HDA1A_XENLA
ID HDA1A_XENLA Reviewed; 480 AA.
AC Q91695; Q66IY9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable histone deacetylase 1-A;
DE Short=HD1-A;
DE EC=3.5.1.98 {ECO:0000250|UniProtKB:O42227};
DE AltName: Full=AB21;
DE AltName: Full=HDM {ECO:0000303|PubMed:9370292};
DE AltName: Full=Maternally-expressed histone deacetylase;
DE AltName: Full=Protein deacetylase HDAC1-A;
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q13547};
DE AltName: Full=Protein decrotonylase HDAC1-A;
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q13547};
GN Name=hdac1-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte;
RX PubMed=9370292; DOI=10.1016/s0378-1119(97)00325-9;
RA Ladomery M.R., Lyons S., Sommerville J.;
RT "Xenopus HDm, a maternally expressed histone deacetylase, belongs to an
RT ancient family of acetyl-metabolizing enzymes.";
RL Gene 198:275-280(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH RBBP4.
RX PubMed=10381399; DOI=10.1242/jcs.112.14.2441;
RA Ryan J., Llinas A.J., White D.A., Turner B.M., Sommerville J.;
RT "Maternal histone deacetylase is accumulated in the nuclei of Xenopus
RT oocytes as protein complexes with potential enzyme activity.";
RL J. Cell Sci. 112:2441-2452(1999).
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. Also functions as
CC deacetylase for non-histone proteins. In addition to protein
CC deacetylase activity, also has protein-lysine deacylase activity: acts
CC as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl)
CC of histones. {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:O42227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC Evidence={ECO:0000250|UniProtKB:O42227};
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 -!- SUBUNIT: Part of a large multiprotein complex that also contains RBBP4.
CC {ECO:0000269|PubMed:10381399}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O42227}. Cytoplasm
CC {ECO:0000250|UniProtKB:O42227}.
CC -!- TISSUE SPECIFICITY: Oocyte. {ECO:0000269|PubMed:10381399}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Accumulates in previtellogenic oocytes and is maintained at constant
CC level throughout oogenesis and into early embryogenesis. Declines
CC through gastrula to neurula. Not detectable between neurula and
CC tailbud, nor in adult tissues other than ovary.
CC {ECO:0000269|PubMed:10381399, ECO:0000269|PubMed:9370292}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; X78454; CAA55211.1; -; mRNA.
DR EMBL; BC081136; AAH81136.1; -; mRNA.
DR PIR; S60381; S60381.
DR RefSeq; NP_001081491.1; NM_001088022.1.
DR AlphaFoldDB; Q91695; -.
DR SMR; Q91695; -.
DR BioGRID; 99206; 1.
DR GeneID; 397868; -.
DR KEGG; xla:397868; -.
DR CTD; 397868; -.
DR Xenbase; XB-GENE-6252325; hdac1.L.
DR OMA; IKHVMEW; -.
DR OrthoDB; 732770at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 397868; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004407; F:histone deacetylase activity; ISS:UniProtKB.
DR GO; GO:0160009; F:histone decrotonylase activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
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 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Developmental protein; Hydrolase; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..480
FT /note="Probable histone deacetylase 1-A"
FT /id="PRO_0000114691"
FT REGION 10..321
FT /note="Histone deacetylase"
FT REGION 388..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"
SQ SEQUENCE 480 AA; 54748 MW; 7B831822235DADB5 CRC64;
MALTLGTKKK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIFRPHKAS
AEDMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSAGGSVAS
AVKLNKQQTD ISVNWSGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV VYIDIDIHHG
DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYALRD GIDDESYEAI
FKPVMSKVME MFQPSAVVLQ CGADSLSGDR LGCFNLTIKG HAKCVEFIKT FNLPLLMLGG
GGYTIRNVAR CWTYETAVAL DSEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE
KIKQRLFENL RMLPHAPGVQ MQAVAEDSIH DDSGEEDEDD PDKRISIRSS DKRIACDEEF
SDSEDEGEGG RKNVANFKKV KRVKTEEEKE GEDKKDVKEE EKAKDEKTDS KRVKEETKSV
