ECR_BOMMO
ID ECR_BOMMO Reviewed; 606 AA.
AC P49881;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 131.
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 Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Mysore; TISSUE=Ovary;
RX PubMed=7633470; DOI=10.1016/0965-1748(95)00024-p;
RA Swevers L., Drevet J.R., Lunke M.D., Iatrou K.;
RT "The silkmoth homolog of the Drosophila ecdysone receptor (B1 isoform):
RT cloning and analysis of expression during follicular cell
RT differentiation.";
RL Insect Biochem. Mol. Biol. 25:857-866(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 61-606.
RC STRAIN=Kinshu X Showa; TISSUE=Fat body;
RA Kamimura M., Tomita S., Fujiwara H.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for ecdysone. Binds to ecdysone response elements
CC (ECRES). May play a role in the implementation of the choriogenic
CC program at the end of vitellogenesis.
CC -!- SUBUNIT: Heterodimer of ECR and CF1. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49881-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49881-2; Sequence=VSP_003663;
CC -!- DEVELOPMENTAL STAGE: It is present in constant amounts in follicular
CC cells throughout vitellogenesis but disappears transiently at the onset
CC of choriogenesis and reappears during the later stages of
CC choriogenesis.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-61 is the initiator.
CC {ECO:0000305}.
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DR EMBL; L35266; AAA87341.1; -; mRNA.
DR EMBL; L35266; AAA87340.1; -; mRNA.
DR EMBL; D43943; BAA07890.1; -; mRNA.
DR RefSeq; NP_001037331.2; NM_001043866.2. [P49881-2]
DR RefSeq; NP_001166846.1; NM_001173375.1. [P49881-1]
DR AlphaFoldDB; P49881; -.
DR SMR; P49881; -.
DR STRING; 7091.BGIBMGA006767-TA; -.
DR BindingDB; P49881; -.
DR ChEMBL; CHEMBL3868; -.
DR GeneID; 692756; -.
DR KEGG; bmor:692756; -.
DR CTD; 35540; -.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; P49881; -.
DR OrthoDB; 1137281at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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 Alternative splicing; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..606
FT /note="Ecdysone receptor"
FT /id="PRO_0000053526"
FT DOMAIN 352..589
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 207..279
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 207..227
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 243..267
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..206
FT /note="Modulating"
FT /evidence="ECO:0000255"
FT REGION 134..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 380..382
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003663"
FT CONFLICT 67
FT /note="N -> D (in Ref. 2; BAA07890)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="S -> T (in Ref. 2; BAA07890)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="R -> G (in Ref. 2; BAA07890)"
FT /evidence="ECO:0000305"
FT CONFLICT 469..470
FT /note="QG -> KA (in Ref. 2; BAA07890)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="A -> P (in Ref. 2; BAA07890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 606 AA; 68202 MW; 960E8B9A1E4F2202 CRC64;
MRVENVDNVS FALNGRADEW CMSVETRLDS LVREKSEVKA YVGGCPSVIT DAGAYDALFD
MRRRWSNNGG FPLRMLEESS SEVTSSSALG LPPAMVMSPE SLASPEYRAL ELWSYDDGIT
YNTAQSLLGA CNMQQQQLQP QQPHPAPPTL PTMPLPMPPT TPKSENESMS SGREELSPAS
SINGCSADAD ARRQKKGPAP RQQEELCLVC GDRASGYHYN ALTCEGCKGF FRRSVTKNAV
YICKFGHACE MDMYMRRKCQ ECRLKKCLAV GMRPECVIQE PSKNKDRQRQ KKDKGILLPV
STTTVEDHMP PIMQCDPPPP EAARIHEVVP RYLSEKLMEQ NRQKNIPPLS ANQKSLIARL
VWYQEGYEQP SDEDLKRVTQ TWQSDEEDEE SDLPFRQITE MTILTVQLIV EFAKGLPGFS
KISQSDQITL LKASSSEVMM LRVARRYDAA SDSVLFANNK AYTRDNYRQG GMAYVIEDLL
HFCRCMFAMG MDNVHFALLT AIVIFSDRPG LEQPSLVEEI QRYYLNTLRI YIINQNSASS
RCAVIYGRIL SVLTELRTLG TQNSNMCISL KLKNRKLPPF LEEIWDVAEV ATTHPTVLPP
TNPVVL
