HR78_DROME
ID HR78_DROME Reviewed; 601 AA.
AC Q24142; A4V288; Q24108; Q8IPT4; Q9VP28;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Nuclear hormone receptor HR78;
DE Short=dHR78;
DE AltName: Full=Nuclear receptor XR78E/F;
DE AltName: Full=Nuclear receptor subfamily 2 group D member 1;
GN Name=Hr78; Synonyms=Hr78D, NR2D1; ORFNames=CG7199;
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 B), FUNCTION, INDUCTION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=7479849; DOI=10.1073/pnas.92.23.10604;
RA Fisk G.J., Thummel C.S.;
RT "Isolation, regulation, and DNA-binding properties of three Drosophila
RT nuclear hormone receptor superfamily members.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10604-10608(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=7479823; DOI=10.1073/pnas.92.23.10477;
RA Zelhof A.C., Yao T.-P., Evans R.M., McKeown M.;
RT "Identification and characterization of a Drosophila nuclear receptor with
RT the ability to inhibit the ecdysone response.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10477-10481(1995).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14599492; DOI=10.1016/j.ibmb.2003.06.011;
RA Astle J., Kozlova T., Thummel C.S.;
RT "Essential roles for the Dhr78 orphan nuclear receptor during molting of
RT the Drosophila tracheal system.";
RL Insect Biochem. Mol. Biol. 33:1201-1209(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Binds to direct repeats of the sequence 5'-AGGTCA-3'.
CC Inhibits the ecdysone response. Plays an essential role in regulating
CC molting of the tracheal cuticle during larval development.
CC {ECO:0000269|PubMed:14599492, ECO:0000269|PubMed:7479823,
CC ECO:0000269|PubMed:7479849}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7479823}.
CC -!- INTERACTION:
CC Q24142; P13098: E(spl)m8-HLH; NbExp=3; IntAct=EBI-163133, EBI-185388;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:7479823}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=C, D;
CC IsoId=Q24142-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q24142-2; Sequence=VSP_015110;
CC -!- DEVELOPMENTAL STAGE: Highest expression in third instar larvae and
CC prepupae. {ECO:0000269|PubMed:7479823, ECO:0000269|PubMed:7479849}.
CC -!- INDUCTION: By 20-hydroxyecdysone (20HE) 106 hours after egg laying.
CC {ECO:0000269|PubMed:7479849}.
CC -!- DISRUPTION PHENOTYPE: Death during the larval stages, due to defects in
CC tracheal development characterized by fluid filling of the second
CC instar tracheae. Mutant larvae that survive into the third instar are
CC smaller than wild-type larvae and fail to pupariate.
CC {ECO:0000269|PubMed:14599492}.
CC -!- MISCELLANEOUS: [Isoform A]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; U36791; AAC46927.1; -; mRNA.
DR EMBL; U31517; AAC46924.1; -; mRNA.
DR EMBL; AE014296; AAF51731.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12168.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12169.1; -; Genomic_DNA.
DR EMBL; AE014296; AAS65089.1; -; Genomic_DNA.
DR EMBL; AY058317; AAL13546.1; -; mRNA.
DR RefSeq; NP_001189151.1; NM_001202222.1. [Q24142-1]
DR RefSeq; NP_001189152.1; NM_001202223.1. [Q24142-1]
DR RefSeq; NP_524203.2; NM_079479.5. [Q24142-2]
DR RefSeq; NP_730636.1; NM_168907.3. [Q24142-1]
DR RefSeq; NP_730637.1; NM_168908.3. [Q24142-1]
DR RefSeq; NP_996137.1; NM_206415.3. [Q24142-1]
DR AlphaFoldDB; Q24142; -.
DR SMR; Q24142; -.
DR BioGRID; 65625; 278.
DR IntAct; Q24142; 274.
DR STRING; 7227.FBpp0089291; -.
DR iPTMnet; Q24142; -.
DR PaxDb; Q24142; -.
DR DNASU; 40378; -.
