HDA10_RAT
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 03-AUG-2022, entry version 102.
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}.
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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 PaxDb; Q569C4; -.
DR Ensembl; ENSRNOT00000055865; ENSRNOP00000052717; ENSRNOG00000031915.
DR GeneID; 362981; -.
DR KEGG; rno:362981; -.
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 OMA; RTCAVLP; -.
DR OrthoDB; 1484694at2759; -.
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 tissues.
DR Genevisible; Q569C4; RN.
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; 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:RGD.
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:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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:0006476; P:protein deacetylation; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
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..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
