HDA10_MOUSE
ID HDA10_MOUSE Reviewed; 666 AA.
AC Q6P3E7; G3X9I8;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Polyamine deacetylase HDAC10;
DE EC=3.5.1.48 {ECO:0000250|UniProtKB:Q969S8};
DE EC=3.5.1.62 {ECO:0000250|UniProtKB:Q969S8};
DE AltName: Full=Histone deacetylase 10;
DE Short=HD10;
GN Name=Hdac10;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RC TISSUE=Hepatoma;
RX PubMed=11677242; DOI=10.1074/jbc.m108931200;
RA Kao H.-Y., Lee C.-H., Komarov A., Han C.C., Evans R.M.;
RT "Isolation and characterization of mammalian HDAC10, a novel histone
RT deacetylase.";
RL J. Biol. Chem. 277:187-193(2002).
CC -!- FUNCTION: Polyamine deacetylase (PDAC), which acts preferentially on
CC N(8)-acetylspermidine, and also on acetylcadaverine and
CC acetylputrescine. Exhibits attenuated catalytic activity toward
CC N(1),N(8)-diacetylspermidine and very low activity, if any, toward
CC N(1)-acetylspermidine. Histone deacetylase activity has been observed
CC in vitro. Has also been shown to be involved in MSH2 deacetylation. The
CC physiological relevance of protein/histone deacetylase activity is
CC unclear and could be very weak. May play a role in the promotion of
CC late stages of autophagy, possibly autophagosome-lysosome fusion and/or
CC lysosomal exocytosis in neuroblastoma cells. May play a role in
CC homologous recombination. May promote DNA mismatch repair.
CC {ECO:0000250|UniProtKB:Q969S8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(8)-acetylspermidine = acetate + spermidine;
CC Xref=Rhea:RHEA:23928, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:58535; EC=3.5.1.48;
CC Evidence={ECO:0000250|UniProtKB:Q969S8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetylputrescine = acetate + putrescine;
CC Xref=Rhea:RHEA:23412, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:58263, ChEBI:CHEBI:326268; EC=3.5.1.62;
CC Evidence={ECO:0000250|UniProtKB:Q969S8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetylcadaverine = acetate + cadaverine;
CC Xref=Rhea:RHEA:51892, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:58384, ChEBI:CHEBI:134408;
CC Evidence={ECO:0000250|UniProtKB:Q969S8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-
CC [protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:Q969S8};
CC -!- SUBUNIT: Interacts with HDAC3. Interacts with HDAC2 and NCOR2/SMRT.
CC Interacts with HSPA8/HSC70. Interacts with MSH2.
CC {ECO:0000250|UniProtKB:Q969S8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q969S8}. Nucleus
CC {ECO:0000250|UniProtKB:Q969S8}. Note=Excluded from nucleoli.
CC {ECO:0000250|UniProtKB:Q969S8}.
CC -!- TISSUE SPECIFICITY: widely expressed. {ECO:0000269|PubMed:11677242}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Protein/histone deacetylase activity in vivo is uncertain. The
CC 3D structure analysis of the zebrafish ortholog shows that a glutamate
CC gatekeeper and a sterically constricted active site confer specificity
CC for N(8)-acetylspermidine hydrolysis and disfavour acetyllysine
CC hydrolysis. Supporting this observation, has been shown to exhibit only
CC very low activity, if any, towards acetyl-lysine peptide substrates.
CC However, histone deacetylase activity has been observed in vitro and
CC HDAC10 has also been shown to be involved in MSH2 deacetylation.
CC {ECO:0000250|UniProtKB:Q969S8}.
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DR EMBL; AC113069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466550; EDL04375.1; -; Genomic_DNA.
DR EMBL; BC064018; AAH64018.1; -; mRNA.
DR CCDS; CCDS27739.1; -.
DR RefSeq; NP_954668.2; NM_199198.2.
DR AlphaFoldDB; Q6P3E7; -.
DR SMR; Q6P3E7; -.
DR BioGRID; 228438; 6.
DR IntAct; Q6P3E7; 8.
DR STRING; 10090.ENSMUSP00000080832; -.
DR BindingDB; Q6P3E7; -.
DR ChEMBL; CHEMBL3832944; -.
