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Database: UniProt
Entry: ERBB_ALV
LinkDB: ERBB_ALV
Original site: ERBB_ALV 
ID   ERBB_ALV                Reviewed;         634 AA.
AC   P00534;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=Tyrosine-protein kinase transforming protein erbB;
DE            EC=2.7.10.1;
GN   Name=V-ERBB;
OS   Avian leukosis virus (ALV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=11864;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2988784; DOI=10.1016/s0092-8674(85)80052-0;
RA   Nilsen T.W., Maroney P.A., Goodwin R.G., Rottman F.M., Crittenden L.B.,
RA   Raines M.A., Kung H.-J.;
RT   "c-erbB activation in ALV-induced erythroblastosis: novel RNA processing
RT   and promoter insertion result in expression of an amino-truncated EGF
RT   receptor.";
RL   Cell 41:719-726(1985).
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   -!- MISCELLANEOUS: This protein is produced by erythroleukemia cells in
CC       chickens which have been injected with the avian leukosis virus and
CC       subsequently develop leukemia. The leukemias are induced by the
CC       insertion of retroviral promoter elements in or near the c-erbB gene,
CC       which leads to c-erbB activation.
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-Env-ErbB protein.
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=AAA48763.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M10066; AAA48763.1; ALT_INIT; mRNA.
DR   PIR; B00643; TVFVLV.
DR   SMR; P00534; -.
DR   BRENDA; 2.7.10.1; 590.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05108; PTKc_EGFR; 1.
DR   CDD; cd12093; TM_ErbB1; 1.
DR   Gene3D; 6.10.250.2930; -; 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; 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   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Oncogene; Phosphoprotein;
KW   Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..634
FT                   /note="Tyrosine-protein kinase transforming protein erbB"
FT                   /id="PRO_0000160251"
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"
SQ   SEQUENCE   634 AA;  70891 MW;  E705E33A0BE01FCC CRC64;
     MKCAHFIDGP HCVKACPAGV LGENDTLVWK YADANAVCQL CHPNCTRGCK GPGLEGCPNG
     SKTPSIAAGV VGGLLCLVVV GLGIGLYLRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN
     QAHLRILKET EFKKVKVLGS GAFGTVYKGL 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 NNISLTAISK
     LPMDSRYQNS HSTAVDNPEY LNTNQSPLAK TVFESSPYWI QSGNHQINLD NPDYQQDFLP
     NETKPNGLLK VPAAENPEYL RVAAPKSEYI EASA
//
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