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Histone deacetylase Rpd3 (HD) (dRPD3) (EC 3 5 1 98)

 HDAC1_DROME             Reviewed;         521 AA.
Q94517; O17429; O77213; Q9VZA1;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 2.
23-MAY-2018, entry version 169.
RecName: Full=Histone deacetylase Rpd3;
Short=HD;
Short=dRPD3;
EC=3.5.1.98;
Name=Rpd3; Synonyms=HDAC1; ORFNames=CG7471;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryo;
PubMed=8955276; DOI=10.1038/384589a0;
de Rubertis F., Kadosh D., Henchoz S., Pauli D., Reuter G., Struhl K.,
Spierer P.;
"The histone deacetylase RPD3 counteracts genomic silencing in
Drosophila and yeast.";
Nature 384:589-591(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10655219;
Mottus R., Sobel R.E., Grigliatti T.A.;
"Mutational analysis of a histone deacetylase in Drosophila
melanogaster: missense mutations suppress gene silencing associated
with position effect variegation.";
Genetics 154:657-668(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Johnson C.A., White D., O'Neill L.P., Turner B.M.;
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Ovary;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[7]
INTERACTION WITH SU(VAR)3-9.
PubMed=11571273; DOI=10.1093/embo-reports/kve210;
Czermin B., Schotta G., Huelsmann B.B., Brehm A., Becker P.B.,
Reuter G., Imhof A.;
"Physical and functional association of SU(VAR)3-9 and HDAC1 in
Drosophila.";
EMBO Rep. 2:915-919(2001).
[8]
IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1; ESC AND E(Z).
PubMed=12533794; DOI=10.1002/gene.10173;
Furuyama T., Tie F., Harte P.J.;
"Polycomb group proteins ESC and E(Z) are present in multiple distinct
complexes that undergo dynamic changes during development.";
Genesis 35:114-124(2003).
[9]
IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1; ESC; E(Z) AND
SU(Z)12, AND METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
PubMed=12408863; DOI=10.1016/S0092-8674(02)00975-3;
Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.;
"Drosophila Enhancer of zeste/ESC complexes have a histone H3
methyltransferase activity that marks chromosomal Polycomb sites.";
Cell 111:185-196(2002).
[10]
IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1; ESC; E(Z); PCL AND
SU(Z)12.
PubMed=12697833; DOI=10.1128/MCB.23.9.3352-3362.2003;
Tie F., Prasad-Sinha J., Birve A., Rasmuson-Lestander A., Harte P.J.;
"A 1-megadalton ESC/E(Z) complex from Drosophila that contains
polycomblike and RPD3.";
Mol. Cell. Biol. 23:3352-3362(2003).
[11]
IDENTIFICATION IN THE DREAM COMPLEX.
PubMed=15545624; DOI=10.1101/gad.1255204;
Lewis P.W., Beall E.L., Fleischer T.C., Georlette D., Link A.J.,
Botchan M.R.;
"Identification of a Drosophila Myb-E2F2/RBF transcriptional repressor
complex.";
Genes Dev. 18:2929-2940(2004).
[12]
INTERACTION WITH COREST.
PubMed=15306652; DOI=10.1523/JNEUROSCI.0238-04.2004;
Dallman J.E., Allopenna J., Bassett A., Travers A., Mandel G.;
"A conserved role but different partners for the transcriptional
corepressor CoREST in fly and mammalian nervous system formation.";
J. Neurosci. 24:7186-7193(2004).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-419; SER-421;
SER-455 AND THR-457, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Catalyzes the deacetylation of lysine residues on the N-
terminal part of the core histones (H2A, H2B, H3 and H4). Histone
deacetylation may constitute a tag for epigenetic repression and
plays an important role in transcriptional regulation, cell cycle
progression and developmental events. For instance, deacetylation
of histone H3 may be a prerequisite for the subsequent recruitment
of the histone methyltransferase Su(var)3-9 to histones. Involved
in position-effect variegation (PEV).
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- SUBUNIT: Interacts with Su(var)3-9. Component of a form of the
Esc/E(z) complex present specifically during early embryogenesis
which is composed of Caf1, esc, E(z), Su(z)12, Pcl and Rpd3. The
Esc/E(z) complex may also associate with Pcl and Rpd3 during early
embryogenesis. This complex is distinct from the PRC1 complex,
which contains many other PcG proteins like Pc, Ph, Psc, Su(z)2.
