P04412 (EGFR_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Epidermal growth factor receptor
Short name=Egfr
EC=2.7.10.1

Alternative name(s):
Drosophila relative of ERBB
Gurken receptor
Protein torpedo

Gene names

Name:	Egfr
Synonyms:	c-erbB, DER, top
ORF Names:	CG10079

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	1426 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to four ligands: Spitz, Gurken, Vein and Argos, which is an antagonist. Transduces the signal through the ras-raf-MAPK pathway. Involved in a myriad of developmental decisions. Critical for the proliferation of imaginal tissues, and for the determination of both the antero-posterior and dorso-ventral polarities of the oocyte. In the embryo, plays a role in the establishment of ventral cell fates, maintenance of amnioserosa and ventral neuroectodermal cells, germ band retraction, cell fate specification in the central nervous system and production of cuticle.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Ubiquitously expressed in embryos. In larvae, uniform expression is seen in wing disks, genital disk, anlagen of testis and ovary, and brain cortex. In eye-antenna disk, highest expression is anterior to morphogenetic furrow, levels remain high in photoreceptor precursor cells. This pattern is reversed in posterior eye disk. In adults expression is high in brain cortex and thoracic and abdominal ganglia. Ref.5
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Traceable author statement. Source: FlyBase Malpighian tubule morphogenesis Inferred from mutant phenotype. Source: FlyBase R7 cell differentiation Traceable author statement. Source: FlyBase antennal development Non-traceable author statement. Source: FlyBase anti-apoptosis Non-traceable author statement. Source: FlyBase behavioral response to ethanol Inferred from mutant phenotype. Source: FlyBase border follicle cell migration Inferred from mutant phenotype. Source: FlyBase brain development Traceable author statement. Source: FlyBase branched duct epithelial cell fate determination, open tracheal system Traceable author statement. Source: FlyBase cell projection assembly Inferred from mutant phenotype. Source: FlyBase cell-cell adhesion Inferred from mutant phenotype. Source: FlyBase chorion-containing eggshell pattern formation Inferred from genetic interaction. Source: FlyBase compound eye cone cell fate commitment Traceable author statement. Source: FlyBase compound eye photoreceptor fate commitment Traceable author statement. Source: FlyBase determination of genital disc primordium Inferred from mutant phenotype. Source: FlyBase dorsal appendage formation Inferred from mutant phenotype. Source: FlyBase dorsal closure Inferred from mutant phenotype. Source: FlyBase establishment or maintenance of apical/basal cell polarity Inferred from mutant phenotype. Source: FlyBase eye-antennal disc morphogenesis Inferred from mutant phenotype. Source: FlyBase female germ-line cyst encapsulation Traceable author statement. Source: FlyBase gastrulation Traceable author statement. Source: FlyBase germ-band shortening Inferred from mutant phenotype. Source: FlyBase germ-line stem cell maintenance Inferred from genetic interaction. Source: FlyBase gonad development Inferred from mutant phenotype. Source: FlyBase haltere development Inferred from mutant phenotype. Source: FlyBase heart process Inferred from mutant phenotype. Source: FlyBase imaginal disc-derived wing vein morphogenesis Inferred from mutant phenotype. Source: FlyBase imaginal disc-derived wing vein specification Traceable author statement. Source: FlyBase leg disc proximal/distal pattern formation Inferred from mutant phenotype. Source: FlyBase maintenance of epithelial integrity, open tracheal system Inferred from mutant phenotype. Source: FlyBase male germ-line cyst encapsulation Traceable author statement. Source: FlyBase maternal determination of dorsal/ventral axis, ovarian follicular epithelium, soma encoded Inferred from mutant phenotype. Source: FlyBase muscle attachment Traceable author statement. Source: FlyBase muscle cell fate specification Traceable author statement. Source: FlyBase negative regulation of S phase of mitotic cell cycle Inferred from mutant phenotype. Source: FlyBase negative regulation of compound eye retinal cell programmed cell death Inferred from mutant phenotype. Source: FlyBase notum cell fate specification Inferred from mutant phenotype. Source: FlyBase notum development Inferred from mutant phenotype. Source: FlyBase oenocyte differentiation Traceable author statement. Source: FlyBase ommatidial rotation Inferred from mutant phenotype. Source: FlyBase oocyte anterior/posterior axis specification Non-traceable author statement. Source: FlyBase oocyte dorsal/ventral axis specification Non-traceable author statement. Source: FlyBase peripheral nervous system development Inferred from mutant phenotype. Source: FlyBase positive regulation of cell proliferation Inferred from mutant phenotype. Source: FlyBase progression of morphogenetic furrow involved in compound eye morphogenesis Traceable author statement. Source: FlyBase regulation of R8 cell spacing in compound eye Non-traceable author statement. Source: FlyBase regulation of hemocyte differentiation Inferred from mutant phenotype. Source: FlyBase salivary gland development Inferred from mutant phenotype. Source: FlyBase second mitotic wave involved in compound eye morphogenesis Inferred from mutant phenotype. Source: FlyBase segment polarity determination Inferred from mutant phenotype. Source: FlyBase spiracle morphogenesis, open tracheal system Inferred from mutant phenotype. Source: FlyBase stomatogastric nervous system development Traceable author statement. Source: FlyBase tracheal pit formation in open tracheal system Traceable author statement. Source: FlyBase wing disc proximal/distal pattern formation Traceable author statement. Source: FlyBase
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW epidermal growth factor-activated receptor activity Traceable author statement. Source: FlyBase protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
spi	Q01083	4	EBI-197863,EBI-91342

