P34021 (ECR_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ecdysone receptor

Alternative name(s):
20-hydroxy-ecdysone receptor
Short name=20E receptor
EcRH
Ecdysteroid receptor
Nuclear receptor subfamily 1 group H member 1

Gene names

Name:	EcR
Synonyms:	NR1H1
ORF Names:	CG1765

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	878 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for ecdysone. Binds to ecdysone response elements (ECRES) following ecdysone-binding, and recruitment of a complex containing the histone methyltransferase trr, leads to activate transcription of target genes. Ref.1
Subunit structure	Heterodimer of USP and ECR. Only the heterodimer is capable of high-affinity binding to ecdysone. Interacts with trr in an ecdysone-dependent manner. Ref.7 Ref.9
Subcellular location	Nucleus Ref.1.
Tissue specificity	Isoform B1 predominates over isoform A in larval tissues, imaginal histoblast nests and midgut islands. Isoform A predominates over B1 in imaginal disks, and the larval prothoracic gland. Ref.1
Developmental stage	In the salivary glands of mid instar larvae levels increase during puff stage 1 at 86-94 hours of development then remain relatively constant until the premetamorphic pulse of ecdysone in late larvae. Levels diminish dramatically from puff stage 7 onwards. Levels increase in the prepupal period during puff stage 13-14, the level remains stable until stage 21. A decrease in levels at puff stage 7 is also seen in the Malpighian tubules and less dramatically in the fat body and gut. In the wing disk the relatively low level remains unchanged. Ref.1 Ref.8
Sequence similarities	Belongs to the nuclear hormone receptor family. NR1 subfamily. Contains 1 nuclear receptor DNA-binding domain.
Sequence caution	The sequence AAL13804.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Receptor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	autophagy Inferred from mutant phenotype. Source: FlyBase axonogenesis Inferred from mutant phenotype. Source: FlyBase border follicle cell migration Inferred from mutant phenotype. Source: FlyBase cardiac muscle tissue development Inferred from mutant phenotype. Source: FlyBase cardioblast differentiation Inferred from mutant phenotype. Source: FlyBase cell adhesion Inferred from mutant phenotype. Source: FlyBase chitin-based embryonic cuticle biosynthetic process Inferred from mutant phenotype. Source: FlyBase dendrite morphogenesis Inferred from mutant phenotype. Source: FlyBase determination of adult lifespan Inferred from mutant phenotype. Source: FlyBase dorsal vessel heart proper cell fate commitment Inferred from mutant phenotype. Source: FlyBase ecdysis, chitin-based cuticle Inferred from mutant phenotype. Source: FlyBase ecdysone-mediated induction of salivary gland cell autophagic cell death Non-traceable author statement. Source: FlyBase epidermis development Inferred from mutant phenotype. Source: FlyBase germ-band shortening Inferred from mutant phenotype. Source: FlyBase hatching Inferred from mutant phenotype. Source: FlyBase head involution Inferred from mutant phenotype. Source: FlyBase histoblast morphogenesis Inferred from mutant phenotype. Source: FlyBase imaginal disc eversion Traceable author statement. Source: FlyBase imaginal disc-derived wing morphogenesis Inferred from mutant phenotype. Source: FlyBase larval central nervous system remodeling Inferred from mutant phenotype. Source: FlyBase larval wandering behavior Inferred from mutant phenotype. Source: FlyBase long-term memory Inferred from mutant phenotype. Source: FlyBase muscle organ development Inferred from mutant phenotype. Source: FlyBase mushroom body development Inferred from genetic interaction. Source: FlyBase negative regulation of growth of symbiont in host Inferred from mutant phenotype. Source: FlyBase negative regulation of transcription, DNA-dependent Traceable author statement. Source: FlyBase neuron remodeling Inferred from mutant phenotype. Source: FlyBase peripheral nervous system development Inferred from mutant phenotype. Source: FlyBase positive regulation of apoptotic process Inferred from mutant phenotype. Source: FlyBase positive regulation of circadian sleep/wake cycle, sleep Inferred from mutant phenotype. Source: FlyBase pupariation Inferred from mutant phenotype. Source: FlyBase regulation of Malpighian tubule diameter Inferred from mutant phenotype. Source: FlyBase regulation of development, heterochronic Traceable author statement. Source: FlyBase regulation of rhodopsin gene expression Inferred from mutant phenotype. Source: FlyBase regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: FlyBase response to cocaine Inferred from genetic interaction. Source: FlyBase sperm individualization Inferred from mutant phenotype. Source: FlyBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: FlyBase dendrite Inferred from mutant phenotype. Source: FlyBase polytene chromosome Non-traceable author statement. Source: FlyBase repressor ecdysone receptor complex Inferred from physical interaction. Source: FlyBase
Molecular function	ecdysteroid hormone receptor activity Inferred from direct assay Ref.6. Source: FlyBase protein heterodimerization activity Inferred from direct assay. Source: FlyBase repressing transcription factor binding Inferred from physical interaction. Source: FlyBase sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro steroid binding Non-traceable author statement. Source: FlyBase zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform ECR-B1 (identifier: P34021-1)

