EGFR_DROME
ID EGFR_DROME Reviewed; 1426 AA.
AC P04412; O18370; O61601; P81868; Q9W2G0;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Epidermal growth factor receptor;
DE Short=Egfr;
DE EC=2.7.10.1;
DE AltName: Full=Drosophila relative of ERBB;
DE AltName: Full=Gurken receptor;
DE AltName: Full=Protein torpedo;
DE Flags: Precursor;
GN Name=Egfr; Synonyms=c-erbB, DER, top; ORFNames=CG10079;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS TYPE I AND TYPE II), AND
RP FUNCTION.
RX PubMed=8070664; DOI=10.1093/genetics/137.2.531;
RA Clifford R., Schuepbach T.;
RT "Molecular analysis of the Drosophila EGF receptor homolog reveals that
RT several genetically defined classes of alleles cluster in subdomains of the
RT receptor protein.";
RL Genetics 137:531-550(1994).
RN [2]
RP SEQUENCE REVISION.
RA Clifford R., Schuepbach T.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=2982499; DOI=10.1016/0092-8674(85)90208-9;
RA Livneh E., Glazer L., Segal D., Schlessinger J., Shilo B.-Z.;
RT "The Drosophila EGF receptor gene homolog: conservation of both hormone
RT binding and kinase domains.";
RL Cell 40:599-607(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=3093080; DOI=10.1016/0092-8674(86)90709-9;
RA Schejter E.D., Segal D., Glazer L., Shilo B.-Z.;
RT "Alternative 5' exons and tissue-specific expression of the Drosophila EGF
RT receptor homolog transcripts.";
RL Cell 46:1091-1101(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS TYPE I AND TYPE II), FUNCTION,
RP TISSUE SPECIFICITY, AND MUTANTS.
RX PubMed=9882502; DOI=10.1006/dbio.1998.9121;
RA Lesokhin A.M., Yu S.-Y., Katz J., Baker N.E.;
RT "Several levels of EGF receptor signaling during photoreceptor
RT specification in wild-type, Ellipse, and null mutant Drosophila.";
RL Dev. Biol. 205:129-144(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM TYPE I).
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [7]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 959-1078.
RC STRAIN=Daekwanryeong;
RX PubMed=2983232; DOI=10.1038/314178a0;
RA Wadsworth S.C., Vincent W.S. III, Bilodeau-Wentworth D.;
RT "A Drosophila genomic sequence with homology to human epidermal growth
RT factor receptor.";
RL Nature 314:178-180(1985).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1069-1121.
RC TISSUE=Embryo;
RX PubMed=9731193; DOI=10.1006/bbrc.1998.9003;
RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.;
RT "Sampling the genomic pool of protein tyrosine kinase genes using the
RT polymerase chain reaction with genomic DNA.";
RL Biochem. Biophys. Res. Commun. 249:660-667(1998).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1133-1137; 1155-1167 AND 1209-1216,
RP AND MUTANTS.
RX PubMed=1936959; DOI=10.1093/genetics/129.1.191;
RA Raz E., Schejter E.D., Shilo B.Z.;
RT "Interallelic complementation among DER/flb alleles: implications for the
RT mechanism of signal transduction by receptor-tyrosine kinases.";
RL Genetics 129:191-201(1991).
RN [11]
RP REVIEW.
RX PubMed=9094709; DOI=10.1016/s0092-8674(00)80177-4;
RA Perrimon N., Perkins L.A.;
RT "There must be 50 ways to rule the signal: the case of the Drosophila EGF
RT receptor.";
RL Cell 89:13-16(1997).
RN [12]
RP INTERACTION WITH VAV.
RX PubMed=10781813; DOI=10.1016/s0014-5793(00)01413-7;
RA Dekel I., Russek N., Jones T., Mortin M.A., Katzav S.;
RT "Identification of the Drosophila melanogaster homologue of the mammalian
RT signal transducer protein, Vav.";
RL FEBS Lett. 472:99-104(2000).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22140578; DOI=10.1371/journal.pone.0028349;
RA Geiger J.A., Carvalho L., Campos I., Santos A.C., Jacinto A.;
RT "Hole-in-one mutant phenotypes link EGFR/ERK signaling to epithelial tissue
RT repair in Drosophila.";
RL PLoS ONE 6:E28349-E28349(2011).