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Type I (identifier: P04412-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Type II (identifier: P04412-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: MLLRRRNGPC...NKNEFVKGKI → MMIISMWMSI...GYVDNGNMKV

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Potential

Chain

31 – 1426

1396

Epidermal growth factor receptor

PRO_0000016676

Regions

Topological domain

31 – 868

838

Extracellular Potential

Transmembrane

869 – 889

21

Helical; Potential

Topological domain

890 – 1426

537

Cytoplasmic Potential

Domain

938 – 1198

261

Protein kinase

Nucleotide binding

944 – 952

9

ATP By similarity

Sites

Active site

1063

1

Proton acceptor By similarity

Binding site

971

1

ATP By similarity

Amino acid modifications

Modified residue

902

1

Phosphothreonine; by PKC By similarity

Modified residue

1310

1

Phosphotyrosine; by autocatalysis By similarity

Glycosylation

128

1

N-linked (GlcNAc...) Potential

Glycosylation

241

1

N-linked (GlcNAc...) Potential

Glycosylation

419

1

N-linked (GlcNAc...) Potential

Glycosylation

443

1

N-linked (GlcNAc...) Potential

Glycosylation

482

1

N-linked (GlcNAc...) Potential

Glycosylation

569

1

N-linked (GlcNAc...) Potential

Glycosylation

599

1

N-linked (GlcNAc...) Potential

Glycosylation

617

1

N-linked (GlcNAc...) Potential

Glycosylation

816

1

N-linked (GlcNAc...) Potential

Glycosylation

823

1

N-linked (GlcNAc...) Potential

Glycosylation

828

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1 – 101

101

MLLRR…VKGKI → MMIISMWMSISRGLWDSSSI LSVLLILACMASITTSSSVS NAGYVDNGNMKV in isoform Type II.

VSP_002897

Experimental info

Mutagenesis

793

1

C → R in EGFR-ELP-1.

Mutagenesis

936

1

A → T in EGFR-ELP-B1 and EGFR-ELP-B1RB1.

Mutagenesis

1058

1

R → Q in EGFR-ELP-B1RB1.

Mutagenesis

1135

1

T → I in EGFR-2W74.

Mutagenesis

1156

1

G → S in EGFR-2C82.

Mutagenesis

1162

1

P → L in EGFR-1F26.

Mutagenesis

1166

1

S → L in EGFR-2L65.

Mutagenesis

1210 – 1216

7

DKFTRLP → EKVHPAA in EGFR-2X51.

