ERBB3_MOUSE
ID ERBB3_MOUSE Reviewed; 1339 AA.
AC Q61526; Q3KQR1; Q68J64; Q810U8; Q8K317;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Receptor tyrosine-protein kinase erbB-3;
DE EC=2.7.10.1;
DE AltName: Full=Glial growth factor receptor;
DE AltName: Full=Proto-oncogene-like protein c-ErbB-3;
DE Flags: Precursor;
GN Name=Erbb3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Yamauchi J., Shooter E.M.;
RT "Involvement of the ErbB3 signaling pathway in Schwann cell migration.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Thyroid;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1061-1154.
RC TISSUE=Muscle fibroblast;
RX PubMed=7589796; DOI=10.1006/dbio.1995.0012;
RA Moscoso L.M., Chu G.C., Gautam M., Noakes P.G., Merlie J.P., Sanes J.R.;
RT "Synapse-associated expression of an acetylcholine receptor-inducing
RT protein, ARIA/heregulin, and its putative receptors, ErbB2 and ErbB3, in
RT developing mammalian muscle.";
RL Dev. Biol. 172:158-169(1995).
RN [4]
RP INTERACTION WITH MYOC.
RX PubMed=23897819; DOI=10.1074/jbc.m112.446138;
RA Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C.,
RA Tomarev S.I.;
RT "Myocilin mediates myelination in the peripheral nervous system through
RT ErbB2/3 signaling.";
RL J. Biol. Chem. 288:26357-26371(2013).
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 and MUC1 (By
CC similarity). Interacts with MYOC (PubMed:23897819). Found in a ternary
CC complex with NRG1 and ITGAV:ITGB3 or ITGA6:ITGB4 (By similarity).
CC {ECO:0000250|UniProtKB:P21860, ECO:0000269|PubMed:23897819,
CC ECO:0000305}.
CC -!- INTERACTION:
CC Q61526; P70424: Erbb2; NbExp=2; IntAct=EBI-931878, EBI-2945468;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In the muscle, expression localizes to the synaptic
CC sites of muscle fibers.
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}.
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; AY686636; AAT95433.1; -; mRNA.
DR EMBL; BC029028; AAH29028.1; -; mRNA.
DR EMBL; BC049279; AAH49279.1; -; mRNA.
DR EMBL; BC106091; AAI06092.1; -; mRNA.
DR EMBL; L47240; AAA93533.1; -; mRNA.
DR CCDS; CCDS24283.1; -.
DR RefSeq; NP_034283.1; NM_010153.1.
DR AlphaFoldDB; Q61526; -.
DR SMR; Q61526; -.
DR BioGRID; 199497; 26.
DR IntAct; Q61526; 2.
DR STRING; 10090.ENSMUSP00000080716; -.
DR GlyConnect; 2676; 3 N-Linked glycans (1 site).
DR GlyGen; Q61526; 10 sites, 3 N-linked glycans (1 site).
DR iPTMnet; Q61526; -.
DR PhosphoSitePlus; Q61526; -.
DR MaxQB; Q61526; -.
DR PaxDb; Q61526; -.
DR PeptideAtlas; Q61526; -.
DR PRIDE; Q61526; -.
DR ProteomicsDB; 275878; -.
DR ABCD; Q61526; 1 sequenced antibody.
DR Antibodypedia; 3428; 2347 antibodies from 52 providers.
DR DNASU; 13867; -.
DR Ensembl; ENSMUST00000082059; ENSMUSP00000080716; ENSMUSG00000018166.
DR GeneID; 13867; -.
DR KEGG; mmu:13867; -.
DR UCSC; uc007hnm.1; mouse.
DR CTD; 2065; -.
DR MGI; MGI:95411; Erbb3.
DR VEuPathDB; HostDB:ENSMUSG00000018166; -.
DR eggNOG; KOG1025; Eukaryota.
DR GeneTree; ENSGT00940000156107; -.
DR HOGENOM; CLU_003384_2_0_1; -.
DR InParanoid; Q61526; -.
DR OMA; THEEVCP; -.
DR OrthoDB; 81952at2759; -.
DR PhylomeDB; Q61526; -.
DR TreeFam; TF106002; -.
DR BRENDA; 2.7.10.1; 3474.
DR Reactome; R-MMU-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR BioGRID-ORCS; 13867; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Erbb3; mouse.
DR PRO; PR:Q61526; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q61526; protein.
DR Bgee; ENSMUSG00000018166; Expressed in small intestine Peyer's patch and 263 other tissues.
