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E75BC_DROME
ID   E75BC_DROME             Reviewed;        1199 AA.
AC   P17671; B3DN68; B3DN69; Q8IQS1; Q8IQS3;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 197.
DE   RecName: Full=Ecdysone-induced protein 75B, isoforms C/D;
DE   AltName: Full=E75-A;
DE   AltName: Full=Nuclear receptor subfamily 1 group D member 3, isoforms C/D;
GN   Name=Eip75B; Synonyms=NR1D3; ORFNames=CG8127;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), AND ALTERNATIVE SPLICING.
RC   STRAIN=Canton-S;
RX   PubMed=2110921; DOI=10.1101/gad.4.2.204;
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 superfamily.";
RL   Genes Dev. 4:204-219(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C AND D).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=8223281; DOI=10.1242/dev.118.2.613;
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 of
CC       the larval molt by 20-OH-ecdysone. {ECO:0000269|PubMed:8223281}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=C; Synonyms=E75A;
CC         IsoId=P17671-1; Sequence=Displayed;
CC       Name=A; Synonyms=E75B;
CC         IsoId=P17672-1; Sequence=External;
CC       Name=B; Synonyms=E75C;
CC         IsoId=P13055-2; Sequence=External;
CC       Name=D;
CC         IsoId=P17671-2; Sequence=VSP_014915, VSP_014916;
CC   -!- DEVELOPMENTAL STAGE: In mid instar larvae salivary glands, low basal
CC       levels are observed in puff stage 1. Levels increase in late larvae
CC       from puff stages 3-10, then decrease abruptly at stage 11. In prepupae,
CC       isoform C is the predominant form during the transition between puff
CC       stages 18-19. At puff stage 1, expression is also present in the gut.
CC       By stage 3 it is present in the wing disks, Malpighian tubules and the
CC       fat body. At stage 11, expression is only present in the gut and wing
CC       disks. {ECO:0000269|PubMed:8223281}.
CC   -!- INDUCTION: The expression of this protein is developmentally regulated
CC       and is correlated with the 20-OH-ecdysone induced activity of puff 75B.
CC       {ECO:0000269|PubMed:8223281}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA35923.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X51548; CAA35923.1; ALT_FRAME; mRNA.
DR   EMBL; AE014296; AAN11687.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAN11689.1; -; Genomic_DNA.
DR   EMBL; BT032856; ACD81870.1; -; mRNA.
DR   EMBL; BT032857; ACD81871.1; -; mRNA.
DR   PIR; A34598; A34598.
DR   RefSeq; NP_730322.1; NM_168756.2. [P17671-1]
DR   RefSeq; NP_730323.1; NM_168757.1. [P17671-2]
DR   AlphaFoldDB; P17671; -.
DR   SMR; P17671; -.
DR   BioGRID; 65284; 18.
DR   IntAct; P17671; 3.
DR   DNASU; 39999; -.
DR   EnsemblMetazoa; FBtr0075149; FBpp0074915; FBgn0000568. [P17671-1]
DR   EnsemblMetazoa; FBtr0075151; FBpp0074917; FBgn0000568. [P17671-2]
DR   GeneID; 39999; -.
DR   CTD; 39999; -.
DR   FlyBase; FBgn0000568; Eip75B.
DR   VEuPathDB; VectorBase:FBgn0000568; -.
DR   SignaLink; P17671; -.
DR   BioGRID-ORCS; 39999; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; Eip75B; fly.
DR   GenomeRNAi; 39999; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0000568; Expressed in brain and 27 other tissues.
DR   ExpressionAtlas; P17671; baseline and differential.
DR   Genevisible; P17671; DM.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR   GO; GO:0020037; F:heme binding; IDA:FlyBase.
DR   GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0018990; P:ecdysis, chitin-based cuticle; IMP:FlyBase.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0007591; P:molting cycle, chitin-based cuticle; IMP:FlyBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:FlyBase.
DR   GO; GO:0048477; P:oogenesis; NAS:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007553; P:regulation of ecdysteroid metabolic process; IMP:FlyBase.
DR   GO; GO:0010468; P:regulation of gene expression; IDA:FlyBase.