Sequence conflict

137

1

K → E Ref.5

Sequence conflict

137

1

K → E Ref.6

Sequence conflict

329 – 331

3

AVS → GVC Ref.5

Sequence conflict

329 – 331

3

AVS → GVC Ref.6

Sequence conflict

458

1

R → L Ref.5

Sequence conflict

458

1

R → L Ref.6

Sequence conflict

789

1

R → C Ref.5

Sequence conflict

789

1

R → C Ref.6

Sequence conflict

959

1

P → A in CAA26157. Ref.8

Sequence conflict

995

1

E → V Ref.5

Sequence conflict

995

1

E → V Ref.6

Sequence conflict

1072 – 1080

9

QTPSLVKIT → RLLAGEDH Ref.3

Sequence conflict

1072 – 1080

9

QTPSLVKIT → RLLAGEDH Ref.4

Sequence conflict

1072 – 1080

9

QTPSLVKIT → RLLAGEDH Ref.9

Sequence conflict

1097 – 1098

2

AA → I in CAA05747. Ref.9

Sequence conflict

1118

1

T → R in CAA05747. Ref.9

Sequence conflict

1242

1

K → E Ref.5

Sequence conflict

1242

1

K → E Ref.6

Sequence conflict

1265

1

M → I Ref.5

Sequence conflict

1265

1

M → I Ref.6

Sequence conflict

1287

1

R → T Ref.5

Sequence conflict

1287

1

R → T Ref.6

Sequence conflict

1325

1

M → I in AAF46732. Ref.6

Sequence conflict

1383

1

G → V Ref.5

Sequence conflict

1383

1

G → V Ref.6

Sequence conflict

1412 – 1426

15

ELQPL…TETRV → SCSHASKPQHGDEGVGSSRV GAIANEEGESCQVPLEAMRY AFAGCYLR Ref.3

Sequence conflict

1412 – 1426

15

ELQPL…TETRV → SCSHASKPQHGDEGVGSSRV GAIANEEGESCQVPLEAMRY AFAGCYLR Ref.4

Secondary structure

1

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1426

Helix Strand Turn

Details...

