ID   ERBB_AVIEU              Reviewed;         540 AA.
AC   P11273;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-SEP-2026, entry version 121.
DE   RecName: Full=Tyrosine-protein kinase transforming protein erbB;
DE            EC=2.7.10.1;
GN   Name=V-ERBB;
OS   Avian erythroblastosis virus (strain ts167) (AEV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus;
OC   Alpharetrovirus avileu; Avian leukosis virus.
OX   NCBI_TaxID=103898;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2878364; DOI=10.1128/mcb.6.5.1751-1759.1986;
RA   Choi O.R., Trainor C., Graf T., Beug H., Engel J.D.;
RT   "A single amino acid substitution in v-erbB confers a thermolabile
RT   phenotype to ts167 avian erythroblastosis virus-transformed erythroid
RT   cells.";
RL   Mol. Cell. Biol. 6:1751-1759(1986).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
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; M13179; AAA42401.1; -; Genomic_RNA.
DR   PIR; A25231; TVFVEB.
DR   SMR; P11273; -.
DR   BRENDA; 2.7.10.1; 589.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0038128; P:ERBB2 signaling pathway; IEA:UniProtKB-ARBA.
DR   CDD; cd05108; PTKc_EGFR; 1.
DR   CDD; cd12093; TM_ErbB1; 1.
DR   FunFam; 1.10.510.10:FF:000027; Receptor protein-tyrosine kinase; 1.
DR   FunFam; 2.10.220.10:FF:000008; Receptor protein-tyrosine kinase; 1.
DR   FunFam; 3.30.200.20:FF:000044; Receptor protein-tyrosine kinase; 1.
DR   FunFam; 4.10.1140.10:FF:000001; Receptor protein-tyrosine kinase; 1.
DR   Gene3D; 6.10.250.2930; -; 1.
DR   Gene3D; 2.10.220.10; Hormone Receptor, Insulin-like Growth Factor Receptor 1, Chain A, domain 2; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR044912; Egfr_JX_dom.
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; IPR050122; RTK.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR049328; TM_ErbB1.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24416:SF91; EPIDERMAL GROWTH FACTOR RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF21314; TM_ErbB1; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Oncogene; Phosphoprotein;
KW   Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..540
FT                   /note="Tyrosine-protein kinase transforming protein erbB"
FT                   /id="PRO_0000160253"
FT   DOMAIN          132..399
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        257
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         138..146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   VARIANT         270
FT                   /note="H -> D (in thermolabile v-erbB)"
SQ   SEQUENCE   540 AA;  60413 MW;  5B53297AA068B65D CRC64;
     MKCAHFIDGP HCVKACPAGV LGENDTLVWK YADANAVCQL CHPNCTRGCK GPGLEGCPNG
     SKTPSIAAGV VGGLLCLVVV GLGIGLYLRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN
     QAHLRILKET EFKKVKVLGF GAFGTVYKGL WIPEGEKVTI PVAIKELREA TSPKANKEIL
     DEAYVMASVD NPHVCRLLGI CLTSTVQLIT QLMPYGCLLD YIREHKDNIG SQYLLNWCVQ
     IAKGMNYLEE RHMVHRDLAA RNVLVKTPQH VKITDFGLAK QLGADEKEYH AEGGKVPIKW
     MALESILHRI YTHQSDVWSY GVTVWELMTF GSKPYDGIPA SEISSVLEKG ERLPQPPICT
     IDVYMIMVKC WMSDADSRPK FRELIAEFSK MARDPPRYLV IQGDERMHLP SPTDSKFYRT
     LMEEEDMEDI VDADEYLVPH QGFFNSPSTS RTPLLSSLSA TSNNSATNCI DRNGGHPVRE
     DGFLPAPEYV NQLMPKKPST AMVQNQIYNY ISLTAISKLP IDSRYQNSHS TAVDNPEYLE
//