Also known as: B;

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 ECR-A (identifier: P34021-2)

Also known as: A; D;

The sequence of this isoform differs from the canonical sequence as follows:
     1-226: MKRRWSNNGG...RSDSVNSISS → MLTTSGQQQS...YDPYSPTGKT

Isoform ECR-B2 (identifier: P34021-3)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-226: MKRRWSNNGG...RSDSVNSISS → MDTCGLVAELAHYIDAY

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 878

878

Ecdysone receptor

PRO_0000053524

Regions

DNA binding

264 – 336

73

Nuclear receptor

Zinc finger

264 – 284

21

NR C4-type

Zinc finger

300 – 324

25

NR C4-type

Region

1 – 263

263

Modulating

Region

431 – 651

221

Hormone-binding

Compositional bias

165 – 211

47

Gly-rich

Compositional bias

193 – 197

5

Poly-Gly

Compositional bias

700 – 705

6

Poly-Ala

Compositional bias

706 – 781

76

Gln/Pro-rich

Natural variations

Alternative sequence

1 – 226

226

MKRRW…NSISS → MLTTSGQQQSKQKLSTLPSH ILLQQQLAASAGPSSSVSLS PSSSAALTLHVASANGGARE TTSAAAVKDKLRPTPTAIKI EPMPDVISVGTVAGGSSVAT VVAPAATTTSNKPNSTAAPS TSAAAANGHLVLVPNKRPRL DVTEDWMSTPSPGSVPSSAP PLSPSPGSQNHSYNMSNGYA SPMSAGSYDPYSPTGKT in isoform ECR-A.

VSP_003661

Alternative sequence

1 – 226

226

MKRRW…NSISS → MDTCGLVAELAHYIDAY in isoform ECR-B2.

VSP_003662

Experimental info

Sequence conflict

867 – 878

12

GVAVK…HSTTA → EWRLSRSTRRLHSRRRVSST NITTTTSTSCWSRKRS in AAL68274. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

878

Helix Strand Turn

Details...

