ID   HDA11_MACFA             Reviewed;         347 AA.
AC   Q9GKU5;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Histone deacetylase 11;
DE            Short=HD11;
DE            EC=3.5.1.98;
GN   Name=HDAC11; ORFNames=QccE-18183;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Interacts with HDAC6. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- MISCELLANEOUS: Its activity is inhibited by trapoxin, a known histone
CC       deacetylase inhibitor. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB18987.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB052134; BAB18987.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001270923.1; NM_001283994.1.
DR   RefSeq; XP_005547935.1; XM_005547878.2.
DR   RefSeq; XP_015300840.1; XM_015445354.1.
DR   AlphaFoldDB; Q9GKU5; -.
DR   SMR; Q9GKU5; -.
DR   STRING; 9541.XP_005547935.1; -.
DR   GeneID; 102133368; -.
DR   KEGG; mcf:102133368; -.
DR   CTD; 79885; -.
DR   eggNOG; KOG1344; Eukaryota.
DR   OrthoDB; 1037375at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; TAS:UniProtKB.
DR   GO; GO:0004407; F:histone deacetylase activity; TAS:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
DR   GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR   CDD; cd09993; HDAC_classIV; 1.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR044150; HDAC_classIV.
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   2: Evidence at transcript level;
KW   Chromatin regulator; Hydrolase; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..347
FT                   /note="Histone deacetylase 11"
FT                   /id="PRO_0000114716"
FT   REGION          14..318
FT                   /note="Histone deacetylase"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   347 AA;  39179 MW;  4C3DADC2D8770B0D CRC64;
     MLHTTQLYQH VPETRWPIVY SPRYNITFMG LEKLHPFDAG KWGKVINFLK EEKLLSDSML
     VEAREASEED LLVVHTRRYL NELKWSFAVA TITEIPPVIF LPNFLVQRKV LRPLRTQTGG
     TIMAGKLAVE RGWAINVGGG FHHCSSDRGG GFCAYADITL AIKFLFERVE GISRATIIDL
     DAHQGNGHER DFMDDKRVYI MDVYNRHIYP GDRFAKQAIR RKVELEWGTE DDEYLDKVER
     NIEKSLQEHL PDVVVYNAGT DILEGDRLGG LSISPAGIVK RDELVFRMVR GRHVPILMVT
     SGGYQKRTAR IIADSILNLF GLGLIGPESP SISAQNSDTP LLPPAVP