ID A0A2Y9L224_ENHLU Unreviewed; 1108 AA.
AC A0A2Y9L224;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, 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=LOC111158026 {ECO:0000313|RefSeq:XP_022375520.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022375520.1};
RN [1] {ECO:0000313|RefSeq:XP_022375520.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022375520.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_022375520.1; XM_022519812.1.
DR AlphaFoldDB; A0A2Y9L224; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
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; cd10007; HDAC5; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000248482};
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 58..146
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 690..1008
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 29..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 108..159
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 231..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..603
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 819
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 682
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 684
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 690
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 767
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 992
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 1108 AA; 120387 MW; C09E018ED8624DDB CRC64;
MSGREPALEI LPRTPLQGIP VAVEVKPVLP GAMPSSMGGG GGGSPSPAEL RGALAGPVDP
ALREQQLQQE LLALKQQQQL QKQLLFAEFQ KQHDHLTRQH EVQLQKHLKQ QQEMLAAKRQ
QELEQQRQRE QQRQEELEKQ RLEQQLLILR NKEKSKESAI ASTEVKLRLQ EFLLSKSKEP
TPGGLNHSLP QHPKCWGAHH ASLDQSSPPQ SGPPGTPPSY KLPLLGPYDS RDDFPLRKTA
SEPNLKVRSR LKQKVAERRS SPLLRRKDGT VISTFKKRAV EITGAGPGVS SVCNSAPGSG
PSSPNSSHST IAENGFTGSV PNIPTEMLPQ HRALPLDSSP NQFSLYTSPS LPNISLGLQA
TVTVTNSHLT ASPKLSTQQE AERQALQSLR QGGALTGKFM STSSIPGCLL GVALEGDSSP
HGHASLLQHV LLLEQARQQS TLIAVPLHGQ SPLVTGERVA TSMRTVGKLP RHRPLSRTQS
SPLPQSPQAL QQLVMQQQHQ QFLEKQKQQQ LQLGKILTKT GELSRQPTTH PEETEEELTE
QQEALLGEGA LTIPREGSTE SESTQEDLEE EEEEEEEEEE EEGEEDCIQV KDEEGESGPE
EGPDLDESSA GYKKVFSDAQ QLQPLQVFQA PLSLATVPHQ ALGRTQSSPA APGGLKSPPD
QPAKHLFTTG VVYDTFMLKH QCMCGNTHVH PEHAGRIQSI WSRLQETGLL SKCERIRGRK
ATLDEIQTVH SEYHTLLYGT SPLNRQKLDS KKLLGPISQK MYAVLPCGGI GVDSDTVWNE
MHSSSAVRMA VGCLVELAFK VASGELKNGF AIIRPPGHHA EESTAMGFCF FNSVAITTKL
LQQKLNVGKV LIVDWDIHHG NGTQQAFYND PSVLYISLHR YDNGNFFPGS GAPEEVGGGP
GVGYNVNVAW TGGVDPPIGD VEYLTAFRTV VMPIAHEFSP DVVLVSAGFD AVEGHLSPLG
GYSVTARCFG HLTRQLMTLA GGRVVLALEG GHDLTAICDA SEACVSALLS VELQPLDEAV
LQQKPNINAV ATLEKVIEIQ SKHWSCVQRF AAGLGRSLRE AQAGETEEAE TVSAMALLSV
GAEQAQAAAA REHSPRPPEE PMEQEPAL
//
