ID   ECR_MANSE               Reviewed;         556 AA.
AC   P49883;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 112.
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   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7633469; DOI=10.1016/0965-1748(95)00023-o;
RA   Fujiwara H., Jindra M., Newitt R., Palli S.R., Hiruma K., Riddiford L.M.;
RT   "Cloning of an ecdysone receptor homolog from Manduca sexta and the
RT   developmental profile of its mRNA in wings.";
RL   Insect Biochem. Mol. Biol. 25:845-856(1995).
CC   -!- FUNCTION: Receptor for ecdysone. Binds to ecdysone response elements
CC       (ECRES).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: It is found in both larval wing disks and pupal
CC       wings and in prothoracic glands.
CC   -!- DEVELOPMENTAL STAGE: In the wing disks levels increase on day 2 fifth
CC       larval instar reaching a maximum on day 5, and then decrease sharply on
CC       day 6. In the prothoracic glands levels increase sharply on day 2 then
CC       remain high throughout the larval-pupal transformation and after pupal
CC       ecdysis.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U19812; AAA86699.1; -; mRNA.
DR   AlphaFoldDB; P49883; -.
DR   SMR; P49883; -.
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..556
FT                   /note="Ecdysone receptor"
FT                   /id="PRO_0000053530"
FT   DOMAIN          293..531
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        147..219
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         147..167
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         183..207
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..146
FT                   /note="Modulating"
FT                   /evidence="ECO:0000255"
FT   REGION          72..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   556 AA;  62830 MW;  9AF83AA33D551EB1 CRC64;
     MRRRWSNNGC FPLRMFEESS SEVTSSSAFG MPAAMVMSPE SLASPEYGGL ELWSYDETMT
     NYPAQSLLGA CNAPQQQQQQ QQQQPSAQPL PSMPLPMPPT TPKSENESMS SGREELSPAS
     SINGCSTDGE PRRQKKGPAP RQQEELCLVC GDRASGYHYN ALTCEGCKGF FRRSVTKNAV
     YICKFGHACE MDMYMRRKCQ ECRLKKCLAV GMRPECVVPE STCKNKRREK EAQREKDKLP
     VSTTTVDDHM PAIMQCDPPP PEAARIHEVV PRFLTEKLME QNRLKNVTPL SANQKSLIAR
     LVWYQEGYEQ PSEEDLKRVT QTWQLEEEEE EETDMPFRQI TEMTILTVQL IVEFAKGLPG
     FSKISQSDQI TLLKASSSEV MMLRVARRYD AATDSVLFAN NQAYTRDNYR KAGMSYVIED
     LLHFCRCMYS MSMDNVHYAL LTAIVIFSDR PGLEQPLLVE EIQRYYLKTL RVYILNQHSA
     SPRCAVLFGK ILGVLTELRT LGTQNSNMCI SLKLKNRKLP PFLEEIWDVA EVSTTQPTPG
     VAAQVTPIVV DNPAAL