ID ET96B_DROME Reviewed; 640 AA.
AC Q8MRW5; Q9VC38;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 170.
DE RecName: Full=ETV5-related protein Ets96B {ECO:0000305};
GN Name=Ets96B {ECO:0000312|FlyBase:FBgn0039225};
GN ORFNames=CG6892 {ECO:0000312|FlyBase:FBgn0039225};
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 {ECO:0000312|EMBL:AAM51090.1};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAM51090.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM51090.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM51090.1};
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Celniker S.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY STARVATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=27280443; DOI=10.1371/journal.pgen.1006104;
RA Williams M.J., Klockars A., Eriksson A., Voisin S., Dnyansagar R.,
RA Wiemerslage L., Kasagiannis A., Akram M., Kheder S., Ambrosi V.,
RA Hallqvist E., Fredriksson R., Schioeth H.B.;
RT "The Drosophila ETV5 homologue Ets96B: molecular link between obesity and
RT bipolar disorder.";
RL PLoS Genet. 12:E1006104-E1006104(2016).
CC -!- FUNCTION: Required in dopaminergic neurons to regulate expression of
CC genes involved in dopamine signaling. Decreases expression of the
CC dopamine transporter DAT and increases expression of the dopamine
CC transporter Vmat and the tyrosine 3-monooxygenase ple which is involved
CC in dopamine biosynthesis. Also involved in negatively regulating the
CC expression of a group of endoplasmic reticulum proteins, the molecular
CC chaperone Calr and the protein disulfide isomerases CaBP1 and ERp60.
CC {ECO:0000269|PubMed:27280443}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000255|PROSITE-
CC ProRule:PRU00237}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000312|FlyBase:FBgn0039225};
CC IsoId=Q8MRW5-1; Sequence=Displayed;
CC Name=C {ECO:0000312|FlyBase:FBgn0039225};
CC IsoId=Q8MRW5-2; Sequence=VSP_058542;
CC -!- TISSUE SPECIFICITY: In the adult brain, expressed almost exclusively in
CC dopaminergic neurons. {ECO:0000269|PubMed:27280443}.
CC -!- DEVELOPMENTAL STAGE: [Isoform C]: Expressed only in the adult.
CC {ECO:0000269|PubMed:27280443}.
CC -!- INDUCTION: By starvation. {ECO:0000269|PubMed:27280443}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the central nervous
CC system (CNS) during development increases the expression of CaBP1, Calr
CC and ERp60 and regulates expression of other genes involved in a variety
CC of processes including oxidative phosphorylation and redox reactions,
CC lipid and sugar homeostasis, and translation. It increases
CC susceptibility to starvation but has no effect on feeding behavior. It
CC increases triacylglyceride (TAG) levels in normal-fed flies but has no
CC effect on TAG levels 12 or 24 hours after starvation. It also induces a
CC heightened startle-response, increases hyperactivity and reduces sleep.
CC RNAi-mediated knockdown specifically in dopaminergic neurons throughout
CC development influences the expression of genes involved in dopamine
CC signaling by increasing expression of ple and Vmat and decreasing
CC expression of DAT. It also recapitulates the effects seen following CNS
CC knockdown, namely increased susceptibility to starvation, heightened
CC startle-response and reduced sleep. RNAi-mediated knockdown
CC specifically in the adult CNS increases resistance to starvation with
CC no effect on feeding behavior, decreases TAG levels in normal-fed flies
CC and has no effect on hyperactivity or sleep.
CC {ECO:0000269|PubMed:27280443}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000255,
CC ECO:0000255|RuleBase:RU004019}.
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DR EMBL; AE014297; AAF56337.3; -; Genomic_DNA.
DR EMBL; AE014297; AAS65212.1; -; Genomic_DNA.
DR EMBL; AY119230; AAM51090.1; -; mRNA.