Turn

265 – 267

3

Beta strand

273 – 280

8

Helix

282 – 293

12

Helix

312 – 315

4

Helix

317 – 326

10

Helix

331 – 333

3

Helix

339 – 343

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform ECR-B1 (B) [UniParc]. Last modified February 1, 1994. Version 1. Checksum: B48D610D722F014F	FASTA	878	93,853
	10 20 30 40 50 60 MKRRWSNNGG FMRLPEESSS EVTSSSNGLV LPSGVNMSPS SLDSHDYCDQ DLWLCGNESG 70 80 90 100 110 120 SFGGSNGHGL SQQQQSVITL AMHGCSSTLP AQTTIIPING NANGNGGSTN GQYVPGATNL 130 140 150 160 170 180 GALANGMLNG GFNGMQQQIQ NGHGLINSTT PSTPTTPLHL QQNLGGAGGG GIGGMGILHH 190 200 210 220 230 240 ANGTPNGLIG VVGGGGGVGL GVGGGGVGGL GMQHTPRSDS VNSISSGRDD LSPSSSLNGY 250 260 270 280 290 300 SANESCDAKK SKKGPAPRVQ EELCLVCGDR ASGYHYNALT CEGCKGFFRR SVTKSAVYCC 310 320 330 340 350 360 KFGRACEMDM YMRRKCQECR LKKCLAVGMR PECVVPENQC AMKRREKKAQ KEKDKMTTSP 370 380 390 400 410 420 SSQHGGNGSL ASGGGQDFVK KEILDLMTCE PPQHATIPLL PDEILAKCQA RNIPSLTYNQ 430 440 450 460 470 480 LAVIYKLIWY QDGYEQPSEE DLRRIMSQPD ENESQTDVSF RHITEITILT VQLIVEFAKG 490 500 510 520 530 540 LPAFTKIPQE DQITLLKACS SEVMMLRMAR RYDHSSDSIF FANNRSYTRD SYKMAGMADN 550 560 570 580 590 600 IEDLLHFCRQ MFSMKVDNVE YALLTAIVIF SDRPGLEKAQ LVEAIQSYYI DTLRIYILNR 610 620 630 640 650 660 HCGDSMSLVF YAKLLSILTE LRTLGNQNAE MCFSLKLKNR KLPKFLEEIW DVHAIPPSVQ 670 680 690 700 710 720 SHLQITQEEN ERLERAERMR ASVGGAITAG IDCDSASTSA AAAAAQHQPQ PQPQPQPSSL 730 740 750 760 770 780 TQNDSQHQTQ PQLQPQLPPQ LQGQLQPQLQ PQLQTQLQPQ IQPQPQLLPV SAPVPASVTA 790 800 810 820 830 840 PGSLSAVSTS SEYMGGSAAI GPITPATTSS ITAAVTASST TSAVPMGNGV GVGVGVGGNV 850 860 870 SMYANAQTAM ALMGVALHSH QEQLIGGVAV KSEHSTTA
	Isoform ECR-A (A) (D) [UniParc]. Checksum: E93D93A38236AD58	FASTA	849	91,182
	10 20 30 40 50 60 MLTTSGQQQS KQKLSTLPSH ILLQQQLAAS AGPSSSVSLS PSSSAALTLH VASANGGARE 70 80 90 100 110 120 TTSAAAVKDK LRPTPTAIKI EPMPDVISVG TVAGGSSVAT VVAPAATTTS NKPNSTAAPS 130 140 150 160 170 180 TSAAAANGHL VLVPNKRPRL DVTEDWMSTP SPGSVPSSAP PLSPSPGSQN HSYNMSNGYA 190 200 210 220 230 240 SPMSAGSYDP YSPTGKTGRD DLSPSSSLNG YSANESCDAK KSKKGPAPRV QEELCLVCGD 250 260 270 280 290 300 RASGYHYNAL TCEGCKGFFR RSVTKSAVYC CKFGRACEMD MYMRRKCQEC RLKKCLAVGM 310 320 330 340 350 360 RPECVVPENQ CAMKRREKKA QKEKDKMTTS PSSQHGGNGS LASGGGQDFV KKEILDLMTC 370 380 390 400 410 420 EPPQHATIPL LPDEILAKCQ ARNIPSLTYN QLAVIYKLIW YQDGYEQPSE EDLRRIMSQP 430 440 450 460 470 480 DENESQTDVS FRHITEITIL TVQLIVEFAK GLPAFTKIPQ EDQITLLKAC SSEVMMLRMA 490 500 510 520 530 540 RRYDHSSDSI FFANNRSYTR DSYKMAGMAD NIEDLLHFCR QMFSMKVDNV EYALLTAIVI 550 560 570 580 590 600 FSDRPGLEKA QLVEAIQSYY IDTLRIYILN RHCGDSMSLV FYAKLLSILT ELRTLGNQNA 610 620 630 640 650 660 EMCFSLKLKN RKLPKFLEEI WDVHAIPPSV QSHLQITQEE NERLERAERM RASVGGAITA 670 680 690 700 710 720 GIDCDSASTS AAAAAAQHQP QPQPQPQPSS LTQNDSQHQT QPQLQPQLPP QLQGQLQPQL 730 740 750 760 770 780 QPQLQTQLQP QIQPQPQLLP VSAPVPASVT APGSLSAVST SSEYMGGSAA IGPITPATTS 790 800 810 820 830 840 SITAAVTASS TTSAVPMGNG VGVGVGVGGN VSMYANAQTA MALMGVALHS HQEQLIGGVA VKSEHSTTA
	Isoform ECR-B2 (C) [UniParc]. Checksum: A9DE3D365161A34E	FASTA	669	73,348
	10 20 30 40 50 60 MDTCGLVAEL AHYIDAYGRD DLSPSSSLNG YSANESCDAK KSKKGPAPRV QEELCLVCGD 70 80 90 100 110 120 RASGYHYNAL TCEGCKGFFR RSVTKSAVYC CKFGRACEMD MYMRRKCQEC RLKKCLAVGM 130 140 150 160 170 180 RPECVVPENQ CAMKRREKKA QKEKDKMTTS PSSQHGGNGS LASGGGQDFV KKEILDLMTC 190 200 210 220 230 240 EPPQHATIPL LPDEILAKCQ ARNIPSLTYN QLAVIYKLIW YQDGYEQPSE EDLRRIMSQP 250 260 270 280 290 300 DENESQTDVS FRHITEITIL TVQLIVEFAK GLPAFTKIPQ EDQITLLKAC SSEVMMLRMA 310 320 330 340 350 360 RRYDHSSDSI FFANNRSYTR DSYKMAGMAD NIEDLLHFCR QMFSMKVDNV EYALLTAIVI 370 380 390 400 410 420 FSDRPGLEKA QLVEAIQSYY IDTLRIYILN RHCGDSMSLV FYAKLLSILT ELRTLGNQNA 430 440 450 460 470 480 EMCFSLKLKN RKLPKFLEEI WDVHAIPPSV QSHLQITQEE NERLERAERM RASVGGAITA 490 500 510 520 530 540 GIDCDSASTS AAAAAAQHQP QPQPQPQPSS LTQNDSQHQT QPQLQPQLPP QLQGQLQPQL 550 560 570 580 590 600 QPQLQTQLQP QIQPQPQLLP VSAPVPASVT APGSLSAVST SSEYMGGSAA IGPITPATTS 610 620 630 640 650 660 SITAAVTASS TTSAVPMGNG VGVGVGVGGN VSMYANAQTA MALMGVALHS HQEQLIGGVA VKSEHSTTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Drosophila EcR gene encodes an ecdysone receptor, a new member of the steroid receptor superfamily." Koelle M.R., Talbot W.S., Segraves W.A., Bender M.T., Cherbas P., Hogness D.S. Cell 67:59-77(1991) [PubMed: 1913820] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ECR-B1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]	"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]. Strain: Berkeley.
[3]	"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, ALTERNATIVE SPLICING. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ECR-A). Strain: Berkeley. Tissue: Embryo.
[5]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ECR-B1). Strain: Berkeley. Tissue: Embryo.
[6]	"Drosophila tissues with different metamorphic responses to ecdysone express different ecdysone receptor isoforms." Talbot W.S., Swyryd E.A., Hogness D.S. Cell 73:1323-1337(1993) [PubMed: 8324824] [Abstract] Cited for: ALTERNATIVE SPLICING.
[7]	"Functional ecdysone receptor is the product of EcR and Ultraspiracle genes." Yao T.-P., Froman B.M., Jiang Z., Cherbas L., Chen J.-D., McKeown M.M., Cherbas P., Evans R.M. Nature 366:476-479(1993) [PubMed: 8247157] [Abstract] Cited for: SUBUNIT.
[8]	"Puffs and PCR: the in vivo dynamics of early gene expression during ecdysone responses in Drosophila." Huet F., Ruiz C., Richards G. Development 118:613-627(1993) [PubMed: 8223281] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[9]	"Methylation at lysine 4 of histone H3 in ecdysone-dependent development of Drosophila." Sedkov Y., Cho E., Petruk S., Cherbas L., Smith S.T., Jones R.S., Cherbas P., Canaani E., Jaynes J.B., Mazo A. Nature 426:78-83(2003) [PubMed: 14603321] [Abstract] Cited for: INTERACTION WITH TRR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M74078 mRNA. Translation: AAA28498.1.
S63761 mRNA. Translation: AAB27496.2.
AE013599 Genomic DNA. Translation: AAF57278.3.
AE013599 Genomic DNA. Translation: AAF57280.2.
AE013599 Genomic DNA. Translation: AAM68347.1.
AY075461 mRNA. Translation: AAL68274.1.
AY058575 mRNA. Translation: AAL13804.1. Different initiation.
BT012469 mRNA. Translation: AAS93740.1.
BT015234 mRNA. Translation: AAT94463.1.

