ID HDA10_RAT Reviewed; 588 AA. AC Q569C4; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 111. 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 Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; 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). 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC092573; AAH92573.1; -; mRNA. DR RefSeq; NP_001030172.1; NM_001035000.1. DR AlphaFoldDB; Q569C4; -. DR SMR; Q569C4; -. DR BioGRID; 263876; 1. DR STRING; 10116.ENSRNOP00000052717; -. DR PhosphoSitePlus; Q569C4; -. DR PaxDb; 10116-ENSRNOP00000052717; -. DR Ensembl; ENSRNOT00000055865.4; ENSRNOP00000052717.2; ENSRNOG00000031915.5. DR GeneID; 362981; -. DR KEGG; rno:362981; -. DR AGR; RGD:1305874; -. DR CTD; 83933; -. DR RGD; 1305874; Hdac10. DR eggNOG; KOG1343; Eukaryota. DR GeneTree; ENSGT00940000160061; -. DR HOGENOM; CLU_007727_6_0_1; -. DR InParanoid; Q569C4; -. DR OrthoDB; 124800at2759; -. DR Reactome; R-RNO-350054; Notch-HLH transcription pathway. DR PRO; PR:Q569C4; -. DR Proteomes; UP000002494; Chromosome 7. DR Bgee; ENSRNOG00000031915; Expressed in pancreas and 19 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0000118; C:histone deacetylase complex; ISO:RGD. DR GO; GO:0005654; C:nucleoplasm; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISO:RGD. 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:RGD. DR GO; GO:0004407; F:histone deacetylase activity; ISO:RGD. DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD. DR GO; GO:0033558; F:protein lysine deacetylase activity; ISO:RGD. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0035825; P:homologous recombination; ISS:UniProtKB. DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0014003; P:oligodendrocyte development; IEP:RGD. 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 DNA-templated transcription; ISO:RGD. DR GO; GO:0106048; P:spermidine deacetylation; ISS:UniProtKB. DR Gene3D; 3.40.800.20; Histone deacetylase domain; 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; HISTONE DEACETYLASE HDAC1-RELATED; 1. DR PANTHER; PTHR10625:SF18; POLYAMINE DEACETYLASE HDAC10; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PRINTS; PR01270; HDASUPER. DR SUPFAM; SSF52768; Arginase/deacetylase; 2. DR Genevisible; Q569C4; RN. 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..588 FT /note="Polyamine deacetylase HDAC10" FT /id="PRO_0000114714" FT REGION 1..302 FT /note="Histone deacetylase" FT ACT_SITE 135 FT /evidence="ECO:0000250" SQ SEQUENCE 588 AA; 63957 MW; 3708DDEAE2D5EA59 CRC64; MGTALVYHED MTATRLLWDD PECEIECPER LTAALDGLRQ RGLEERCQCL SVCEASEEEL GLVHSPEYIA LVQKTQTLDK EELHTLSKQY DAVYFHPDTF HCARLAAGAA LRLVDAVLTG AVHNGVALVR PPGHHSQRAA ANGFCVFNNV AIAARHAKQK YGLQRILIVD WDVHHGQGIQ YIFEDDPSVL YFSWHRYEHG NFWPFLPESD ADTVGRGRGQ GFTVNLPWNQ VGMGNADYLA AFLHVLLPLA FEFDPELVLV SAGFDSAIGD PEGQMQATPE CFAHLTQLLQ VLAGGRICAV LECPGVYPEC SDSPDPSLDK PPTNSTCTVA EDSLSPCLDR PCHRPTPPIC IAVALAVSGA ALDLPPGVLH QEGSALREET EAWARLHKSQ FQDDDLAALG KSLCLLDGIL DGQIRSAIAT TTALATAATL GVLIQRCVAH RGQRRILWLS IRGKEADIWS MFHFSTPLPQ TTGGFLSFIL GLVLPLAYGF QPDMVLMALG PAHGLQNAQA ALLAAMLRSP VGGRILALVE EESILQLART LAQVLHGETP PSLGPFSMAS PEEIQALMFL KAQLEPRWKL LQVAAPPP //