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Database: UniProt/SWISS-PROT
Entry: HDAC8_DANRE
LinkDB: HDAC8_DANRE
Original site: 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   22-NOV-2017, entry version 85.
DE   RecName: Full=Histone deacetylase 8;
DE            Short=HD8;
DE            EC=3.5.1.98;
GN   Name=hdac8;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; 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: 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; BC055541; AAH55541.1; -; mRNA.
DR   RefSeq; NP_998596.1; NM_213431.1.
DR   UniGene; Dr.3849; -.
DR   ProteinModelPortal; Q7SXM0; -.
DR   SMR; Q7SXM0; -.
DR   STRING; 7955.ENSDARP00000077625; -.
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   eggNOG; ENOG410XPJZ; LUCA.
DR   HOGENOM; HOG000225180; -.
DR   HOVERGEN; HBG057112; -.
DR   InParanoid; Q7SXM0; -.
DR   KO; K11405; -.
DR   PhylomeDB; Q7SXM0; -.
DR   PRO; PR:Q7SXM0; -.
DR   Proteomes; UP000000437; Unplaced.
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; Complete proteome; Cytoplasm; Hydrolase;
KW   Metal-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    378       Histone deacetylase 8.
FT                                /FTId=PRO_0000389509.
FT   REGION       15    325       Histone deacetylase. {ECO:0000250}.
FT   ACT_SITE    144    144       Proton acceptor. {ECO:0000250}.
FT   METAL       179    179       Divalent metal cation. {ECO:0000250}.
FT   METAL       181    181       Divalent metal cation. {ECO:0000250}.
FT   METAL       268    268       Divalent metal cation. {ECO:0000250}.
FT   BINDING     102    102       Substrate. {ECO:0000250}.
FT   BINDING     152    152       Substrate; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   BINDING     307    307       Substrate. {ECO:0000250}.
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
//
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