DR RefSeq; NP_651286.3; NM_143029.3. [Q8MRW5-2]
DR RefSeq; NP_996290.1; NM_206567.2. [Q8MRW5-1]
DR AlphaFoldDB; Q8MRW5; -.
DR SMR; Q8MRW5; -.
DR IntAct; Q8MRW5; 2.
DR STRING; 7227.FBpp0089401; -.
DR PaxDb; 7227-FBpp0089401; -.
DR EnsemblMetazoa; FBtr0084697; FBpp0089401; FBgn0039225. [Q8MRW5-1]
DR EnsemblMetazoa; FBtr0339254; FBpp0308361; FBgn0039225. [Q8MRW5-2]
DR GeneID; 42952; -.
DR KEGG; dme:Dmel_CG6892; -.
DR UCSC; CG6892-RA; d. melanogaster.
DR UCSC; CG6892-RB; d. melanogaster. [Q8MRW5-1]
DR AGR; FB:FBgn0039225; -.
DR CTD; 42952; -.
DR FlyBase; FBgn0039225; Ets96B.
DR VEuPathDB; VectorBase:FBgn0039225; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000158142; -.
DR InParanoid; Q8MRW5; -.
DR OMA; TLMEAIC; -.
DR OrthoDB; 3915960at2759; -.
DR PhylomeDB; Q8MRW5; -.
DR Reactome; R-DME-5687128; MAPK6/MAPK4 signaling.
DR BioGRID-ORCS; 42952; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42952; -.
DR PRO; PR:Q8MRW5; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039225; Expressed in testis and 1 other cell type or tissue.
DR ExpressionAtlas; Q8MRW5; baseline and differential.
DR Genevisible; Q9VC38; DM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IMP:UniProtKB.
DR GO; GO:0060159; P:regulation of dopamine receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
DR GO; GO:0001964; P:startle response; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; ETS; 1.
DR PANTHER; PTHR11849:SF282; ETV5-RELATED PROTEIN ETS96B; 1.
DR Pfam; PF00178; Ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..640
FT /note="ETV5-related protein Ets96B"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437485"
FT DNA_BIND 498..579
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 315..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 321..356
FT /evidence="ECO:0000255"
FT COMPBIAS 317..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 2..15
FT /note="TISWRALSHFLIPQ -> DTAKL (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_058542"
SQ SEQUENCE 640 AA; 70284 MW; 80D1EE94AAE53F82 CRC64;
MTISWRALSH FLIPQSDYGE AKTHLEQLQQ TLTHLDHPHH HHAHHPHHHL GLYHGALPNT
STITTDSVVS CVSSTLPAVA KAISASSSCD GLQSERKKCP ISDLDSGGHG HGQGHGLMEA
ICAGQKTSPI PPPPPPCCLT LGESSSSPNP IATAALMNAS TSGSSSAGGA SASLCNDLTR
ESSWYAHHHH HHHHHHHQLP DELVMYATPT PTPAIGKFGL DTSTEGYLNA RYNVNVKGVR
HDRTSSFFDI PAVTHPHNHP HPHPHPHPHP YCYRFPSSPP AGILKKSDEE ATSAAVYCSD
VSSGQHFPHH TKIEHADSTT TAAQQQQQQQ EQQQQQQQQQ QQQQHQQQLQ QAAALHPHHH
HSHHGHHGHQ QAEQQALTHL TPLHAASAFK FSHTAVISSS AVYATPSHYA HQQQTQSQSV
YRDLSPTTLA AVSDADLKYD SGPYNAAISS TYPSALRPNV VDSTTSSDAE LRLDQFYASN
GISTSSNGQA ISQRRGSLQL WQFLVALLDE PTTSASCIAW TGRGMEFKLI EPEEVARRWG
LQKNRPAMNY DKLSRSLRYY YEKGIMQKVN GERYVYRFVC DPDALFNMAY GHLTTGSGKG
DQHQLTLSLA KTPPTSGDSQ TQSPRVAKSE YYDTAALHKY
//
