E75_GALME
ID E75_GALME Reviewed; 711 AA.
AC P50239; Q24994;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Ecdysone-inducible protein E75;
DE AltName: Full=Nuclear receptor subfamily 1 group D member 3;
GN Name=E75; Synonyms=NR1D3;
OS Galleria mellonella (Greater wax moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC Pyralidae; Galleriinae; Galleria.
OX NCBI_TaxID=7137;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=8174547; DOI=10.1111/j.1432-1033.1994.tb18779.x;
RA Jindra M., Sehnal F., Riddiford L.M.;
RT "Isolation, characterization and developmental expression of the
RT ecdysteroid-induced E75 gene of the wax moth Galleria mellonella.";
RL Eur. J. Biochem. 221:665-675(1994).
CC -!- FUNCTION: Orphan receptor possibly involved in the regulation of genes
CC in the ecdysteroid cascade.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist. Isoforms differ in their
CC N-termini.;
CC Name=1; Synonyms=E75A;
CC IsoId=P50239-1; Sequence=Displayed;
CC Name=2; Synonyms=E75B;
CC IsoId=P50239-2; Sequence=VSP_003652;
CC -!- DEVELOPMENTAL STAGE: Both isoforms first expressed in stage-2 larvae
CC and then highly expressed during larval and pupal molts. Only isoform
CC E75A is expressed at the time of pupal ecdysis.
CC -!- INDUCTION: Expression is induced by 20-OH-ecdysone which initiates and
CC coordinates the molts.
CC -!- MISCELLANEOUS: [Isoform 2]: Lacks the first zinc-finger. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U02620; AAA19579.1; -; mRNA.
DR EMBL; U51008; AAA93484.1; -; Genomic_DNA.
DR PIR; S43464; S43464.
DR AlphaFoldDB; P50239; -.
DR SMR; P50239; -.
DR Proteomes; UP000504614; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001728; ThyrH_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; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR PRINTS; PR00546; THYROIDHORMR.
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..711
FT /note="Ecdysone-inducible protein E75"
FT /id="PRO_0000053508"
FT DOMAIN 153..400
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 44..120
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 47..67
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 84..108
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 405..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..711
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..68
FT /note="MTLVMSPDSSYGRYDAPAPADNRIMSPVHKEREPELHIEFDGTTVLCRVCGD
FT KASGFHYGVHSCEGCK -> MVRAMSCGAELRERHSVLVSMLESRRESSDSGCSSDESS
FT DLERNSNCRCDSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8174547"
FT /id="VSP_003652"
SQ SEQUENCE 711 AA; 78530 MW; BA591C6E7735B6EC CRC64;
MTLVMSPDSS YGRYDAPAPA DNRIMSPVHK EREPELHIEF DGTTVLCRVC GDKASGFHYG
VHSCEGCKGF FRRSIQQKIQ YRPCTKNQQC SILRINRNRC QYCRLKKCIA VGMSRDAVRF
GRVPKREKAR ILAAMQSSTT RAHEQAAAAE LDDGPRLLAR VVRAHLDTCE FTRDRVAAMR
NGARDCPTYS QPTLACPLNP APELQSEKEF SQRFAHVIRG VIDFAGLIPG FQLLTQDDKF
TLLKSGLFDA LFVRLICMFD APLNSIICLN GQLMKRDSIQ SGANARFLVD STFKFAERMN
SMNLTDAEIG LFCAIVLITP DRPGLRNVEL VERMHSRLKS CLQTVIAQNR SDGPGFLREL
MDTLPDLRTL STLHTEKLVV FRTEHKELLR QQMWVEDEGA LWADSGADDS ARSPIGSVSS
SESSETTGDC GTPLLAATLA GRRRLDSRGS VDEEALGVAH LAHNGLTVTP VRPPPRYRKL
DSPTDSGIES GNEKHERIVG PESGCSSPRS SLEEHSDDRR PIAPADDMPV LKRVLQAPPL
YDASSLMDEA YKPHKKFRAM RRDTWSEAEA RPGRPTPSPQ PPHHPHPASP AHPAHSPRPI
RAPLSSTHSV LAKSLMEGPR MTPEQLKRTD IIQQYMRRGE TGAPTEGCPL RAGGLLTCFR
GASPAPQPVI ALQVDVAETD APQPLNLSKK SPSPSPPPPP PRSYMPPMLP A