RN [14]
RP FUNCTION.
RX PubMed=23579691; DOI=10.1371/journal.pone.0060180;
RA Shen W., Chen X., Cormier O., Cheng D.C., Reed B., Harden N.;
RT "Modulation of morphogenesis by Egfr during dorsal closure in Drosophila.";
RL PLoS ONE 8:E60180-E60180(2013).
RN [15]
RP FUNCTION.
RX PubMed=24855950; DOI=10.1016/j.cell.2014.03.045;
RA Cai D., Chen S.C., Prasad M., He L., Wang X., Choesmel-Cadamuro V.,
RA Sawyer J.K., Danuser G., Montell D.J.;
RT "Mechanical feedback through E-cadherin promotes direction sensing during
RT collective cell migration.";
RL Cell 157:1146-1159(2014).
RN [16]
RP FUNCTION, AND MUTAGENESIS OF TYR-1095; TYR-1204; TYR-1218; TYR-1246;
RP TYR-1271; TYR-1310; TYR-1342; TYR-1357 AND 1405-TYR-TYR-1406.
RX PubMed=34411095; DOI=10.1371/journal.pgen.1009738;
RA Soler Beatty J., Molnar C., Luque C.M., de Celis J.F., Martin-Bermudo M.D.;
RT "EGFRAP encodes a new negative regulator of the EGFR acting in both normal
RT and oncogenic EGFR/Ras-driven tissue morphogenesis.";
RL PLoS Genet. 17:e1009738-e1009738(2021).
RN [17] {ECO:0007744|PDB:3I2T}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 100-644, GLYCOSYLATION AT
RP ASN-443, FUNCTION, SUBUNIT, GLYCOSYLATION AT ASN-419; ASN-443 AND ASN-482,
RP AND MUTAGENESIS OF ILE-101; TYR-131; TYR-341; ASN-342; THR-344; TYR-346;
RP VAL-347; LEU-348; TYR-358; HIS-369; 592-THR--VAL-1426; ASP-646; HIS-649;
RP LYS-658 AND 688-THR--VAL-1426.
RX PubMed=19718021; DOI=10.1038/nature08297;
RA Alvarado D., Klein D.E., Lemmon M.A.;
RT "ErbB2 resembles an autoinhibited invertebrate epidermal growth factor
RT receptor.";
RL Nature 461:287-291(2009).
RN [18]
RP INTERACTION WITH GRAF, UBIQUITINATION, AND MUTAGENESIS OF TYR-1271.
RX PubMed=28993397; DOI=10.1242/dev.153288;
RA Kim S., Nahm M., Kim N., Kwon Y., Kim J., Choi S., Choi E.Y., Shim J.,
RA Lee C., Lee S.;
RT "Graf regulates hematopoiesis through GEEC endocytosis of EGFR.";
RL Development 144:4159-4172(2017).
RN [19] {ECO:0007744|PDB:3LTF, ECO:0007744|PDB:3LTG}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 100-688 IN COMPLEX WITH MANNOSE,
RP FUNCTION, SUBUNIT, AND GLYCOSYLATION AT ASN-128; ASN-443; ASN-482 AND
RP ASN-569.
RX PubMed=20723758; DOI=10.1016/j.cell.2010.07.015;
RA Alvarado D., Klein D.E., Lemmon M.A.;
RT "Structural basis for negative cooperativity in growth factor binding to an
RT EGF receptor.";
RL Cell 142:568-579(2010).
RN [20]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23029159; DOI=10.1371/journal.pone.0045649;
RA Ruiz O.E., Nikolova L.S., Metzstein M.M.;
RT "Drosophila Zpr1 (Zinc finger protein 1) is required downstream of both
RT EGFR and FGFR signaling in tracheal subcellular lumen formation.";
RL PLoS ONE 7:E45649-E45649(2012).
