E75_MANSE
ID E75_MANSE Reviewed; 699 AA.
AC Q08893; Q08892;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Ecdysone-inducible protein E75;
DE AltName: Full=Nuclear receptor subfamily 1 group D member 3;
GN Name=E75; Synonyms=NR1D3;
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.
RX PubMed=8485520; DOI=10.1016/0965-1748(93)90086-8;
RA Segraves W.A., Woldin C.;
RT "The E75 gene of Manduca sexta and comparison with its Drosophila
RT homolog.";
RL Insect Biochem. Mol. Biol. 23:91-97(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1-114.
RA Zhou B., Hiruma K., Jindra M., Shinoda T., Segraves W.A., Riddiford L.M.;
RT "Developmental expression and hormonal regulation of the E75A and E75B
RT homologs in the epidermis of the tobacco hornworm, Manduca sexta.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Implicated in the regulation of ecdysone-triggered gene
CC hierarchies. Probably plays a key role in mediating the regulation of
CC the larval molt by 20-OH-ecdysone.
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=Q08893-1; Sequence=Displayed;
CC Name=2; Synonyms=E75B;
CC IsoId=Q08893-2; Sequence=VSP_003653;
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}.
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DR EMBL; S60738; AAC60499.1; -; mRNA.
DR EMBL; S60782; AAC60497.1; -; Genomic_DNA.
DR EMBL; U73683; AAC35424.1; -; mRNA.
DR PIR; A56591; A56591.
DR PIR; C56591; C56591.
DR AlphaFoldDB; Q08893; -.
DR SMR; Q08893; -.
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 Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..699
FT /note="Ecdysone-inducible protein E75"
FT /id="PRO_0000053509"
FT DOMAIN 152..399
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 42..118
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 45..65
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 82..106
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..592
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..66
FT /note="MTLVMSPDSSYGRYDAPTPTDVTSPVHREREPELHIEFDGTTVLCRVCGDKA
FT SGFHYGVHSCEGCK -> MVRAMSCGAELRERHSVLVSMLEARRESSDSGCSSDDGSDV
FT ERDCKCRCDPQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003653"
SQ SEQUENCE 699 AA; 77570 MW; A6E243EBB346464B CRC64;
MTLVMSPDSS YGRYDAPTPT DVTSPVHRER EPELHIEFDG TTVLCRVCGD KASGFHYGVH
SCEGCKGFFR RSIQQKIQYR PCTKNQQCSI LRINRNRCQY CRLKKCIAVG MSRDAVRFGR
VPKREKARIL AAMQQSSTSR AHEQAAAAEL DDAPRLLARV VRAHLDTCEF TRDRVAAMRA
RARDCPTYSQ PTLACPLNPA PELQSEKEFS QRFAHVIRGV IDFAGLIPGF QLLTQDDKFT
LLKSGLFDAL FVRLICMFDA PLNSIICLNG QLMKRDSIQS GANARFLVDS TFKFAERMNS
MNLTDAEIGL FCAIVLITPD RPGLRNVELV ERMHTRLKAC LQTVIAQNRP DRPGFLRELM
DTLPDLRTLS TLHTEKLVVF RTEHKELLRQ QMWSEEEAVS WVDSGADELA RSPIGSVSSS
ESGEAVGDCG TPLLAATLAG RRRLDSRGSV DEEALGVAHL AHNGLTVTPV RQPPRYRKLD
SPTDSGIESG NEKHERIVGT GSGCSSPRSS LEEHNEDRRP PVSADDMPVL KRVLQAPPLY
GGTPSLMDEA YRRHKKFRAL RRDTGEAEAR TVRPTPSPQP QHPHPANPAH PAHSPRPQRA
SLSSTHSVLA KSLMEGPRMT PEQLKRTDII QQYMRRGESS APAEGCPLRA GGLLTCYRGA
SPAPQPVLAL QVDVTDAPLN LSKKSPSPPR TYMPQMLEA