Helix

115 – 126

12

Beta strand

136 – 141

6

Helix

149 – 151

3

Beta strand

161 – 166

6

Beta strand

169 – 172

4

Beta strand

194 – 200

7

Beta strand

204 – 207

4

Turn

230 – 232

3

Helix

235 – 237

3

Beta strand

281 – 285

5

Beta strand

305 – 308

4

Beta strand

320 – 326

7

Beta strand

331 – 334

4

Beta strand

338 – 342

5

Turn

343 – 346

4

Beta strand

347 – 350

4

Beta strand

361 – 365

5

Beta strand

377 – 380

4

Beta strand

385 – 387

3

Beta strand

392 – 394

3

Helix

414 – 417

4

Beta strand

421 – 423

3

Beta strand

427 – 429

3

Helix

431 – 434

4

Helix

455 – 463

9

Beta strand

471 – 473

3

Helix

484 – 486

3

Turn

499 – 502

4

Beta strand

504 – 509

6

Beta strand

528 – 531

4

Turn

539 – 541

3

Helix

544 – 547

4

Beta strand

555 – 561

7

Helix

563 – 567

5

Beta strand

591 – 597

7

Beta strand

602 – 605

4

Beta strand

616 – 618

3

Beta strand

628 – 630

3

Beta strand

638 – 640

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Type I [UniParc]. Last modified December 15, 1998. Version 3. Checksum: 4D424C3C99DA4AF4	FASTA	1,426	159,718
	10 20 30 40 50 60 MLLRRRNGPC PFPLLLLLLA HCICIWPASA ARDRYARQNN RQRHQDIDRD RDRDRFLYRS 70 80 90 100 110 120 SSAQNRQRGG ANFALGLGAN GVTIPTSLED KNKNEFVKGK ICIGTKSRLS VPSNKEHHYR 130 140 150 160 170 180 NLRDRYTNCT YVDGNLKLTW LPNENLDLSF LDNIREVTGY ILISHVDVKK VVFPKLQIIR 190 200 210 220 230 240 GRTLFSLSVE EEKYALFVTY SKMYTLEIPD LRDVLNGQVG FHNNYNLCHM RTIQWSEIVS 250 260 270 280 290 300 NGTDAYYNYD FTAPERECPK CHESCTHGCW GEGPKNCQKF SKLTCSPQCA GGRCYGPKPR 310 320 330 340 350 360 ECCHLFCAGG CTGPTQKDCI ACKNFFDEAV SKEECPPMRK YNPTTYVLET NPEGKYAYGA 370 380 390 400 410 420 TCVKECPGHL LRDNGACVRS CPQDKMDKGG ECVPCNGPCP KTCPGVTVLH AGNIDSFRNC 430 440 450 460 470 480 TVIDGNIRIL DQTFSGFQDV YANYTMGPRY IPLDPERREV FSTVKEITGY LNIEGTHPQF 490 500 510 520 530 540 RNLSYFRNLE TIHGRQLMES MFAALAIVKS SLYSLEMRNL KQISSGSVVI QHNRDLCYVS 550 560 570 580 590 600 NIRWPAIQKE PEQKVWVNEN LRADLCEKNG TICSDQCNED GCWGAGTDQC LTCKNFNFNG 610 620 630 640 650 660 TCIADCGYIS NAYKFDNRTC KICHPECRTC NGAGADHCQE CVHVRDGQHC VSECPKNKYN 670 680 690 700 710 720 DRGVCRECHA TCDGCTGPKD TIGIGACTTC NLAIINNDAT VKRCLLKDDK CPDGYFWEYV 730 740 750 760 770 780 HPQEQGSLKP LAGRAVCRKC HPLCELCTNY GYHEQVCSKC THYKRREQCE TECPADHYTD 790 800 810 820 830 840 EEQRECFQRH PECNGCTGPG ADDCKSCRNF KLFDANETGP YVNSTMFNCT SKCPLEMRHV 850 860 870 880 890 900 NYQYTAIGPY CAASPPRSSK ITANLDVNMI FIITGAVLVP TICILCVVTY ICRQKQKAKK 910 920 930 940 950 960 ETVKMTMALS GCEDSEPLRP SNIGANLCKL RIVKDAELRK GGVLGMGAFG RVYKGVWVPE 970 980 990 1000 1010 1020 GENVKIPVAI KELLKSTGAE SSEEFLREAY IMASEEHVNL LKLLAVCMSS QMMLITQLMP 1030 1040 1050 1060 1070 1080 LGCLLDYVRN NRDKIGSKAL LNWSTQIAKG MSYLEEKRLV HRDLAARNVL VQTPSLVKIT 1090 1100 1110 1120 1130 1140 DFGLAKLLSS DSNEYKAAGG KMPIKWLALE CIRNRVFTSK SDVWAFGVTI WELLTFGQRP 1150 1160 1170 1180 1190 1200 HENIPAKDIP DLIEVGLKLE QPEICSLDIY CTLLSCWHLD AAMRPTFKQL TTVFAEFARD 1210 1220 1230 1240 1250 1260 PGRYLAIPGD KFTRLPAYTS QDEKDLIRKL APTTDGSEAI AKPDDYLQPK AAPGPSHRTD 1270 1280 1290 1300 1310 1320 CTDEMPKLNR YCKDPSNKNS STGDDERDSS AREVGVGNLR LDLPVDEDDY LMPTCQPGPN 1330 1340 1350 1360 1370 1380 NNNNMNNPNQ NNMAAVGVAA GYMDLIGVPV SVDNPEYLLN AQTLGVGESP IPTQTIGIPV 1390 1400 1410 1420 MGGPGTMEVK VPMPGSEPTS SDHEYYNDTQ RELQPLHRNR NTETRV
	Isoform Type II [UniParc]. Checksum: AEA869BD7849A0D5	FASTA	1,377	153,700
	10 20 30 40 50 60 MMIISMWMSI SRGLWDSSSI LSVLLILACM ASITTSSSVS NAGYVDNGNM KVCIGTKSRL 70 80 90 100 110 120 SVPSNKEHHY RNLRDRYTNC TYVDGNLKLT WLPNENLDLS FLDNIREVTG YILISHVDVK 130 140 150 160 170 180 KVVFPKLQII RGRTLFSLSV EEEKYALFVT YSKMYTLEIP DLRDVLNGQV GFHNNYNLCH 190 200 210 220 230 240 MRTIQWSEIV SNGTDAYYNY DFTAPERECP KCHESCTHGC WGEGPKNCQK FSKLTCSPQC 250 260 270 280 290 300 AGGRCYGPKP RECCHLFCAG GCTGPTQKDC IACKNFFDEA VSKEECPPMR KYNPTTYVLE 310 320 330 340 350 360 TNPEGKYAYG ATCVKECPGH LLRDNGACVR SCPQDKMDKG GECVPCNGPC PKTCPGVTVL 370 380 390 400 410 420 HAGNIDSFRN CTVIDGNIRI LDQTFSGFQD VYANYTMGPR YIPLDPERRE VFSTVKEITG 430 440 450 460 470 480 YLNIEGTHPQ FRNLSYFRNL ETIHGRQLME SMFAALAIVK SSLYSLEMRN LKQISSGSVV 490 500 510 520 530 540 IQHNRDLCYV SNIRWPAIQK EPEQKVWVNE NLRADLCEKN GTICSDQCNE DGCWGAGTDQ 550 560 570 580 590 600 CLTCKNFNFN GTCIADCGYI SNAYKFDNRT CKICHPECRT CNGAGADHCQ ECVHVRDGQH 610 620 630 640 650 660 CVSECPKNKY NDRGVCRECH ATCDGCTGPK DTIGIGACTT CNLAIINNDA TVKRCLLKDD 670 680 690 700 710 720 KCPDGYFWEY VHPQEQGSLK PLAGRAVCRK CHPLCELCTN YGYHEQVCSK CTHYKRREQC 