ECR_DROME
ID ECR_DROME Reviewed; 878 AA.
AC P34021; Q0E9N8; Q6AWL4; Q8SY10; Q95TS4; Q9V9K8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Ecdysone receptor;
DE AltName: Full=20-hydroxy-ecdysone receptor;
DE Short=20E receptor;
DE AltName: Full=EcRH;
DE AltName: Full=Ecdysteroid receptor;
DE AltName: Full=Nuclear receptor subfamily 1 group H member 1;
GN Name=EcR; Synonyms=NR1H1; ORFNames=CG1765;
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 [MRNA] (ISOFORM ECR-B1), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=1913820; DOI=10.1016/0092-8674(91)90572-g;
RA Koelle M.R., Talbot W.S., Segraves W.A., Bender M.T., Cherbas P.,
RA Hogness D.S.;
RT "The Drosophila EcR gene encodes an ecdysone receptor, a new member of the
RT steroid receptor superfamily.";
RL Cell 67:59-77(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ECR-A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ECR-B1).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ALTERNATIVE SPLICING.
RX PubMed=8324824; DOI=10.1016/0092-8674(93)90359-x;
RA Talbot W.S., Swyryd E.A., Hogness D.S.;
RT "Drosophila tissues with different metamorphic responses to ecdysone
RT express different ecdysone receptor isoforms.";
RL Cell 73:1323-1337(1993).
RN [7]
RP SUBUNIT.
RX PubMed=8247157; DOI=10.1038/366476a0;
RA Yao T.-P., Froman B.M., Jiang Z., Cherbas L., Chen J.-D., McKeown M.M.,
RA Cherbas P., Evans R.M.;
RT "Functional ecdysone receptor is the product of EcR and Ultraspiracle
RT genes.";
RL Nature 366:476-479(1993).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=8223281; DOI=10.1242/dev.118.2.613;
RA Huet F., Ruiz C., Richards G.;
RT "Puffs and PCR: the in vivo dynamics of early gene expression during
RT ecdysone responses in Drosophila.";
RL Development 118:613-627(1993).
RN [9]
RP INTERACTION WITH TRR.
RX PubMed=14603321; DOI=10.1038/nature02080;
RA Sedkov Y., Cho E., Petruk S., Cherbas L., Smith S.T., Jones R.S.,
RA Cherbas P., Canaani E., Jaynes J.B., Mazo A.;
RT "Methylation at lysine 4 of histone H3 in ecdysone-dependent development of
RT Drosophila.";
RL Nature 426:78-83(2003).
RN [10]
RP INTERACTION WITH NUP98.
RX PubMed=28366641; DOI=10.1016/j.molcel.2017.02.020;
RA Pascual-Garcia P., Debo B., Aleman J.R., Talamas J.A., Lan Y., Nguyen N.H.,
RA Won K.J., Capelson M.;
RT "Metazoan nuclear pores provide a scaffold for poised genes and mediate
RT induced enhancer-promoter contacts.";
RL Mol. Cell 66:63-76(2017).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=30293839; DOI=10.1016/j.devcel.2018.09.012;
RA Okamoto N., Viswanatha R., Bittar R., Li Z., Haga-Yamanaka S., Perrimon N.,
RA Yamanaka N.;
RT "A Membrane Transporter Is Required for Steroid Hormone Uptake in
RT Drosophila.";
RL Dev. Cell 47:294-305(2018).
CC -!- FUNCTION: Receptor for ecdysone (PubMed:1913820, PubMed:30293839).
CC Binds to ecdysone response elements (ECRES) following ecdysone-binding,
CC and recruitment of a complex containing the histone methyltransferase
CC trr, leads to activate transcription of target genes (PubMed:1913820,
CC PubMed:30293839). {ECO:0000269|PubMed:1913820,
CC ECO:0000269|PubMed:30293839}.