DR   GO; GO:0035075; P:response to ecdysone; IMP:FlyBase.
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; Developmental protein; DNA-binding; Metal-binding;
KW   Nucleus; Receptor; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1199
FT                   /note="Ecdysone-induced protein 75B, isoforms C/D"
FT                   /id="PRO_0000053506"
FT   DOMAIN          352..600
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        242..318
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         245..265
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         282..306
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          130..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          771..808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          831..851
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1155..1188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..665
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..807
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        831..849
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        897..919
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..961
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1155..1176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..293
FT                   /note="Missing (in isoform D)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_014915"
FT   VAR_SEQ         294..315
FT                   /note="NRNRCQYCRLKKCIAVGMSRDA -> MGEELPILKGILKGNVNYHNAP (in
FT                   isoform D)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_014916"
FT   CONFLICT        239
FT                   /note="D -> G (in Ref. 4; ACD81870)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        572
FT                   /note="T -> N (in Ref. 4; ACD81870)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        578
FT                   /note="L -> P (in Ref. 4; ACD81870)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        889
FT                   /note="H -> R (in Ref. 4; ACD81870)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1199 AA;  128534 MW;  E29372F5E295F595 CRC64;
     MLMSADSSDS AKTSVICSTV SASMLAPPAP EQPSTTAPPI LGVTGRSHLE NALKLPPNTS
     VSAYYQHNSK LGMGQNYNPE FRSLVAPVTD LDTVPPTGVT MASSSNSPNS SVKLPHSGVI
     FVSKSSAVST TDGPTAVLQQ QQPQQQMPQH FESLPHHHPQ QEHQPQQQQQ QHHLQHHPHP
     HVMYPHGYQQ ANLHHSGGIA VVPADSRPQT PEYIKSYPVM DTTVASSVKG EPELNIEFDG
     TTVLCRVCGD KASGFHYGVH SCEGCKGFFR RSIQQKIQYR PCTKNQQCSI LRINRNRCQY
     CRLKKCIAVG MSRDAVRFGR VPKREKARIL AAMQQSTQNR GQQRALATEL DDQPRLLAAV
     LRAHLETCEF TKEKVSAMRQ RARDCPSYSM PTLLACPLNP APELQSEQEF SQRFAHVIRG
     VIDFAGMIPG FQLLTQDDKF TLLKAGLFDA LFVRLICMFD SSINSIICLN GQVMRRDAIQ
     NGANARFLVD STFNFAERMN SMNLTDAEIG LFCAIVLITP DRPGLRNLEL IEKMYSRLKG
     CLQYIVAQNR PDQPEFLAKL LETMPDLRTL STLHTEKLVV FRTEHKELLR QQMWSMEDGN
     NSDGQQNKSP SGSWADAMDV EAAKSPLGSV SSTESADLDY GSPSSSQPQG VSLPSPPQQQ
     PSALASSAPL LAATLSGGCP LRNRANSGSS GDSGAAEMDI VGSHAHLTQN GLTITPIVRH
     QQQQQQQQQI GILNNAHSRN LNGGHAMCQQ QQQHPQLHHH LTAGAARYRK LDSPTDSGIE
     SGNEKNECKA VSSGGSSSCS SPRSSVDDAL DCSDAAANHN QVVQHPQLSV VSVSPVRSPQ
     PSTSSHLKRQ IVEDMPVLKR VLQAPPLYDT NSLMDEAYKP HKKFRALRHR EFETAEADAS
     SSTSGSNSLS AGSPRQSPVP NSVATPPPSA ASAAAGNPAQ SQLHMHLTRS SPKASMASSH
     SVLAKSLMAE PRMTPEQMKR SDIIQNYLKR ENSTAASSTT NGVGNRSPSS SSTPPPSAVQ
     NQQRWGSSSV ITTTCQQRQQ SVSPHSNGSS SSSSSSSSSS SSSSSTSSNC SSSSASSCQY
     FQSPHSTSNG TSAPASSSSG SNSATPLLEL QVDIADSAQP LNLSKKSPTP PPSKLHALVA
     AANAVQRYPT LSADVTVTAS NGGPPSAAAS PAPSSSPPAS VGSPNPGLSA AVHKVMLEA
 
 
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