ERBB_AVIEU
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 03-AUG-2022, entry version 108.
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).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
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=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}.
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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 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..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