730 740 750 760 770 780 ETECPADHYT DEEQRECFQR HPECNGCTGP GADDCKSCRN FKLFDANETG PYVNSTMFNC 790 800 810 820 830 840 TSKCPLEMRH VNYQYTAIGP YCAASPPRSS KITANLDVNM IFIITGAVLV PTICILCVVT 850 860 870 880 890 900 YICRQKQKAK KETVKMTMAL SGCEDSEPLR PSNIGANLCK LRIVKDAELR KGGVLGMGAF 910 920 930 940 950 960 GRVYKGVWVP EGENVKIPVA IKELLKSTGA ESSEEFLREA YIMASEEHVN LLKLLAVCMS 970 980 990 1000 1010 1020 SQMMLITQLM PLGCLLDYVR NNRDKIGSKA LLNWSTQIAK GMSYLEEKRL VHRDLAARNV 1030 1040 1050 1060 1070 1080 LVQTPSLVKI TDFGLAKLLS SDSNEYKAAG GKMPIKWLAL ECIRNRVFTS KSDVWAFGVT 1090 1100 1110 1120 1130 1140 IWELLTFGQR PHENIPAKDI PDLIEVGLKL EQPEICSLDI YCTLLSCWHL DAAMRPTFKQ 1150 1160 1170 1180 1190 1200 LTTVFAEFAR DPGRYLAIPG DKFTRLPAYT SQDEKDLIRK LAPTTDGSEA IAKPDDYLQP 1210 1220 1230 1240 1250 1260 KAAPGPSHRT DCTDEMPKLN RYCKDPSNKN SSTGDDERDS SAREVGVGNL RLDLPVDEDD 1270 1280 1290 1300 1310 1320 YLMPTCQPGP NNNNNMNNPN QNNMAAVGVA AGYMDLIGVP VSVDNPEYLL NAQTLGVGES 1330 1340 1350 1360 1370 PIPTQTIGIP VMGGPGTMEV KVPMPGSEPT SSDHEYYNDT QRELQPLHRN RNTETRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular analysis of the Drosophila EGF receptor homolog reveals that several genetically defined classes of alleles cluster in subdomains of the receptor protein." Clifford R., Schuepbach T. Genetics 137:531-550(1994) [PubMed: 8070664] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS TYPE I AND TYPE II).
[2]	Clifford R., Schuepbach T. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"The Drosophila EGF receptor gene homolog: conservation of both hormone binding and kinase domains." Livneh E., Glazer L., Segal D., Schlessinger J., Shilo B.-Z. Cell 40:599-607(1985) [PubMed: 2982499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[4]	"Alternative 5' exons and tissue-specific expression of the Drosophila EGF receptor homolog transcripts." Schejter E.D., Segal D., Glazer L., Shilo B.-Z. Cell 46:1091-1101(1986) [PubMed: 3093080] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, ALTERNATIVE SPLICING. Strain: Oregon-R. Tissue: Embryo.
[5]	"Several levels of EGF receptor signaling during photoreceptor specification in wild-type, Ellipse, and null mutant Drosophila." Lesokhin A.M., Yu S.-Y., Katz J., Baker N.E. Dev. Biol. 205:129-144(1999) [PubMed: 9882502] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS TYPE I AND TYPE II), TISSUE SPECIFICITY, MUTANTS.
[6]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM TYPE I). Strain: Berkeley.
[7]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[8]	"A Drosophila genomic sequence with homology to human epidermal growth factor receptor." Wadsworth S.C., Vincent W.S. III, Bilodeau-Wentworth D. Nature 314:178-180(1985) [PubMed: 2983232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 959-1078. Strain: Daekwanryeong.
[9]	"Sampling the genomic pool of protein tyrosine kinase genes using the polymerase chain reaction with genomic DNA." Oates A.C., Wollberg P., Achen M.G., Wilks A.F. Biochem. Biophys. Res. Commun. 249:660-667(1998) [PubMed: 9731193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1069-1121. Tissue: Embryo.
[10]	"Interallelic complementation among DER/flb alleles: implications for the mechanism of signal transduction by receptor-tyrosine kinases." Raz E., Schejter E.D., Shilo B.Z. Genetics 129:191-201(1991) [PubMed: 1936959] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1133-1137; 1155-1167 AND 1209-1216, MUTANTS.
[11]	"There must be 50 ways to rule the signal: the case of the Drosophila EGF receptor." Perrimon N., Perkins L.A. Cell 89:13-16(1997) [PubMed: 9094709] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF052754, AF052753 Genomic DNA. Translation: AAC08536.1.
AF052754, AF052752 Genomic DNA. Translation: AAC08535.1.
K03054 Genomic DNA. Translation: AAA51462.1.
K03417 mRNA. Translation: AAA51460.1.
K03416 mRNA. Translation: AAA50965.1.
AF109077 Genomic DNA. Translation: AAD26134.1.
AF109078, AF109082 Genomic DNA. Translation: AAD26132.1.
AF109078, AF109084 Genomic DNA. Translation: AAD26133.1.
AF109079, AF109081 Genomic DNA. Translation: AAD26130.1.
AF109079, AF109083 Genomic DNA. Translation: AAD26131.1.
AF109080 Genomic DNA. Translation: AAD26135.1.
AE013599 Genomic DNA. Translation: AAF46732.1.
X02293 Genomic DNA. Translation: CAA26157.1.
AJ002912 Genomic DNA. Translation: CAA05747.1.
X78920 Genomic DNA. Translation: CAA55523.1.
X78918 Genomic DNA. Translation: CAA55521.1.
X78919 Genomic DNA. Translation: CAA55522.1.

