ID H2NHN2_PONAB Unreviewed; 1273 AA.
AC H2NHN2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 77.
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=ERBB3 {ECO:0000313|Ensembl:ENSPPYP00000005288.3};
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 {ECO:0000313|Ensembl:ENSPPYP00000005288.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000005288.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000005288.3}
RP IDENTIFICATION.
RG Ensembl;
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: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane 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 Ensembl; ENSPPYT00000005496.3; ENSPPYP00000005288.3; ENSPPYG00000004643.3.
DR GeneTree; ENSGT00940000156107; -.
DR HOGENOM; CLU_003384_2_1_1; -.
DR InParanoid; H2NHN2; -.
DR OMA; PDPNQCC; -.
DR OrthoDB; 1614410at2759; -.
DR TreeFam; TF106002; -.
DR Proteomes; UP000001595; Chromosome 12.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0038143; C:ERBB3:ERBB2 complex; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043125; F:ErbB-3 class receptor binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0038132; F:neuregulin binding; IEA:Ensembl.
DR GO; GO:0038131; F:neuregulin receptor activity; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; IEA:Ensembl.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0021545; P:cranial nerve development; IEA:Ensembl.
DR GO; GO:0003197; P:endocardial cushion development; IEA:Ensembl.
DR GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0051048; P:negative regulation of secretion; IEA:Ensembl.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:Ensembl.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR GO; GO:0055025; P:positive regulation of cardiac muscle tissue development; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0014044; P:Schwann cell development; IEA:Ensembl.
DR CDD; cd00064; FU; 3.
DR CDD; cd05111; PTK_HER3; 1.
DR CDD; cd12095; TM_ErbB3; 1.
DR Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 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; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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:UP000001595};
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 TRANSMEM 573..597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 640..897
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 968..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 646..654
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT BINDING 673
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
SQ SEQUENCE 1273 AA; 140677 MW; 4776E11A047088B3 CRC64;
MPTSPSCRLW IREVTGYVLV AMNEFSTLPL PNLRVVRGTQ VYDGKFAIFV MLNYNTNSSH
ALRQLRLTQL TEILSGGVYI EKNDKLCHMD TIDWRDIVRD RDAEIVVKDN GKSCPPCHEV
CKGRCWGSGP EDCQTLTKTI CAPQCNGHCF GPNPNQCCHD ECAGGCSGPQ DTDCFACRHF
NDSGACVPRC PQPLVYNKLT FQLEPNPHTK YQYGGVCVAS CPHNFVVDQT SCVRACPPDK
MEVDKNGLKM CEPCGGLCPK ACEGTGSGSR FQTVDSSNID GFVNCTKILG NLDFLITGLN
GDPWHKIPAL DPEKLNVFQT VREITGYLNI QSWPPHMHNF SVFSNLTTIG GRSLYNRGFS
LLIMKNLNVT SLGFRSLKEI SAGRIYISAN RQLCYHHSLN WTKVLRGPTE ERLDIKHNRP
RRDCVAEGKV CDPLCSSGGC WGPGPGQCLS CRNYSRGGVC VTHCNFLNGE PREFAHEAEC
FSCHPECQPM EGTATCNGSG SDTCAQCAHF RDGPHCVSSC PHGVLGAKGP IYKYPDVQNE
CRPCHENCTQ GCKGPELQDC LGQTLVLIGK THLTMALTVI AGLVVIFMML GGTFLYWRGR
RIQNKRAMRR YLERGESIEP LDPSEKANKV LARIFKETEL KKLKVLGSGV FGTVHKGVWI
PEGESIKIPV CIKVIEDKSG RQSFQAVTDH MLAIGSLDHA HIVRLLGLCP GSSLQLVTQY
LPLGSLLDHV RQHRGALGPQ LLLNWGVQIA KGMYYLEEHG MVHRNLAARN VLLKSPSQVQ
VADFGVADLL PPDDKQLLYS EAKTPIKWMA LESIHFGKYT HQSDVWSYGV TVWELMTFGA
EPYAGLRLAE VPDLLEKGER LAQPQICTID VYMVMVKCWM IDENIRPTFK ELANEFTRMA
RDPPRYLVIK RESGPGIAPG PEPHGLTNKK LEEVELEPEL DLDLDLEAEE DNLATTTLGS
ALSLPVGTLN RPRGSQSLLS PSSGYMPMNQ GNLGESCQES TVSGSNEQCP RPVSLYPMPR
GCLASESSEG HVTHSEAELQ EKVSMCRSRS RSRSPRPRGD SAYHSQRHSL LTPVTPLSPP
GLEEEDVNGY VMPDTHLKGT PSSREGTLSS VGLSSVLGTE EEDEDEEYEY MNRRRRHSPP
HPPRPSSLEE LGYEYMDVGS DLSASLGSTQ SCPLHPVPIM PNAGTTPDED YEYMNRQRGG
GGPGGDYAAM GACPASEQGY EEMRAFQGPG HQAPHVHYAR LKTLRSLEAT DSAFDNPDYW
HSRLFPKANA QRT
//
