ID HDAC8_XENTR Reviewed; 369 AA.
AC B1H369;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2008) 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; BC161282; AAI61282.1; -; mRNA.
DR RefSeq; NP_001120462.1; NM_001126990.1.
DR AlphaFoldDB; B1H369; -.
DR SMR; B1H369; -.
DR STRING; 8364.ENSXETP00000048414; -.
DR PaxDb; 8364-ENSXETP00000044353; -.
DR Ensembl; ENSXETT00000095452; ENSXETP00000091308; ENSXETG00000020527.
DR Ensembl; ENSXETT00000112302; ENSXETP00000114551; ENSXETG00000020527.
DR GeneID; 100145561; -.
DR KEGG; xtr:100145561; -.
DR AGR; Xenbase:XB-GENE-5863426; -.
DR CTD; 55869; -.
DR Xenbase; XB-GENE-5863426; hdac8.
DR eggNOG; KOG1342; Eukaryota.
DR HOGENOM; CLU_007727_7_6_1; -.
DR InParanoid; B1H369; -.
DR OMA; CFWHSTG; -.
DR OrthoDB; 1327607at2759; -.
DR PhylomeDB; B1H369; -.
DR TreeFam; TF106175; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Bgee; ENSXETG00000020527; Expressed in 4-cell stage embryo and 13 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..369
FT /note="Histone deacetylase 8"
FT /id="PRO_0000389511"
FT REGION 5..316
FT /note="Histone deacetylase"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 170
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 259
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
SQ SEQUENCE 369 AA; 41006 MW; 9ED5BBE73D188A75 CRC64;
MEESLLPVYI HSAEYVELCD NVQSKVPRRA SMVHSLIEAY GLLKEMRVVK PKVASMEEMA
AFHTDSYLQH LHKVSEEGDN DDPETLEYGL GYDCPITEGI YDYAAAVGGA TLTAAEQLMA
GKTRIAINWP GGWHHAKKDE ASGFCYLNDA VLGILKLREK FDRVLYVDMD LHHGDGVEDA
FSFTSKVMTV SLHKFSPGFF PGTGDVSDIG LGKGRYYSVN VPLQDGIQDE KYYQICEGVL
KEVFTTFNPE AVVLQLGADT IAGDPMCSFN MTPQGIGKCL KYVLQWQLPT LILGGGGYHL
PNTARCWTYL TALIVGRTLS SEIPDHEFFT EYGPDYVLEV TPSCRPDRND SQKVQEILQS
IKGHLKQVV
//
