RCOR_DROME
ID RCOR_DROME Reviewed; 590 AA.
AC Q59E36; A4V4S3; Q494F9; Q59E35; Q8MSX7; Q95TC9; Q9VWH3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=REST corepressor;
DE AltName: Full=CoREST;
GN Name=CoRest; ORFNames=CG33525;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-590 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 267-590 (ISOFORM 1/3).
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
RP AND INTERACTION WITH TTK; HDAC1 AND SU(VAR)3-3.
RX PubMed=15306652; DOI=10.1523/jneurosci.0238-04.2004;
RA Dallman J.E., Allopenna J., Bassett A., Travers A., Mandel G.;
RT "A conserved role but different partners for the transcriptional
RT corepressor CoREST in fly and mammalian nervous system formation.";
RL J. Neurosci. 24:7186-7193(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-34; SER-36 AND
RP SER-560, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-22; THR-25; THR-65;
RP SER-68; SER-69; THR-375; THR-411 AND SER-414, AND IDENTIFICATION BY MASS
RP 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: Essential component of a corepressor complex that represses
CC transcription of neuron-specific genes in non-neuronal cells. The BHC
CC complex is recruited by Ttk88 and probably acts by deacetylating and
CC demethylating specific sites on histones, thereby acting as a chromatin
CC modifier. May serve as a molecular beacon for the recruitment of
CC molecular machinery that imposes silencing across a chromosomal
CC interval. {ECO:0000269|PubMed:15306652}.
CC -!- SUBUNIT: Component of a complex that contains at least HDAC1/Rpd3,
CC CoRest and Su(var)3-3/Hdm. Interacts with neuronal repressor ttk/Ttk88.
CC {ECO:0000269|PubMed:15306652}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:15306652}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=F;
CC IsoId=Q59E36-2; Sequence=Displayed;
CC Name=2; Synonyms=A, C, D, dCRS;
CC IsoId=Q59E36-3; Sequence=VSP_017466, VSP_017467;
CC Name=3; Synonyms=E;
CC IsoId=Q59E36-4; Sequence=VSP_055323;
CC -!- TISSUE SPECIFICITY: Present in all of the tissues examined including
CC both glia and neurons of the CNS (at protein level). Expressed
CC ubiquitously in the embryo. In contrast, expression of isoform 3 is
CC highly enriched in the nervous system. {ECO:0000269|PubMed:15306652}.
CC -!- SIMILARITY: Belongs to the CoREST family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL25265.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM49876.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF48966.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09497.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09498.1; -; Genomic_DNA.
DR EMBL; AE014298; AAX52507.2; -; Genomic_DNA.
DR EMBL; AE014298; AAX52508.1; -; Genomic_DNA.
DR EMBL; BT023817; AAZ66324.1; -; mRNA.
DR EMBL; AY060226; AAL25265.1; ALT_INIT; mRNA.
DR EMBL; AY118507; AAM49876.1; ALT_INIT; mRNA.
DR RefSeq; NP_001014752.2; NM_001014752.4. [Q59E36-2]
DR RefSeq; NP_001014753.1; NM_001014753.3. [Q59E36-4]
DR RefSeq; NP_001014754.1; NM_001014754.1. [Q59E36-3]
DR RefSeq; NP_001014755.1; NM_001014755.2. [Q59E36-3]
DR RefSeq; NP_001014756.1; NM_001014756.2. [Q59E36-3]
DR AlphaFoldDB; Q59E36; -.
DR BioGRID; 59243; 13.
DR IntAct; Q59E36; 5.
DR iPTMnet; Q59E36; -.
DR PaxDb; Q59E36; -.
DR DNASU; 32941; -.
DR EnsemblMetazoa; FBtr0302859; FBpp0291999; FBgn0261573. [Q59E36-3]
DR EnsemblMetazoa; FBtr0302860; FBpp0292000; FBgn0261573. [Q59E36-3]
DR EnsemblMetazoa; FBtr0302861; FBpp0292001; FBgn0261573. [Q59E36-3]
DR EnsemblMetazoa; FBtr0302862; FBpp0292002; FBgn0261573. [Q59E36-4]
DR EnsemblMetazoa; FBtr0302864; FBpp0292004; FBgn0261573. [Q59E36-2]
DR GeneID; 32941; -.
DR KEGG; dme:Dmel_CG42687; -.
DR UCSC; CG33525-RA; d. melanogaster. [Q59E36-2]
DR CTD; 32941; -.
DR FlyBase; FBgn0261573; CoRest.
DR VEuPathDB; VectorBase:FBgn0261573; -.
DR eggNOG; KOG1194; Eukaryota.
DR GeneTree; ENSGT00940000154196; -.
DR HOGENOM; CLU_026741_2_0_1; -.
DR InParanoid; Q59E36; -.
DR Reactome; R-DME-3214815; HDACs deacetylate histones.
DR Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 32941; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 32941; -.
DR PRO; PR:Q59E36; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0261573; Expressed in wing disc and 21 other tissues.
DR ExpressionAtlas; Q59E36; baseline and differential.
DR Genevisible; Q59E36; DM.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0017053; C:transcription repressor complex; IPI:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; IMP:FlyBase.
DR GO; GO:2000619; P:negative regulation of histone H4-K16 acetylation; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF01448; ELM2; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Coiled coil; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..590
FT /note="REST corepressor"
FT /id="PRO_0000226784"
FT DOMAIN 90..175
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 176..227
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 302..353
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 256..283
FT /evidence="ECO:0000255"
FT COMPBIAS 14..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 65
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 375
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VAR_SEQ 265..273
FT /note="IQKNRQVME -> IIAVPAHIS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_017466"
FT VAR_SEQ 265..266
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055323"
FT VAR_SEQ 274..590
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_017467"
SQ SEQUENCE 590 AA; 62696 MW; 17B010081DB57AD7 CRC64;
MVLAERNTTD VVRNGRRSRG PSPNTHTTGG VTNSASLVGS GNNSGHSGNA NANEKTTTAV
PGAGTPESSD DDNSTKRNGK SKAKQSEYEE KIRVGRDYQA VCPPLVPEAE RRPEQMNERA
LLVWSPTKEI PDLKLEEYIS VAKEKYGYNG EQALGMLFWH KHDLERAVMD LANFTPFPDE
WTIEDKVLFE QAFQFHGKSF HRIRQMLPDK SIASLVKYYY SWKKTRHRSS AMDRQEKAIK
AVVKDGSENG SEVGSNEESD NDDKIQKNRQ VMEQLDKECE TINVDDVLSK PAAANTESAQ
PRISARWLPD EIQVALLAIR EYGKNFPTIA KVVATKTEAH VRTFYLNNRR RYNLDQIVKE
YEAGKSEESG AEEQTEPAVD AAAAGAATAS APSAADSTSA ASATADRKQS TENSNNGVET
MQESLPKKED PKKPELAAAV LKIGVAEAAD AVATVASSTA SGVIGAATSA SKPSTSATIT
IIDESDTATN SSSDVVTTGL ATSTGSSALS STTSAPASKT QTSSEELSAQ KSNPASGIAA
IGAATGGGQT ANSSGSKRDS SVLPVAEQPP AKKIALSTGG GSSVAEFLAN