The 2 complexes however cooperate and interact together during the
first 3 hours of development to establish PcG silencing. Interacts
with the histone methyltransferase Su(var)3-9. Component of a
complex that contains at least Rpd3, CoRest and Su(var)3-3/Hdm.
Component of the DREAM complex at least composed of Myb, Caf1,
mip40, mip120, mip130, E2f2, Dp, Rbf, Rbf2, lin-52, Rpd3 and
l(3)mbt. Interacts with neuronal repressor Ttk88.
{ECO:0000269|PubMed:11571273, ECO:0000269|PubMed:12408863,
ECO:0000269|PubMed:12533794, ECO:0000269|PubMed:12697833,
ECO:0000269|PubMed:15306652, ECO:0000269|PubMed:15545624}.
-!- INTERACTION:
Q24572:Caf1; NbExp=4; IntAct=EBI-302197, EBI-75924;
P42124:E(z); NbExp=9; IntAct=EBI-302197, EBI-112315;
Q24338:esc; NbExp=11; IntAct=EBI-302197, EBI-88911;
A1Z9E2:mip120; NbExp=2; IntAct=EBI-302197, EBI-75953;
Q24459:Pcl; NbExp=5; IntAct=EBI-302197, EBI-430086;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y09258; CAA70455.1; -; mRNA.
EMBL; AF086715; AAC61494.1; -; Genomic_DNA.
EMBL; AF026949; AAC23917.1; -; mRNA.
EMBL; AE014296; AAF47924.1; -; Genomic_DNA.
EMBL; AY058487; AAL13716.1; -; mRNA.
RefSeq; NP_647918.2; NM_139661.4.
UniGene; Dm.2976; -.
ProteinModelPortal; Q94517; -.
SMR; Q94517; -.
BioGrid; 64037; 62.
DIP; DIP-29512N; -.
IntAct; Q94517; 19.
MINT; Q94517; -.
STRING; 7227.FBpp0073173; -.
iPTMnet; Q94517; -.
PaxDb; Q94517; -.
PRIDE; Q94517; -.
EnsemblMetazoa; FBtr0073317; FBpp0073173; FBgn0015805.
GeneID; 38565; -.
KEGG; dme:Dmel_CG7471; -.
CTD; 3065; -.
FlyBase; FBgn0015805; Rpd3.
eggNOG; KOG1342; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00910000144047; -.
InParanoid; Q94517; -.
KO; K06067; -.
OMA; KRVCYFF; -.
OrthoDB; EOG091G067J; -.
PhylomeDB; Q94517; -.
Reactome; R-DME-1538133; G0 and Early G1.
Reactome; R-DME-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-DME-209394; Transcriptional activtion and repression of REL-68 target genes.
Reactome; R-DME-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-DME-3214815; HDACs deacetylate histones.
Reactome; R-DME-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
Reactome; R-DME-9018519; Estrogen-dependent gene expression.
Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
ChiTaRS; HDAC1; fly.
GenomeRNAi; 38565; -.
PRO; PR:Q94517; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0015805; -.
ExpressionAtlas; Q94517; baseline and differential.
Genevisible; Q94517; DM.
GO; GO:0000785; C:chromatin; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0035098; C:ESC/E(Z) complex; IDA:FlyBase.
GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
GO; GO:0031523; C:Myb complex; IDA:FlyBase.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0016581; C:NuRD complex; IPI:FlyBase.
GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
GO; GO:0005705; C:polytene chromosome interband; IDA:FlyBase.
GO; GO:0016580; C:Sin3 complex; NAS:FlyBase.
GO; GO:0070822; C:Sin3-type complex; IDA:FlyBase.
GO; GO:0017053; C:transcriptional repressor complex; IPI:FlyBase.
GO; GO:0004407; F:histone deacetylase activity; IDA:FlyBase.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0003714; F:transcription corepressor activity; IPI:FlyBase.
GO; GO:0008134; F:transcription factor binding; TAS:UniProtKB.
GO; GO:0007350; P:blastoderm segmentation; IMP:FlyBase.
GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
GO; GO:0006342; P:chromatin silencing; IMP:FlyBase.
