Swiss-Prot entry

ID   E75B_DROME     STANDARD;      PRT;  1394 AA.
AC   P17672;
DT   01-AUG-1990 (Rel. 15, Created)
DT   01-AUG-1990 (Rel. 15, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Ecdysone-induced protein 75B isoform B (E75-B).
GN   Name=Eip75B; Synonyms=NR1D3;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; 
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; 
OC   Ephydroidea; Drosophilidae; Drosophila. 
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND ALTERNATIVE SPLICING.
RC   STRAIN=Canton-S;
RX   MEDLINE=90249727; PubMed=2110921 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Segraves W.A., Hogness D.S.;
RT   "The E75 ecdysone-inducible gene responsible for the 75B early puff in
RT   Drosophila encodes two new members of the steroid receptor
RT   superfamily.";
RL   Genes Dev. 4:204-219(1990).
RN   [2]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=94038699; PubMed=8223281 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Huet F., Ruiz C., Richards G.;
RT   "Puffs and PCR: the in vivo dynamics of early gene expression during
RT   ecdysone responses in Drosophila.";
RL   Development 118:613-627(1993).
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=3;
CC       Name=B; Synonyms=E75B;
CC         IsoId=P17672-1; Sequence=Displayed;
CC       Name=A; Synonyms=E75A;
CC         IsoId=P17671-1; Sequence=External;
CC       Name=C; Synonyms=E75C;
CC         IsoId=P13055-2; Sequence=External;
CC   -!- DEVELOPMENTAL STAGE: In mid instar larvae salivary glands, levels
CC       are low during puff stage 1, increase during puff stages 2-4 and
CC       diminish from stage 5 onwards. In prepupae, isoform B is the
CC       predominant form during puff stage 19 and the transition to stage
CC       20. By stage 3 it is present in the gut, Malpighian tubules and
CC       the fat body, levels persist beyond stage 11.
CC   -!- INDUCTION: The expression of this protein is developmentally
CC       regulated and is correlated with the 20-OH-ecdysone induced
CC       activity of puff 75B.
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; X51549; CAA35924.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; B34598; B34598.
DR   HSSP; P20393; 1A6Y. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; P17672; 415-480.
DR   TRANSFAC; T01368; -.
DR   FlyBase; FBgn0000568; Eip75B.
DR   GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS.
DR   GO; GO:0018990; P:ecdysis (sensu Insecta); IMP.
DR   GO; GO:0035072; P:ecdysone-mediated induction of salivary gla...; NAS.
DR   GO; GO:0007553; P:regulation of ecdysteroid metabolism; IMP.
DR   InterPro; IPR000536; Hrmon_recept_lig.
DR   InterPro; IPR001723; Stdhrmn_receptor.
DR   InterPro; IPR008946; Str_ncl_receptor.
DR   InterPro; IPR001728; ThyrH_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; PR00546; THYROIDHORMR.
DR   ProDom; PD000035; Znf_C4steroid; 1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   CMR; P17672.
DR   BLOCKS; P17672.
DR   ProtoNet; P17672.
DR   ProtoMap; P17672.
DR   PRESAGE; P17672.
DR   DIP; P17672.
DR   ModBase; P17672.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Alternative splicing; Developmental protein; DNA-binding;
KW   Metal-binding; Nuclear protein; Receptor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   DOMAIN       12     21       Poly-Gln.
FT   DOMAIN       24     31       Poly-Gln.
FT   DOMAIN      104    107       Poly-Gln.
FT   DOMAIN      116    123       Poly-Gln.
FT   DOMAIN      135    139       Poly-Gln.
FT   DOMAIN      147    150       Poly-Thr.
FT   DOMAIN      166    172       Poly-Gln.
FT   DOMAIN      181    184       Poly-Ala.
FT   DOMAIN      300    306       Poly-Gln.
FT   DOMAIN      311    325       Poly-Gln.
FT   DNA_BIND    385    475       Nuclear receptor-type.
