HDAC1_CHICK
ID HDAC1_CHICK Reviewed; 480 AA.
AC P56517;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Histone deacetylase 1;
DE Short=HD1;
DE EC=3.5.1.98 {ECO:0000250|UniProtKB:Q13547};
DE AltName: Full=Protein deacetylase HDAC1;
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q13547};
DE AltName: Full=Protein decrotonylase HDAC1;
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q13547};
GN Name=HDAC1; Synonyms=HDAC1A;
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].
RA Takami Y.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sun J.M., Chen H.Y., Davie J.R.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
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) (By similarity). Histone deacetylation gives a tag for
CC epigenetic repression and plays an important role in transcriptional
CC regulation, cell cycle progression and developmental events (By
CC similarity). Histone deacetylases act via the formation of large
CC multiprotein complexes (By similarity). Also functions as deacetylase
CC for non-histone proteins. In addition to protein deacetylase activity,
CC also has protein-lysine deacylase activity: acts as a protein
CC decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones
CC (By similarity). {ECO:0000250|UniProtKB:O42227,
CC ECO:0000250|UniProtKB:Q13547}.
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:Q13547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC Evidence={ECO:0000250|UniProtKB:Q13547};
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:Q13547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC Evidence={ECO:0000250|UniProtKB:Q13547};
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:Q13547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC Evidence={ECO:0000250|UniProtKB:Q13547};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13547}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF039751; AAB96923.1; -; mRNA.
DR EMBL; AF043328; AAB99850.1; -; mRNA.
DR EMBL; AF044169; AAC00504.1; -; mRNA.
DR RefSeq; NP_989487.1; NM_204156.1.
DR AlphaFoldDB; P56517; -.
DR SMR; P56517; -.
DR BioGRID; 675010; 2.
DR STRING; 9031.ENSGALP00000005212; -.
DR PaxDb; P56517; -.
DR Ensembl; ENSGALT00000084635; ENSGALP00000059784; ENSGALG00000003297.
DR GeneID; 373961; -.
DR KEGG; gga:373961; -.
DR CTD; 3065; -.
DR VEuPathDB; HostDB:geneid_373961; -.
DR eggNOG; KOG1342; Eukaryota.
DR GeneTree; ENSGT00940000154301; -.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; P56517; -.
DR OMA; HFGMTHP; -.
DR OrthoDB; 732770at2759; -.
DR PhylomeDB; P56517; -.
DR TreeFam; TF106171; -.
DR BRENDA; 3.5.1.98; 1306.
DR Reactome; R-GGA-1538133; G0 and Early G1.
DR Reactome; R-GGA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-GGA-3214815; HDACs deacetylate histones.
DR Reactome; R-GGA-350054; Notch-HLH transcription pathway.
DR Reactome; R-GGA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-GGA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-GGA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-GGA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-GGA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-GGA-9701898; STAT3 nuclear events downstream of ALK signaling.
DR Reactome; R-GGA-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P56517; -.
DR Proteomes; UP000000539; Chromosome 23.
DR Bgee; ENSGALG00000003297; Expressed in colon and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IEA:Ensembl.
DR GO; GO:0016580; C:Sin3 complex; IEA:Ensembl.
DR GO; GO:0017053; C:transcription repressor complex; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; TAS:UniProtKB.
DR GO; GO:0070888; F:E-box binding; IEA:Ensembl.
DR GO; GO:0004407; F:histone deacetylase activity; ISS:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0160009; F:histone decrotonylase activity; ISS:UniProtKB.
DR GO; GO:0035851; F:Krueppel-associated box domain binding; IEA:Ensembl.
DR GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0001222; F:transcription corepressor binding; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; IEA:Ensembl.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin assembly; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0007492; P:endoderm development; IEA:Ensembl.
DR GO; GO:0009913; P:epidermal cell differentiation; IEA:Ensembl.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
DR GO; GO:0061198; P:fungiform papilla formation; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0070932; P:histone H3 deacetylation; IEA:Ensembl.
DR GO; GO:0070933; P:histone H4 deacetylation; IEA:Ensembl.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IEA:Ensembl.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:2000273; P:positive regulation of signaling receptor activity; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0052548; P:regulation of endopeptidase activity; IEA:Ensembl.
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 Chromatin regulator; Hydrolase; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..480
FT /note="Histone deacetylase 1"
FT /id="PRO_0000114689"
FT REGION 9..321
FT /note="Histone deacetylase"
FT REGION 376..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT CONFLICT 3..4
FT /note="LT -> VM (in Ref. 2; AAB99850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 54939 MW; 82C78CE285C779D9 CRC64;
MALTQGTKRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN
AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSAGGSVAS
AVKLNKQQTD IAVNWAGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV LYIDIDIHHG
DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI
FKPVISKVME TFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG
GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE
KIKQRLFENL RMLPHAPGVQ MQPIPEDAVQ EDSGDEEEED PEKRISIRNS DKRISCDEEF
SDSEDEGEGG RKNVANFKKA KRVKTEEEKE EEEKKDEKEE EKAKEEKAEP KGVKEETKST
