HDA2_CAEEL
ID HDA2_CAEEL Reviewed; 507 AA.
AC Q09440;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Putative histone deacetylase 2;
DE EC=3.5.1.98;
GN Name=hda-2; ORFNames=C08B11.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND IDENTIFICATION IN HISTONE DEACETYLASE COMPLEX.
RX PubMed=21573134; DOI=10.1371/journal.pgen.1002065;
RA Hao Y., Xu N., Box A.C., Schaefer L., Kannan K., Zhang Y., Florens L.,
RA Seidel C., Washburn M.P., Wiegraebe W., Mak H.Y.;
RT "Nuclear cGMP-dependent kinase regulates gene expression via activity-
RT dependent recruitment of a conserved histone deacetylase complex.";
RL PLoS Genet. 7:E1002065-E1002065(2011).
CC -!- FUNCTION: Probably responsible for the deacetylation of lysine residues
CC on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (By
CC similarity). Histone deacetylation gives a tag for epigenetic
CC repression and plays an important role in transcriptional regulation,
CC cell cycle progression and developmental events (By similarity).
CC Histone deacetylases act via the formation of large multiprotein
CC complexes (By similarity). As a likely component of a histone
CC deacetylase complex, together with saeg-1 and hda-2, functions
CC downstream of the cAMP-dependent kinase egl-4 to regulate the
CC expression of genes required for egg-laying and forgaging
CC (PubMed:21573134). {ECO:0000250|UniProtKB:Q92769,
CC ECO:0000269|PubMed:21573134}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC -!- SUBUNIT: May be a component of a histone deacetylase complex containing
CC saeg-2, saeg-1 and hda-2. {ECO:0000269|PubMed:21573134}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; Z46676; CAA86662.1; -; Genomic_DNA.
DR PIR; T19067; T19067.
DR RefSeq; NP_495678.1; NM_063277.5.
DR AlphaFoldDB; Q09440; -.
DR SMR; Q09440; -.
DR BioGRID; 39617; 4.
DR IntAct; Q09440; 1.
DR MINT; Q09440; -.
DR STRING; 6239.C08B11.2; -.
DR EPD; Q09440; -.
DR PaxDb; Q09440; -.
DR PeptideAtlas; Q09440; -.
DR EnsemblMetazoa; C08B11.2.1; C08B11.2.1; WBGene00001835.
DR GeneID; 174285; -.
DR KEGG; cel:CELE_C08B11.2; -.
DR UCSC; C08B11.2; c. elegans.
DR CTD; 174285; -.
DR WormBase; C08B11.2; CE01472; WBGene00001835; hda-2.
DR eggNOG; KOG1342; Eukaryota.
DR GeneTree; ENSGT00940000160487; -.
DR HOGENOM; CLU_007727_7_1_1; -.
DR InParanoid; Q09440; -.
DR OMA; RMIRGAP; -.
DR OrthoDB; 732770at2759; -.
DR PhylomeDB; Q09440; -.
DR PRO; PR:Q09440; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001835; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000118; C:histone deacetylase complex; ISS:WormBase.
DR GO; GO:0004407; F:histone deacetylase activity; ISS:WormBase.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:WormBase.
DR GO; GO:0006325; P:chromatin organization; ISS:WormBase.
DR GO; GO:0042262; P:DNA protection; IMP:WormBase.
DR GO; GO:0016575; P:histone deacetylation; ISS:WormBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR003084; His_deacetylse_1.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; SSF52768; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Hydrolase; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..507
FT /note="Putative histone deacetylase 2"
FT /id="PRO_0000114720"
FT REGION 29..342
FT /note="Histone deacetylase"
FT REGION 444..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 162
FT /evidence="ECO:0000250"
SQ SEQUENCE 507 AA; 57138 MW; F500D405F7595BAF CRC64;
MSSDKFKLDT LFDDNDEIIE PDGADVKKRN VAYYYHKDVG HFHYGQLHPM KPQRLVVCND
LVVSYEMPKY MTVVESPKLD AADISVFHTE DYVNFLQTVT PKLGLTMPDD VLRQFNIGED
CPIFAGLWDY CTLYAGGSVE GARRLNHKMN DIVINWPGGL HHAKKSEASG FCYVNDIVLG
ILELLKYHKR VLYIDIDIHH GDGVQEAFNN SDRVMTVSFH RFGQYFPGSG SIMDKGVGPG
KYFAINVPLM AAIRDEPYLK LFESVISGVE ENFNPEAIVL QCGSDSLCED RLGQFALSFN
AHARAVKYVK SLGKPLMVLG GGGYTLRNVA RCWALETGVI LGLRMDDEIP GTSLYSHYFT
PRLLRPNLVP KMNDANSAAY LASIEKETLA CLRMIRGAPS VQMQNIVGIR LDEIEQIEEN
ERLQKSSKSS IEYEVGKVSE KMEEECFVEE DSKPPSFPPG QDPRRIGQYW GYDRSGLAPP
RSHSDVIEEA KYEDRDRRKD LNIPGIP