DR PhosphoSitePlus; Q6P3E7; -.
DR EPD; Q6P3E7; -.
DR MaxQB; Q6P3E7; -.
DR PaxDb; Q6P3E7; -.
DR PRIDE; Q6P3E7; -.
DR ProteomicsDB; 271497; -.
DR Antibodypedia; 14233; 523 antibodies from 37 providers.
DR DNASU; 170787; -.
DR Ensembl; ENSMUST00000082197; ENSMUSP00000080832; ENSMUSG00000062906.
DR GeneID; 170787; -.
DR KEGG; mmu:170787; -.
DR UCSC; uc007xfj.2; mouse.
DR CTD; 83933; -.
DR MGI; MGI:2158340; Hdac10.
DR VEuPathDB; HostDB:ENSMUSG00000062906; -.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000160061; -.
DR InParanoid; Q6P3E7; -.
DR OMA; PQVTGEM; -.
DR OrthoDB; 1484694at2759; -.
DR PhylomeDB; Q6P3E7; -.
DR TreeFam; TF106173; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR BioGRID-ORCS; 170787; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Hdac10; mouse.
DR PRO; PR:Q6P3E7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q6P3E7; protein.
DR Bgee; ENSMUSG00000062906; Expressed in cortical plate and 157 other tissues.
DR ExpressionAtlas; Q6P3E7; baseline and differential.
DR Genevisible; Q6P3E7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0047609; F:acetylputrescine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0047611; F:acetylspermidine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0019213; F:deacetylase activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0004407; F:histone deacetylase activity; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0033558; F:protein lysine deacetylase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; ISO:MGI.
DR GO; GO:0035825; P:homologous recombination; ISS:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0034983; P:peptidyl-lysine deacetylation; ISS:UniProtKB.
DR GO; GO:0106047; P:polyamine deacetylation; ISS:UniProtKB.
DR GO; GO:0032425; P:positive regulation of mismatch repair; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0106048; P:spermidine deacetylation; ISS:UniProtKB.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; SSF52768; 2.
PE 2: Evidence at transcript level;
KW Autophagy; Cytoplasm; DNA damage; DNA recombination; DNA repair; Hydrolase;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..666
FT /note="Polyamine deacetylase HDAC10"
FT /id="PRO_0000114713"
FT REGION 1..323
FT /note="Histone deacetylase"
FT ACT_SITE 135
FT /evidence="ECO:0000250"
FT CONFLICT 91
FT /note="N -> D (in Ref. 3; AAH64018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 666 AA; 72109 MW; 1F011B546D5D9A17 CRC64;
MGTALVYHED MTATRLLWDD PECEIECPER LTAALDGLRQ RGLEERCLCL SACEASEEEL
GLVHSPEYIA LVQKTQTLDK EELHALSKQY NAVYFHPDTF HCARLAAGAA LQLVDAVLTG
AVHNGLALVR PPGHHSQRAA ANGFCVFNNV ALAAKHAKQK YGLQRILIVD WDVHHGQGIQ
YIFNDDPSVL YFSWHRYEHG SFWPFLPESD ADAVGQGQGQ GFTVNLPWNQ VGMGNADYLA
AFLHVLLPLA FEFDPELVLV SAGFDSAIGD PEGQMQATPE CFAHLTQLLQ VLAGGRICAV
LEGGYHLESL AQSVCMMVQT LLGDPTPPLL GLMVPCQSAL ESIQSVQTAQ TPYWTSLQQN
VAPVLSSSTH SPEERSLRLL GESPTCAVAE DSLSPLLDQL CLRPAPPICT AVASTVPGAA
LCLPPGVLHQ EGSVLREETE AWARLHKSRF QDEDLATLGK ILCLLDGIMD GQIRNAIATT
TALATAATLD VLIQRCLARR AQRVLCVALG QLDRPLDLAD DGRILWLNIR GKDAAIQSMF
HFSTPLPQTT GGFLSLILGL VLPLAYGFQP DMVLMALGPA HGLQNAQAAL LAAMLRSPVG
GRILAVVEEE SIRLLARSLA QALHGETPPS LGPFSKATPE EIQALMFLKA RLEARWKLLQ
VAAPPP