CC -!- FUNCTION: Receptor tyrosine kinase, binding ligands of the EGF family
CC and activating several signaling cascades to convert extracellular cues
CC into appropriate cellular responses (PubMed:8070664, PubMed:9882502,
CC PubMed:22140578, PubMed:23579691). Known ligands include spitz, gurken,
CC vein and giant-lens (PubMed:9882502, PubMed:22140578, PubMed:19718021,
CC PubMed:20723758). Transduces the signal through the ras-raf-MAPK
CC pathway (PubMed:9094709). Critical for the proliferation of imaginal
CC tissues, and for the determination of both the antero-posterior and
CC dorso-ventral polarities of the oocyte (PubMed:9882502,
CC PubMed:23579691, PubMed:34411095). In the embryo, plays a role in the
CC establishment of ventral cell fates, maintenance of amnioserosa and
CC ventral neuroectodermal cells, germ band retraction, cell fate
CC specification in the central nervous system, and production and repair
CC of the cuticle (PubMed:22140578, PubMed:23579691, PubMed:9094709,
CC PubMed:23029159). During dorsal closure (DC) functions with the
CC dpp- and ACK-signaling pathways to regulate expression of the myosin
CC zip in the embryonic epidermis and amnioserosa (AS), and thus
CC coordinate the progression of epidermal cell shape changes required for
CC correct DC (PubMed:23579691). In the embryonic epidermis, functions by
CC negatively regulating dpp and consequently the dpp-dependent expression
CC of the myosin zip (PubMed:23579691). In the AS, negatively regulates
CC the production/ and or secretion of a diffusible signal which, is
CC produced by the ACK-signaling pathway, and acts in the AS and epidermal
CC cells to promote zip expression (PubMed:23579691). Also required in the
CC AS to inhibit or delay apoptosis, and consequently slow the rate of DC
CC (PubMed:23579691). Therefore functions at multiple levels to negatively
CC regulate morphogenesis during DC, suggesting that it acts as a general
CC brake mechanism for adjusting the rate of dorsal closure to ensure that
CC closure proceeds smoothly and without loss of epidermal integrity
CC (PubMed:23579691). During oogenesis, one of two tyrosine kinase
CC chemoattractant receptors (Egfr and Pvr), that function in the border
CC cells (BC) to detect guidance cues from the oocyte and transduce this
CC information to the guidance pathway that regulate the collective
CC migration of the BC cluster through the nurse cells to the oocyte
CC (PubMed:24855950). {ECO:0000269|PubMed:19718021,
CC ECO:0000269|PubMed:20723758, ECO:0000269|PubMed:22140578,
CC ECO:0000269|PubMed:23029159, ECO:0000269|PubMed:23579691,
CC ECO:0000269|PubMed:24855950, ECO:0000269|PubMed:34411095,
CC ECO:0000269|PubMed:8070664, ECO:0000269|PubMed:9882502,
CC ECO:0000303|PubMed:9094709}.
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 -!- SUBUNIT: Homodimer (PubMed:19718021, PubMed:20723758). Binding of the
CC ligand spitz triggers homodimerization of the receptor however, it is
CC able to form dimers, albeit weakly, in the absence of spitz
CC (PubMed:19718021, PubMed:20723758). Interacts (when phosphorylated on
CC tyrosine residues) with Vav (via SH2 domain) (PubMed:10781813).
CC Interacts (when ubiquitinated) with Graf (PubMed:28993397). May
CC interact (when phosphorylated) with EGFRAP (via SH2 domain)
CC (PubMed:34411095). {ECO:0000269|PubMed:10781813,
CC ECO:0000269|PubMed:19718021, ECO:0000269|PubMed:20723758,
CC ECO:0000269|PubMed:28993397, ECO:0000269|PubMed:34411095}.
CC -!- INTERACTION:
CC P04412; P91643: kek1; NbExp=2; IntAct=EBI-197863, EBI-6896313;
CC P04412; Q01083: spi; NbExp=4; IntAct=EBI-197863, EBI-91342;
CC P04412-1; P04412-1: Egfr; NbExp=4; IntAct=EBI-15802052, EBI-15802052;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Type I;
CC IsoId=P04412-1; Sequence=Displayed;
CC Name=Type II;
CC IsoId=P04412-2; Sequence=VSP_002897;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in embryos. In larvae,
CC uniform expression is seen in wing disks, genital disk, anlagen of
CC testis and ovary, and brain cortex. In eye-antenna disk, highest
CC expression is anterior to morphogenetic furrow, levels remain high in
CC photoreceptor precursor cells. This pattern is reversed in posterior
CC eye disk. In adults expression is high in brain cortex and thoracic and
CC abdominal ganglia. {ECO:0000269|PubMed:9882502}.