CC -!- SUBUNIT: Heterodimer of USP and ECR (PubMed:8247157). Only the
CC heterodimer is capable of high-affinity binding to ecdysone
CC (PubMed:8247157). Interacts with trr in an ecdysone-dependent manner
CC (PubMed:14603321). Upon ecdysone stimulation, interacts with Nup98
CC (PubMed:28366641). {ECO:0000269|PubMed:14603321,
CC ECO:0000269|PubMed:28366641, ECO:0000269|PubMed:8247157}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:1913820, ECO:0000269|PubMed:30293839}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=ECR-B1; Synonyms=B;
CC IsoId=P34021-1; Sequence=Displayed;
CC Name=ECR-A; Synonyms=A, D;
CC IsoId=P34021-2; Sequence=VSP_003661;
CC Name=ECR-B2; Synonyms=C;
CC IsoId=P34021-3; Sequence=VSP_003662;
CC -!- TISSUE SPECIFICITY: Isoform B1 predominates over isoform A in larval
CC tissues, imaginal histoblast nests and midgut islands. Isoform A
CC predominates over B1 in imaginal disks, and the larval prothoracic
CC gland. {ECO:0000269|PubMed:1913820}.
CC -!- DEVELOPMENTAL STAGE: In the salivary glands of mid instar larvae levels
CC increase during puff stage 1 at 86-94 hours of development then remain
CC relatively constant until the premetamorphic pulse of ecdysone in late
CC larvae. Levels diminish dramatically from puff stage 7 onwards. Levels
CC increase in the prepupal period during puff stage 13-14, the level
CC remains stable until stage 21. A decrease in levels at puff stage 7 is
CC also seen in the Malpighian tubules and less dramatically in the fat
CC body and gut. In the wing disk the relatively low level remains
CC unchanged. {ECO:0000269|PubMed:1913820, ECO:0000269|PubMed:8223281}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown blocks ecdysone-dependent
CC fat body cell migration into the pupal head.
CC {ECO:0000269|PubMed:30293839}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13804.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M74078; AAA28498.1; -; mRNA.
DR EMBL; S63761; AAB27496.2; -; mRNA.
DR EMBL; AE013599; AAF57278.3; -; Genomic_DNA.
DR EMBL; AE013599; AAF57280.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68347.1; -; Genomic_DNA.
DR EMBL; AY075461; AAL68274.1; -; mRNA.
DR EMBL; AY058575; AAL13804.1; ALT_INIT; mRNA.
DR EMBL; BT012469; AAS93740.1; -; mRNA.
DR EMBL; BT015234; AAT94463.1; -; mRNA.
DR PIR; A40709; A40709.
DR PIR; A41055; A41055.
DR RefSeq; NP_001163061.1; NM_001169590.2. [P34021-1]
DR RefSeq; NP_724456.1; NM_165461.3. [P34021-2]
DR RefSeq; NP_724457.1; NM_165462.2. [P34021-2]
DR RefSeq; NP_724458.1; NM_165463.2. [P34021-2]
DR RefSeq; NP_724459.1; NM_165464.3. [P34021-3]
DR RefSeq; NP_724460.1; NM_165465.3. [P34021-1]
DR PDB; 1R0N; X-ray; 2.60 A; B=256-364.
DR PDB; 1R0O; X-ray; 2.24 A; B=256-364.
DR PDB; 2HAN; X-ray; 1.95 A; B=256-365.
DR PDBsum; 1R0N; -.
DR PDBsum; 1R0O; -.
DR PDBsum; 2HAN; -.
DR AlphaFoldDB; P34021; -.
DR SMR; P34021; -.
DR BioGRID; 61444; 120.
DR DIP; DIP-158N; -.
DR IntAct; P34021; 38.
DR MINT; P34021; -.
DR STRING; 7227.FBpp0291631; -.
DR BindingDB; P34021; -.
DR ChEMBL; CHEMBL5676; -.
DR PaxDb; P34021; -.
DR PRIDE; P34021; -.
DR EnsemblMetazoa; FBtr0086008; FBpp0085349; FBgn0000546. [P34021-2]
DR EnsemblMetazoa; FBtr0086009; FBpp0085350; FBgn0000546. [P34021-2]
DR EnsemblMetazoa; FBtr0086010; FBpp0085351; FBgn0000546. [P34021-2]
DR EnsemblMetazoa; FBtr0086011; FBpp0085352; FBgn0000546. [P34021-1]
DR EnsemblMetazoa; FBtr0086012; FBpp0085353; FBgn0000546. [P34021-3]
DR EnsemblMetazoa; FBtr0302439; FBpp0291631; FBgn0000546. [P34021-1]
DR GeneID; 35540; -.
DR KEGG; dme:Dmel_CG1765; -.
DR CTD; 35540; -.
DR FlyBase; FBgn0000546; EcR.
DR VEuPathDB; VectorBase:FBgn0000546; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000173863; -.
