ID Q6SAX8_DROME Unreviewed; 1325 AA.
AC Q6SAX8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE SubName: Full=Epidermal growth factor receptor {ECO:0000313|EMBL:AAR85083.1};
DE Flags: Fragment;
GN Name=Egfr {ECO:0000313|EMBL:AAR85083.1,
GN ECO:0000313|FlyBase:FBgn0003731};
GN ORFNames=CG10079 {ECO:0000313|EMBL:AAR85083.1,
GN ECO:0000313|FlyBase:FBgn0003731};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAR85083.1};
RN [1] {ECO:0000313|EMBL:AAR85083.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA046 {ECO:0000313|EMBL:AAR85083.1};
RX PubMed=15280235; DOI=10.1534/genetics.104.026252;
RA Palsson A., Rouse A., Riley-Berger R., Dworkin I., Gibson G.;
RT "Nucleotide variation in the Egfr locus of Drosophila melanogaster.";
RL Genetics 167:1199-1212(2004).
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:0000256|ARBA:ARBA00001171};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; AY461125; AAR85083.1; -; Genomic_DNA.
DR AGR; FB:FBgn0003731; -.
DR FlyBase; FBgn0003731; Egfr.
DR ChiTaRS; Egfr; fly.
DR GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR GO; GO:0000003; P:reproduction; IEA:UniProt.
DR CDD; cd00064; FU; 3.
DR Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24416:SF566; 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; PF01030; Recep_L_domain; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
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 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000313|EMBL:AAR85083.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 768..791
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 837..1101
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1166..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 870
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAR85083.1"
SQ SEQUENCE 1325 AA; 148631 MW; 95989D0DB025BBDE CRC64;
CIGTKSRLSV PSNKEHHYRN LRDRYTNCTY VDGNLELTWL PNENLDLSFL DNIREVTGYI
LISHVDVKKV VFPKLQIIRG RTLFSLSVEE EKYALFVTYS KMYTLEIPDL RDVLNGQVGF
HNNYNLCHMR TIQWSEIVSN GTDAYYNYDF TAPERXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXDVY ANYTMGPRYI PLDPERLEVF
STVKEITGYL NIEGTHPQFR NLSYFRNLET IHGRQLMESM FAALAIVKSS LYSLEMRNLK
QISSGSVVIQ HNRDLCYVSN IRWPAIQKEP EQKVWVNENL RADLCEKNGT ICSDQCNEDG
CWGAGXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX ICHPECRTCN GAGADHCQEC
VHVRDGQHCV SECPKNKYND RGVCRECHAT CDGCTGPKDT IGIGACTTCN LAIINNDATV
KRCLLKDDKC PDGYFWEYVH PQEQGSLKPL AGRAVCRKCH PLCELCTNYG YHEQVCSKCT
HYKRREQCET ECPADHYTDE EQRECFQCHX XXXXXXXXXX XXXXXXXXXK LFDANETGPY
VNSTMFNCTS KCPLEMRHVN YQYTAIGPYC AASPPRSSKI TANLDVNMIF IITGAVLVPT
ICILCVVTYI CRQKQKAKKE TVKMTMALSG CEDSEPLRPS NIGANLCKLR IVKDAELRKG
GVLGMGAFGR VYKGVWVPEG ENVKIPVAIK ELLKSTGAES SEEFLREAYI MASVEHVNLL
KLLAVCMSSQ MMLITQLMPL GCLLDYVRNN RDKIGSKALL NWSTQIAKGM SYLEEKRLVH
RDLAARNVLV QTPSLVKITD FGLAKLLSSD SNEYKAAGGK MPIKWLALEC IRNRVFTSKS
DVWAFGVTIW ELLTFGQRPH ENIPAKDIPD LIEVGLKLEQ XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXRY CKDPSNKNSS TGDDETDSSA REVGVGNLRL
DLPVDEDDYL MPTCQPGPNN NNNMNNPNQN NMAAVGVAAG YMDLIGVPVS VDNPEYLLNA
QTLGVGESPI PTQTIGIPVM GVPGTMEVKV PMPGSEPTSS DHEYYNDTQR ELQPLHRNRN
TETRV
//
