ID Q6SAU7_DROME Unreviewed; 1325 AA.
AC Q6SAU7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE SubName: Full=Epidermal growth factor receptor {ECO:0000313|EMBL:AAR85114.1};
DE Flags: Fragment;
GN Name=Egfr {ECO:0000313|EMBL:AAR85114.1,
GN ECO:0000313|FlyBase:FBgn0003731};
GN ORFNames=CG10079 {ECO:0000313|EMBL:AAR85114.1,
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:AAR85114.1};
RN [1] {ECO:0000313|EMBL:AAR85114.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA096 {ECO:0000313|EMBL:AAR85114.1};
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; AY461156; AAR85114.1; -; 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; 5.
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; 5.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
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:AAR85114.1};
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 1162..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..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:AAR85114.1"
SQ SEQUENCE 1325 AA; 147957 MW; 009F45D33008A07B CRC64;
CIGTKSRLSV PSNKEHHYRN LRDRYTNCTY VDGNLELTWL PNENLDLSFL DNIREVTGYI
LISHXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXQDVY ANYTMGPRYI PLDPERLEVF
STVKEITGYL NIEGTHPQFR NLSYFRNLET IHGRQLMESM FAALAIVKSS LYSLEMRNLK
QISSGSVVIQ HNRDLCYVSN IRWPAIQKEP EQKVWVNENL RADLCEKNGT ICSDQCNEDG
CWGAGTDQCL NCKNFNFNGT CIADCGYISN AYKFDNRTCK ICHPECRTCN GAGADHCQEC
VHVRDGQHCV SECPKNKYND RGVCRECHAT CDGCTGPKDT IGIGACTTCN LAIINNDATV
KRCLLKDDKC PDGYFWEYVH PQEQGSLKPL AGRAVCRKCH XLCELCTNYG YHEQVCSKCT
HYKRREQCET ECPADHYTDE EQRECFQCHP ECNGCTGPGA DDCKSXRNFK 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 LIEXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXKNSS TGDDETDSSA REVGVGNLRL
DLPVDEDDYL MPTCQPGPNN NNNMNNPNQN NMAAVGVAAG YMDLIGVPVS VDNPEYLLNA
QTLGVGESPI PTQTIGIPVM GVPGTMEVKV PMPGSEPTSS DHEYYNDTQR ELQPLHRNRN
TETRV
//
