ID A0A2K6Q6C4_RHIRO Unreviewed; 1084 AA.
AC A0A2K6Q6C4;
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=HDAC4 {ECO:0000313|Ensembl:ENSRROP00000024329.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000024329.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000024329.1}
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}.
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DR Ensembl; ENSRROT00000048532.1; ENSRROP00000024320.1; ENSRROG00000035950.1.
DR Ensembl; ENSRROT00000048541.1; ENSRROP00000024329.1; ENSRROG00000035950.1.
DR GeneTree; ENSGT00940000157440; -.
DR OMA; XAVASTE; -.
DR Proteomes; UP000233200; Unplaced.
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 GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd10162; ClassIIa_HDAC4_Gln-rich-N; 1.
DR CDD; cd10006; HDAC4; 1.
DR Gene3D; 6.10.250.1550; -; 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; IPR024643; Hist_deacetylase_Gln_rich_N.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364:SF11; HISTONE DEACETYLASE; 1.
DR PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR Pfam; PF12203; HDAC4_Gln; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 1.
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
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 62..152
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 675..992
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 133..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1084
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 803
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 667
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 675
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 751
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 976
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 1084 AA; 119014 MW; 5E42F1FD9639F40E CRC64;
MSSQSHPDGL SGRDQPVELL NPARVNHMPS TVDVATALPL QVAPSAVPMD LRLDHQFSLP
VAEPALREQQ LQQELLALKQ KQQIQRQILI AEFQRQHEQL SRQHEAQLHE HIKQQQEMLA
MKHQQELLEH QRKLERHRQE QELEKQHREQ KLQQLKNKEK GKESAVASTE VKMKLQEFVL
NKKKALAHRN LNHCISSDPR YWYGKTQHSS LDQSSPPQSG VSTSYNHPVL GMYDAKDDFP
LRKTASEPNL KLRSRLKQKV AERRSSPLLR RKDGPVVTAL KKRPLDVTDS ACSSAPGSGP
SSPNNSSGSV SAENGIAPAV PSIPAETSLA HRLVTREGSA APLPLYTSPS LPNITLGLPA
TGPAAGTAGQ RDAERLALPT LQQRLSLFPG THLTPYLSTS PLERDGGAAH SPLLQHMVLL
EQPPAQAPLV TGLGALPLHA QSLVGADRVS PSIHKLRQHR PLGRTQSAPL PQNAQALQHL
VIQQQHQQFL EKHKQQFQQQ QLHMNKIIPK PSEPARQPES HPEETEEELR EHQALLDEPY
LDRLPAQKEA HAPAGVQVKQ EPIESDDEEA EPPREVDPGQ RQPSEQELLF RQQALLLEQQ
RIHQLRNYQA SMEAAGIPVS FGSHRPLSRA QSSPASATFP VSVQEPPTKP RFTTGLVYDT
LMLKHQCTCG SSSSHPEHAG RIQSIWSRLQ ETGLRGKCEC IRGRKATLEE LQTVHSEAHT
LLYGTNPLNR QKLDSKKLLG SLASVFVRLP CGGVGVDSDT IWNEVHSAGA ARLAVGCVVE
LVFKVATGEL KNGFAVVRPP GHHAEESTPM GFCYFNSVAV AAKLLQQRLS VSKILIVDWD
VHHGNGTQQA FYSDPSVLYV SLHRYDDGNF FPGSGAPDEV GTGPGVGFNV NMAFTGGLDP
PMGDAEYLAA FRTVVMPIAS EFAPDVVLVS SGFDAVEGHP TPLGGYNLSA RCFGYLTKQL
MGLAGGRIVL ALEGGHDLTA ICDASEACVS ALLGNELDPL PEKVLQQRPN ANAVRSMEKV
MEIHSKYWRC LQRATSTAGR SLIEAQTCEN EEAETVTAMA SLSVGVKPAE KRPDEEPMEE
EPPL
//
