HDAC3_CHICK
ID HDAC3_CHICK Reviewed; 428 AA.
AC P56520;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Histone deacetylase 3;
DE Short=HD3;
DE EC=3.5.1.98 {ECO:0000250|UniProtKB:O15379};
DE AltName: Full=Protein deacetylase HDAC3;
DE EC=3.5.1.- {ECO:0000250|UniProtKB:O15379};
DE AltName: Full=Protein deacylase HDAC3;
DE EC=3.5.1.- {ECO:0000250|UniProtKB:O15379};
GN Name=HDAC3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10748092; DOI=10.1074/jbc.m908066199;
RA Takami Y., Nakayama T.;
RT "N-terminal region, C-terminal region, nuclear export signal, and
RT deacetylation activity of histone deacetylase-3 are essential for the
RT viability of the DT40 chicken B cell line.";
RL J. Biol. Chem. 275:16191-16201(2000).
CC -!- FUNCTION: Histone deacetylase that catalyzes the deacetylation of
CC lysine residues on the N-terminal part of the core histones (H2A, H2B,
CC H3 and H4), and some other non-histone substrates. 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. Histone deacetylases act via the formation of
CC large multiprotein complexes. Participates in the BCL6 transcriptional
CC repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer
CC elements, antagonizing EP300 acetyltransferase activity and repressing
CC proximal gene expression. Also functions as deacetylase for non-histone
CC targets. In addition to protein deacetylase activity, also acts as
CC protein-lysine deacylase by recognizing other acyl groups: catalyzes
CC removal of (2E)-butenoyl (crotonyl) and 2-hydroxyisobutanoyl (2-
CC hydroxyisobutyryl) acyl groups from lysine residues, leading to protein
CC decrotonylation and de-2-hydroxyisobutyrylation, respectively.
CC {ECO:0000250|UniProtKB:O15379}.
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:0000250|UniProtKB:O15379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC Evidence={ECO:0000250|UniProtKB:O15379};
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:O15379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC Evidence={ECO:0000250|UniProtKB:O15379};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate
CC + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:35899, ChEBI:CHEBI:137954;
CC Evidence={ECO:0000250|UniProtKB:O15379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC Evidence={ECO:0000250|UniProtKB:O15379};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] = 2-
CC hydroxy-2-methylpropanoate + L-lysyl-[protein]; Xref=Rhea:RHEA:69176,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:19641, ChEBI:CHEBI:29969, ChEBI:CHEBI:144968;
CC Evidence={ECO:0000250|UniProtKB:O15379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69177;
CC Evidence={ECO:0000250|UniProtKB:O15379};
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; AF039753; AAB96925.1; -; mRNA.
DR RefSeq; NP_990078.1; NM_204747.1.
DR AlphaFoldDB; P56520; -.
DR SMR; P56520; -.
DR BioGRID; 675790; 1.
DR STRING; 9031.ENSGALP00000004141; -.
DR PaxDb; P56520; -.
DR GeneID; 395506; -.
DR KEGG; gga:395506; -.
DR CTD; 8841; -.
DR VEuPathDB; HostDB:geneid_395506; -.
DR eggNOG; KOG1342; Eukaryota.
DR InParanoid; P56520; -.
DR OrthoDB; 732770at2759; -.
DR PhylomeDB; P56520; -.
DR PRO; PR:P56520; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:AgBase.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0160009; F:histone decrotonylase activity; ISS:UniProtKB.
DR GO; GO:0160010; F:protein de-2-hydroxyisobutyrylase activity; ISS:UniProtKB.
DR GO; GO:0160008; F:protein decrotonylase activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:AgBase.
DR GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 2: Evidence at transcript level;
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_0000114698"
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|UniProtKB:Q13547"
SQ SEQUENCE 428 AA; 48902 MW; 42E32733AD2BBF07 CRC64;
MAKTVAYFYD PDVGNFHYGA GHPMKPHRLA LTHSLVLHYG LYKKMIVFKP YQASQHDMCR
FHSEDYIDFL QRVSPNNMQG FTKSLNAFNV GDDCPVFPGL FEFCSRYTGA SLQGATQLNN
KICDIAINWA GGLHHAKKFE ASGFCYVNDI VIGILELLKY HPRVLYIDID IHHGDGVQEA
FYLTDRVMTV SFHKYGNYFF PGTGDMYEVG AESGRYYALN VPLRDGIDDQ SYKHLFQPVI
NQVVDYYQPT CIVLQCGADS LGRDRLGCFN LSIRGHGECV EYVKSFNIPL LVLGGGGYTV
RNVARCWTYE TSLLVDEAIS EELPYSEYFE YFAPDFTLHP DVSTRIENQN SRQYLDQIRQ
TIFENLKMLN HAPSVQIHDV PSDLLSYDRT DEPDPEERGS EENYSRPEAA NEFYDGDHDN
DKESDVEI