DR InParanoid; P34021; -.
DR OMA; GMSLNTH; -.
DR PhylomeDB; P34021; -.
DR Reactome; R-DME-159418; Recycling of bile acids and salts.
DR Reactome; R-DME-196791; Vitamin D (calciferol) metabolism.
DR Reactome; R-DME-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-DME-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-DME-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-DME-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR SignaLink; P34021; -.
DR BioGRID-ORCS; 35540; 1 hit in 3 CRISPR screens.
DR EvolutionaryTrace; P34021; -.
DR GenomeRNAi; 35540; -.
DR PRO; PR:P34021; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0000546; Expressed in wing disc and 23 other tissues.
DR ExpressionAtlas; P34021; baseline and differential.
DR Genevisible; P34021; DM.
DR GO; GO:0008232; C:activator ecdysone receptor complex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0030425; C:dendrite; IMP:FlyBase.
DR GO; GO:0008230; C:ecdysone receptor holocomplex; IMP:CAFA.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
DR GO; GO:0008231; C:repressor ecdysone receptor complex; IPI:FlyBase.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IMP:CAFA.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0035100; F:ecdysone binding; IDA:FlyBase.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IMP:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0005102; F:signaling receptor binding; IPI:CAFA.
DR GO; GO:0005496; F:steroid binding; NAS:FlyBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:FlyBase.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:FlyBase.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:FlyBase.
DR GO; GO:0010002; P:cardioblast differentiation; IMP:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IMP:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0040003; P:chitin-based cuticle development; IMP:FlyBase.
DR GO; GO:0008362; P:chitin-based embryonic cuticle biosynthetic process; IMP:FlyBase.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; NAS:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0035053; P:dorsal vessel heart proper cell fate commitment; IMP:FlyBase.
DR GO; GO:0018990; P:ecdysis, chitin-based cuticle; IMP:FlyBase.
DR GO; GO:0035076; P:ecdysone receptor-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0035072; P:ecdysone-mediated induction of salivary gland cell autophagic cell death; NAS:FlyBase.
DR GO; GO:0008544; P:epidermis development; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:0007390; P:germ-band shortening; IMP:FlyBase.
DR GO; GO:0035188; P:hatching; IMP:FlyBase.
DR GO; GO:0008258; P:head involution; IMP:FlyBase.
DR GO; GO:0007488; P:histoblast morphogenesis; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0035193; P:larval central nervous system remodeling; IMP:FlyBase.
DR GO; GO:0002164; P:larval development; IMP:UniProtKB.
DR GO; GO:0035180; P:larval wandering behavior; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0007443; P:Malpighian tubule morphogenesis; IMP:FlyBase.
DR GO; GO:0007552; P:metamorphosis; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:FlyBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
DR GO; GO:1904801; P:positive regulation of neuron remodeling; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0035073; P:pupariation; IMP:FlyBase.
DR GO; GO:0010506; P:regulation of autophagy; IMP:FlyBase.
DR GO; GO:0043457; P:regulation of cellular respiration; IMP:FlyBase.
DR GO; GO:0040034; P:regulation of development, heterochronic; TAS:FlyBase.
DR GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0035297; P:regulation of Malpighian tubule diameter; IMP:FlyBase.
DR GO; GO:1904799; P:regulation of neuron remodeling; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0042220; P:response to cocaine; IGI:FlyBase.
DR GO; GO:0035075; P:response to ecdysone; IMP:FlyBase.
DR GO; GO:0035071; P:salivary gland cell autophagic cell death; IMP:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR CDD; cd06938; NR_LBD_EcR; 1.
DR DisProt; DP01569; -. [P34021-2]
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID50251; -.