DR Genevisible; Q61526; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0038143; C:ERBB3:ERBB2 complex; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0044214; C:spanning component of plasma membrane; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043125; F:ErbB-3 class receptor binding; ISO:MGI.
DR GO; GO:0019838; F:growth factor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0038132; F:neuregulin binding; ISS:UniProtKB.
DR GO; GO:0038131; F:neuregulin receptor activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0021545; P:cranial nerve development; IMP:MGI.
DR GO; GO:0003197; P:endocardial cushion development; IMP:MGI.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; IDA:MGI.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR GO; GO:0097049; P:motor neuron apoptotic process; IMP:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0051048; P:negative regulation of secretion; ISO:MGI.
DR GO; GO:0009968; P:negative regulation of signal transduction; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IGI:MGI.
DR GO; GO:0055025; P:positive regulation of cardiac muscle tissue development; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
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:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0014037; P:Schwann cell differentiation; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:MGI.
DR CDD; cd00064; FU; 3.
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_0000042231"
FT TOPO_DOM 20..641
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..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 1028..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1100
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 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:0000250|UniProtKB:P21860"
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 1067
FT /note="A -> V (in Ref. 3; AAA93533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1339 AA; 147613 MW; 59D56FD9C9536FBE CRC64;
MSAIGTLQVL GFLLSLARGS EMGNSQAVCP GTLNGLSVTG DADNQYQTLY KLYEKCEVVM
GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSVLPLP NLRVVRGTQV YDGKFAIFVM
LNYNTNSSHA LRQLRFTQLT EILLGGVYIE KNDKLCHMDT IDWRDIVRVP DAEIVVKNNG
GNCPPCHEVC KGRCWGPGPE DCQILTKTIC APQCNGRCFG PNPNQCCHDE CAGGCSGPQD
TDCFACRHFN DSGACVPRCP APLVYNKLTF QLEPNPHIKY QYGGVCVASC PHNFVVDQTF
CVRACPADKM EVDKNGLKMC EPCRGLCPKA CEGTGSGSRY QTVDSSNIDG FVNCTKILGN
LDFLITGLNG DPWHKIPALD PEKLNVFRTV REITGYLNIQ SWPPHMHNFS VFSNLTTIGG
RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS AGRVYISANQ QLCYHHSLNW TRLLRGPAEE
RLDIKYNRPL GECVAEGKVC DPLCSSGGCW GPGPGQCLSC RNYSREGVCV THCNVLQGEP
REFVHEAHCF SCHPECQPME GTSTCNGSGS DACARCAHFR DGPHCVNSCP HGILGAKGPI
YKYPDAQNEC RPCHENCTQG CKGPELQDCL GQAEVLMSKP HLVIAVTVGL TVIFLILGGS
FLYWRGRRIQ NKRAMRRYLE RGESIEPLDP SEKANKVLAR IFKETELRKL KVLGSGVFGT
VHKGIWIPEG ESIKIPVCIK VIEDKSGRQS FQAVTDHMLA VGSLDHAHIV RLLGLCPGSS
LQLVTQYLPL GSLLDHVRQH RETLGPQLLL NWGVQIAKGM YYLEEHSMVH RDLALRNVML
KSPSQVQVAD FGVADLLPPD DKQLLHSEAK TPIKWMALES IHFGKYTHQS DVWSYGVTVW
ELMTFGAEPY AGLRLAEIPD LLEKGERLAQ PQICTIDVYM VMVKCWMIDE NIRPTFKELA
NEFTRMARDP PRYLVIKRAS GPGIPPAAEP SALSTKELQD AELEPDLDLD LDVEVEEEGL
ATTLGSALSL PTGTLTRPRG SQSLLSPSSG YMPMNQSNLG EACLDSAVLG GREQFSRPIS
LHPIPRGRQT SESSEGHVTG SEAELQERVS MCRSRSRSRS PRPRGDSAYH SQRHSLLTPV
TPLSPPGLEE EDGNGYVMPD THLRGTSSSR EGTLSSVGLS SVLGTEEEDE DEEYEYMNRK
RRGSPARPPR PGSLEELGYE YMDVGSDLSA SLGSTQSCPL HPMAIVPSAG TTPDEDYEYM
NRRRGAGGSG GDYAAMGACP AAEQGYEEMR AFQGPGHQAP HVRYARLKTL RSLEATDSAF
DNPDYWHSRL FPKANAQRI