PIR

GQFFE. A00640.

RefSeq

NP_476759.1. NM_057411.3.

UniGene

Dm.20748.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3I2T	X-ray	2.70	A	100-644	[»]
3LTF	X-ray	3.20	A/C	100-688	[»]
3LTG	X-ray	3.40	A/C	100-688	[»]

ProteinModelPortal

P04412.

SMR

P04412. Positions 98-838, 893-1249.

ModBase

Search...

Protein-protein interaction databases

IntAct

P04412. 3 interactions.

MINT

MINT-806082.

STRING

P04412.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

37455.

KEGG

dme:Dmel_CG10079.

Organism-specific databases

CTD

1956.

FlyBase

FBgn0003731. Egfr.

Phylogenomic databases

eggNOG

inNOG05958.

InParanoid

P04412.

OrthoDB

EOG4CRJDV.

Enzyme and pathway databases

BRENDA

2.7.10.1. 1994.

Gene expression databases

ArrayExpress

P04412.

Bgee

P04412.

GermOnline

CG10079. Drosophila melanogaster.

Family and domain databases

InterPro

IPR000494. EGF_rcpt_L.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]

KO

K04361.

Pfam

PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]

PRINTS

PR00109. TYRKINASE.

SMART

SM00261. FU. 7 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF57184. Grow_fac_recept. 3 hits.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

803734.

Entry information

Entry name

EGFR_DROME

Accession

Primary (citable) accession number: P04412
Secondary accession number(s): O18370 , O61601, P81868, Q9W2G0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	December 15, 1998
Last modified:	January 25, 2012
This is version 147 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project