ID A0A6J0X7N1_ODOVR Unreviewed; 1143 AA.
AC A0A6J0X7N1;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 08-OCT-2025, sequence version 2.
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=HDAC5 {ECO:0000313|RefSeq:XP_020744279.2,
GN ECO:0000313|RefSeq:XP_020744281.2};
OS Odocoileus virginianus (White-tailed deer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Odocoileinae; Odocoileus.
OX NCBI_TaxID=9874 {ECO:0000313|Proteomes:UP001652640, ECO:0000313|RefSeq:XP_020744279.2};
RN [1] {ECO:0000313|Proteomes:UP001652640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=35511871;
RA London E.W., Roca A.L., Novakofski J.E., Mateus-Pinilla N.E.;
RT "A De Novo Chromosome-Level Genome Assembly of the White-Tailed Deer,
RT Odocoileus Virginianus.";
RL J. Hered. 113:479-489(2022).
RN [2] {ECO:0000313|RefSeq:XP_020744279.2, ECO:0000313|RefSeq:XP_020744281.2}
RP IDENTIFICATION.
RC TISSUE=Tongue muscle {ECO:0000313|RefSeq:XP_020744279.2,
RC ECO:0000313|RefSeq:XP_020744281.2};
RG RefSeq;
RL Submitted (MAY-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 RefSeq; XP_020744279.2; XM_020888620.2.
DR RefSeq; XP_020744281.2; XM_020888622.2.
DR AlphaFoldDB; A0A6J0X7N1; -.
DR GeneID; 110134258; -.
DR KEGG; ovr:110134258; -.
DR OrthoDB; 424012at2759; -.
DR Proteomes; UP001652640; Chromosome 17.
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; cd10164; ClassIIa_HDAC5_Gln-rich-N; 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; 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:SF12; 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:UP001652640};
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 68..121
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 725..1043
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..523
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..622
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 854
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 717
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 719
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 725
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 802
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 1027
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 1143 AA; 124164 MW; D1EA95872AB3B67E CRC64;
MNSPTESADG MPGREPALEI LPRTPLHGIP VTVEVKPVLP GAMPSSMGGG GGGSPSPVEL
RGALAGPVDP ALREQQLQQE LLALKQQQQL QKQLLFAEFQ KQHDHLTRQH EVQLQKHLKV
STGARAPRPL SPALDSAHPA SPLPLQQQQE MLAAKRQQEL EQQRQREQQR QEELEKQRLE
QQLLILRNKE KSKESAIAST EVKLRLQEFL LSKSKEPTPG GLNHSLPQHP KCWGTHHASL
DQSSPPQSGP PGTPPSYKLP LLGPYDSRDD FPLRKTASEP NLKVRSRLKQ KVAERRSSPL
LRRKDGTVIS TFKKRAVEIT GAGPGVSAVC NSAPGSGPSS PNSSHSTIAE NGFTGSVPNI
PTEMLPQHRA LPPDTSPNQF SLYTSPSLPN ISLGLQATVT VTNSHLTASP KLSTQQEAER
QALQSLRQGG ALTGKFMSTS SIPGCLLGVA LEGDSSPHGH ASLLQHVLLL EQARQQSTLI
AVPLHGQSPL VTGERVATSM RTVGKLPRHR PLSRTQSSPL PQSPQALQQL VMQQQHQQFL
EKQKQQQLQL GKILTKTGEL PRQPTTHPEE TEEELTEQQE ALLGEGALTI PREGSTESES
TQEDLEEEEE EEEEEEEEEE DCIQVKDEER ESGAEEGPDL EESSAGYKKA FADTQQLQPL
QVYQAPLSLA TVPHQALGRT QSSPAAPGGM KSPPDQPTKH LFTTGVVYDT FMLKHQCMCG
NTHVHPEHAG RIQSIWSRLQ ETGLLSKCER IRGRKATLDE IQTVHSEYHT LLYGTSPLNR
QKLDSKKLLG PISQKMYAML PCGGIGVDSD TVWNEMHSSS AVRMAVGCLV ELAFKVAAGE
LKNGFAIIRP PGHHAEESTA MGFCFFNSVA ITTKLLQQKL NVGKVLIVDW DIHHGNGTQQ
AFYNDPSVLY ISLHRYDNGN FFPGSGAPEE VGGGPGVGYN VNVAWTGGVD PPIGDVEYLT
AFRTVVMPIA HEFSPDVVLV SAGFDAVEGH LSPLGGYSVT ARCFGHLTRQ LMTLAGGRVV
LALEGGHDLT AICDASEACV SALLSVELQP LDETVLQQKP NINAVATLEK VIEIQSKHWS
CVQRFAAGLG RSLREAQAGE TEEAETVSAM ALLSVGAEQA QAAAAREHSP RPVEEPMEQE
PAL
//
