HDA1_CAEEL
ID HDA1_CAEEL Reviewed; 461 AA.
AC O17695;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Histone deacetylase 1;
DE EC=3.5.1.98;
GN Name=hda-1 {ECO:0000312|WormBase:C53A5.3};
GN ORFNames=C53A5.3 {ECO:0000312|WormBase:C53A5.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP INTERACTION WITH LIN-53, AND DISRUPTION PHENOTYPE.
RX PubMed=9875852; DOI=10.1016/s0092-8674(00)81722-5;
RA Lu X., Horvitz H.R.;
RT "lin-35 and lin-53, two genes that antagonize a C. elegans Ras pathway,
RT encode proteins similar to Rb and its binding protein RbAp48.";
RL Cell 95:981-991(1998).
RN [3]
RP FUNCTION, AND INTERACTION WITH POP-1.
RX PubMed=11742996; DOI=10.1093/emboj/20.24.7197;
RA Calvo D., Victor M., Gay F., Sui G., Luke M.P.-S., Dufourcq P., Wen G.,
RA Maduro M., Rothman J., Shi Y.;
RT "A POP-1 repressor complex restricts inappropriate cell type-specific gene
RT transcription during Caenorhabditis elegans embryogenesis.";
RL EMBO J. 20:7197-7208(2001).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP GLY-186.
RX PubMed=11940660; DOI=10.1128/mcb.22.9.3024-3034.2002;
RA Dufourcq P., Victor M., Gay F., Calvo D., Hodgkin J., Shi Y.;
RT "Functional requirement for histone deacetylase 1 in Caenorhabditis elegans
RT gonadogenesis.";
RL Mol. Cell. Biol. 22:3024-3034(2002).
RN [5]
RP SUMOYLATION.
RX PubMed=15990876; DOI=10.1038/sj.emboj.7600726;
RA Poulin G., Dong Y., Fraser A.G., Hopper N.A., Ahringer J.;
RT "Chromatin regulation and sumoylation in the inhibition of Ras-induced
RT vulval development in Caenorhabditis elegans.";
RL EMBO J. 24:2613-2623(2005).
RN [6] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH TRA-4 AND NASP-1.
RX PubMed=17011494; DOI=10.1016/j.devcel.2006.07.015;
RA Grote P., Conradt B.;
RT "The PLZF-like protein TRA-4 cooperates with the Gli-like transcription
RT factor TRA-1 to promote female development in C. elegans.";
RL Dev. Cell 11:561-573(2006).
RN [7]
RP IDENTIFICATION IN COMPLEX WITH LIN-53.
RX PubMed=17075059; DOI=10.1073/pnas.0608461103;
RA Harrison M.M., Ceol C.J., Lu X., Horvitz H.R.;
RT "Some C. elegans class B synthetic multivulva proteins encode a conserved
RT LIN-35 Rb-containing complex distinct from a NuRD-like complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16782-16787(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25446273; DOI=10.1016/j.ydbio.2014.10.014;
RA Krueger A.V., Jelier R., Dzyubachyk O., Zimmerman T., Meijering E.,
RA Lehner B.;
RT "Comprehensive single cell-resolution analysis of the role of chromatin
RT regulators in early C. elegans embryogenesis.";
RL Dev. Biol. 398:153-162(2015).
RN [9] {ECO:0000305}
RP INTERACTION WITH HPL-1.
RX PubMed=26476455; DOI=10.1093/nar/gkv1063;
RA Vandamme J., Sidoli S., Mariani L., Friis C., Christensen J., Helin K.,
RA Jensen O.N., Salcini A.E.;
RT "H3K23me2 is a new heterochromatic mark in Caenorhabditis elegans.";
RL Nucleic Acids Res. 43:9694-9710(2015).
RN [10]
RP FUNCTION, AND INTERACTION WITH AKIR-1.
RX PubMed=30036395; DOI=10.1371/journal.pgen.1007494;
RA Polanowska J., Chen J.X., Soule J., Omi S., Belougne J., Taffoni C.,
RA Pujol N., Selbach M., Zugasti O., Ewbank J.J.;
RT "Evolutionary plasticity in the innate immune function of Akirin.";
RL PLoS Genet. 14:E1007494-E1007494(2018).
