ID A0A674IEG1_9SAUR Unreviewed; 993 AA.
AC A0A674IEG1;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
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:ENSTMTP00000007826.1};
OS Terrapene triunguis (Three-toed box turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Emydidae; Terrapene.
OX NCBI_TaxID=2587831 {ECO:0000313|Ensembl:ENSTMTP00000007826.1, ECO:0000313|Proteomes:UP000472274};
RN [1] {ECO:0000313|Ensembl:ENSTMTP00000007826.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSTMTP00000007826.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) 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=N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] +
CC acetate; 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 AlphaFoldDB; A0A674IEG1; -.
DR Ensembl; ENSTMTT00000008082.1; ENSTMTP00000007826.1; ENSTMTG00000005021.1.
DR GeneTree; ENSGT00940000157440; -.
DR Proteomes; UP000472274; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0141221; F:histone deacetylase activity, hydrolytic mechanism; IEA:UniProtKB-EC.
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; cd10162; ClassIIa_HDAC4_Gln-rich-N; 1.
DR FunFam; 3.40.800.20:FF:000002; Histone deacetylase; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR046949; HDAC4/5/7/9.
DR InterPro; IPR000286; HDACs.
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:SF13; 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|ARBA:ARBA00022853,
KW ECO:0000256|PIRNR:PIRNR037911};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037911-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000472274};
KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|PIRNR:PIRNR037911};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR037911};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR037911};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 40..79
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 583..901
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 60..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..240
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..509
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 712
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 577
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 583
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 885
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 993 AA; 109602 MW; 3C71AE6FCFA594AA CRC64;
MYSNTSASSY NSSCLAHCGM KALGGQTTCI HFFFPFTSQQ QQQEMLAMKH QQELLEHQRK
LEQHRQEQEL EKQHREQKLQ QLKNKEKGKE SAVASTEVKM KLQEFVLNKK KALAHRNLNH
CISNDPRFWK TQHSSLDQSS PPQSGISGTY NHPVLGMYDS KDDFPLRKTA SEPNLKLRSR
LKQKVAERRS SPLLRRKDGP VVTALKKRPL DVTDSACNSA PGSGPSSPNN SSNNISAENG
ITGSVTSIQT SLAHRLANRE GSVTQLPLYT SPSLPNITLG LPATGPASVS DLNTLPVVYL
QGGSGQQDAE RLAIPTLQQR LSLFPGTHLT PYLSSTTLER DGGTSHNSLL QHMVLLEQPT
AQTPLVTGLG PLPLHAQSLV GADRVSPSIH KLRQHRPLGR TQSAPLPQNA QALQQLVIQQ
QHQQFLEKHK QQFQQQQLHI NKVGTLIPAR QHESHPEETE EELREHQALL EEPYSDRVSS
QKEVQGLANM VQVKQEPIES DEEETEPPPE LEPGQRQAEQ ELLFRQVRYN RVTMSLVHSR
GFFFHVSQDS FLLQAIFVTS AAGLVYDTLM LKHQCTCGNT NSHPEHAGRI QSIWSRLQET
GLRGKCECIR GRKATLEELQ TVHSEAHTLL YGTNPLNRQK LDSKKLLGTE GGHASLPLWS
YIHKVDSDTI WNEVHSSGAA RLAVGCVIEL VFKVATGELK NGFAVVRPPG HHAEESTPMG
FCYFNSVAIA AKLLQQRLNV SKILIVDWDV HHGNGTQQAF YSDPNVLYIS LHRYDDGNFF
PGSGAPDEVG TGPGVGFNVN MAFTGGLEPP MGDTEYLTAF RTVVMPIANE FAPDVVLVSS
GFDAVEGHPT PLGGYNLSAK CFGYLTKQLM GLAGGRIVLA LEGGHDLTAI CDASEACVSA
LLGNELDPLP EKVLQQRANA NAVHSMEKVI EIHSKYWHSL QRYSSTVGYS LIEAQKCETE
EAETVTAMAS LSVGVKPADK RPDDEPMEEE PPM
//