CC -!- PTM: Ubiquitination by Cbl in response to high spi, promotes its
CC interaction with Graf and thus facilitates its GPI-enriched endocytic
CC compartment (GEEC) mediated endocytosis and its subsequent degradation.
CC {ECO:0000269|PubMed:28993397}.
CC -!- DISRUPTION PHENOTYPE: Embryonic wound healing defects. RNAi-mediated
CC knockdown in tracheal cells results in defective gas-filling lumen in
CC terminal branches (PubMed:23029159). {ECO:0000269|PubMed:22140578,
CC ECO:0000269|PubMed:23029159}.
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 EMBL; AF052754; AAC08536.1; -; Genomic_DNA.
DR EMBL; AF052753; AAC08536.1; JOINED; Genomic_DNA.
DR EMBL; AF052754; AAC08535.1; -; Genomic_DNA.
DR EMBL; AF052752; AAC08535.1; JOINED; Genomic_DNA.
DR EMBL; K03054; AAA51462.1; -; Genomic_DNA.
DR EMBL; K03417; AAA51460.1; -; mRNA.
DR EMBL; K03416; AAA50965.1; -; mRNA.
DR EMBL; AF109077; AAD26134.1; -; Genomic_DNA.
DR EMBL; AF109078; AAD26132.1; -; Genomic_DNA.
DR EMBL; AF109082; AAD26132.1; JOINED; Genomic_DNA.
DR EMBL; AF109078; AAD26133.1; -; Genomic_DNA.
DR EMBL; AF109084; AAD26133.1; JOINED; Genomic_DNA.
DR EMBL; AF109079; AAD26130.1; -; Genomic_DNA.
DR EMBL; AF109081; AAD26130.1; JOINED; Genomic_DNA.
DR EMBL; AF109079; AAD26131.1; -; Genomic_DNA.
DR EMBL; AF109083; AAD26131.1; JOINED; Genomic_DNA.
DR EMBL; AF109080; AAD26135.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF46732.1; -; Genomic_DNA.
DR EMBL; X02293; CAA26157.1; -; Genomic_DNA.
DR EMBL; AJ002912; CAA05747.1; -; Genomic_DNA.
DR EMBL; X78920; CAA55523.1; -; Genomic_DNA.
DR EMBL; X78918; CAA55521.1; -; Genomic_DNA.
DR EMBL; X78919; CAA55522.1; -; Genomic_DNA.
DR PIR; A00640; GQFFE.
DR RefSeq; NP_476759.1; NM_057411.4.
DR PDB; 3I2T; X-ray; 2.70 A; A=100-644.
DR PDB; 3LTF; X-ray; 3.20 A; A/C=100-688.
DR PDB; 3LTG; X-ray; 3.40 A; A/C=100-688.
DR PDBsum; 3I2T; -.
DR PDBsum; 3LTF; -.
DR PDBsum; 3LTG; -.
DR AlphaFoldDB; P04412; -.
DR SMR; P04412; -.
DR BioGRID; 63083; 168.
DR DIP; DIP-17316N; -.
DR IntAct; P04412; 5.
DR MINT; P04412; -.
DR STRING; 7227.FBpp0071571; -.
DR TCDB; 8.A.23.1.13; the basigin (basigin) family.
DR GlyGen; P04412; 11 sites.
DR PaxDb; P04412; -.
DR PRIDE; P04412; -.
DR EnsemblMetazoa; FBtr0071654; FBpp0071571; FBgn0003731.
DR GeneID; 37455; -.
DR KEGG; dme:Dmel_CG10079; -.
DR CTD; 1956; -.
DR FlyBase; FBgn0003731; Egfr.
DR VEuPathDB; VectorBase:FBgn0003731; -.
DR eggNOG; KOG1025; Eukaryota.
DR HOGENOM; CLU_003384_5_1_1; -.
DR InParanoid; P04412; -.
DR PhylomeDB; P04412; -.
DR BRENDA; 2.7.10.1; 1994.
DR Reactome; R-DME-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-DME-1253288; Downregulation of ERBB4 signaling.
DR Reactome; R-DME-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR Reactome; R-DME-177929; Signaling by EGFR.
DR Reactome; R-DME-179812; GRB2 events in EGFR signaling.