RN [11] {ECO:0000305}
RP IDENTIFICATION IN THE SIN3S COMPLEX, INTERACTION WITH WDR-5.1 AND CFP-1,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=31602465; DOI=10.1093/nar/gkz880;
RA Beurton F., Stempor P., Caron M., Appert A., Dong Y., Chen R.A., Cluet D.,
RA Coute Y., Herbette M., Huang N., Polveche H., Spichty M., Bedet C.,
RA Ahringer J., Palladino F.;
RT "Physical and functional interaction between SET1/COMPASS complex component
RT CFP-1 and a Sin3S HDAC complex in C. elegans.";
RL Nucleic Acids Res. 47:11164-11180(2019).
RN [12]
RP FUNCTION, INTERACTION WITH DVE-1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=32934238; DOI=10.1038/s41467-020-18501-w;
RA Shao L.W., Peng Q., Dong M., Gao K., Li Y., Li Y., Li C.Y., Liu Y.;
RT "Histone deacetylase HDA-1 modulates mitochondrial stress response and
RT longevity.";
RL Nat. Commun. 11:4639-4639(2020).
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. Plays an important
CC role in transcriptional regulation, cell cycle progression and
CC developmental events (PubMed:25446273). Histone deacetylases act via
CC the formation of large multiprotein complexes. Involved in the endoderm
CC determination possibly by repressing end-1 expression. Also involved in
CC vulval development, possibly by repressing lag-2 expression. Required
CC during mitochondrial stress for the activation of genes involved in the
CC mitochondrial unfolded protein response (mtUPR), in concert with
CC homeobox protein dve-1 (PubMed:32934238). Promotes normal hermaphrodite
CC (XX) development, in concert with zinc finger protein tra-4 and nasp-1,
CC perhaps as components of a complex (PubMed:17011494). Plays a role in
CC the regulation of longevity and mtUPR-associated innate immunity
CC (PubMed:32934238). In association with akir-1, plays a role in
CC regulating the transcription of antimicrobial peptide genes in response
CC to fungal infection (PubMed:30036395). {ECO:0000269|PubMed:11742996,
CC ECO:0000269|PubMed:11940660, ECO:0000269|PubMed:17011494,
CC ECO:0000269|PubMed:25446273, ECO:0000269|PubMed:30036395,
CC ECO:0000269|PubMed:32934238}.
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 -!- SUBUNIT: Component of the SIN3S complex, which contains at least sin-3,
CC hda-1, athp-1 and mrg-1 (PubMed:31602465). Probable component of a
CC NuRD-like complex, composed of at least lin-53 and hda-1
CC (PubMed:17075059). Interacts with lin-53 (PubMed:9875852,
CC PubMed:17075059). Interacts with pop-1 (PubMed:11742996). Interacts
CC with akir-1 (PubMed:30036395). Interacts with wdr-5.1
CC (PubMed:31602465). Interacts with cfp-1 (PubMed:31602465). Interacts
CC with dve-1 (PubMed:32934238). Interacts with tra-4 (PubMed:17011494).
CC May interact with nasp-1 (PubMed:17011494). Interacts with chromobox
CC protein homolog hpl-1. {ECO:0000269|PubMed:11742996,
CC ECO:0000269|PubMed:17011494, ECO:0000269|PubMed:17075059,
CC ECO:0000269|PubMed:26476455, ECO:0000269|PubMed:30036395,
CC ECO:0000269|PubMed:31602465, ECO:0000269|PubMed:32934238,
CC ECO:0000269|PubMed:9875852}.
CC -!- INTERACTION:
CC O17695; Q94131: pie-1; NbExp=3; IntAct=EBI-318045, EBI-300501;
CC O17695; Q10666: pop-1; NbExp=3; IntAct=EBI-318045, EBI-317870;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32934238}. Cytoplasm.
CC Chromosome {ECO:0000269|PubMed:32934238}. Note=Except in the germ line
CC where it is also cytoplasmic.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed throughout embryonic and
CC postembryonic development. {ECO:0000269|PubMed:11940660}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:11940660}.
