GenomeNet

Database: UniProt/SWISS-PROT
Entry: HDAC8_XENLA
LinkDB: HDAC8_XENLA
Original site: HDAC8_XENLA 
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   22-NOV-2017, entry version 66.
DE   RecName: Full=Histone deacetylase 8;
DE            Short=HD8;
DE            EC=3.5.1.98;
GN   Name=hdac8;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC       Note=Binds 1 divalent metal cation per subunit.;
CC   -!- ENZYME REGULATION: Its activity is inhibited by trichostatin A
CC       (TSA) and butyrate, 2 well known histone deacetylase inhibitors.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
DR   EMBL; BC073234; AAH73234.1; -; mRNA.
DR   RefSeq; NP_001085711.1; NM_001092242.1.
DR   UniGene; Xl.7001; -.
DR   ProteinModelPortal; Q6GPA7; -.
DR   SMR; Q6GPA7; -.
DR   GeneID; 444137; -.
DR   KEGG; xla:444137; -.
DR   CTD; 444137; -.
DR   Xenbase; XB-GENE-5863488; hdac8.
DR   HOVERGEN; HBG057112; -.
DR   KO; K11405; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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   PANTHER; PTHR10625; PTHR10625; 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; SSF52768; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN         1    325       Histone deacetylase 8.
FT                                /FTId=PRO_0000389510.
FT   REGION        1    272       Histone deacetylase. {ECO:0000250}.
FT   ACT_SITE     91     91       Proton acceptor. {ECO:0000250}.
FT   METAL       126    126       Divalent metal cation. {ECO:0000250}.
FT   METAL       128    128       Divalent metal cation. {ECO:0000250}.
FT   METAL       215    215       Divalent metal cation. {ECO:0000250}.
FT   BINDING      49     49       Substrate. {ECO:0000250}.
FT   BINDING      99     99       Substrate; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   BINDING     254    254       Substrate. {ECO:0000250}.
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
//
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