ECR_HELVI
ID ECR_HELVI Reviewed; 576 AA.
AC O18473;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=HvEcR;
DE AltName: Full=Nuclear receptor subfamily 1 group H member 1;
GN Name=EcR; Synonyms=NR1H1;
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BRC;
RX PubMed=10528411; DOI=10.1016/s0965-1748(99)00067-3;
RA Martinez A., Scanlon D., Gross B., Perara S.C., Palli S.R., Greenland A.J.,
RA Windass J., Pongs O., Broad P., Jepson I.;
RT "Transcriptional activation of the cloned Heliothis virescens (Lepidoptera)
RT ecdysone receptor (HvEcR) by muristeroneA.";
RL Insect Biochem. Mol. Biol. 29:915-930(1999).
CC -!- FUNCTION: Receptor for ecdysone. Binds to ecdysone response elements
CC (ECRES) (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O18473; Q7SIF6; NbExp=2; IntAct=EBI-1037411, EBI-1037399;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; Y09009; CAA70212.1; -; mRNA.
DR PDB; 1R1K; X-ray; 2.90 A; D=305-550.
DR PDB; 1R20; X-ray; 3.00 A; D=306-550.
DR PDB; 2R40; X-ray; 2.40 A; D=305-550.
DR PDB; 4UMM; EM; 11.60 A; E=157-243, G=305-550.
DR PDB; 7BJU; X-ray; 2.85 A; D=298-550.
DR PDB; 7BJV; X-ray; 3.05 A; D/E/F=298-550.
DR PDBsum; 1R1K; -.
DR PDBsum; 1R20; -.
DR PDBsum; 2R40; -.
DR PDBsum; 4UMM; -.
DR PDBsum; 7BJU; -.
DR PDBsum; 7BJV; -.
DR AlphaFoldDB; O18473; -.
DR SMR; O18473; -.
DR IntAct; O18473; 1.
DR BindingDB; O18473; -.
DR ChEMBL; CHEMBL2366582; -.
DR PRIDE; O18473; -.
DR EvolutionaryTrace; O18473; -.
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 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Metal-binding; Nucleus; Receptor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..576
FT /note="Ecdysone receptor"
FT /id="PRO_0000053528"
FT DOMAIN 314..548
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 163..235
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 163..183
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 199..223
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..162
FT /note="Modulating"
FT /evidence="ECO:0000255"
FT REGION 87..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 313..328
FT /evidence="ECO:0007829|PDB:2R40"
FT HELIX 334..341
FT /evidence="ECO:0007829|PDB:2R40"
FT HELIX 352..374
FT /evidence="ECO:0007829|PDB:2R40"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:2R40"
FT HELIX 383..403
FT /evidence="ECO:0007829|PDB:2R40"
FT TURN 408..411
FT /evidence="ECO:0007829|PDB:2R40"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2R40"
FT TURN 418..421
FT /evidence="ECO:0007829|PDB:7BJU"
FT HELIX 423..428
FT /evidence="ECO:0007829|PDB:2R40"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:1R1K"
FT HELIX 432..446
FT /evidence="ECO:0007829|PDB:2R40"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:2R40"
FT HELIX 452..463
FT /evidence="ECO:0007829|PDB:2R40"
FT HELIX 473..494
FT /evidence="ECO:0007829|PDB:2R40"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:2R40"
FT HELIX 501..531
FT /evidence="ECO:0007829|PDB:2R40"
FT HELIX 538..543
FT /evidence="ECO:0007829|PDB:2R40"
SQ SEQUENCE 576 AA; 64638 MW; D13EF7877BF263A8 CRC64;
MSLGARGYRR CDTLADMRRR WYNNGPFQTL RMLEESSSEV TSSSALGLPP AMVMSPESLA
SPEIGGLELW GYDDGITYSM AQSLGTCTME QQQPQPQQQP QQTQPLPSMP LPMPPTTPKS
ENESMSSGRE ELSPASSVNG CSTDGEARRQ KKGPAPRQQE ELCLVCGDRA SGYHYNALTC
EGCKGFFRRS VTKNAVYICK FGHACEMDIY MRRKCQECRL KKCLAVGMRP ECVVPENQCA
MKRKEKKAQR EKDKLPVSTT TVDDHMPPIM QCDPPPPEAA RILECVQHEV VPRFLNEKLM
EQNRLKNVPP LTANQKSLIA RLVWYQEGYE QPSEEDLKRV TQSDEDDEDS DMPFRQITEM
TILTVQLIVE FAKGLPGFAK ISQSDQITLL KACSSEVMML RVARRYDAAT DSVLFANNQA
YTRDNYRKAG MAYVIEDLLH FCRCMYSMMM DNVHYALLTA IVIFSDRPGL EQPLLVEEIQ
RYYLNTLRVY ILNQNSASPR GAVIFGEILG ILTEIRTLGM QNSNMCISLK LKNRKLPPFL
EEIWDVADVA TTATPVAAEA PAPLAPAPPA RPPATV
