ID   HDAC3_TETNG             Reviewed;         428 AA.
AC   Q4SFA0;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Histone deacetylase 3;
DE            Short=HD3;
DE            EC=3.5.1.98;
GN   Name=hdac3; ORFNames=GSTENG00019185001;
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC       N-terminal part of the core histones (H2A, H2B, H3 and H4) (By
CC       similarity). Histone deacetylation gives a tag for epigenetic
CC       repression and plays an important role in transcriptional regulation,
CC       cell cycle progression and developmental events (By similarity).
CC       Histone deacetylases act via the formation of large multiprotein
CC       complexes (By similarity). May play a role in the regulation of the
CC       circadian clock in a deacetylase activity-independent manner (By
CC       similarity). {ECO:0000250|UniProtKB:O15379,
CC       ECO:0000250|UniProtKB:O88895}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15379}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O15379}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CAAE01014606; CAG00682.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4SFA0; -.
DR   SMR; Q4SFA0; -.
DR   STRING; 99883.ENSTNIP00000013021; -.
DR   KEGG; tng:GSTEN00019185G001; -.
DR   HOGENOM; CLU_007727_7_6_1; -.
DR   InParanoid; Q4SFA0; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003714; F:transcription corepressor activity; ISS:AgBase.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR   GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
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   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; SSF52768; 1.
PE   3: Inferred from homology;
KW   Biological rhythms; Chromatin regulator; Cytoplasm; Hydrolase; Nucleus;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..428
FT                   /note="Histone deacetylase 3"
FT                   /id="PRO_0000352679"
FT   REGION          3..316
FT                   /note="Histone deacetylase"
FT   REGION          385..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..405
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        135
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   428 AA;  49144 MW;  8B6B3AFDCAE53887 CRC64;
     MTNRTSYFYD PDVGNFHYGA GHPMKPHRLS LTHSLVLHYG LYKKMMVFKP YKASQHDMCR
     FHSEDYIDFL QKVSPNNMQG FTKSLNTFNV GDDCPVFPGL FEFCSRYTGA SLQGATQLNH
     KICDIAINWA GGLHHAKKFE ASGFCYVNDI VISILELLKY HPRVLYIDID IHHGDGVQEA
     FYLTDRVMTV SFHKYGNYFF PGTGDMYEVG AESGRYYCLN VPLRDGIDDQ SYRQLFQPVI
     KQVVDFYQPT CIVLQCGADS LGCDRLGCFN LSIRGHGECV EFVKSFKIPL LVLGGGGYTV
     RNVARCWTFE TSLLLEESIS DELPYSEYFE YFAPDFTLHP DVSTRIENQN SRQYLEQIRQ
     TVFENLKMLN HAPSVQIHDV PSDMLNYERN DEPDPDERGA EENYTRPEAA NEFYDGDHDN
     DKESDVEI