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E75BB_DROME
ID   E75BB_DROME             Reviewed;        1412 AA.
AC   P13055; Q9VVM9;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 204.
DE   RecName: Full=Ecdysone-induced protein 75B, isoform B;
DE   AltName: Full=E75-C;
DE   AltName: Full=Nuclear receptor subfamily 1 group D member 3, isoform B;
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], AND ALTERNATIVE SPLICING.
RC   STRAIN=Canton-S; TISSUE=Head;
RX   PubMed=2508058; DOI=10.1093/nar/17.18.7167;
RA   Feigl G., Gram M., Pongs O.;
RT   "A member of the steroid hormone receptor gene family is expressed in the
RT   20-OH-ecdysone inducible puff 75B in Drosophila melanogaster.";
RL   Nucleic Acids Res. 17:7167-7178(1989).
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   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=B; Synonyms=E75C;
CC         IsoId=P13055-2; Sequence=Displayed;
CC       Name=C; Synonyms=E75A;
CC         IsoId=P17671-1; Sequence=External;
CC       Name=A; Synonyms=E75B;
CC         IsoId=P17672-1; Sequence=External;
CC       Name=D;
CC         IsoId=P17671-2; Sequence=External;
CC   -!- DEVELOPMENTAL STAGE: In mid instar larvae salivary glands, levels
CC       increase during puff stage 1, then remain relatively constant until the
CC       premetamorphic pulse of ecdysone at puff stage 5. Levels increase again
CC       in late larvae at puff stages 9-10. At puff stage 1 expression is also
CC       seen in the gut. Levels are low in the gut, Malpighian tubules, fat
CC       body and wing disks between stages 1 and 11.
CC       {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=CAA33611.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X15586; CAA33611.1; ALT_FRAME; mRNA.
DR   EMBL; AE014296; AAF49282.3; -; Genomic_DNA.
DR   PIR; S05979; S05979.
DR   RefSeq; NP_001246821.1; NM_001259892.1. [P13055-2]
DR   RefSeq; NP_001246822.1; NM_001259893.2. [P13055-2]
DR   RefSeq; NP_730321.1; NM_168755.1. [P13055-2]
DR   AlphaFoldDB; P13055; -.
DR   SMR; P13055; -.
DR   BioGRID; 65284; 18.
DR   IntAct; P13055; 9.
DR   STRING; 7227.FBpp0297726; -.
DR   PaxDb; P13055; -.
DR   PRIDE; P13055; -.
DR   DNASU; 39999; -.
DR   EnsemblMetazoa; FBtr0075148; FBpp0074914; FBgn0000568. [P13055-2]
DR   EnsemblMetazoa; FBtr0306813; FBpp0297725; FBgn0000568. [P13055-2]
DR   EnsemblMetazoa; FBtr0306814; FBpp0297726; FBgn0000568. [P13055-2]
DR   GeneID; 39999; -.
DR   KEGG; dme:Dmel_CG8127; -.
DR   CTD; 39999; -.
DR   FlyBase; FBgn0000568; Eip75B.
DR   VEuPathDB; VectorBase:FBgn0000568; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   InParanoid; P13055; -.
DR   OMA; IVRHHQQ; -.
DR   PhylomeDB; P13055; -.
DR   Reactome; R-DME-200425; Carnitine metabolism.
DR   Reactome; R-DME-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR   Reactome; R-DME-381340; Transcriptional regulation of white adipocyte differentiation.
DR   Reactome; R-DME-383280; Nuclear Receptor transcription pathway.
DR   Reactome; R-DME-400206; Regulation of lipid metabolism by PPARalpha.
DR   Reactome; R-DME-4090294; SUMOylation of intracellular receptors.
DR   Reactome; R-DME-5362517; Signaling by Retinoic Acid.
DR   Reactome; R-DME-9616222; Transcriptional regulation of granulopoiesis.
DR   Reactome; R-DME-9707564; Cytoprotection by HMOX1.
DR   SignaLink; P13055; -.
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; P13055; baseline and differential.
