ERBB3_RAT
ID ERBB3_RAT Reviewed; 1339 AA.
AC Q62799; Q62955;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Receptor tyrosine-protein kinase erbB-3;
DE EC=2.7.10.1;
DE AltName: Full=Proto-oncogene-like protein c-ErbB-3;
DE Flags: Precursor;
GN Name=Erbb3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8522190; DOI=10.1016/0378-1119(95)00436-a;
RA Hellyer N.J., Kim H.-H., Greaves C.H., Sierke S.L., Koland J.G.;
RT "Cloning of the rat ErbB3 cDNA and characterization of the recombinant
RT protein.";
RL Gene 165:279-284(1995).
RN [2]
RP SEQUENCE REVISION TO 85; 513 AND 565.
RA Hellyer N.J., Koland J.G.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 922-1097.
RC STRAIN=Sprague-Dawley; TISSUE=Sciatic nerve;
RX PubMed=9030624; DOI=10.1523/jneurosci.17-05-01642.1997;
RA Carroll S.L., Miller M.L., Frohnert P.W., Kim S.S., Corbett J.A.;
RT "Expression of neuregulins and their putative receptors, ErbB2 and ErbB3,
RT is induced during Wallerian degeneration.";
RL J. Neurosci. 17:1642-1659(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Tyrosine-protein kinase that plays an essential role as cell
CC surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is
CC activated by it; ligand-binding increases phosphorylation on tyrosine
CC residues and promotes its association with the p85 subunit of
CC phosphatidylinositol 3-kinase. May also be activated by CSPG5. Involved
CC in the regulation of myeloid cell differentiation.
CC {ECO:0000250|UniProtKB:P21860}.
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:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Monomer and homodimer. Heterodimer with each of the other ERBB
CC receptors (Potential). Interacts with CSPG5, PA2G4, GRB7, MYOC and
CC MUC1. Found in a ternary complex with NRG1 and ITGAV:ITGB3 or
CC ITGA6:ITGB4 (By similarity). {ECO:0000250|UniProtKB:P21860,
CC ECO:0000250|UniProtKB:Q61526, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DOMAIN: The cytoplasmic part of the receptor may interact with the SH2
CC or SH3 domains of many signal-transducing proteins.
CC -!- PTM: Autophosphorylated. Ligand-binding increases phosphorylation on
CC tyrosine residues and promotes its association with the p85 subunit of
CC phosphatidylinositol 3-kinase. {ECO:0000250|UniProtKB:P21860}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; U29339; AAC28498.2; -; mRNA.
DR EMBL; U52530; AAC53050.1; -; mRNA.
DR PIR; JC4387; JC4387.
DR RefSeq; NP_058914.2; NM_017218.3.
DR AlphaFoldDB; Q62799; -.
DR SMR; Q62799; -.
DR BioGRID; 248136; 7.
DR DIP; DIP-41029N; -.
DR ELM; Q62799; -.
DR IntAct; Q62799; 1.
DR STRING; 10116.ENSRNOP00000006796; -.
DR GlyGen; Q62799; 10 sites.
DR iPTMnet; Q62799; -.
DR PhosphoSitePlus; Q62799; -.
DR PaxDb; Q62799; -.
DR PRIDE; Q62799; -.
DR ABCD; Q62799; 1 sequenced antibody.
DR DNASU; 29496; -.
DR GeneID; 29496; -.
DR KEGG; rno:29496; -.
DR UCSC; RGD:69323; rat.
DR CTD; 2065; -.
DR RGD; 69323; Erbb3.
DR eggNOG; KOG1025; Eukaryota.
DR InParanoid; Q62799; -.
DR PhylomeDB; Q62799; -.
DR BRENDA; 2.7.10.1; 5301.
DR Reactome; R-RNO-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR PRO; PR:Q62799; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0038143; C:ERBB3:ERBB2 complex; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0044214; C:spanning component of plasma membrane; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043125; F:ErbB-3 class receptor binding; ISO:RGD.
DR GO; GO:0019838; F:growth factor binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0038132; F:neuregulin binding; IMP:RGD.
DR GO; GO:0038131; F:neuregulin receptor activity; IMP:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; ISO:RGD.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; IEP:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0021545; P:cranial nerve development; ISO:RGD.
DR GO; GO:0003197; P:endocardial cushion development; ISO:RGD.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:RGD.
DR GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; ISO:RGD.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0060056; P:mammary gland involution; IEP:RGD.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0051048; P:negative regulation of secretion; ISO:RGD.