DR Reactome; R-DME-180292; GAB1 signalosome.
DR Reactome; R-DME-180336; SHC1 events in EGFR signaling.
DR Reactome; R-DME-182971; EGFR downregulation.
DR Reactome; R-DME-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-DME-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-DME-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DME-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR Reactome; R-DME-9652282; Drug-mediated inhibition of ERBB2 signaling.
DR SignaLink; P04412; -.
DR BioGRID-ORCS; 37455; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Egfr; fly.
DR EvolutionaryTrace; P04412; -.
DR GenomeRNAi; 37455; -.
DR PRO; PR:P04412; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003731; Expressed in capitellum (Drosophila) and 66 other tissues.
DR ExpressionAtlas; P04412; baseline and differential.
DR Genevisible; P04412; DM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005006; F:epidermal growth factor receptor activity; IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0030031; P:cell projection assembly; IMP:FlyBase.
DR GO; GO:0030381; P:chorion-containing eggshell pattern formation; IGI:FlyBase.
DR GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0001751; P:compound eye photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0035225; P:determination of genital disc primordium; IMP:FlyBase.
DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:UniProtKB.
DR GO; GO:0007395; P:dorsal closure, spreading of leading edge cells; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:CACAO.
DR GO; GO:0009880; P:embryonic pattern specification; IGI:FlyBase.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0061331; P:epithelial cell proliferation involved in Malpighian tubule morphogenesis; IMP:FlyBase.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:FlyBase.
DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IMP:FlyBase.
DR GO; GO:0001654; P:eye development; IMP:FlyBase.
DR GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:FlyBase.
DR GO; GO:0007390; P:germ-band shortening; IMP:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IGI:FlyBase.
DR GO; GO:0008406; P:gonad development; IMP:FlyBase.
DR GO; GO:0007482; P:haltere development; IMP:FlyBase.
DR GO; GO:0003015; P:heart process; IMP:FlyBase.
DR GO; GO:0007444; P:imaginal disc development; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0007479; P:leg disc proximal/distal pattern formation; IMP:FlyBase.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IGI:FlyBase.
DR GO; GO:0035160; P:maintenance of epithelial integrity, open tracheal system; IMP:FlyBase.
DR GO; GO:0007443; P:Malpighian tubule morphogenesis; IMP:FlyBase.
DR GO; GO:0008071; P:maternal determination of dorsal/ventral axis, ovarian follicular epithelium, soma encoded; IMP:FlyBase.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:FlyBase.
DR GO; GO:0016333; P:morphogenesis of follicular epithelium; IMP:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IGI:FlyBase.
DR GO; GO:0046673; P:negative regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IGI:FlyBase.
DR GO; GO:0035310; P:notum cell fate specification; IMP:FlyBase.
DR GO; GO:0007477; P:notum development; IMP:FlyBase.
DR GO; GO:0001742; P:oenocyte differentiation; IMP:FlyBase.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:0016318; P:ommatidial rotation; IMP:FlyBase.
DR GO; GO:0007309; P:oocyte axis specification; IMP:FlyBase.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase.
DR GO; GO:0046530; P:photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0043703; P:photoreceptor cell fate determination; IMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IGI:FlyBase.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045572; P:positive regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IMP:UniProtKB.
DR GO; GO:0090303; P:positive regulation of wound healing; IMP:FlyBase.
DR GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
DR GO; GO:0007431; P:salivary gland development; IMP:FlyBase.
DR GO; GO:0016330; P:second mitotic wave involved in compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
DR GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase.
DR GO; GO:0048865; P:stem cell fate commitment; IMP:FlyBase.
DR GO; GO:0007426; P:tracheal outgrowth, open tracheal system; IMP:FlyBase.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0035309; P:wing and notum subfield formation; IMP:FlyBase.
DR GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
DR CDD; cd00064; FU; 6.
DR Gene3D; 3.80.20.20; -; 2.
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 Pfam; PF00757; Furin-like; 1.