PIR

A40709.
A41055.

RefSeq

NP_001163061.1. NM_001169590.1.
NP_724456.1. NM_165461.2.
NP_724457.1. NM_165462.2.
NP_724458.1. NM_165463.2.
NP_724459.1. NM_165464.2.
NP_724460.1. NM_165465.2.

UniGene

Dm.4159.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R0N	X-ray	2.60	B	256-364	[»]
1R0O	X-ray	2.24	B	256-364	[»]
2HAN	X-ray	1.95	B	256-365	[»]

ProteinModelPortal

P34021.

SMR

P34021. Positions 258-652.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-158N.

IntAct

P34021. 30 interactions.

MINT

MINT-294442.

STRING

P34021.

Proteomic databases

PRIDE

P34021.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0086011; FBpp0085352; FBgn0000546.
FBtr0302439; FBpp0291631; FBgn0000546.

GeneID

35540.

KEGG

dme:Dmel_CG1765.

Organism-specific databases

CTD

35540.

FlyBase

FBgn0000546. EcR.

Phylogenomic databases

eggNOG

inNOG06886.

GeneTree

EMGT00070000025663.

InParanoid

P34021.

OMA

MALMGVP.

OrthoDB

EOG431ZD7.

PhylomeDB

P34021.

Gene expression databases

Bgee

P34021.

GermOnline

CG1765. Drosophila melanogaster.

Family and domain databases

InterPro

IPR003069. Ecdystd_rcpt.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]

Gene3D

G3DSA:1.10.565.10. Nucl_hrmn_rcpt_lig_bd. 2 hits.
G3DSA:3.30.50.10. Znf_NHR/GATA. 1 hit.

KO

K14034.

Pfam

PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR01283. ECDYSTEROIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

793933.

Entry information

Entry name

ECR_DROME

Accession

Primary (citable) accession number: P34021
Secondary accession number(s): Q0E9N8 , Q6AWL4, Q8SY10, Q95TS4, Q9V9K8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	January 25, 2012
This is version 140 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project