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Database: UniProt
Entry: A0A2K5W8M4_MACFA
LinkDB: A0A2K5W8M4_MACFA
Original site: A0A2K5W8M4_MACFA 
ID   A0A2K5W8M4_MACFA        Unreviewed;       255 AA.
AC   A0A2K5W8M4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Histone deacetylase 8 {ECO:0000256|ARBA:ARBA00040347};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE   AltName: Full=Protein deacetylase HDAC8 {ECO:0000256|ARBA:ARBA00041964};
DE   AltName: Full=Protein decrotonylase HDAC8 {ECO:0000256|ARBA:ARBA00042783};
GN   Name=HDAC8 {ECO:0000313|Ensembl:ENSMFAP00000033418.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000033418.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000033418.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000033418.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00029357};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC         Evidence={ECO:0000256|ARBA:ARBA00029357};
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:0000256|ARBA:ARBA00029372};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC         Evidence={ECO:0000256|ARBA:ARBA00029372};
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:0000256|ARBA:ARBA00029349};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC         Evidence={ECO:0000256|ARBA:ARBA00029349};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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DR   AlphaFoldDB; A0A2K5W8M4; -.
DR   SMR; A0A2K5W8M4; -.
DR   Ensembl; ENSMFAT00000007645.2; ENSMFAP00000033418.2; ENSMFAG00000003160.2.
DR   VEuPathDB; HostDB:ENSMFAG00000003160; -.
DR   GeneTree; ENSGT00940000157843; -.
DR   Proteomes; UP000233100; Chromosome X.
DR   Bgee; ENSMFAG00000003160; Expressed in pituitary gland and 13 other cell types or tissues.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0000118; C:histone deacetylase complex; IEA:UniProt.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProt.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 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:SF39; HISTONE DEACETYLASE 8; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT   DOMAIN          35..246
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
SQ   SEQUENCE   255 AA;  28533 MW;  D63801AEAB13F5F5 CRC64;
     MEEPEEPADS GQSLIPVYIY SPEYVSMCDS LAKIPKRASM VHSLIEAYAL HKQMRIVKPK
     VASMEEMATF HTDAYLQHLQ KVSQEGDDDH PDSIEYGLGY DCPATEGIFD YAAAVGGATI
     TAAQCLIDGM CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFE RILYVDLDLH
     HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG DVSDVGLGKG RYYSVNVPIQ DGIQDEKYYQ
     IFESDLILWQ QLNKF
//
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