DR InterPro; IPR003069; Ecdystd_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR041889; NR_LBD_EcR.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR01283; ECDYSTEROIDR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Receptor; Reference proteome; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..878
FT /note="Ecdysone receptor"
FT /id="PRO_0000053524"
FT DOMAIN 419..654
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 264..336
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 264..284
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 300..324
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..263
FT /note="Modulating"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..226
FT /note="MKRRWSNNGGFMRLPEESSSEVTSSSNGLVLPSGVNMSPSSLDSHDYCDQDL
FT WLCGNESGSFGGSNGHGLSQQQQSVITLAMHGCSSTLPAQTTIIPINGNANGNGGSTNG
FT QYVPGATNLGALANGMLNGGFNGMQQQIQNGHGLINSTTPSTPTTPLHLQQNLGGAGGG
FT GIGGMGILHHANGTPNGLIGVVGGGGGVGLGVGGGGVGGLGMQHTPRSDSVNSISS ->
FT MLTTSGQQQSKQKLSTLPSHILLQQQLAASAGPSSSVSLSPSSSAALTLHVASANGGAR
FT ETTSAAAVKDKLRPTPTAIKIEPMPDVISVGTVAGGSSVATVVAPAATTTSNKPNSTAA
FT PSTSAAAANGHLVLVPNKRPRLDVTEDWMSTPSPGSVPSSAPPLSPSPGSQNHSYNMSN
FT GYASPMSAGSYDPYSPTGKT (in isoform ECR-A)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_003661"
FT VAR_SEQ 1..226
FT /note="MKRRWSNNGGFMRLPEESSSEVTSSSNGLVLPSGVNMSPSSLDSHDYCDQDL
FT WLCGNESGSFGGSNGHGLSQQQQSVITLAMHGCSSTLPAQTTIIPINGNANGNGGSTNG
FT QYVPGATNLGALANGMLNGGFNGMQQQIQNGHGLINSTTPSTPTTPLHLQQNLGGAGGG
FT GIGGMGILHHANGTPNGLIGVVGGGGGVGLGVGGGGVGGLGMQHTPRSDSVNSISS ->
FT MDTCGLVAELAHYIDAY (in isoform ECR-B2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003662"
FT CONFLICT 867..878
FT /note="GVAVKSEHSTTA -> EWRLSRSTRRLHSRRRVSSTNITTTTSTSCWSRKRS
FT (in Ref. 4; AAL68274)"
FT /evidence="ECO:0000305"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:2HAN"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:1R0N"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:2HAN"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:2HAN"
FT HELIX 282..293
FT /evidence="ECO:0007829|PDB:2HAN"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:2HAN"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:2HAN"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:2HAN"
FT HELIX 339..343
FT /evidence="ECO:0007829|PDB:2HAN"
SQ SEQUENCE 878 AA; 93853 MW; B48D610D722F014F CRC64;
MKRRWSNNGG FMRLPEESSS EVTSSSNGLV LPSGVNMSPS SLDSHDYCDQ DLWLCGNESG
SFGGSNGHGL SQQQQSVITL AMHGCSSTLP AQTTIIPING NANGNGGSTN GQYVPGATNL
GALANGMLNG GFNGMQQQIQ NGHGLINSTT PSTPTTPLHL QQNLGGAGGG GIGGMGILHH
ANGTPNGLIG VVGGGGGVGL GVGGGGVGGL GMQHTPRSDS VNSISSGRDD LSPSSSLNGY
SANESCDAKK SKKGPAPRVQ EELCLVCGDR ASGYHYNALT CEGCKGFFRR SVTKSAVYCC
KFGRACEMDM YMRRKCQECR LKKCLAVGMR PECVVPENQC AMKRREKKAQ KEKDKMTTSP
SSQHGGNGSL ASGGGQDFVK KEILDLMTCE PPQHATIPLL PDEILAKCQA RNIPSLTYNQ
LAVIYKLIWY QDGYEQPSEE DLRRIMSQPD ENESQTDVSF RHITEITILT VQLIVEFAKG
LPAFTKIPQE DQITLLKACS SEVMMLRMAR RYDHSSDSIF FANNRSYTRD SYKMAGMADN
IEDLLHFCRQ MFSMKVDNVE YALLTAIVIF SDRPGLEKAQ LVEAIQSYYI DTLRIYILNR
HCGDSMSLVF YAKLLSILTE LRTLGNQNAE MCFSLKLKNR KLPKFLEEIW DVHAIPPSVQ
SHLQITQEEN ERLERAERMR ASVGGAITAG IDCDSASTSA AAAAAQHQPQ PQPQPQPSSL
TQNDSQHQTQ PQLQPQLPPQ LQGQLQPQLQ PQLQTQLQPQ IQPQPQLLPV SAPVPASVTA
PGSLSAVSTS SEYMGGSAAI GPITPATTSS ITAAVTASST TSAVPMGNGV GVGVGVGGNV
SMYANAQTAM ALMGVALHSH QEQLIGGVAV KSEHSTTA
