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Epidermal growth factor receptor (CER) (EC 2.7.10.1) (Fragment)

 EGFR_CHICK              Reviewed;         703 AA.
P13387;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
25-APR-2018, entry version 139.
RecName: Full=Epidermal growth factor receptor;
Short=CER;
EC=2.7.10.1;
Flags: Precursor; Fragment;
Name=EGFR;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
PHOSPHORYLATION.
PubMed=3260329; DOI=10.1128/MCB.8.5.1970;
Lax I., Johnson A., Howk R., Sap J., Bellot F., Winkler M.,
Ullrich A., Vennstrom B., Schlessinger J., Givol D.;
"Chicken epidermal growth factor (EGF) receptor: cDNA cloning,
expression in mouse cells, and differential binding of EGF and
transforming growth factor alpha.";
Mol. Cell. Biol. 8:1970-1978(1988).
-!- FUNCTION: Receptor tyrosine kinase binding ligands of the EGF
family and activating several signaling cascades to convert
extracellular cues into appropriate cellular responses
(PubMed:3260329). Known ligands include EGF and TGFA/TGF-alpha
(PubMed:3260329). Ligand binding triggers receptor homo-and/or
heterodimerization and autophosphorylation on key cytoplasmic
residues (By similarity). The phosphorylated receptor recruits
adapter proteins like GRB2 which in turn activates complex
downstream signaling cascades (By similarity). Activates at least
4 major downstream signaling cascades including the RAS-RAF-MEK-
ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (By
similarity). May also activate the NF-kappa-B signaling cascade
(By similarity). {ECO:0000250|UniProtKB:P00533,
ECO:0000269|PubMed:3260329}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Endocytosis and inhibition of the activated
EGFR by phosphatases constitute immediate regulatory mechanisms.
Moreover, inducible feedback inhibitors may constitute alternative
regulatory mechanisms for the EGFR signaling.
-!- SUBUNIT: Binding of the ligand triggers homo- and/or
heterodimerization of the receptor triggering its
autophosphorylation. {ECO:0000250|UniProtKB:P00533}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3260329};
Single-pass type I membrane protein
{ECO:0000250|UniProtKB:P00533}. Endoplasmic reticulum membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Golgi apparatus membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}. Endosome
{ECO:0000250|UniProtKB:P00533}. Endosome membrane. Nucleus
{ECO:0000250|UniProtKB:P00533}. Note=In response to EGF,
translocated from the cell membrane to the nucleus via Golgi and
ER. Endocytosed upon activation by ligand (By similarity).
{ECO:0000250|UniProtKB:P00533}.
-!- PTM: Phosphorylated. Autophosphorylates.
{ECO:0000269|PubMed:3260329}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; M20386; AAA48760.1; -; mRNA.
RefSeq; NP_990828.2; NM_205497.2.
UniGene; Gga.35024; -.
ProteinModelPortal; P13387; -.
SMR; P13387; -.
STRING; 9031.ENSGALP00000020165; -.
iPTMnet; P13387; -.
PaxDb; P13387; -.
PRIDE; P13387; -.
GeneID; 396494; -.
KEGG; gga:396494; -.
CTD; 1956; -.
eggNOG; KOG1025; Eukaryota.
eggNOG; ENOG410XNSR; LUCA.
HOGENOM; HOG000230982; -.
HOVERGEN; HBG000490; -.
InParanoid; P13387; -.
KO; K04361; -.
PhylomeDB; P13387; -.
Proteomes; UP000000539; Unplaced.
Bgee; ENSGALG00000012363; -.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
Gene3D; 3.80.20.20; -; 2.
InterPro; IPR006211; Furin-like_Cys-rich_dom.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR032778; GF_recep_IV.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR000494; Rcpt_L-dom.
InterPro; IPR036941; Rcpt_L-dom_sf.
Pfam; PF00757; Furin-like; 1.
Pfam; PF14843; GF_recep_IV; 1.
Pfam; PF01030; Recep_L_domain; 2.
SMART; SM00261; FU; 5.
SUPFAM; SSF57184; SSF57184; 2.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus;
Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
Receptor; Reference proteome; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase.
SIGNAL 1 30 {ECO:0000250|UniProtKB:P00533}.
CHAIN 31 >703 Epidermal growth factor receptor.
/FTId=PRO_0000016667.
TOPO_DOM 31 654 Extracellular. {ECO:0000255}.
TRANSMEM 655 667 Helical. {ECO:0000255}.
TOPO_DOM 668 >703 Cytoplasmic. {ECO:0000255}.
MOD_RES 687 687 Phosphothreonine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 702 702 Phosphothreonine.
{ECO:0000250|UniProtKB:P00533}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 190 190 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 359 359 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 420 420 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 573 573 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 578 578 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 613 613 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 633 633 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 648 648 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 37 64 {ECO:0000250|UniProtKB:P00533}.
DISULFID 164 194 {ECO:0000250|UniProtKB:P00533}.
DISULFID 197 206 {ECO:0000250|UniProtKB:P00533}.
DISULFID 201 214 {ECO:0000250|UniProtKB:P00533}.
DISULFID 222 230 {ECO:0000250|UniProtKB:P00533}.
DISULFID 226 238 {ECO:0000250|UniProtKB:P00533}.
DISULFID 239 247 {ECO:0000250|UniProtKB:P00533}.
DISULFID 243 255 {ECO:0000250|UniProtKB:P00533}.
DISULFID 258 267 {ECO:0000250|UniProtKB:P00533}.
DISULFID 271 298 {ECO:0000250|UniProtKB:P00533}.
DISULFID 302 314 {ECO:0000250|UniProtKB:P00533}.
DISULFID 318 333 {ECO:0000250|UniProtKB:P00533}.
DISULFID 336 340 {ECO:0000250|UniProtKB:P00533}.
DISULFID 344 369 {ECO:0000250|UniProtKB:P00533}.
DISULFID 477 506 {ECO:0000250|UniProtKB:P00533}.
DISULFID 513 522 {ECO:0000250|UniProtKB:P00533}.
DISULFID 517 530 {ECO:0000250|UniProtKB:P00533}.
DISULFID 533 542 {ECO:0000250|UniProtKB:P00533}.
DISULFID 546 562 {ECO:0000250|UniProtKB:P00533}.
DISULFID 565 581 {ECO:0000250|UniProtKB:P00533}.
DISULFID 569 589 {ECO:0000250|UniProtKB:P00533}.
DISULFID 592 601 {ECO:0000250|UniProtKB:P00533}.
DISULFID 605 627 {ECO:0000250|UniProtKB:P00533}.
DISULFID 630 638 {ECO:0000250|UniProtKB:P00533}.
DISULFID 634 646 {ECO:0000250|UniProtKB:P00533}.
NON_TER 703 703
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


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