ID L9KQU7_TUPCH Unreviewed; 1209 AA.
AC L9KQU7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 ORFNames=TREES_T100020692 {ECO:0000313|EMBL:ELW63537.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW63537.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
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 EMBL; KB320773; ELW63537.1; -; Genomic_DNA.
DR STRING; 246437.L9KQU7; -.
DR InParanoid; L9KQU7; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
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 Gene3D; 3.40.800.20; Histone deacetylase domain; 4.
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; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF36; HISTONE DEACETYLASE 4; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 2.
DR PIRSF; PIRSF037911; HDAC_II_euk; 6.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 3.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518};
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 532..798
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 874..994
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 722
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 524
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 526
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 658
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 978
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 1209 AA; 129886 MW; 640887E388F93E2B CRC64;
MQPRISEASP SGASEPNLKL RSRLKQKVAE RRSSPLLRRK DGPVVTALKK RPLDVTVNSV
QSSEQNVAPE HPPQQRSQAQ SPPNSACSSA PGSGPSSPNN SSGNVSTENG IAPAVPSLTA
EPSLAHRLVT RDASVAPLPL YTSPSLPNIT LGLPATGPSA GTAAQQDAER LALPALQQRL
SLFPGTHLAP YLSSSPLERD GGPAHSPLLQ HMGLLEQPPX XXXXXXXXXX XXXXPLAPSL
SSSPLERDGG PAHSPLLQHM VLLEQPPAQP PLVTGLGALP LHAQSLVGAD RVSPCIHKLR
QDLADPPEVM SLQAPVPSVP PNLTNPLEMI PKPGEPARQP ESHPEETEEE LREHQALVDE
PYSDRLPGQK EALVLAGVQV KQEPVESDEE EAEPPREGEH GQRQPTEQEL LFRQQALLLE
QQRIHQLRNY QASLEAAGIP VSFGGHRPLS RAQSSPASAT FPVTVQEPPA KPRFTTGAQK
LLTFPGGSHA PTHVLVGPVR AFPFLPMVSG DGLVYDTLML KHQCTCGSTS SHPEHAGRIQ
SIWSRLQETG LRSKCECIRG RKATLEELQT VHSEAHTLLY GTNPLNRQKL DNPGPWLDSC
GIRIAPRLCA ASRAGAALSM LSLPRREVKG PAEKASLSSV NEPLFFYACV LLADLCVCQA
PLWRRWGEYL FNVQVDSDTI WNEVHSSGAA RLAVGCVVEL VFKVATGELK NGFAVVRPPG
HHAEESTPMG FCYFNSVAVA AKLLQQRLNV SKILIVDWDV HHGNGSQQAF YSDPSVLYVS
LHRYDDGNFF PGSGAPDEDV HHGNGSQQAF YSDPSVLYVS LHRYDDGNFF PGSGAPDEVG
TGPGVGFNVN MAFTGGLDPP MGDTEYLAAF RLASFPDSPD RVGTGPGVGF NVNMAFTGGL
DPPMGDTEYL AAFRTVVMPI ANEFAPDVVL VSSGFDAVEG HPTPLGGYNL SAKCFGYLTK
QLMGLAGGRV VLALEGGHDL TAICDASEAC VSALLGNELD PLPEKVLQQR PNANAVRSMQ
RVLEIHSKYW RCLQRVASAV GHSLVEAQNC ENEEAETVTA MASLSVGVKA AEKRPDEEPM
EEEPPLLLSX XXXXXXXXXX CVEPQPGTCP RSRVLRGAPG STGTRCSSGK PFCRPDHGLQ
THVHTGMAAS RGAWDRPATS RHGRLDAQQL WWPGRPRRRS AGDRPHLRVL PAGGKASESP
SLTEQNRPD
//