FT   DOMAIN      878    886       Poly-Gln.
FT   DOMAIN      906    910       Poly-Gln.
FT   DOMAIN     1164   1169       Poly-Ser.
FT   DOMAIN     1206   1225       Poly-Ser.
FT   DOMAIN     1228   1234       Poly-Ser.
FT   DOMAIN     1253   1260       Poly-Ser.
SQ   SEQUENCE   1394 AA;  152097 MW;  45CACF77BDE9FB80 CRC64;
     MVCAMQEVAA VQHQQQQQQL QLPQQQQQQQ QTTQQQHATT IVLLTGNGGG NLHIVATPQQ
     HQPMHQLHHQ HQHQHQHQQQ AKSQQLKQQH SALVKLLESA PIKQQQQTPK QIVYLQQQQQ
     QPQRKRLKNE AAIVQQQQQT PATLVKTTTT SNSNSNNTQT TNSISQQQQQ HQIVLQHQQP
     AAAATPKPCA DLSAKNDSES GIDEDCPNSD EDCPNANPAG TSLEDSSYEQ YQCPWKKIRY
     ARELLKQREL EQQQTTGGSN AQQQVEAKPA AIPTSNIKQL HCDSPFSAQT HKEIANLLRQ
     QSQQQQVVAT QQQQQQQQQH QHQQQRRDSS DSNCSLMSNS SNSSAGNCCT CNAGDDQQLE
     EMDEAHDSGC DDELCEQHHQ RLDSSQLNYL CQKFDEKLDT ALSNSSANTG RNTPAVTANE
     DADGFFRRSI QQKIQYRPCT KNQQCSILRI NRNRCQYCRL KKCIAVGMSR DAVRFGRVPK
     REKARILAAM QQSTQNRGQQ RALATELDDQ PRLLAAVLRA HLETCEFTKE KVSAMRQRAR
     DCPSYSMPTL LACPLNPAPE LQSEQEFSQR FAHVIRGVID FAGMIPGFQL LTQDDKFTLL
     KAGLFDALFV RLICMFDSSI NSIICLNGQV MRRDAIQNGA NARFLVDSTF NFAERMNSMN
     LTDAEIGLFC AIVLITPDRP GLRNLELIEK MYSRLKGCLQ YIVAQNRPDQ PEFLAKLLET
     MPDLRTLSTL HTEKLVVFRT EHKELLRQQM WSMEDGNNSD GQQNKSPSGS WADAMDVEAA
     KSPLGSVSST ESADLDYGSP SSSQPQGVSL PSPPQQQPSA LASSAPLLAA TLSGGCPLRN
     RANSGSSGDS GAAEMDIVGS HAHLTQNGLT ITPIVRHQQQ QQQQQQIGIL NNAHSRNLNG
     GHAMCQQQQQ HPQLHHHLTA GAARYRKLDS PTDSGIESGN EKNECKAVSS GGSSSCSSPR
     SSVDDALDCS DAAANHNQVV QHPQLSVVSV SPVRSPQPST SSHLKRQIVE DMPVLKRVLQ
     APPLYDTNSL MDEAYKPHKK FRALRHREFE TAEADASSST SGSNSLSAGS PRQSPVPNSV
     ATPPPSAASA AAGNPAQSQL HMHLTRSSPK ASMASSHSVL AKSLMAEPRM TPEQMKRSDI
     IQNYLKRENS TAASSTTNGV GNRSPSSSST PPPSAVQNQQ RWGSSSVITT TCQQRQQSVS
     PHSNGSSSSS SSSSSSSSSS SSTSSNCSSS SASSCQYFQS PHSTSNGTSA PASSSSGSNS
     ATPLLELQVD IADSAQPLNL SKKSPTPPPS KLHALVAAAN AVQRYPTLSA DVTVTASNGG
     SSVGGGESGR QQQSAGECGL PQSGPERRRA QGNAGGVRAG GGRWFYAEKW ERQRLGVAVQ
     RSRKQDHLER RELN
//