ID   A2AWS5_MOUSE            Unreviewed;      1030 AA.
AC   A2AWS5;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 122.
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|Ensembl:ENSMUSP00000102769.3,
GN   ECO:0000313|MGI:MGI:1333784};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000102769.3, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000102769.3, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000102769.3,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000102769.3}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000102769.3};
RG   Ensembl;
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   AlphaFoldDB; A2AWS5; -.
DR   SMR; A2AWS5; -.
DR   MaxQB; A2AWS5; -.
DR   PeptideAtlas; A2AWS5; -.
DR   ProteomicsDB; 351625; -.
DR   Antibodypedia; 3425; 866 antibodies from 44 providers.
DR   Ensembl; ENSMUST00000107151.9; ENSMUSP00000102769.3; ENSMUSG00000008855.18.
DR   AGR; MGI:1333784; -.
DR   MGI; MGI:1333784; Hdac5.
DR   VEuPathDB; HostDB:ENSMUSG00000008855; -.
DR   GeneTree; ENSGT00940000160534; -.
DR   ChiTaRS; Hdac5; mouse.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000008855; Expressed in retinal neural layer and 257 other cell types or tissues.
DR   ExpressionAtlas; A2AWS5; baseline and differential.
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   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; 2.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|EPD:A2AWS5,
KW   ECO:0007829|MaxQB:A2AWS5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
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          68..156
FT                   /note="Histone deacetylase glutamine rich N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12203"
FT   DOMAIN          695..930
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          39..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1005..1030
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..608
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        741
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT   BINDING         689
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT   SITE            914
FT                   /note="Contributes to catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ   SEQUENCE   1030 AA;  111463 MW;  BC08380109B0477B CRC64;
     MNSPNESADG MSGREPSLEI LPRTPLHSIP VAVEVKPVLP GAMPSSMGGG GGGSPSPVEL
     RGALAGPMDP ALREQQLQQE LLVLKQQQQL QKQLLFAEFQ KQHDHLTRQH EVQLQKHLKQ
     QQEMLAAKRQ QELEQQRQRE QQRQEELEKQ RLEQQLLILR NKEKSKESAI ASTEVKLRLQ
     EFLLSKSKEP TPGGLNHSLP QHPKCWGAHH ASLDQSSPPQ SGPPGTPPSY KLPLLGPYDS
     RDDFPLRKTA SEPNLKVRSR LKQKVAERRS SPLLRRKDGT VISTFKKRAV EITGTGPGVS
     SVCNSAPGSG PSSPNSSHST IAENGFTGSV PNIPTEMIPQ HRALPLDSSP NQFSLYTSPS
     LPNISLGLQA TVTVTNSHLT ASPKLSTQQE AERQALQSLR QGGTLTGKFM STSSIPGCLL
     GVALEGDTSP HGHASLLQHV LLLEQARQQS TLIAVPLHGQ SPLVTGERVA TSMRTVGKLP
     RHRPLSRTQS SPLPQSPQAL QQLVMQQQHQ QFLEKQKQQQ MQLGKILTKT GELSRQPTTH
     PEETEEELTE QQEALLGEGA LTIPREGSTE SESTQEDLEE EEEEEEEEEE DCIQVKDEDG
     ESGPDEGPDL EESSAGYKKL FADAQQLQPL QVYQAPLSLA TVPHQALGRT QSSPAAPGSM
     KSPTDQPTVV KHLFTTGPIS QKMYAMLPCG GIGVDSDTVW NEMHSSSAVR MAVGCLVELA
     FKVAAGELKN GFAIIRPPGH HAEESTAMGF CFFNSVAITA KLLQQKLSVG KVLIVDWDIH
     HGNGTQQAFY NDPSVLYISL HRYDNGNFFP GSGAPEEVGG GPGVGYNVNV AWTGGVDPPI
     GDVEYLTAFR TVVMPIAQEF SPDVVLVSAG FDAVEGHLSP LGGYSVTARC FGHLTRQLMT
     LAGGRVVLAL EGGHDLTAIC DASEACVSAL LSVELQPLDE AVLQQKPSVN AVATLEKVIE
     IQSKHWSCVQ RFAAGLGCSL REAQTGEKEE AETVSAMALL SVGAEQAQAV ATQEHSPRPA
     EEPMEQEPAL
//