ERBB3_PONAB
ID ERBB3_PONAB Reviewed; 1342 AA.
AC Q5RB22;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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; CR858836; CAH91038.1; -; mRNA.
DR RefSeq; NP_001127366.1; NM_001133894.1.
DR RefSeq; XP_009246148.1; XM_009247873.1.
DR AlphaFoldDB; Q5RB22; -.
DR SMR; Q5RB22; -.
DR STRING; 9601.ENSPPYP00000005288; -.
DR GeneID; 100174431; -.
DR KEGG; pon:100174431; -.
DR CTD; 2065; -.
DR eggNOG; KOG1025; Eukaryota.
DR InParanoid; Q5RB22; -.
DR OrthoDB; 81952at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
DR GO; GO:0043235; C:receptor complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0038132; F:neuregulin binding; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
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; 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 SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript 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..1342
FT /note="Receptor tyrosine-protein kinase erbB-3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042232"
FT TOPO_DOM 20..641
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..1342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 709..966
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1037..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 834
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 715..723
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 742
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 788..790
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 834..839
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21860"
FT MOD_RES 982
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"
SQ SEQUENCE 1342 AA; 148104 MW; F7FB7E27C573916D CRC64;
MRANDALQVL GLLFSLARGS EVGNSQAVCP GTLNGLSVTG DAENQYQTLY KLYERCEVVM
GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSTLPLP NLRVVRGTQV YDGKFAIFVM
LNYNTNSSHA LRQLRLTQLT EILSGGVYIE KNDKLCHMDT IDWRDIVRDR DAEIVVKDNG
KSCPPCHEVC KGRCWGSGPE DCQTLTKTIC APQCNGHCFG PNPNQCCHDE CAGGCSGPQD
TDCFACRHFN DSGACVPRCP QPLVYNKLTF QLEPNPHTKY QYGGVCVASC PHNFVVDQTS
CVRACPPDKM EVDKNGLKMC EPCGGLCPKA CEGTGSGSRF QTVDSSNIDG FVNCTKILGN
LDFLITGLNG DPWHKIPALD PEKLNVFQTV REITGYLNIQ SWPPHMHNFS VFSNLTTIGG
RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS AGRIYISANR QLCYHHSLNW TKVLRGPTEE
RLDIKHNRPR RDCVAEGKVC DPLCSSGGCW GPGPGQCLSC RNYSRGGVCV THCNFLNGEP
REFAHEAECF SCHPECQPME GTATCNGSGS DTCAQCAHFR DGPHCVSSCP HGVLGAKGPI
YKYPDVQNEC RPCHENCTQG CKGPELQDCL GQTLVLIGKT HLTMALTVIA GLVVIFMMLG
GTFLYWRGRR IQNKRAMRRY LERGESIEPL DPSEKANKVL ARIFKETELK KLKVLGSGVF
GTVHKGVWIP EGESIKIPVC IKVIEDKSGR QSFQAVTDHM LAIGSLDHAH IVRLLGLCPG
SSLQLVTQYL PLGSLLDHVR QHRGALGPQL LLNWGVQIAK GMYYLEEHGM VHRNLAARNV
LLKSPSQVQV ADFGVADLLP PDDKQLLYSE AKTPIKWMAL ESIHFGKYTH QSDVWSYGVT
VWELMTFGAE PYAGLRLAEV PDLLEKGERL AQPQICTIDV YMVMVKCWMI DENIRPTFKE
LANEFTRMAR DPPRYLVIKR ESGPGIAPGP EPHGLTNKKL EEVELEPELD LDLDLEAEED
NLATTTLGSA LSLPVGTLNR PRGSQSLLSP SSGYMPMNQG NLGESCQEST VSGSNEQCPR
PVSLYPMPRG CLASESSEGH VTHSEAELQE KVSMCRSRSR SRSPRPRGDS AYHSQRHSLL
TPVTPLSPPG LEEEDVNGYV MPDTHLKGTP SSREGTLSSV GLSSVLGTEE EDEDEEYEYM
NRRRRHSPPH PPRPSSLEEL GYEYMDVGSD LSASLGSTQS CPLHPVPIMP NAGTTPDEDY
EYMNRQRGGG GPGGDYAAMG ACPASEQGYE EMRAFQGPGH QAPHVHYARL KTLRSLEATD
SAFDNPDYWH SRLFPKANAQ RT
