HDAC8_BOVIN
ID HDAC8_BOVIN Reviewed; 377 AA.
AC Q0VCB2;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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 cohesin complex protein SMC3 regulating release of
CC cohesin complexes from chromatin. May play a role in smooth muscle cell
CC contractility. In addition to protein deacetylase activity, also has
CC protein-lysine deacylase activity: acts as a protein decrotonylase by
CC mediating decrotonylation ((2E)-butenoyl) of histones.
CC {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 -!- SUBUNIT: Interacts with CBFA2T3 (By similarity). Interacts with
CC phosphorylated SMG5/EST1B; this interaction protects SMG5 from
CC ubiquitin-mediated degradation. Associates with alpha-SMA (smooth
CC muscle alpha-actin). {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 -!- PTM: Phosphorylated by PKA on serine 39. Phosphorylation reduces
CC deacetylase activity observed preferentially on histones H3 and H4 (By
CC similarity). {ECO:0000250|UniProtKB:Q9BY41}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC120257; AAI20258.1; -; mRNA.
DR RefSeq; NP_001069699.1; NM_001076231.2.
DR AlphaFoldDB; Q0VCB2; -.
DR SMR; Q0VCB2; -.
DR STRING; 9913.ENSBTAP00000054707; -.
DR PaxDb; Q0VCB2; -.
DR PRIDE; Q0VCB2; -.
DR GeneID; 540666; -.
DR KEGG; bta:540666; -.
DR CTD; 55869; -.
DR eggNOG; KOG1342; Eukaryota.
DR InParanoid; Q0VCB2; -.
DR OrthoDB; 732770at2759; -.
DR Proteomes; UP000009136; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR GO; GO:0071922; P:regulation of cohesin loading; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007062; P:sister chromatid cohesion; ISS:UniProtKB.
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; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..377
FT /note="Histone deacetylase 8"
FT /id="PRO_0000389507"
FT REGION 14..324
FT /note="Histone deacetylase"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 178
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 180
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 267
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY41"
SQ SEQUENCE 377 AA; 41683 MW; 1120A71660F14E7D CRC64;
MEESEEPADA GQSLPPVYIY SPEYVSVCDS LAKVPKRASM VHSLIEAYAL HKQMRIVKPK
VASMEEMASF HTDAYLQHLQ KVSEDGDDDH PDSIEYGLGY DCPATEGIFD YAAAVGGATI
TAAQCLIDGM CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFD RILYVDLDLH
HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG TGDVSDVGLG KGRYYSVNVP IQDCIQDERY
YHICESVLKE VYIAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY ILQWELATLI
LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP SCRPDRNEPH
RVQQILNYIK GNLKHVV
