E75BA_DROME
ID E75BA_DROME Reviewed; 1355 AA.
AC P17672; Q8IQS2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Ecdysone-induced protein 75B, isoform A;
DE Short=E75-B;
DE AltName: Full=Nuclear receptor subfamily 1 group D member 3, isoform A;
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;
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 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=A; Synonyms=E75B;
CC IsoId=P17672-1; Sequence=Displayed;
CC Name=C; Synonyms=E75A;
CC IsoId=P17671-1; Sequence=External;
CC Name=B; Synonyms=E75C;
CC IsoId=P13055-2; Sequence=External;
CC Name=D;
CC IsoId=P17671-2; Sequence=External;
CC -!- DEVELOPMENTAL STAGE: In mid instar larvae salivary glands, levels are
CC low during puff stage 1, increase during puff stages 2-4 and diminish
CC from stage 5 onwards. In prepupae, isoform A is the predominant form
CC during puff stage 19 and the transition to stage 20. By stage 3 it is
CC present in the gut, Malpighian tubules and the fat body, levels persist
CC beyond stage 11. {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=CAA35924.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X51549; CAA35924.1; ALT_FRAME; mRNA.
DR EMBL; AE014296; AAN11688.1; -; Genomic_DNA.
DR PIR; B34598; B34598.
DR RefSeq; NP_524133.2; NM_079409.3. [P17672-1]
DR AlphaFoldDB; P17672; -.
DR SMR; P17672; -.
DR BioGRID; 65284; 18.
DR IntAct; P17672; 4.
DR PRIDE; P17672; -.
DR DNASU; 39999; -.
DR EnsemblMetazoa; FBtr0075150; FBpp0074916; FBgn0000568. [P17672-1]
DR GeneID; 39999; -.
DR CTD; 39999; -.
DR FlyBase; FBgn0000568; Eip75B.
DR VEuPathDB; VectorBase:FBgn0000568; -.
DR HOGENOM; CLU_004897_0_0_1; -.
DR PhylomeDB; P17672; -.
DR SignaLink; P17672; -.
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; P17672; baseline and differential.
DR Genevisible; P17672; 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; 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; 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..1355
FT /note="Ecdysone-induced protein 75B, isoform A"
FT /id="PRO_0000053504"
FT DOMAIN 508..756
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 384..474
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 387..421
FT /note="NR C4-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 438..457
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 60..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 206
FT /note="S -> C (in Ref. 1; CAA35924)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="L -> LL (in Ref. 1; CAA35924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1355 AA; 147171 MW; 6EF19BACEC9562F5 CRC64;
MVCAMQEVAA VQHQQQQQQL QLPQQQQQQQ QTTQQQHATT IVLLTGNGGG NLHIVATPQQ
HQPMHQLHHQ HQHQHQHQQQ AKSQQLKQQH SALVKLLESA PIKQQQQTPK QIVYLQQQQQ
QPQRKRLKNE AAIVQQQQQT PATLVKTTTT SNSNSNNTQT TNSISQQQQQ HQIVLQHQQP
AAAATPKPCA DLSAKNDSES GIDEDSPNSD EDCPNANPAG TSLEDSSYEQ YQCPWKKIRY
ARELKQRELE QQQTTGGSNA QQQVEAKPAA IPTSNIKQLH CDSPFSAQTH KEIANLLRQQ
SQQQQVVATQ QQQQQQQQHQ HQQQRRDSSD SNCSLMSNSS NSSAGNCCTC NAGDDQQLEE
MDEAHDSGCD DELCEQHHQR LDSSQLNYLC QKFDEKLDTA LSNSSANTGR NTPAVTANED
ADGFFRRSIQ QKIQYRPCTK NQQCSILRIN RNRCQYCRLK KCIAVGMSRD AVRFGRVPKR
EKARILAAMQ QSTQNRGQQR ALATELDDQP RLLAAVLRAH LETCEFTKEK VSAMRQRARD
CPSYSMPTLL ACPLNPAPEL QSEQEFSQRF AHVIRGVIDF AGMIPGFQLL TQDDKFTLLK
AGLFDALFVR LICMFDSSIN SIICLNGQVM RRDAIQNGAN ARFLVDSTFN FAERMNSMNL
TDAEIGLFCA IVLITPDRPG LRNLELIEKM YSRLKGCLQY IVAQNRPDQP EFLAKLLETM
PDLRTLSTLH TEKLVVFRTE HKELLRQQMW SMEDGNNSDG QQNKSPSGSW ADAMDVEAAK
SPLGSVSSTE SADLDYGSPS SSQPQGVSLP SPPQQQPSAL ASSAPLLAAT LSGGCPLRNR
ANSGSSGDSG AAEMDIVGSH AHLTQNGLTI TPIVRHQQQQ QQQQQIGILN NAHSRNLNGG
HAMCQQQQQH PQLHHHLTAG AARYRKLDSP TDSGIESGNE KNECKAVSSG GSSSCSSPRS
SVDDALDCSD AAANHNQVVQ HPQLSVVSVS PVRSPQPSTS SHLKRQIVED MPVLKRVLQA
PPLYDTNSLM DEAYKPHKKF RALRHREFET AEADASSSTS GSNSLSAGSP RQSPVPNSVA
TPPPSAASAA AGNPAQSQLH MHLTRSSPKA SMASSHSVLA KSLMAEPRMT PEQMKRSDII
QNYLKRENST AASSTTNGVG NRSPSSSSTP PPSAVQNQQR WGSSSVITTT CQQRQQSVSP
HSNGSSSSSS SSSSSSSSSS STSSNCSSSS ASSCQYFQSP HSTSNGTSAP ASSSSGSNSA
TPLLELQVDI ADSAQPLNLS KKSPTPPPSK LHALVAAANA VQRYPTLSAD VTVTASNGGP
PSAAASPAPS SSPPASVGSP NPGLSAAVHK VMLEA