DR Pfam; PF14843; GF_recep_IV; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 7.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Developmental protein;
KW Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1426
FT /note="Epidermal growth factor receptor"
FT /id="PRO_0000016676"
FT TOPO_DOM 31..868
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 869..889
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 890..1426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 938..1198
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1232..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1063
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 944..952
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 971
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 902
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 1310
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:3LTF"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:3I2T, ECO:0007744|PDB:3LTF"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:3LTF"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:3LTF"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..101
FT /note="MLLRRRNGPCPFPLLLLLLAHCICIWPASAARDRYARQNNRQRHQDIDRDRD
FT RDRFLYRSSSAQNRQRGGANFALGLGANGVTIPTSLEDKNKNEFVKGKI -> MMIISM
FT WMSISRGLWDSSSILSVLLILACMASITTSSSVSNAGYVDNGNMKV (in isoform
FT Type II)"
FT /evidence="ECO:0000305"
FT /id="VSP_002897"
FT MUTAGEN 101
FT /note="I->A: Increased binding to spitz; when associated
FT with A-101; A-358 and S-369."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 131
FT /note="Y->A: Increased binding to spitz; when associated
FT with A-131; A-358 and S-369."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 341
FT /note="Y->E: In dim-arm; Does not form dimers even in the
FT presence of spitz; when associated with A-342; D-344; E-
FT 346; A-347 and D-348."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 342
FT /note="N->A: In dim-arm; Does not form dimers even in the
FT presence of spitz; when associated with E-341; D-344; E-
FT 346; A-347 and D-348."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 344
FT /note="T->D: >D: In dim-arm; Does not form dimers even in
FT the presence of spitz; when associated with E-341; A-342;
FT E-346; A-347 and D-348."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 346
FT /note="Y->E: In dim-arm; Does not form dimers even in the
FT presence of spitz; when associated with E-341; A-342; D-
FT 344; A-347 and D-348."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 347
FT /note="V->A: In dim-arm; Does not form dimers even in the
FT presence of Spitz; when associated with E-341; A-342; D-
FT 344; E-346 and D-348."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 348
FT /note="L->D: In dim-arm; Does not form dimers even in the
FT presence of spitz; when associated with E-341; A-342; D-
FT 344; E-346 and A-347."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 358
FT /note="Y->A: Reduced dissociation and increased binding to
FT spitz; when associated with S-369. Increased binding to
FT spitz; when associated with A-101; A-131 and S-369."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 369
FT /note="H->S: Reduced dissociation and increased binding to
FT spitz; when associated with A-358. Increased binding to
FT spitz; when associated with A-101; A-131 and A-358."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 592..1426
FT /note="Missing: Slightly reduced affinity for spitz."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 646
FT /note="D->A: In tether; No effect on binding to spitz; when
FT associated with A-649 and A-658."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 649
FT /note="H->A: In tether; No effect on binding to spitz; when
FT associated with A-646 and A-658."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 658
FT /note="K->A: In tether; No effect on binding to spitz; when
FT associated with A-646 and A-649."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 688..1426
FT /note="Missing: Forms dimers in presence of spitz. Forms
FT weak dimers in the absence of spitz."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 793
FT /note="C->R: In EGFR-ELP-1."
FT MUTAGEN 936
FT /note="A->T: In EGFR-ELP-B1 and EGFR-ELP-B1RB1."
FT MUTAGEN 1058
FT /note="R->Q: In EGFR-ELP-B1RB1."
FT MUTAGEN 1095
FT /note="Y->F: Weak interaction with EGFRAP; when associated
FT with F-1204; F-1218; F-1246; F-1271; F-1310; F-1342. Very
FT weak interaction with EGFRAP; when associated with F-1204;
FT F-1218; F-1246; F-1271; F-1310; F-1342 and 1405-F-F-1406."
FT /evidence="ECO:0000269|PubMed:34411095"
FT MUTAGEN 1135
FT /note="T->I: In EGFR-2W74."
FT MUTAGEN 1156
FT /note="G->S: In EGFR-2C82."
FT MUTAGEN 1162
FT /note="P->L: In EGFR-1F26."
FT MUTAGEN 1166
FT /note="S->L: In EGFR-2L65."
FT MUTAGEN 1204
FT /note="Y->F: Weak interaction with EGFRAP; when associated
FT with F-1095; F-1218; F-1246; F-1271; F-1310; F-1342. Very
FT weak interaction with EGFRAP; when associated with F-1095;
FT F-1218; F-1246; F-1271; F-1310; F-1342 and 1405-F-F-1406."
