ID   HDAC8_XENLA             Reviewed;         325 AA.
AC   Q6GPA7;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Histone deacetylase 8;
DE            Short=HD8;
DE            EC=3.5.1.98 {ECO:0000250|UniProtKB:Q9BY41};
DE   AltName: Full=Protein deacetylase HDAC8 {ECO:0000305};
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q9BY41};
DE   AltName: Full=Protein decrotonylase HDAC8 {ECO:0000305};
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q9BY41};
GN   Name=hdac8;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone deacetylase that catalyzes the deacetylation of
CC       lysine residues on the N-terminal part of the core histones (H2A, H2B,
CC       H3 and H4). Histone deacetylation gives a tag for epigenetic repression
CC       and plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via the
CC       formation of large multiprotein complexes. Also involved in the
CC       deacetylation of non-histone proteins. In addition to protein
CC       deacetylase activity, also has protein-lysine deacylase activity: acts
CC       as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl)
CC       of histones. {ECO:0000250|UniProtKB:Q9BY41}.
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         Evidence={ECO:0000250|UniProtKB:Q9BY41};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC         Evidence={ECO:0000250|UniProtKB:Q9BY41};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-
CC         [protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:Q9BY41};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC         Evidence={ECO:0000250|UniProtKB:Q9BY41};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate
CC         + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:35899, ChEBI:CHEBI:137954;
CC         Evidence={ECO:0000250|UniProtKB:Q9BY41};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC         Evidence={ECO:0000250|UniProtKB:Q9BY41};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:Q9BY41};
CC       Note=Binds 1 divalent metal cation per subunit.
CC       {ECO:0000250|UniProtKB:Q9BY41};
CC   -!- ACTIVITY REGULATION: Its activity is inhibited by trichostatin A (TSA)
CC       and butyrate, 2 well known histone deacetylase inhibitors.
CC       {ECO:0000250|UniProtKB:Q9BY41}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BY41}.
CC       Chromosome {ECO:0000250|UniProtKB:Q9BY41}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9BY41}. Note=Excluded from the nucleoli. Found
CC       in the cytoplasm of cells showing smooth muscle differentiation.
CC       {ECO:0000250|UniProtKB:Q9BY41}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC073234; AAH73234.1; -; mRNA.
DR   RefSeq; NP_001085711.1; NM_001092242.1.
DR   AlphaFoldDB; Q6GPA7; -.
DR   SMR; Q6GPA7; -.
DR   DNASU; 444137; -.
DR   GeneID; 444137; -.
DR   KEGG; xla:444137; -.
DR   AGR; Xenbase:XB-GENE-5863488; -.
DR   CTD; 444137; -.
DR   Xenbase; XB-GENE-5863488; hdac8.L.
DR   OrthoDB; 1327607at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 444137; Expressed in egg cell and 19 other cell types or tissues.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004407; F:histone deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0160009; F:histone decrotonylase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd10000; HDAC8; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 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   PANTHER; PTHR10625:SF39; HISTONE DEACETYLASE 8; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Chromosome; Cytoplasm; Hydrolase; Metal-binding;
KW   Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..325
FT                   /note="Histone deacetylase 8"
FT                   /id="PRO_0000389510"
FT   REGION          1..272
FT                   /note="Histone deacetylase"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT   BINDING         126
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT   BINDING         128
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT   BINDING         215
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT   BINDING         254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BY41"
SQ   SEQUENCE   325 AA;  36006 MW;  409E71978A0439AC CRC64;
     MSRVVKPKVA SMEEMAAFHT DAYLQHLHKV SEEGDNDDPE TLEYGLGYDC PITEGIYDYA
     AAVGGATLTA AEQLIEGKTR IAVNWPGGWH HAKKDEASGF CYLNDAVLGI LKLREKFDRV
     LYVDMDLHHG DGVEDAFSFT SKVMTVSLHK FSPGFFPGTG DVSDIGLGKG RYYSINVPLQ
     DGIQDDKYYQ ICEGVLKEVF TTFNPEAVVL QLGADTIAGD PMCSFNMTPE GIGKCLKYVL
     QWQLPTLILG GGGYHLPNTA RCWTYLTALI VGRTLSSEIP DHEFFTEYGP DYVLEITPSC
     RPDRNDTQKV QEILQSIKGN LKRVV
//