ID EGFR_APIME Reviewed; 1292 AA.
AC P0CY46;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Epidermal growth factor receptor;
DE Short=Egfr;
DE EC=2.7.10.1;
GN Name=Egfr;
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=7460;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND ACTIVITY
RP REGULATION.
RX PubMed=21516106; DOI=10.1038/nature10093;
RA Kamakura M.;
RT "Royalactin induces queen differentiation in honeybees.";
RL Nature 473:478-483(2011).
CC -!- FUNCTION: Upon binding to its ligands, transduces the signal through
CC the ras-raf-MAPK pathway and is involved in a myriad of developmental
CC decisions (By similarity). Involved in the determination of adult size,
CC ovary development, and development timing, especially during queen
CC determination of honeybee larvae. May have an important role in the
CC prolongation of longevity in queens. {ECO:0000250,
CC ECO:0000269|PubMed:21516106}.
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: Activated by MRJP1 during queen determination of
CC honeybee larvae. {ECO:0000269|PubMed:21516106}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Reduced adult size and ovary size, and prolonged
CC developmental time. {ECO:0000269|PubMed:21516106}.
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 AlphaFoldDB; P0CY46; -.
DR SMR; P0CY46; -.
DR STRING; 7460.P0CY46; -.
DR GlyCosmos; P0CY46; 7 sites, No reported glycans.
DR PaxDb; 7460-GB54477-PA; -.
DR eggNOG; KOG1025; Eukaryota.
DR InParanoid; P0CY46; -.
DR Proteomes; UP000005203; Genome assembly.
DR Proteomes; UP001105180; Unplaced.
DR GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
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:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProt.
DR GO; GO:0000003; P:reproduction; IEA:UniProt.
DR CDD; cd00064; FU; 5.
DR CDD; cd05057; PTKc_EGFR_like; 1.
DR Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR PANTHER; PTHR24416:SF566; EPIDERMAL GROWTH FACTOR RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 1.
DR PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 7.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR SUPFAM; SSF52058; L domain-like; 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; Developmental protein; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT CHAIN 1..1292
FT /note="Epidermal growth factor receptor"
FT /id="PRO_0000409832"
FT TOPO_DOM 1..641
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 663..1292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 711..978
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1022..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 836
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 717..725
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 744
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 675
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 1166
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1292 AA; 144362 MW; 94912A425125E43C CRC64;
MYNNYNLCHI RTINWEEIIT GPSAMYSYVY NFTSPERACT PCDKSCEQGC WGEGPENCQK
YSKTNCSPQC WQGRCFGPNP RECCHLFCAG GCTGPKQSDC IACKNFFDDG VCTQECPPMQ
KYNPTTYSWE PNPDGKYAYG ATCVRRCPEH LLKDNGACVR SCPPKKKALN GECVPCDGPC
PKTCKGVEKV HSGNIDSFKD CTIIEGSITI LDQSFQGFQH VYRNFSFGKR YEKMHPDKLE
VFSTLKEITG FLNIQGDHKD FKNLSYFRNL EVIGGRTLTE YFASLYVVKT SLVSFGLSSL
KKIYSGSIAI LENKNLCYAQ SINWTRIKKS SEHESLLSNN RNESECIKDG LVCDEQCSDE
GCWGPGPAQC LSCKNFILGN DCLQDCTAPG IYQADEKTCK VCHEECDGSC IGPNTDHCKK
CKHARDGPFC VPECPASKYN DNGVCKSCHG NCVGGCEGPE NNIGPNGCHS CDKAILNDHV
PEGCLQKKES CPDGYYYEWV SPLEQGPLKP LASKAVCRKC HSRCKKCTGY GFHEHVCQEC
TKYKRGEQCE DECPADYFAD ANKLCIPCFS ECRGCFGPGP NQCYKCRNYK IYIDEDTDGN
TTSFNCTETC TPEYPHKIFN PDSEPYCSLE TAGLIENELQ PAILAGVAVF ALAFLVVAAI
IMYFWRVRAK AKENTVKMTM ALTGLDDNEP LRPTGVKPNL AKLRIIKEEE MRKGGILGYG
AFGNVYKGVW VPEGENVKIP VAIKVLHDGT GANTSKEFLD EAYIMASVEH PNLLQLLAVC
MTSQMMLVTQ LMPLGCLLDF VRRFKDKIGS KALLNWCTQI ARGMAYLEER RLVHRDLAAR
NVLVQTPNCV KITDFGLAKL LDINEEQYKA AGGKMPIKWL ALECIQHRVF THKSDVWAFG
VTIWEVLTYG GRPYENVPAR NVPELLEKGE RLPQPAICTI DVYMIMIKCW MLDAESRPSF
KELAEDFAKM SRDPGRYLAI KGDKYMRLPS YTLQDEKEMI RNLASAMDGP EALVDADEYL
QPKSRAPIPP GLSASSTSGS PPNTPVKPCW PNGKPLAADS PTPQNQQNWD RELLRYGANH
RNGNVSSHEP GNSAQHGHYT PPNGHCGHVV GSDSTASRYC SDPLKMIDVR DCDVTDDCFD
GEVNSAHQQA QVGNLKLDLP LDEDDYLMPS PQLPTNTTQY MDLIGDSKPT EMEPKRVNNG
YRKYPEFLTI QGKTSLDNPE YIMSQDEGPL TPQTIGIPTP DLEKVLTNGT FGSQVRQRSS
EEESDHEYYN DFDRLERELQ PLKPLRKNET TV
//