FT /evidence="ECO:0000269|PubMed:34411095"
FT MUTAGEN 1210..1216
FT /note="DKFTRLP->EKVHPAA: In EGFR-2X51."
FT MUTAGEN 1218
FT /note="Y->F: Weak interaction with EGFRAP; when associated
FT with F-1095; F-1204; F-1246; F-1271; F-1310; F-1342. Very
FT weak interaction with EGFRAP; when associated with F-1095;
FT F-1204; F-1246; F-1271; F-1310; F-1342 and 1405-F-F-1406."
FT /evidence="ECO:0000269|PubMed:34411095"
FT MUTAGEN 1246
FT /note="Y->F: Weak interaction with EGFRAP; when associated
FT with F-1095; F-1204; F-1218; F-1271; F-1310; F-1342. Very
FT weak interaction with EGFRAP; when associated with F-1095;
FT F-1204; F-1218; F-1271; F-1310; F-1342 and 1405-F-F-1406."
FT /evidence="ECO:0000269|PubMed:34411095"
FT MUTAGEN 1271
FT /note="Y->F: Cbl-mediated ubiquitination, in response to
FT high levels of Egfr ligand spi, is impaired resulting in
FT reduced interaction with Graf and thus decreased GEEC-
FT mediated endocytosis and degradation. Weak interaction with
FT EGFRAP; when associated with F-1095; F-1204; F-1218; F-
FT 1246; F-1310; F-1342. Very weak interaction with EGFRAP;
FT when associated with F-1095; F-1204; F-1218; F-1246; F-
FT 1310; F-1342 and 1405-F-F-1406."
FT /evidence="ECO:0000269|PubMed:28993397,
FT ECO:0000269|PubMed:34411095"
FT MUTAGEN 1310
FT /note="Y->F: Weak interaction with EGFRAP; when associated
FT with F-1095; F-1204; F-1218; F-1246; F-1271; F-1342. Very
FT weak interaction with EGFRAP; when associated with F-1095;
FT F-1204; F-1218; F-1246; F-1271; F-1342 and 1405-F-F-1406."
FT /evidence="ECO:0000269|PubMed:34411095"
FT MUTAGEN 1357
FT /note="Y->F: No effect on interaction with EGFRAP.
FT Decreased interaction with EGFRAP; when associated with
FT 1405-F-F-1406. Very weak interaction with EGFRAP; when
FT associated with F-1095; F-1204; F-1218; F-1246; F-1271; F-
FT 1310."
FT /evidence="ECO:0000269|PubMed:34411095"
FT MUTAGEN 1405..1406
FT /note="YY->FF: Decreased interaction with EGFRAP; when
FT associated with F-1357."
FT /evidence="ECO:0000269|PubMed:34411095"
FT CONFLICT 137
FT /note="K -> E (in Ref. 5 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 329..331
FT /note="AVS -> GVC (in Ref. 5 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="R -> L (in Ref. 5 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 789
FT /note="R -> C (in Ref. 5 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 959
FT /note="P -> A (in Ref. 8; CAA26157)"
FT /evidence="ECO:0000305"
FT CONFLICT 995
FT /note="E -> V (in Ref. 5 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1072..1080
FT /note="QTPSLVKIT -> RLLAGEDH (in Ref. 3, 4 and 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 1097..1098
FT /note="AA -> I (in Ref. 9; CAA05747)"
FT /evidence="ECO:0000305"
FT CONFLICT 1118
FT /note="T -> R (in Ref. 9; CAA05747)"
FT /evidence="ECO:0000305"
FT CONFLICT 1242
FT /note="K -> E (in Ref. 5 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1265
FT /note="M -> I (in Ref. 5 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1287
FT /note="R -> T (in Ref. 5 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1325
FT /note="M -> I (in Ref. 6; AAF46732)"
FT /evidence="ECO:0000305"
FT CONFLICT 1383
FT /note="G -> V (in Ref. 5 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1412..1426
FT /note="ELQPLHRNRNTETRV -> SCSHASKPQHGDEGVGSSRVGAIANEEGESCQV
