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Database: UniProt/SWISS-PROT
Entry: HDA10_MOUSE
LinkDB: HDA10_MOUSE
Original site: 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   13-FEB-2019, entry version 113.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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
CC       on 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
CC       observed in vitro. Has also been shown to be involved in MSH2
CC       deacetylation. The physiological relevance of protein/histone
CC       deacetylase activity is unclear and could be very weak. May play a
CC       role in the promotion of late stages of autophagy, possibly
CC       autophagosome-lysosome fusion and/or lysosomal exocytosis in
CC       neuroblastoma cells. May play a role in homologous recombination.
CC       May promote DNA mismatch repair. {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,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:61930;
CC         Evidence={ECO:0000250|UniProtKB:Q969S8};
CC   -!- SUBUNIT: Interacts with HDAC3. Interacts with HDAC2 and
CC       NCOR2/SMRT. Interacts with HSPA8/HSC70. Interacts with MSH2.
CC       {ECO:0000250|UniProtKB:Q969S8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q969S8}.
CC       Nucleus {ECO:0000250|UniProtKB:Q969S8}. Note=Excluded from
CC       nucleoli. {ECO:0000250|UniProtKB:Q969S8}.
CC   -!- TISSUE SPECIFICITY: widely expressed.
CC       {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
CC       uncertain. The 3D structure analysis of the zebrafish ortholog
CC       shows that a glutamate gatekeeper and a sterically constricted
CC       active site confer specificity for N(8)-acetylspermidine
CC       hydrolysis and disfavour acetyllysine hydrolysis. Supporting this
CC       observation, has been shown to exhibit only very low activity, if
CC       any, towards acetyl-lysine peptide substrates. However, histone
CC       deacetylase activity has been observed in vitro and HDAC10 has
CC       also been shown to be involved in MSH2 deacetylation.
CC       {ECO:0000250|UniProtKB:Q969S8}.
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   UniGene; Mm.203954; -.
DR   ProteinModelPortal; Q6P3E7; -.
DR   SMR; Q6P3E7; -.
DR   BioGrid; 228438; 6.
DR   IntAct; Q6P3E7; 2.
DR   STRING; 10090.ENSMUSP00000080832; -.
DR   ChEMBL; CHEMBL3832944; -.
DR   PhosphoSitePlus; Q6P3E7; -.
DR   MaxQB; Q6P3E7; -.
DR   PaxDb; Q6P3E7; -.
DR   PRIDE; Q6P3E7; -.
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   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   GeneTree; ENSGT00940000160061; -.
DR   HOGENOM; HOG000225183; -.
DR   HOVERGEN; HBG051892; -.
DR   InParanoid; Q6P3E7; -.
DR   KO; K18671; -.
DR   OrthoDB; 1484694at2759; -.
DR   TreeFam; TF106173; -.
DR   Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR   ChiTaRS; Hdac10; mouse.
DR   PRO; PR:Q6P3E7; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000062906; Expressed in 166 organ(s), highest expression level in mesenteric lymph node.
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 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   PANTHER; PTHR10625; PTHR10625; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; SSF52768; 2.
PE   2: Evidence at transcript level;
KW   Autophagy; Complete proteome; Cytoplasm; DNA damage;
KW   DNA recombination; DNA repair; Hydrolase; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Zinc.
FT   CHAIN         1    666       Polyamine deacetylase HDAC10.
FT                                /FTId=PRO_0000114713.
FT   REGION        1    323       Histone deacetylase.
FT   ACT_SITE    135    135       {ECO:0000250}.
FT   CONFLICT     91     91       N -> D (in Ref. 3; AAH64018).
FT                                {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
//
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