ID   HDA1B_XENLA             Reviewed;         480 AA.
AC   O42227;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Probable histone deacetylase 1-B;
DE            Short=HD1-B;
DE            EC=3.5.1.98 {ECO:0000269|PubMed:10454532};
DE   AltName: Full=Protein deacetylase HDAC1-B;
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q13547};
DE   AltName: Full=Protein decrotonylase HDAC1-B;
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q13547};
DE   AltName: Full=RPD3 homolog;
GN   Name=hdac1-b;
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].
RX   PubMed=9430643; DOI=10.1093/emboj/17.2.520;
RA   Wong J., Patterton D., Imhof A., Guschin D., Shi Y.-B., Wolffe A.P.;
RT   "Distinct requirements for chromatin assembly in transcriptional repression
RT   by thyroid hormone receptor and histone deacetylase.";
RL   EMBO J. 17:520-534(1998).
RN   [2]
RP   IDENTIFICATION IN A COMPLEX WITH RBBP4 AND MI-2.
RX   PubMed=9663395; DOI=10.1016/s0960-9822(98)70328-8;
RA   Wade P.A., Jones P.L., Vermaak D., Wolffe A.P.;
RT   "A multiple subunit Mi-2 histone deacetylase from Xenopus laevis
RT   cofractionates with an associated Snf2 superfamily ATPase.";
RL   Curr. Biol. 8:843-846(1998).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH RBBP4,
RP   AND MUTAGENESIS OF HIS-141.
RX   PubMed=10454532; DOI=10.1128/mcb.19.9.5847;
RA   Vermaak D., Wade P.A., Jones P.L., Shi Y.-B., Wolffe A.P.;
RT   "Functional analysis of the SIN3-histone deacetylase RPD3-RbAp48-histone H4
RT   connection in the Xenopus oocyte.";
RL   Mol. Cell. Biol. 19:5847-5860(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) (PubMed:10454532). Histone deacetylation gives a tag for
CC       epigenetic repression and plays an important role in transcriptional
CC       regulation, cell cycle progression and developmental events
CC       (PubMed:10454532). Histone deacetylases act via the formation of large
CC       multiprotein complexes (By similarity). Also functions as a 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:Q13547,
CC       ECO:0000269|PubMed:10454532}.
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:0000269|PubMed:10454532};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC         Evidence={ECO:0000269|PubMed:10454532};
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: Found in a large complex with RBBP4 and MI-2.
CC       {ECO:0000269|PubMed:9663395}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10454532}. Cytoplasm
CC       {ECO:0000269|PubMed:10454532}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF020658; AAC60346.1; -; mRNA.
DR   AlphaFoldDB; O42227; -.
DR   SMR; O42227; -.
DR   IntAct; O42227; 1.
DR   AGR; Xenbase:XB-GENE-865283; -.
DR   Xenbase; XB-GENE-865283; hdac1.S.
DR   Proteomes; UP000186698; Genome assembly.
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:0033558; F:protein lysine deacetylase activity; ISS:UniProtKB.
DR   CDD; cd10010; HDAC1; 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:SF21; HISTONE DEACETYLASE 1; 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   1: Evidence at protein level;
KW   Chromatin regulator; Cytoplasm; Hydrolase; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..480
FT                   /note="Probable histone deacetylase 1-B"
FT                   /id="PRO_0000114692"
FT   REGION          10..321
FT                   /note="Histone deacetylase"
FT   REGION          387..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:0000305|PubMed:10454532"
FT   MUTAGEN         141
FT                   /note="H->A: Abolishes histone deacetylase activity."
FT                   /evidence="ECO:0000269|PubMed:10454532"
SQ   SEQUENCE   480 AA;  54893 MW;  CA92DE34D36E39E8 CRC64;
     MALSQGTKKK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAS
     AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS
     AVKLNKQQTD ISVNWSGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV VYIDIDIHHG
     DGVEEAFYTT DRVMSVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI
     FKPVMTKVME MFQPSAVVLQ CGADSLSGDR LGCFNLTIKG HAKCVEFIKT FNLPMLMLGG
     GGYTIRNVAR CWTYETAVAL DSEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE
     KIKQRLFENL RMLPHAPGVQ MQAIPEDSVH DDSGEEDEED PDKRISIRSS DKRIACDEEF
     SDSEDEGEGG RKNVANFKKV KRVKTEEEKE GEDKKDVKEE EKAKDEKTDS KRVKEETKSV
//