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P13387 (EGFR_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Epidermal growth factor receptor
Short name=CER
EC=2.7.10.1
Gene names
Name:EGFR
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length703 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade.

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

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 structure

Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein By similarity. Golgi apparatus membrane; Single-pass type I membrane protein By similarity. Nucleus membrane; Single-pass type I membrane protein By similarity. Endosome. Endosome membrane. Note: In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand By similarity.

Post-translational modification

Phosphorylated. Autophosphorylates By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030
Chain31 – ›703›673Epidermal growth factor receptor
PRO_0000016667

Regions

Topological domain31 – 654624Extracellular Potential
Transmembrane655 – 66713Helical; Potential
Topological domain668 – ›703›36Cytoplasmic Potential

Amino acid modifications

Modified residue6871Phosphothreonine By similarity
Modified residue7021Phosphothreonine By similarity
Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation2001N-linked (GlcNAc...) Potential
Glycosylation3591N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation4201N-linked (GlcNAc...) Potential
Glycosylation5731N-linked (GlcNAc...) Potential
Glycosylation5781N-linked (GlcNAc...) Potential
Glycosylation6131N-linked (GlcNAc...) Potential
Glycosylation6331N-linked (GlcNAc...) Potential
Glycosylation6481N-linked (GlcNAc...) Potential
Disulfide bond197 ↔ 206 By similarity
Disulfide bond201 ↔ 214 By similarity
Disulfide bond222 ↔ 230 By similarity
Disulfide bond226 ↔ 238 By similarity
Disulfide bond239 ↔ 247 By similarity
Disulfide bond243 ↔ 255 By similarity
Disulfide bond258 ↔ 267 By similarity
Disulfide bond271 ↔ 298 By similarity
Disulfide bond302 ↔ 314 By similarity
Disulfide bond318 ↔ 333 By similarity
Disulfide bond336 ↔ 340 By similarity
Disulfide bond513 ↔ 522 By similarity
Disulfide bond517 ↔ 530 By similarity
Disulfide bond533 ↔ 542 By similarity
Disulfide bond546 ↔ 562 By similarity
Disulfide bond565 ↔ 581 By similarity
Disulfide bond569 ↔ 589 By similarity
Disulfide bond592 ↔ 601 By similarity
Disulfide bond605 ↔ 627 By similarity
Disulfide bond630 ↔ 638 By similarity
Disulfide bond634 ↔ 646 By similarity

Experimental info

Non-terminal residue7031

Sequences

Sequence LengthMass (Da)Tools
P13387 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: AFF2DE11B735A690

FASTA70377,427
        10         20         30         40         50         60 
MGVRSPLSAS GPRGAAVLVL LLLGVALCSA VEEKKVCQGT NNKLTQLGHV EDHFTSLQRM 

        70         80         90        100        110        120 
YNNCEVVLSN LEITYVEHNR DLTFLKTIQE VAGYVLIALN MVDVIPLENL QIIRGNVLYD 

       130        140        150        160        170        180 
NSFALAVLSN YHMNKTQGLR ELPMKRLSEI LNGGVKISNN PKLCNMDTVL WNDIIDTSRK 

       190        200        210        220        230        240 
PLTVLDFASN LSSCPKCHPN CTEDHCWGAG EQNCQTLTKV ICAQQCSGRC RGKVPSDCCH 

       250        260        270        280        290        300 
NQCAAGCTGP RESDCLACRK FRDDATCKDT CPPLVLYNPT TYQMDVNPEG KYSFGATCVR 

       310        320        330        340        350        360 
ECPHNYVVTD HGSCVRSCNT DTYEVEENGV RKCKKCDGLC SKVCNGIGIG ELKGILSINA 

       370        380        390        400        410        420 
TNIDSFKNCT KINGDVSILP VAFLGDAFTK TLPLDPKKLD VFRTVKEISG FLLIQAWPDN 

       430        440        450        460        470        480 
ATDLYAFENL EIIRGRTKQH GQYSLAVVNL KIQSLGLRSL KEISDGDIAI MKNKNLCYAD 

       490        500        510        520        530        540 
TMNWRSLFAT QSQKTKIIQN RNKNDCTADR HVCDPLCSDV GCWGPGPFHC FSCRFFSRQK 

       550        560        570        580        590        600 
ECVKQCNILQ GEPREFERDS KCLPCHSECL VQNSTAYNTT CSGPGPDHCM KCAHFIDGPH 

       610        620        630        640        650        660 
CVKACPAGVL GENDTLVWKY ADANAVCQLC HPNCTRGCKG PGLEGCPNGS KTPSIAAGVV 

       670        680        690        700 
GGLLCLVVVG LGIGLYLRRR HIVRKRTLRR LLQERELVEP LTP

« Hide

References

[1]"Chicken epidermal growth factor (EGF) receptor: cDNA cloning, expression in mouse cells, and differential binding of EGF and transforming growth factor alpha."
Lax I., Johnson A., Howk R., Sap J., Bellot F., Winkler M., Ullrich A., Vennstrom B., Schlessinger J., Givol D.
Mol. Cell. Biol. 8:1970-1978(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M20386 mRNA. Translation: AAA48760.1.
IPIIPI00575097.
RefSeqNP_990828.2. NM_205497.2.
UniGeneGga.35024.

3D structure databases

ProteinModelPortalP13387.
SMRP13387. Positions 31-530, 678-703.
ModBaseSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000020165.

Proteomic databases

PaxDbP13387.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396494.
KEGGgga:396494.

Organism-specific databases

CTD1956.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000230982.
HOVERGENHBG000490.
KOK04361.

Gene expression databases

ArrayExpressP13387.

Family and domain databases

InterProIPR000494. EGF_rcpt_L.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt.
[Graphical view]
PfamPF00757. Furin-like. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
SMARTSM00261. FU. 5 hits.
[Graphical view]
SUPFAMSSF57184. Grow_fac_recept. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. Partial match.
PS50011. PROTEIN_KINASE_DOM. Partial match.
PS00109. PROTEIN_KINASE_TYR. Partial match.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816533.

Entry information

Entry nameEGFR_CHICK
AccessionPrimary (citable) accession number: P13387
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 3, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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