ID Q7ZYT5_XENLA Unreviewed; 480 AA.
AC Q7ZYT5;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
GN Name=hdac1.S {ECO:0000313|RefSeq:NP_001079396.1,
GN ECO:0000313|Xenbase:XB-GENE-865283};
GN Synonyms=gon-10 {ECO:0000313|RefSeq:NP_001079396.1}, HD1
GN {ECO:0000313|RefSeq:NP_001079396.1}, HD1-B
GN {ECO:0000313|RefSeq:NP_001079396.1}, hdac1
GN {ECO:0000313|RefSeq:NP_001079396.1,
GN ECO:0000313|Xenbase:XB-GENE-865283}, hdac1-a
GN {ECO:0000313|RefSeq:NP_001079396.1}, hdac1-b
GN {ECO:0000313|RefSeq:NP_001079396.1}, hdac1b
GN {ECO:0000313|RefSeq:NP_001079396.1}, RPD3
GN {ECO:0000313|RefSeq:NP_001079396.1}, rpd3l1
GN {ECO:0000313|RefSeq:NP_001079396.1};
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 {ECO:0000313|EMBL:AAH41296.1};
RN [1] {ECO:0000313|RefSeq:NP_001079396.1}
RP NUCLEOTIDE SEQUENCE.
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] {ECO:0000313|RefSeq:NP_001079396.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [3] {ECO:0000313|EMBL:AAH41296.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH41296.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:NP_001079396.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26198637;
RA Wang C., Kam R.K., Shi W., Xia Y., Chen X., Cao Y., Sun J., Du Y., Lu G.,
RA Chen Z., Chan W.Y., Chan S.O., Deng Y., Zhao H.;
RT "The Proto-oncogene Transcription Factor Ets1 Regulates Neural Crest
RT Development through Histone Deacetylase 1 to Mediate Output of Bone
RT Morphogenetic Protein Signaling.";
RL J. Biol. Chem. 290:21925-21938(2015).
RN [5] {ECO:0000313|RefSeq:NP_001079396.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25789466;
RA Tao Y., Ruan H., Guo X., Li L., Shen W.;
RT "HDAC1 regulates the proliferation of radial glial cells in the developing
RT Xenopus tectum.";
RL PLoS ONE 10:e0120118-e0120118(2015).
RN [6] {ECO:0000313|RefSeq:NP_001079396.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30002130; DOI=10.1242/dev.163386;
RA Rao A., LaBonne C.;
RT "Histone deacetylase activity has an essential role in establishing and
RT maintaining the vertebrate neural crest. .";
RL Development 145:dev163386-dev163386(2018).
RN [7] {ECO:0000313|RefSeq:NP_001079396.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00029357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC Evidence={ECO:0000256|ARBA:ARBA00029357};
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:0000256|ARBA:ARBA00029372};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC Evidence={ECO:0000256|ARBA:ARBA00029372};
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:0000256|ARBA:ARBA00029349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC Evidence={ECO:0000256|ARBA:ARBA00029349};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037913}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
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DR EMBL; BC041296; AAH41296.1; -; mRNA.
DR RefSeq; NP_001079396.1; NM_001085927.1.
DR IntAct; Q7ZYT5; 1.
DR STRING; 8355.Q7ZYT5; -.
DR PaxDb; 8355-Q7ZYT5; -.
DR DNASU; 379083; -.
DR GeneID; 379083; -.
DR KEGG; xla:379083; -.
DR AGR; Xenbase:XB-GENE-865283; -.
DR CTD; 379083; -.
DR Xenbase; XB-GENE-865283; hdac1.S.
DR OMA; GKIMEWY; -.
DR OrthoDB; 1327607at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 379083; Expressed in egg cell and 19 other cell types or 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; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|PIRNR:PIRNR037913}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037913};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW Nucleus {ECO:0000256|PIRNR:PIRNR037913};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 28..317
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
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 /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 176
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 178
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 264
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 480 AA; 54940 MW; 2B3BE61E39F27D1F 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 RRNMASFKKL KRVKTEEEKE ADDKKDVKEE EKLKDDKTDS KRVKEETKSA
//