DR GO; GO:0009968; P:negative regulation of signal transduction; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR GO; GO:0042476; P:odontogenesis; IEP:RGD.
DR GO; GO:0007422; P:peripheral nervous system development; ISO:RGD.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:RGD.
DR GO; GO:0055025; P:positive regulation of cardiac muscle tissue development; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:RGD.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0014037; P:Schwann cell differentiation; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
DR GO; GO:0043586; P:tongue development; IEP:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00064; FU; 4.
DR Gene3D; 3.80.20.20; -; 2.
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; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
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; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 5.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1339
FT /note="Receptor tyrosine-protein kinase erbB-3"
FT /id="PRO_0000016673"
FT TOPO_DOM 20..643
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 663..1339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 707..964
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1023..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 832
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 713..721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 740
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 786..788
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 832..837
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 186..194
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 190..202
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 210..218
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 214..226
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 227..235
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 231..243
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 246..255
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 259..286
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 290..301
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 305..320
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 323..327
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 500..509
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 504..517
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 520..529
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 533..549
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 552..565
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 556..573
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 576..585
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 589..610
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 613..621
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT DISULFID 617..629
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT CONFLICT 1028
FT /note="L -> P (in Ref. 3; AAC53050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1339 AA; 147546 MW; 0AA5F2402BBFDF1E CRC64;
MRATGTLQVL CFLLSLARGS EMGNSQAVCP GTLNGLSVTG DADNQYQTLY KLYEKCEVVM
GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSVLPLP NLRVVRGTQV YDGKFAIFVM
LNYNTNSSHA LRQLKFTQLT EILSGGVYIE KNDKLCHMDT IDWRDIVRVR GAEIVVKNNG
ANCPPCHEVC KGRCWGPGPD DCQILTKTIC APQCNGRCFG PNPNQCCHDE CAGGCSGPQD
TDCFACRRFN DSGACVPRCP EPLVYNKLTF QLEPNPHTKY QYGGVCVASC PHNFVVDQTF
CVRACPPDKM EVDKHGLKMC EPCGGLCPKA CEGTGSGSRY QTVDSSNIDG FVNCTKILGN
LDFLITGLNV DPWHKIPALD PEKLNVFRTV REITGYLNIQ SWPPHMHNFS VFSNLTTIGG
RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS AGRVYISANQ QLCYHHSLNW TRLLRGPSEE
RLDIKYDRPL GECLAEGKVC DPLCSSGGCW GPGPGQCLSC RNYSREGVCV THCNFLQGEP
REFVHEAQCF SCHPECLPME GTSTCNGSGS DACARCAHFR DGPHCVNSCP HGILGAKGPI
YKYPDAQNEC RPCHENCTQG CNGPELQDCL GQAEVLMSKP HLVIAVTVGL AVILMILGGS
FLYWRGRRIQ NKRAMRRYLE RGESIEPLDP SEKANKVLAR IFKETELRKL KVLGSGVFGT
VHKGIWIPEG ESIKIPVCIK VIEDKSGRQS FQAVTDHMLA VGSLDHAHIV RLLGLCPGSS
LQLVTQYLPL GSLLDHVKQH RETLGPQLLL NWGVQIAKGM YYLEEHSMVH RDLALRNVML
KSPSQVQVAD FGVADLLPPD DKQLLHSEAK TPIKWMALES IHFGKYTHQS DVWSYGVTVW
ELMTFGAEPY AGLRLAEIPD LLEKGERLAQ PQICTIDVYM VMVKCWMIDE NIRPTFKELA
NEFTRMARDP PRYLVIKRAS GPGTPPAAEP SVLTTKELQE AELEPELDLD LDLEAEEEGL
ATSLGSALSL PTGTLTRPRG SQSLLSPSSG YMPMNQSSLG EACLDSAVLG GREQFSRPIS
LHPIPRGRPA SESSEGHVTG SEAELQEKVS VCRSRSRSRS PRPRGDSAYH SQRHSLLTPV
TPLSPPGLEE EDGNGYVMPD THLRGASSSR EGTLSSVGLS SVLGTEEEDE DEEYEYMNRK
RRGSPPRPPR PGSLEELGYE YMDVGSDLSA SLGSTQSCPL HPMAIVPSAG TTPDEDYEYM
NRRRGAGGAG GDYAAMGACP AAEQGYEEMR AFQGPGHHAP HVRYARLKTL RSLEATDSAF
DNPDYWHSRL FPKANAQRT
