ID   HDAC2_CHICK             Reviewed;         488 AA.
AC   P56519;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Histone deacetylase 2;
DE            Short=HD2;
DE            EC=3.5.1.98 {ECO:0000250|UniProtKB:Q92769};
DE   AltName: Full=Protein deacylase HDAC2 {ECO:0000305};
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q92769};
GN   Name=HDAC2;
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.
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). Histone deacetylation gives a tag for epigenetic repression
CC       and plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via the
CC       formation of large multiprotein complexes (By similarity). Also
CC       deacetylates non-histone proteins. In addition to protein deacetylase
CC       activity, also acts as a protein-lysine deacylase by recognizing other
CC       acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl) and 2-
CC       hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine
CC       residues, leading to protein decrotonylation and de-2-
CC       hydroxyisobutyrylation, respectively (By similarity).
CC       {ECO:0000250|UniProtKB:P70288, ECO:0000250|UniProtKB:Q92769}.
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:P70288};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC         Evidence={ECO:0000250|UniProtKB:P70288};
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:Q92769};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC         Evidence={ECO:0000250|UniProtKB:Q92769};
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:Q92769};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC         Evidence={ECO:0000250|UniProtKB:Q92769};
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:Q92769};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69177;
CC         Evidence={ECO:0000250|UniProtKB:Q92769};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92769}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q92769}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF039752; AAB96924.1; -; mRNA.
DR   AlphaFoldDB; P56519; -.
DR   SMR; P56519; -.
DR   BioGRID; 675914; 3.
DR   IntAct; P56519; 1.
DR   STRING; 9031.ENSGALP00000057637; -.
DR   iPTMnet; P56519; -.
DR   PaxDb; 9031-ENSGALP00000024133; -.
DR   VEuPathDB; HostDB:geneid_395635; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   InParanoid; P56519; -.
DR   PhylomeDB; P56519; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR   GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016581; C:NuRD complex; ISS:UniProtKB.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; TAS:UniProtKB.
DR   GO; GO:0004407; F:histone deacetylase activity; ISS:UniProtKB.
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:0006325; P:chromatin organization; TAS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd10011; HDAC2; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 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   PANTHER; PTHR10625:SF2; HISTONE DEACETYLASE 2; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Cytoplasm; Hydrolase; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..488
FT                   /note="Histone deacetylase 2"
FT                   /id="PRO_0000114695"
FT   REGION          9..322
FT                   /note="Histone deacetylase"
FT   REGION          389..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
SQ   SEQUENCE   488 AA;  55153 MW;  4F79B9C0D4A2D065 CRC64;
     MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR KMEIYRPHKA
     TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED CPVFDGLFEF CQLSTGGSVA
     GAVKLNRQQT DMAVNWAGGL HHAKKSEASG FCYVNDIVLA ILELLKYHQR VLYIDIDIHH
     GDGVEEAFYT TDRVMTVSEV SMVNNFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ
     IFKPIISKVM EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVVK TFNLPLLMLG
     GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN MTNQNTPEYM
     EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE DPDKRISIRA SDKRIACDEE
     FSDSEDEGEG GRRNVADHKK GAKKARIEED KKETEDKKAD VKEEDKSKDN SGEKTDTKGA
     KSEQLSNP
//