GO; GO:0030261; P:chromosome condensation; IMP:FlyBase.
GO; GO:0070983; P:dendrite guidance; IMP:FlyBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
GO; GO:0016458; P:gene silencing; IMP:FlyBase.
GO; GO:0016575; P:histone deacetylation; IMP:FlyBase.
GO; GO:0050771; P:negative regulation of axonogenesis; IMP:FlyBase.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; IMP:UniProtKB.
GO; GO:0031061; P:negative regulation of histone methylation; IMP:UniProtKB.
GO; GO:2001229; P:negative regulation of response to gamma radiation; IMP:FlyBase.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IGI:FlyBase.
GO; GO:0048477; P:oogenesis; TAS:FlyBase.
GO; GO:0035065; P:regulation of histone acetylation; IMP:FlyBase.
GO; GO:1902692; P:regulation of neuroblast proliferation; IMP:UniProtKB.
GO; GO:0045664; P:regulation of neuron differentiation; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:FlyBase.
GO; GO:0022904; P:respiratory electron transport chain; IDA:FlyBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006099; P:tricarboxylic acid cycle; IDA:FlyBase.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR003084; His_deacetylse_1.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR037138; His_deacetylse_dom_sf.
InterPro; IPR023696; Ureohydrolase_dom_sf.
PANTHER; PTHR10625; PTHR10625; 1.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037913; His_deacetylse_1; 1.
PRINTS; PR01270; HDASUPER.
PRINTS; PR01271; HISDACETLASE.
SUPFAM; SSF52768; SSF52768; 1.
1: Evidence at protein level;
Chromatin regulator; Complete proteome; Developmental protein;
Hydrolase; Nucleus; Phosphoprotein; Reference proteome; Repressor;
Transcription; Transcription regulation.
CHAIN 1 521 Histone deacetylase Rpd3.
/FTId=PRO_0000114718.
REGION 7 319 Histone deacetylase.
ACT_SITE 139 139 {ECO:0000250}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 421 421 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 455 455 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 457 457 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 50 52 EIY -> DI (in Ref. 1; CAA70455).
{ECO:0000305}.
CONFLICT 67 67 S -> C (in Ref. 1; CAA70455).
{ECO:0000305}.
CONFLICT 97 97 D -> N (in Ref. 3; AAC23917).
{ECO:0000305}.
CONFLICT 106 106 E -> D (in Ref. 3; AAC23917).
{ECO:0000305}.
CONFLICT 296 296 V -> VV (in Ref. 3; AAC23917).
{ECO:0000305}.
CONFLICT 305 305 N -> K (in Ref. 1 and 3). {ECO:0000305}.
CONFLICT 371 371 L -> V (in Ref. 3; AAC23917).
{ECO:0000305}.
CONFLICT 507 507 S -> T (in Ref. 2 and 3). {ECO:0000305}.
SEQUENCE 521 AA; 58331 MW; B0F6503D42A1BCE9 CRC64;
MQSHSKKRVC YYYDSDIGNY YYGQGHPMKP HRIRMTHNLL LNYGLYRKME IYRPHKATAD
EMTKFHSDEY VRFLRSIRPD NMSEYNKQMQ RFNVGEDCPV FDGLYEFCQL SAGGSVAAAV
KLNKQASEIC INWGGGLHHA KKSEASGFCY VNDIVLGILE LLKYHQRVLY IDIDVHHGDG
VEEAFYTTDR VMTVSFHKYG EYFPGTGDLR DIGAGKGKYY AVNIPLRDGM DDDAYESIFV
PIISKVMETF QPAAVVLQCG ADSLTGDRLG CFNLTVKGHG KCVEFVKKYN LPFLMVGGGG
YTIRNVSRCW TYETSVALAV EIANELPYND YFEYFGPDFK LHISPSNMTN QNTSEYLEKI
KNRLFENLRM LPHAPGVQIQ AIPEDAINDE SDDEDKVDKD DRLPQSDKDK RIVPENEYSD
SEDEGEGGRR DNRSYKGQRK RPRLDKDTNS NKASSETSSE IKDEKEKGDG ADGEESTASN
TNSNNNSNNK SDNDAGATAN AGSGSGSGSG AGAKGAKENN I


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Tel 01 43 25 01 50

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GENTAUR GmbH
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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