HDAC8_DANRE
ID HDAC8_DANRE Reviewed; 378 AA.
AC Q7SXM0;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) 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; BC055541; AAH55541.1; -; mRNA.
DR RefSeq; NP_998596.1; NM_213431.1.
DR AlphaFoldDB; Q7SXM0; -.
DR SMR; Q7SXM0; -.
DR PaxDb; Q7SXM0; -.
DR GeneID; 406740; -.
DR KEGG; dre:406740; -.
DR CTD; 55869; -.
DR ZFIN; ZDB-GENE-040426-2772; hdac8.
DR eggNOG; KOG1342; Eukaryota.
DR eggNOG; KOG3635; Eukaryota.
DR InParanoid; Q7SXM0; -.
DR OrthoDB; 732770at2759; -.
DR PhylomeDB; Q7SXM0; -.
DR Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR Reactome; R-DRE-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-DRE-3214815; HDACs deacetylate histones.
DR Reactome; R-DRE-350054; Notch-HLH transcription pathway.
DR PRO; PR:Q7SXM0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
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 GO; GO:0007417; P:central nervous system development; IMP:ZFIN.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:ZFIN.
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 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..378
FT /note="Histone deacetylase 8"
FT /id="PRO_0000389509"
FT REGION 15..325
FT /note="Histone deacetylase"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 179
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 181
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 268
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
SQ SEQUENCE 378 AA; 41583 MW; ED4D6FD03D62C4DF CRC64;
MSEKSDSNDD KSRTRSVVYV YSPEYIQTCD SLSKVPNRAS MVHSLIEAYG LLKYMRVVKP
HVASIEEMAV FHTDSYLQHL HKISQDGDND DPQSADFGLG YDCPVVEGIF DYAAAVGGAT
LTAAQNLLDG KCDVAINWAG GWHHAKKDEA SGSCYVNDAV LGILKLREKY DRVLYVDVDL
HHGDGVEDAF SFTSKVMTVS LHKFSPGFFP GTGDVTDTGL GKGRWYAVNV PFEDGVRDDR
YCQTFTSVMQ EVKALFNPEA VVMQLGADTM AGDPMCSFNM TPVGVAKCLT YILGWELPTL
LLGGGGYNLA NTARCWTYLT GTVLGQTLSS EIPDHEFFTE YGPDYSLEIS PSCRPDRNES
QHLERVISTI KGNLKNVV