DR EnsemblMetazoa; FBtr0078389; FBpp0078044; FBgn0015239. [Q24142-1]
DR EnsemblMetazoa; FBtr0078390; FBpp0078045; FBgn0015239. [Q24142-1]
DR EnsemblMetazoa; FBtr0078391; FBpp0078046; FBgn0015239. [Q24142-2]
DR EnsemblMetazoa; FBtr0078392; FBpp0089291; FBgn0015239. [Q24142-1]
DR EnsemblMetazoa; FBtr0303653; FBpp0292670; FBgn0015239. [Q24142-1]
DR EnsemblMetazoa; FBtr0303654; FBpp0292671; FBgn0015239. [Q24142-1]
DR GeneID; 40378; -.
DR KEGG; dme:Dmel_CG7199; -.
DR CTD; 40378; -.
DR FlyBase; FBgn0015239; Hr78.
DR VEuPathDB; VectorBase:FBgn0015239; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000168581; -.
DR HOGENOM; CLU_007368_16_2_1; -.
DR InParanoid; Q24142; -.
DR OMA; GPMSIET; -.
DR PhylomeDB; Q24142; -.
DR Reactome; R-DME-383280; Nuclear Receptor transcription pathway.
DR SignaLink; Q24142; -.
DR BioGRID-ORCS; 40378; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40378; -.
DR PRO; PR:Q24142; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0015239; Expressed in wing disc and 46 other tissues.
DR ExpressionAtlas; Q24142; baseline and differential.
DR Genevisible; Q24142; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0035002; P:liquid clearance, open tracheal system; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; 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 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 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Receptor; Reference proteome; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..601
FT /note="Nuclear hormone receptor HR78"
FT /id="PRO_0000053591"
FT DOMAIN 329..596
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 49..124
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 52..72
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 88..107
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 140..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 119..121
FT /note="SDS -> T (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_015110"
FT CONFLICT 142
FT /note="S -> G (in Ref. 1; AAC46927)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..188
FT /note="ATPPVHSAPAT -> PRLQCTARQQR (in Ref. 2; AAC46924)"
FT /evidence="ECO:0000305"
FT CONFLICT 194..197
FT /note="ENIF -> AEYI (in Ref. 2; AAC46924)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="V -> A (in Ref. 1; AAC46927)"
FT /evidence="ECO:0000305"
FT CONFLICT 517..519
FT /note="LQQ -> FQH (in Ref. 2; AAC46924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 65393 MW; 82C48A2885EEAA0C CRC64;
MDGVKVETFI KSEENRAMPL IGGGSASGGT PLPGGGVGMG AGASATLSVE LCLVCGDRAS
GRHYGAISCE GCKGFFKRSI RKQLGYQCRG AMNCEVTKHH RNRCQFCRLQ KCLASGMRSD
SVQHERKPIV DRKEGIIAAA GSSSTSGGGN GSSTYLSGKS GYQQGRGKGH SVKAESAATP
PVHSAPATAF NLNENIFPMG LNFAELTQTL MFATQQQQQQ QQQHQQSGSY SPDIPKADPE
DDEDDSMDNS STLCLQLLAN SASNNNSQHL NFNAGEVPTA LPTTSTMGLI QSSLDMRVIH
KGLQILQPIQ NQLERNGNLS VKPECDSEAE DSGTEDAVDA ELEHMELDFE CGGNRSGGSD
FAINEAVFEQ DLLTDVQCAF HVQPPTLVHS YLNIHYVCET GSRIIFLTIH TLRKVPVFEQ
LEAHTQVKLL RGVWPALMAI ALAQCQGQLS VPTIIGQFIQ STRQLADIDK IEPLKISKMA
NLTRTLHDFV QELQSLDVTD MEFGLLRLIL LFNPTLLQQR KERSLRGYVR RVQLYALSSL
RRQGGIGGGE ERFNVLVARL LPLSSLDAEA MEELFFANLV GQMQMDALIP FILMTSNTSG
L