DR   Genevisible; P13055; 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:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; 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..1412
FT                   /note="Ecdysone-induced protein 75B, isoform B"
FT                   /id="PRO_0000053505"
FT   DOMAIN          565..813
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        455..531
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         458..478
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         495..514
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          110..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          837..878
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          984..1021
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1044..1064
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1108..1174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1204..1317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1368..1401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..286
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..878
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        989..1020
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1062
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1110..1132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1147..1174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1368..1389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        20
FT                   /note="V -> F (in Ref. 1; CAA33611)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="Q -> QQ (in Ref. 1; CAA33611)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        337..342
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1142
FT                   /note="S -> V (in Ref. 1; CAA33611)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1216
FT                   /note="V -> L (in Ref. 1; CAA33611)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1231
FT                   /note="Missing (in Ref. 1; CAA33611)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1302
FT                   /note="N -> I (in Ref. 1; CAA33611)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1412 AA;  151292 MW;  6F4C21B075443F8C CRC64;
     MEAVQAAAAA TSSGGSSGSV PGSGSGSASK LIKTEPIDFE MLHLEENERQ QDIEREPSSS
     NSNSNSNSLT PQRYTHVQVQ TVPPRQPTGL TTPGGTQKVI LTPRVEYVQQ RATSSTGGGM
     KHVYSQQQGT AASRSAPPET TALLTTTSGT PQIIITRTLP SNQHLSRRHS ASPSALHHYQ
     QQQPQRQQSP PPLHHQQQQQ QQHVRVIRDG RLYDEATVVV AARRHSVSPP PLHHHSRSAP
     VSPVIARRGG AAAYMDQQYQ QRQTPPLAPP PPPPPPPPPP PPPQQQQQQY ISTGVPPPTA
     AARKFVVSTS TRHVNVIASN HFQQQQQQHQ AQQHQQQHQQ HQQHQQHVIA SVSSSSSSSA
     IGSGGSSSSH IFRTPVVSSS SSSNMHHQQQ QQQQQSSLGN SVMRPPPPPP PPKVKHASSS
     SSGNSSSSNT NNSSSSSNGE EPSSSIPDLE FDGTTVLCRV CGDKASGFHY GVHSCEGCKG
     FFRRSIQQKI QYRPCTKNQQ CSILRINRNR CQYCRLKKCI AVGMSRDAVR FGRVPKREKA
     RILAAMQQST QNRGQQRALA TELDDQPRLL AAVLRAHLET CEFTKEKVSA MRQRARDCPS
     YSMPTLLACP LNPAPELQSE QEFSQRFAHV IRGVIDFAGM IPGFQLLTQD DKFTLLKAGL
     FDALFVRLIC MFDSSINSII CLNGQVMRRD AIQNGANARF LVDSTFNFAE RMNSMNLTDA
     EIGLFCAIVL ITPDRPGLRN LELIEKMYSR LKGCLQYIVA QNRPDQPEFL AKLLETMPDL
     RTLSTLHTEK LVVFRTEHKE LLRQQMWSME DGNNSDGQQN KSPSGSWADA MDVEAAKSPL
     GSVSSTESAD LDYGSPSSSQ PQGVSLPSPP QQQPSALASS APLLAATLSG GCPLRNRANS
     GSSGDSGAAE MDIVGSHAHL TQNGLTITPI VRHQQQQQQQ QQIGILNNAH SRNLNGGHAM
     CQQQQQHPQL HHHLTAGAAR YRKLDSPTDS GIESGNEKNE CKAVSSGGSS SCSSPRSSVD
     DALDCSDAAA NHNQVVQHPQ LSVVSVSPVR SPQPSTSSHL KRQIVEDMPV LKRVLQAPPL
     YDTNSLMDEA YKPHKKFRAL RHREFETAEA DASSSTSGSN SLSAGSPRQS PVPNSVATPP
     PSAASAAAGN PAQSQLHMHL TRSSPKASMA SSHSVLAKSL MAEPRMTPEQ MKRSDIIQNY
     LKRENSTAAS STTNGVGNRS PSSSSTPPPS AVQNQQRWGS SSVITTTCQQ RQQSVSPHSN
     GSSSSSSSSS SSSSSSSSTS SNCSSSSASS CQYFQSPHST SNGTSAPASS SSGSNSATPL
     LELQVDIADS AQPLNLSKKS PTPPPSKLHA LVAAANAVQR YPTLSADVTV TASNGGPPSA
     AASPAPSSSP PASVGSPNPG LSAAVHKVML EA
 
 
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