FT PLEAMRYAFAGCYLR (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:3I2T"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:3I2T"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:3I2T"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:3I2T"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3LTF"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:3I2T"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:3LTF"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 305..316
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:3I2T"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 385..394
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:3I2T"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:3I2T"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 421..425
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:3I2T"
FT HELIX 431..435
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:3I2T"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:3LTG"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:3I2T"
FT HELIX 455..463
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:3I2T"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:3LTF"
FT TURN 499..502
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 503..509
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 525..531
FT /evidence="ECO:0007829|PDB:3I2T"
FT TURN 539..541
FT /evidence="ECO:0007829|PDB:3I2T"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 555..561
FT /evidence="ECO:0007829|PDB:3I2T"
FT HELIX 563..567
FT /evidence="ECO:0007829|PDB:3I2T"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:3LTG"
FT STRAND 582..586
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 590..598
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 601..604
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:3I2T"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:3LTF"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:3I2T"
SQ SEQUENCE 1426 AA; 159718 MW; 4D424C3C99DA4AF4 CRC64;
MLLRRRNGPC PFPLLLLLLA HCICIWPASA ARDRYARQNN RQRHQDIDRD RDRDRFLYRS
SSAQNRQRGG ANFALGLGAN GVTIPTSLED KNKNEFVKGK ICIGTKSRLS VPSNKEHHYR
NLRDRYTNCT YVDGNLKLTW LPNENLDLSF LDNIREVTGY ILISHVDVKK VVFPKLQIIR
GRTLFSLSVE EEKYALFVTY SKMYTLEIPD LRDVLNGQVG FHNNYNLCHM RTIQWSEIVS
NGTDAYYNYD FTAPERECPK CHESCTHGCW GEGPKNCQKF SKLTCSPQCA GGRCYGPKPR
ECCHLFCAGG CTGPTQKDCI ACKNFFDEAV SKEECPPMRK YNPTTYVLET NPEGKYAYGA
TCVKECPGHL LRDNGACVRS CPQDKMDKGG ECVPCNGPCP KTCPGVTVLH AGNIDSFRNC
TVIDGNIRIL DQTFSGFQDV YANYTMGPRY IPLDPERREV FSTVKEITGY LNIEGTHPQF
RNLSYFRNLE TIHGRQLMES MFAALAIVKS SLYSLEMRNL KQISSGSVVI QHNRDLCYVS
NIRWPAIQKE PEQKVWVNEN LRADLCEKNG TICSDQCNED GCWGAGTDQC LTCKNFNFNG
TCIADCGYIS NAYKFDNRTC KICHPECRTC NGAGADHCQE CVHVRDGQHC VSECPKNKYN
DRGVCRECHA TCDGCTGPKD TIGIGACTTC NLAIINNDAT VKRCLLKDDK CPDGYFWEYV
HPQEQGSLKP LAGRAVCRKC HPLCELCTNY GYHEQVCSKC THYKRREQCE TECPADHYTD
EEQRECFQRH PECNGCTGPG ADDCKSCRNF KLFDANETGP YVNSTMFNCT SKCPLEMRHV
NYQYTAIGPY CAASPPRSSK ITANLDVNMI FIITGAVLVP TICILCVVTY ICRQKQKAKK
ETVKMTMALS GCEDSEPLRP SNIGANLCKL RIVKDAELRK GGVLGMGAFG RVYKGVWVPE
GENVKIPVAI KELLKSTGAE SSEEFLREAY IMASEEHVNL LKLLAVCMSS QMMLITQLMP
LGCLLDYVRN NRDKIGSKAL LNWSTQIAKG MSYLEEKRLV HRDLAARNVL VQTPSLVKIT
DFGLAKLLSS DSNEYKAAGG KMPIKWLALE CIRNRVFTSK SDVWAFGVTI WELLTFGQRP
HENIPAKDIP DLIEVGLKLE QPEICSLDIY CTLLSCWHLD AAMRPTFKQL TTVFAEFARD
PGRYLAIPGD KFTRLPAYTS QDEKDLIRKL APTTDGSEAI AKPDDYLQPK AAPGPSHRTD
CTDEMPKLNR YCKDPSNKNS STGDDERDSS AREVGVGNLR LDLPVDEDDY LMPTCQPGPN
NNNNMNNPNQ NNMAAVGVAA GYMDLIGVPV SVDNPEYLLN AQTLGVGESP IPTQTIGIPV
MGGPGTMEVK VPMPGSEPTS SDHEYYNDTQ RELQPLHRNR NTETRV
