EGFR_CHICK
ID EGFR_CHICK Reviewed; 703 AA.
AC P13387;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Epidermal growth factor receptor;
DE Short=CER;
DE EC=2.7.10.1;
DE Flags: Precursor; Fragment;
GN Name=EGFR;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
RX PubMed=3260329; DOI=10.1128/mcb.8.5.1970-1978.1988;
RA Lax I., Johnson A., Howk R., Sap J., Bellot F., Winkler M., Ullrich A.,
RA Vennstrom B., Schlessinger J., Givol D.;
RT "Chicken epidermal growth factor (EGF) receptor: cDNA cloning, expression
RT in mouse cells, and differential binding of EGF and transforming growth
RT factor alpha.";
RL Mol. Cell. Biol. 8:1970-1978(1988).
CC -!- FUNCTION: Receptor tyrosine kinase binding ligands of the EGF family
CC and activating several signaling cascades to convert extracellular cues
CC into appropriate cellular responses (PubMed:3260329). Known ligands
CC include EGF and TGFA/TGF-alpha (PubMed:3260329). Ligand binding
CC triggers receptor homo- and/or heterodimerization and
CC autophosphorylation on key cytoplasmic residues (By similarity). The
CC phosphorylated receptor recruits adapter proteins like GRB2 which in
CC turn activates complex downstream signaling cascades (By similarity).
CC Activates at least 4 major downstream signaling cascades including the
CC RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (By
CC similarity). May also activate the NF-kappa-B signaling cascade (By
CC similarity). {ECO:0000250|UniProtKB:P00533,
CC ECO:0000269|PubMed:3260329}.
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 -!- ACTIVITY REGULATION: Endocytosis and inhibition of the activated EGFR
CC by phosphatases constitute immediate regulatory mechanisms. Moreover,
CC inducible feedback inhibitors may constitute alternative regulatory
CC mechanisms for the EGFR signaling.
CC -!- SUBUNIT: Binding of the ligand triggers homo- and/or heterodimerization
CC of the receptor triggering its autophosphorylation.
CC {ECO:0000250|UniProtKB:P00533}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3260329};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}.
CC Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Nucleus membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC Endosome {ECO:0000250|UniProtKB:P00533}. Endosome membrane. Nucleus
CC {ECO:0000250|UniProtKB:P00533}. Note=In response to EGF, translocated
CC from the cell membrane to the nucleus via Golgi and ER. Endocytosed
CC upon activation by ligand (By similarity).
CC {ECO:0000250|UniProtKB:P00533}.
CC -!- PTM: Phosphorylated. Autophosphorylates. {ECO:0000269|PubMed:3260329}.
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; M20386; AAA48760.1; -; mRNA.
DR RefSeq; NP_990828.2; NM_205497.2.
DR AlphaFoldDB; P13387; -.
DR SMR; P13387; -.
DR BioGRID; 676741; 2.
DR STRING; 9031.ENSGALP00000020165; -.
DR iPTMnet; P13387; -.
DR PaxDb; P13387; -.
DR GeneID; 396494; -.
DR KEGG; gga:396494; -.
DR CTD; 1956; -.
DR VEuPathDB; HostDB:geneid_396494; -.
DR eggNOG; KOG1025; Eukaryota.
DR InParanoid; P13387; -.
DR OrthoDB; 81952at2759; -.
DR PhylomeDB; P13387; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
DR CDD; cd00064; FU; 3.
DR Gene3D; 3.80.20.20; -; 2.
DR Gene3D; 6.10.250.2930; -; 1.
DR InterPro; IPR044912; Egfr_JX_dom.
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; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR SMART; SM00261; FU; 5.
DR SUPFAM; SSF57184; SSF57184; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Endosome; Glycoprotein; Golgi apparatus; Kinase; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..30
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CHAIN 31..>703
FT /note="Epidermal growth factor receptor"
FT /id="PRO_0000016667"
FT TOPO_DOM 31..654
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..>703
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 687
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT MOD_RES 702
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..64
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 164..194
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 197..206
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 201..214
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 222..230
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 226..238
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 239..247
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 243..255
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 258..267
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 271..298
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 302..314
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 318..333
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 336..340
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 344..369
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 477..506
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 513..522
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 517..530
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 533..542
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 546..562
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 565..581
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 569..589
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 592..601
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 605..627
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 630..638
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT DISULFID 634..646
FT /evidence="ECO:0000250|UniProtKB:P00533"
FT NON_TER 703
SQ SEQUENCE 703 AA; 77427 MW; AFF2DE11B735A690 CRC64;
MGVRSPLSAS GPRGAAVLVL LLLGVALCSA VEEKKVCQGT NNKLTQLGHV EDHFTSLQRM
YNNCEVVLSN LEITYVEHNR DLTFLKTIQE VAGYVLIALN MVDVIPLENL QIIRGNVLYD
NSFALAVLSN YHMNKTQGLR ELPMKRLSEI LNGGVKISNN PKLCNMDTVL WNDIIDTSRK
PLTVLDFASN LSSCPKCHPN CTEDHCWGAG EQNCQTLTKV ICAQQCSGRC RGKVPSDCCH
NQCAAGCTGP RESDCLACRK FRDDATCKDT CPPLVLYNPT TYQMDVNPEG KYSFGATCVR
ECPHNYVVTD HGSCVRSCNT DTYEVEENGV RKCKKCDGLC SKVCNGIGIG ELKGILSINA
TNIDSFKNCT KINGDVSILP VAFLGDAFTK TLPLDPKKLD VFRTVKEISG FLLIQAWPDN
ATDLYAFENL EIIRGRTKQH GQYSLAVVNL KIQSLGLRSL KEISDGDIAI MKNKNLCYAD
TMNWRSLFAT QSQKTKIIQN RNKNDCTADR HVCDPLCSDV GCWGPGPFHC FSCRFFSRQK
ECVKQCNILQ GEPREFERDS KCLPCHSECL VQNSTAYNTT CSGPGPDHCM KCAHFIDGPH
CVKACPAGVL GENDTLVWKY ADANAVCQLC HPNCTRGCKG PGLEGCPNGS KTPSIAAGVV
GGLLCLVVVG LGIGLYLRRR HIVRKRTLRR LLQERELVEP LTP
