HDAC1_STRPU
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 03-AUG-2022, entry version 119.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF032919; AAB87685.1; -; mRNA.
DR RefSeq; NP_999711.1; NM_214546.1.
DR AlphaFoldDB; P56518; -.
DR SMR; P56518; -.
DR STRING; 7668.SPU_008768-tr; -.
DR PRIDE; 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; IKHVMEW; -.
DR OrthoDB; 732770at2759; -.
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; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
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:0016575; P:histone deacetylation; IEA:InterPro.
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 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..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