ID   HDA4_CAEBR              Reviewed;         892 AA.
AC   Q613L4; A8XNN9;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Histone deacetylase 4;
DE            EC=3.5.1.98;
GN   Name=hda-4; ORFNames=CBG16328;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC       N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC       deacetylation gives a tag for epigenetic repression and plays an
CC       important role in transcriptional regulation, cell cycle progression
CC       and developmental events. Histone deacetylases act via the formation of
CC       large multiprotein complexes (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; HE600961; CAP34128.1; -; Genomic_DNA.
DR   RefSeq; XP_002643599.1; XM_002643553.1.
DR   AlphaFoldDB; Q613L4; -.
DR   SMR; Q613L4; -.
DR   STRING; 6238.CBG16328; -.
DR   GeneID; 8585593; -.
DR   KEGG; cbr:CBG_16328; -.
DR   CTD; 8585593; -.
DR   WormBase; CBG16328; CBP46312; WBGene00036299; Cbr-hda-4.
DR   eggNOG; KOG1343; Eukaryota.
DR   HOGENOM; CLU_006530_0_0_1; -.
DR   InParanoid; Q613L4; -.
DR   OMA; QKVIAIH; -.
DR   OrthoDB; 1484694at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR   GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR000286; His_deacetylse.
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   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; SSF52768; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Hydrolase; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..892
FT                   /note="Histone deacetylase 4"
FT                   /id="PRO_0000114741"
FT   REGION          145..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..822
FT                   /note="Histone deacetylase"
FT   COMPBIAS        145..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        628
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   892 AA;  97039 MW;  0BF5A1AABCF1106A CRC64;
     MAFFSSSSSS FPVVFARMEE ASSSTGSTGG AMAGIPVIPS TSAALLANTN LEPERIAVLQ
     TQLQEYRQKQ MDLIGHFQRA QQELSVQHMH NLYTALQQQQ QLQSLQERSG INPMLISQTS
     EDATSGPAAP LSLANSLTNL LSSSNGNLSN LSVPQTPTKE HHPTLPPQQP SAPTSSRKSD
     LPRTNSTTIS QLTKDRLKNM IANRSKGESN SQSNLMSNVN GHDNSRRLKN SNSQMNVSSP
     HFEPYRLPTS LANAHNLQQA SEFQLRKVNS EPNLKMKIRA KLLSKGNSPV QHVQQTNNSQ
     FSFTHPQLKR SDSETSNMPI DMLPSGSHSN IPHLMLPSPS LPNLAAATGA FQNLNLPIGQ
     DLTAFMAVAN LSPFLSLPSL LNKKLELGGM TDEGDRNGFS SSASNSSLAS NASLGSHQYQ
     SLLKQQIRDL VLRRKSLVRE DPEGEGMAES YNGLFSHAKL QQLTALAMES GFNPKLEPTF
     STGLGYDPLM ARHECVCSNN SNHVENGERI QRIWSKLTEE GHVAKCERIT AKKASLEQLQ
     MVHSQTYTTF FAVSPTACLK IDANALPLKR FLQLPCGGIG IDSDTYFNDA STQIAARLAA
     GTLIELSSQV AEGRLKNGFA CIRPPGHHAE AEQALGFCFF NNVAVTAKVL QAKYPVQCAK
     IAIIDWDVHH GNGTQLSFDD DPNVLYMSLH RHDNGNFFPG TGSVTEIGKG AGKGFSVNIP
     FSGGVMKDAE YLAAWRTVVE PVLASFCPDF ILVSAGFDAC HGHVNALGGY EITPEMFGYM
     TKCLLSYANG KVVLALEGGY NLDSISAAAE QCVQALIGES DDAGRLCTDS LENLPNQSAL
     ETLQKVIAIH KGFWPALHGQ EAAINTTEMQ WRNVKLQVQM QQQQQLQQQL QQ