ID   ECR_LUCCU               Reviewed;         757 AA.
AC   O18531;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   25-MAY-2022, entry version 110.
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;
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9304790; DOI=10.1016/s0965-1748(97)00019-2;
RA   Hannan G.N., Hill R.J.;
RT   "Cloning and characterization of LcEcR: a functional ecdysone receptor from
RT   the sheep blowfly Lucilia cuprina.";
RL   Insect Biochem. Mol. Biol. 27:479-488(1997).
RN   [2]
RP   SEQUENCE REVISION TO 695-731.
RA   Hannan G.N., Hill R.J.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for ecdysone. Binds to ecdysone response elements
CC       (ECRES) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U75355; AAB81130.2; -; mRNA.
DR   AlphaFoldDB; O18531; -.
DR   SMR; O18531; -.
DR   BindingDB; O18531; -.
DR   ChEMBL; CHEMBL1250403; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035100; F:ecdysone binding; IEA:InterPro.
DR   GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0035076; P:ecdysone receptor-mediated signaling pathway; IEA:InterPro.
DR   CDD; cd06938; NR_LBD_EcR; 1.
DR   Gene3D; 1.10.565.10; -; 1.
DR   Gene3D; 3.30.50.10; -; 1.
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   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Receptor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..757
FT                   /note="Ecdysone receptor"
FT                   /id="PRO_0000053529"
FT   DOMAIN          442..677
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        301..373
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         301..321
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         337..361
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..300
FT                   /note="Modulating"
FT                   /evidence="ECO:0000255"
FT   REGION          126..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          717..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..735
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  82581 MW;  9EFF1AD045063200 CRC64;
     MMKRRWSNNG GFAALKMLEE SSSEVTSSSN GLVLSSDINM SPSSLDSPVY GDQEMWLCND
     SASYNNSHQH SVITSLQGCT SSLPAQTTII PLSALPNSNN ASLNNQNQNY QNGNSMNTNL
     SVNTNNSVGG GGGGGGVPGM TSLNGLGGGG GSQVNNHNHS HNHLHHNSNS NHSNSSSHHT
     NGHMGIGGGG GGLSVNINGP NIVSNAQQLN SLQASQNGQV IHANIGIHSI ISNGLNHHHH
     HHMNNSSMMH HTPRSESANS ISSGRDDLSP SSSLNGFSTS DASDVKKIKK GPAPRLQEEL
     CLVCGDRASG YHYNALTCEG CKGFFRRSVT KNAVYCCKFG HACEMDMYMR RKCQECRLKK
     CLAVGMRPEC VVPENQCAMK RREKKAQKEK DKIQTSVCAT EIKKEILDLM TCEPPSHPTC
     PLLPEDILAK CQARNIPPLS YNQLAVIYKL IWYQDGYEQP SEEDLKRIMS SPDENESQHD
     ASFRHITEIT ILTVQLIVEF AKGLPAFTKI PQEDQITLLK ACSSEVMMLR MARRYDHNSD
     SIFFANNRSY TRDSYKMAGM ADNIEDLLHF CRQMYSMKVD NVEYALLTAI VIFSDRPGLE
     EAELVEAIQS YYIDTLRIYI LNRHCGDPMS LVFFAKLLSI LTELRTLGNQ NAEMCFSLKL
     KNRKLPKFLE EIWDVHAIPP SVQSHIQATQ AEKAAQEAQA TTSAISAAAT SSSSINTSMA
     TSSSSSLSPS AASTPNGGAV DYVGTDMSMS LVQSDNA