ID   ERBB_AVIER              Reviewed;         604 AA.
AC   P00535;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Tyrosine-protein kinase transforming protein erbB;
DE            EC=2.7.10.1;
GN   Name=V-ERBB;
OS   Avian erythroblastosis virus (strain ES4).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=79685;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=H;
RX   PubMed=6313229; DOI=10.1016/0092-8674(83)90209-x;
RA   Yamamoto T., Nishida T., Miyajima N., Kawai S., Ooi T., Toyoshima K.;
RT   "The erbB gene of avian erythroblastosis virus is a member of the src gene
RT   family.";
RL   Cell 35:71-78(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-152.
RX   PubMed=6328658; DOI=10.1126/science.6328658;
RA   Debuire B., Henry C., Benaissa M., Biserte G., Claverie J.-M., Saule S.,
RA   Martin P., Stehelin D.;
RT   "Sequencing the erbA gene of avian erythroblastosis virus reveals a new
RT   type of oncogene.";
RL   Science 224:1456-1459(1984).
CC   -!- FUNCTION: The v-erbB oncogene transforms avian fibroblasts and
CC       erythroblasts in culture and induces sarcomas and erythroleukemias in
CC       chickens. It is a truncated and mutated version of the receptor for
CC       epidermal growth factor.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA42394.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; K02006; AAA42394.1; ALT_INIT; Genomic_RNA.
DR   EMBL; K01216; AAA42400.1; -; Genomic_RNA.
DR   PIR; A00644; TVYUH.
DR   SMR; P00535; -.
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   Gene3D; 6.10.250.2930; -; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF57184; SSF57184; 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..604
FT                   /note="Tyrosine-protein kinase transforming protein erbB"
FT                   /id="PRO_0000160252"
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   CONFLICT        29
FT                   /note="R -> W (in Ref. 2; AAA42394)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140
FT                   /note="S -> F (in Ref. 2; AAA42394)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="I -> V (in Ref. 2; AAA42394)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   604 AA;  67633 MW;  76EBCDD06745D609 CRC64;
     MKCAHFIDGP HCVKACPAGV LGENDTLVRK YADANAVCQL CHPNCTRGCK GPGLEGCPNG
     SKTPSIAAGV VGGLLCLVVV GLGIGLYLRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN
     QAHLRILKET EFKKVKVLGS GAFGTIYKGL WIPEGEKVKI PVAIKELREA TSPKANKEIL
     DEAYVMASVD NPHVCRLLGI CLTSTVQLIT QLMPYGCLLD YIREHKDNIG SQYLLNWCVQ
     IAKGMNYLEE RRLVHRDLAA RNVLVKTPQH VKITDFGLAK LLGADEKEYH AEGGKVPIKW
     MALESILHRI YTHQSDVWSY GVTVWELMTF GSKPYDGIPA SEISSVLEKG ERLPQPPICT
     IDVYMIMVKC WMIDADSRPK FRELIAEFSK MARDPPRYLV IQGDERMHLP SPTDSKFYRT
     LMEEEDMEDI VDADEYLVPH QGFFNSPSTS RTPLLSSLSA TSNNSATNCI DRNGQGHPVR
     EDSFVQRYSS DPTGNFLEES IDDGFLPAPE YVNQLMPKKP STAMVQNQIY NFISLTAISK
     LPMDSRYQNS HSTAVDNPEY LNTNQSPLAK TVFESSPYWI QSGNHQINLD NPDYQQDFLP
     TSCS