
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1305 AA;  145710 MW;  D026607B19759224 CRC64;
     MYKCMCICVN NFTLSLSLSA VGVCTGTQNL LSVTGSSEVQ YKLMKEMYTG CQIVIGNLEI
     TQMEHNRDFS FLQSIREVTG YILIAINQFR RLPLEQLRVI RGTSLYEDKF ALAVLVNYQK
     DGVYGLRELG LTHLTEILEG GVQIIQNKFL SYAPQINWQD IVKNSGAEVI IQDNGPEVPC
     HESCGGPCWG PGNDTCQILT KTVCALQCNV RCFGRSPSEC CHNECAGGCT GPLDTDCFAC
     RNFNNSGSCV SQCPRADIYN KVTFKMEPNP NAKYQFGSMC VSHCPPNFVV DGSSCVSSCP
     ADKMEVDKTG VKRCEKCEGL CPKACVGTGT GTASRQTVDS QNIDSFINCT KIQGSLHFLV
     TGIKGDSYNN ISALDPRKLK IFNTVREITD ILSIQSWPEE LEDLSVFSNL ATIQGRTLYR
     GYSLLVMKIP TLKSLGLRSL KRISDGGIYI TGNTQLCYHH TVNWTRLFGS GPRALRRQKS
     LDIKENRPQE QCRLLGSGTR SVFVLQELQK RRNMCTRLQL HVRGSDECKA CAHLQDGPYC
     VSSCPEGVQG ENGLIIYKFP NRQNKCQPCH ANCTLGSTHY GVNIVRYRLP VTAIVLSVIF
     CVLLAFSVFV LSVLYRRSLS IRRKRAMRRY LQSGESFEPL EPGEKGVKVH ARILRTSELK
     KIKLLGSGVF GTVHKGIWIP EGDTVKIPVA IKTIQDRTGR QTFQEITDHM LAMGSLDHAY
     IVRILGICPG ASLQLVTQLS PQGSLLEHIR QRRDNLNPQR LLNWCVQIAK GMYYLEEQRM
     VHRNLAARNI LLKSDLIVQI ADYGIADLLY PDDKKYFFNE IKTPIKWMAL ESILFRRYTH
     QSDVWSYGVT VWEMMSYGAE PYSAMRPQEV PDLLEKGERL SQPQICTIDV YMVMVKCWMI
     DENVRPTFKE LANEFTRMAR DPHRYLVIKE EDRAPDSASD ETHQNGTEID ILGVALEDQD
     DEVLEDAIDA PRYITPSRSF SRLRIDSHRS SLTPSTTAGY LPMTPGLESS VQTGWASRSR
     LDSACTVSES SEGRGALELE MNDDFSSVGS LRRVRHREDS AYMSQRDSLS GPPETTSTGT
     QGEEDQNEYV LPGFGESPEK ETLLFTSSRS TLSQKRLSRG HSGDFLEANR GAGEEYEYMN
     NQTLSLSHIP GQLKEYNQRA PRNRSASFNP GGMYSNHKPS RPSKRSSIEG SESSGGLSQS
     STDQRSHSDG DFLSSEAEYT DGDLEGGGGE AYEYEDMDSL AAGGASGAEY QNLDGEDEER
     DEDWSGGPRS PGPYVQVHAG TNHNAFDNPD YWHSRSFHKT KAVHT
//
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