ID   HDAC1_STRPU             Reviewed;         576 AA.
AC   P56518;
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 1;
DE            Short=HD1;
DE            EC=3.5.1.98;
GN   Name=HDAC1;
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9865968; DOI=10.1046/j.1440-169x.1998.t01-4-00002.x;
RA   Nemer M.;
RT   "Histone deacetylase mRNA temporally and spatially regulated in its
RT   expression in sea urchin embryos.";
RL   Dev. Growth Differ. 40:583-590(1998).
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. Histone deacetylases act via the formation of
CC       large multiprotein complexes (By similarity). {ECO:0000250}.
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:0000305}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF032919; AAB87685.1; -; mRNA.
DR   RefSeq; NP_999711.1; NM_214546.1.
DR   AlphaFoldDB; P56518; -.
DR   SMR; P56518; -.
DR   STRING; 7668.P56518; -.
DR   EnsemblMetazoa; NM_214546; NP_999711; GeneID_373339.
DR   GeneID; 373339; -.
DR   KEGG; spu:373339; -.
DR   CTD; 3065; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_7_4_1; -.
DR   InParanoid; P56518; -.
DR   OMA; EFCKISC; -.
DR   OrthoDB; 1327607at2759; -.
DR   PhylomeDB; P56518; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016581; C:NuRD complex; IBA:GO_Central.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; TAS:UniProtKB.
DR   GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
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   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:SF13; HISTONE DEACETYLASE HDAC1; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Hydrolase; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..576
FT                   /note="Histone deacetylase 1"
FT                   /id="PRO_0000114690"
FT   REGION          9..320
FT                   /note="Histone deacetylase"
FT   REGION          374..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..566
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   576 AA;  64078 MW;  B3D11A844A2088E9 CRC64;
     MASTGTKKRV CYYYDGDVGN YYYGQGHPMK PHRIRMTHNL ILNYGLYRKM EIYRPHKAVM
     EEMTKYHSDD YVKFLRTIRP DNMSEYTKQM QRFNVGEDCP VFDGLYEFCQ LSSGGSVAGA
     VKLNKQQTDI AINWAGGLHH AKKSEASGFC YVNDIVLAIL ELLKYHQRVL YIDIDIHHGD
     GVEEAFYTTD RVMTVSFHKY GEYFPGTGDL RDIGAGKGKY YAVNFPLRDG IDDESYDKIF
     KPIMCKVMEM YQPSAICLQC GADSLSGDRL GCFNLTLKGH AKCVEFMKQY NLPLLLMGGG
     GYTIRNVARC WTYETSTALG VEIANELPYN DYFEYFGPDF KLHISPSNMT NQNTGEYLDK
     IKTRLYENMR MIPHAPGVQM QPIPEDAIPD DSDAEDEAEN PDKRISIMAQ DKRIQRDDEF
     SDSEDEGETR LPGEGGRRDH RSHKAKRSKI DDSPGKEADK EAKSSDASKE AKPAAEPQAV
     PMDTTPAPPP KKSEDKPEAS KPTEVKAKPA EKEPGEGEAS PADLVVPVPK VSAPSEGATL
     PAVTIPPSSG TSQPPADPPV SAPTPTPASA PAEKQD
//