ID A0A2K5NZD4_CERAT Unreviewed; 954 AA.
AC A0A2K5NZD4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
GN Name=HDAC7 {ECO:0000313|Ensembl:ENSCATP00000042726.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000042726.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000042726.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC deacetylation gives a tag for epigenetic repression and plays an
CC important role in transcriptional regulation, cell cycle progression
CC and developmental events. {ECO:0000256|PIRNR:PIRNR037911}.
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|PIRNR:PIRNR037911};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037911}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00007738,
CC ECO:0000256|PIRNR:PIRNR037911}.
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 RefSeq; XP_011903949.1; XM_012048559.1.
DR AlphaFoldDB; A0A2K5NZD4; -.
DR Ensembl; ENSCATT00000067161.1; ENSCATP00000042726.1; ENSCATG00000043857.1.
DR GeneID; 105580441; -.
DR CTD; 51564; -.
DR GeneTree; ENSGT00940000159065; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000043857; Expressed in thymus and 12 other cell types or tissues.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0019899; F:enzyme binding; IEA:UniProt.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd10008; HDAC7; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR046949; HDAC4/5/7/9.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF44; HISTONE DEACETYLASE 7; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 3.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Repressor {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037911};
KW Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 543..861
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 672
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 535
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 537
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 543
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 620
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 845
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 954 AA; 103012 MW; 6F2DBB5678BF762A CRC64;
MHRPGADGTQ VSPGAHYRSP TGTGCPRPCA DTPGPQSQPM DLRVGQRPPV EPPPEPTLLA
LQRPQRLHHH LFLAGLQQQR SVEPMRLSMD TPMPELQVGP QEQELRQLLH KDKSKRSAVA
SSVVKQKLAE VILKKQQAAL ERTVHSNSPG IPYRTLEPLE TEGAARSMLS SFLPPVPSLP
SDPPEHFPLR KTVSEPNLKL RYKPKKSLER RKNPLLRKES APPSLRRRPA ETLGDSSPSS
SSTPASGCSS PNDSEHGPNP ILGSEADSDR RTHPTLGPRG PILGSPHTPL FLPHGLEPEA
GGTLPSRLQP ILLLDPSGSH APLLTVPGLG PLPFHFAQSL MTTERLSGSG LHWPLSRTRS
EPLPPSATAP PPPGPMQPRL EQLKTHVQVI KRSAKPSEKP RLRQIPSAED LETDGGGPGQ
VVDDGLEHRE LSHGQPEARG PAPLQQHPQV LLWEQQRLAG RLPRGSTGDT VLLPLAQGGH
RPLSRAQSSP AAPASLSAPE PASQARVLSS SETPARTLPF TTGLIYDSVM LKHQCSCGDN
SRHPEHAGRI QSIWSRLQER GLRSQCECLR GRKASLEELQ SVHSERHVLL YGTNPLSRLK
LDNGKLAGLL AQRMFVMLPC GGVGVDTDTI WNELHSSNAA RWAAGSVTDL AFKVASRELK
NGFAVVRPPG HHADHATAMG FCFFNSVAIA CRQLQQQSKA SKILIVDWDV HHGNGTQQTF
YQDPSVLYIS LHRHDDGNFF PGSGAVDEVG AGSGEGFNVN VAWTGGLDPP MGDPEYLAAF
RTVVMPIARE FSPDLVLVSA GFDAAEGHPA PLGGYHVSAK CFGYMTQQLM NLAGGAVVLA
LEGGHDLTAI CDASEACVAA LLGNKVDPLS EEGWKQKPNL NAIRSLEAVI RVHSKYWGCM
QRLASCPDSW VPRVPGADKE EVEAVTALAS LSVGILAEDR PSEQLVEEEE PMNL
//
