Swiss-Prot entry

ID   E75_MANSE      STANDARD;      PRT;   699 AA.
AC   Q08893; Q08892;
DT   01-OCT-1996 (Rel. 34, Created)
DT   15-JUL-1999 (Rel. 38, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Ecdysone-inducible protein E75.
GN   Name=E75; Synonyms=NR1D3;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; 
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Sphingoidea; 
OC   Sphingidae; Sphinginae; Manduca. 
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=93250864; PubMed=8485520 [NCBI, ExPASy, EBI, Israel, Japan]; 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.,
RA   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
CC       of the larval molt by 20-OH-ecdysone.
CC   -!- SUBCELLULAR LOCATION: Nuclear (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist. Isoforms differ in
CC         their 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         Note=Lacks the first zinc-finger;
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; S60738; AAC60499.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; S60782; AAC60497.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; U73683; AAC35424.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; A56591; A56591.
DR   PIR; C56591; C56591.
DR   HSSP; P20393; 1GA5. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; Q08893; 40-123.
DR   InterPro; IPR000536; Hrmon_recept_lig.
DR   InterPro; IPR001723; Stdhrmn_receptor.
DR   InterPro; IPR008946; Str_ncl_receptor.
DR   InterPro; IPR000324; VitD_receptor.
DR   InterPro; IPR001628; Znf_C4steroid.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   PRINTS; PR00350; VITAMINDR.
DR   ProDom; PD000035; Znf_C4steroid; 1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   BLOCKS; Q08893.
DR   ProtoNet; Q08893.
DR   ProtoMap; Q08893.
DR   PRESAGE; Q08893.
DR   DIP; Q08893.
DR   ModBase; Q08893.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Alternative splicing; DNA-binding; Nuclear protein; Receptor;
KW   Transcription; Transcription regulation; Zinc-finger.
FT   DNA_BIND     42    118       Nuclear receptor-type.
FT   ZN_FING      45     65       C4-type.
FT   ZN_FING      82    106       C4-type.
FT   DOMAIN      145    148       Poly-Ala.
FT   DOMAIN      180    389       Ligand-binding (Potential).
FT   VARSPLIC      1     66       MTLVMSPDSSYGRYDAPTPTDVTSPVHREREPELHIEFDGT
FT                                TVLCRVCGDKASGFHYGVHSCEGCK -> MVRAMSCGAELR
FT                                ERHSVLVSMLEARRESSDSGCSSDDGSDVERDCKCRCDPQ
FT                                (in isoform 2).
FT                                /FTId=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
//