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Histone deacetylase 8 (HD8) (EC 3.5.1.98)

 HDAC8_RAT               Reviewed;         377 AA.
B1WC68;
24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
20-MAY-2008, sequence version 1.
12-SEP-2018, entry version 74.
RecName: Full=Histone deacetylase 8;
Short=HD8;
EC=3.5.1.98;
Name=Hdac8;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Responsible for the deacetylation of lysine residues on
the N-terminal part of the core histones (H2A, H2B, H3 and H4).
Histone deacetylation gives a tag for epigenetic repression and
plays an important role in transcriptional regulation, cell cycle
progression and developmental events. Histone deacetylases act via
the formation of large multiprotein complexes. Also involved in
the deacetylation of cohesin complex protein SMC3 regulating
release of cohesin complexes from chromatin. May play a role in
smooth muscle cell contractility (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Note=Binds 1 divalent metal cation per subunit.;
-!- ACTIVITY REGULATION: Its activity is inhibited by trichostatin A
(TSA) and butyrate, 2 well known histone deacetylase inhibitors.
{ECO:0000250}.
-!- SUBUNIT: Interacts with CBFA2T3. Interacts with phosphorylated
SMG5/EST1B; this interaction protects SMG5 from ubiquitin-mediated
degradation. Associates with alpha-SMA (smooth muscle alpha-actin)
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}.
-!- PTM: Phosphorylated by PKA on serine 39. Phosphorylation reduces
deacetylase activity observed preferentially on histones H3 and H4
(By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
subfamily. {ECO:0000305}.
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EMBL; BC162023; AAI62023.1; -; mRNA.
RefSeq; NP_001119845.2; NM_001126373.2.
UniGene; Rn.208476; -.
ProteinModelPortal; B1WC68; -.
SMR; B1WC68; -.
STRING; 10116.ENSRNOP00000004224; -.
iPTMnet; B1WC68; -.
PhosphoSitePlus; B1WC68; -.
PaxDb; B1WC68; -.
PeptideAtlas; B1WC68; -.
Ensembl; ENSRNOT00000004224; ENSRNOP00000004224; ENSRNOG00000003122.
GeneID; 363481; -.
KEGG; rno:363481; -.
UCSC; RGD:1562895; rat.
CTD; 55869; -.
RGD; 1562895; Hdac8.
eggNOG; KOG1342; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00910000144047; -.
HOGENOM; HOG000225180; -.
HOVERGEN; HBG057112; -.
InParanoid; B1WC68; -.
KO; K11405; -.
OMA; CGYDANA; -.
OrthoDB; EOG091G0A9R; -.
PhylomeDB; B1WC68; -.
TreeFam; TF106175; -.
Reactome; R-RNO-2467813; Separation of Sister Chromatids.
Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
PRO; PR:B1WC68; -.
Proteomes; UP000002494; Chromosome X.
Bgee; ENSRNOG00000003122; Expressed in 9 organ(s), highest expression level in colon.
Genevisible; B1WC68; RN.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IDA:RGD.
GO; GO:0019213; F:deacetylase activity; IDA:RGD.
GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:1904322; P:cellular response to forskolin; IDA:RGD.
GO; GO:0035984; P:cellular response to trichostatin A; IDA:RGD.
GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; IMP:RGD.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:RGD.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:0071922; P:regulation of cohesin loading; ISS:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
GO; GO:0032204; P:regulation of telomere maintenance; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007062; P:sister chromatid cohesion; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR003084; His_deacetylse_1.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR037138; His_deacetylse_dom_sf.
InterPro; IPR023696; Ureohydrolase_dom_sf.
PANTHER; PTHR10625; PTHR10625; 1.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037913; His_deacetylse_1; 1.
PRINTS; PR01270; HDASUPER.
PRINTS; PR01271; HISDACETLASE.
SUPFAM; SSF52768; SSF52768; 1.
2: Evidence at transcript level;
Chromatin regulator; Complete proteome; Cytoplasm; Hydrolase;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
Transcription; Transcription regulation.
CHAIN 1 377 Histone deacetylase 8.
/FTId=PRO_0000389508.
REGION 14 324 Histone deacetylase. {ECO:0000250}.
ACT_SITE 143 143 Proton acceptor. {ECO:0000250}.
METAL 178 178 Divalent metal cation. {ECO:0000250}.
METAL 180 180 Divalent metal cation. {ECO:0000250}.
METAL 267 267 Divalent metal cation. {ECO:0000250}.
BINDING 101 101 Substrate. {ECO:0000250}.
BINDING 151 151 Substrate; via carbonyl oxygen.
{ECO:0000250}.
BINDING 306 306 Substrate. {ECO:0000250}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BY41}.
SEQUENCE 377 AA; 41754 MW; AC7D7A3114663505 CRC64;
MEIPEEPANS GHSLPPVYIY SPEYVSICDS LVKVPKRASM VHSLIEAYAL HKQMRIVKPK
VASMEEMATF HTDAYLQHLQ KVSQEGDEDH PDSIEYGLGY DCPATEGIFD YAAAIGGGTI
TAAQCLIDGK CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFD RILYVDLDLH
HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG TGDMSDVGLG KGRYYSVNVP IQDGIQDEKY
YHICESVLKE VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY VLQWQLATLI
LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP SCRPDRNEPH
RIQQILNYIK GNLKHVV


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