CC -!- PTM: Sumoylated. {ECO:0000305|PubMed:15990876}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in embryonic
CC lethality. RNAi-mediated knockdown results in delayed cell cycle
CC progression (PubMed:25446273). RNAi-mediated knockdown inhibits
CC expression of hsp-6 when adults are exposed to conditions causing
CC mitochondrial stress (PubMed:32934238). Reduces the dve-1 protein level
CC (PubMed:32934238). {ECO:0000269|PubMed:25446273,
CC ECO:0000269|PubMed:32934238, ECO:0000269|PubMed:9875852}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; Z81486; CAB03984.1; -; Genomic_DNA.
DR PIR; T20163; T20163.
DR RefSeq; NP_506599.1; NM_074198.7.
DR AlphaFoldDB; O17695; -.
DR SMR; O17695; -.
DR BioGRID; 44961; 40.
DR DIP; DIP-26427N; -.
DR IntAct; O17695; 10.
DR MINT; O17695; -.
DR STRING; 6239.C53A5.3; -.
DR iPTMnet; O17695; -.
DR EPD; O17695; -.
DR PaxDb; O17695; -.
DR PeptideAtlas; O17695; -.
DR EnsemblMetazoa; C53A5.3.1; C53A5.3.1; WBGene00001834.
DR GeneID; 179959; -.
DR KEGG; cel:CELE_C53A5.3; -.
DR UCSC; C53A5.3.1; c. elegans.
DR CTD; 179959; -.
DR WormBase; C53A5.3; CE08952; WBGene00001834; hda-1.
DR eggNOG; KOG1342; Eukaryota.
DR GeneTree; ENSGT00940000165542; -.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; O17695; -.
DR OMA; FHSEEYM; -.
DR OrthoDB; 732770at2759; -.
DR PhylomeDB; O17695; -.
DR Reactome; R-CEL-1538133; G0 and Early G1.
DR Reactome; R-CEL-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-CEL-3214815; HDACs deacetylate histones.
DR Reactome; R-CEL-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-CEL-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-CEL-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-CEL-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-CEL-9018519; Estrogen-dependent gene expression.
DR Reactome; R-CEL-9701898; STAT3 nuclear events downstream of ALK signaling.
DR Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; O17695; -.
DR PRO; PR:O17695; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001834; Expressed in embryo and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043073; C:germ cell nucleus; IDA:WormBase.
DR GO; GO:0000118; C:histone deacetylase complex; IPI:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IMP:UniProtKB.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:WormBase.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0030154; P:cell differentiation; IMP:WormBase.
DR GO; GO:0006325; P:chromatin organization; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:WormBase.
DR GO; GO:0008406; P:gonad development; IMP:WormBase.
DR GO; GO:0042001; P:hermaphrodite somatic sex determination; IMP:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IDA:WormBase.
DR GO; GO:0034514; P:mitochondrial unfolded protein response; IMP:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:WormBase.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IGI:WormBase.
DR GO; GO:1903854; P:negative regulation of stress response to copper ion; IGI:WormBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0040027; P:negative regulation of vulval development; IMP:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0045595; P:regulation of cell differentiation; IGI:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:UniProtKB.
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 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; Chromosome; Cytoplasm; Developmental protein;
KW Hydrolase; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..461
FT /note="Histone deacetylase 1"
FT /id="PRO_0000114719"
FT REGION 13..325
FT /note="Histone deacetylase"
FT REGION 404..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /evidence="ECO:0000250"
FT MUTAGEN 145
FT /note="H->F: Loss of function."
FT MUTAGEN 186
FT /note="G->E: In gon-10; specific defects in gonadogenesis
FT and vulval development."
FT /evidence="ECO:0000269|PubMed:11940660"
SQ SEQUENCE 461 AA; 52138 MW; 9A104E88C5A1C07A CRC64;
MNSNGPLMEH GKRRVAYYYD SNIGNYYYGQ GHVMKPHRIR MTHHLVLNYG LYRNLEIFRP
FPASFEDMTR FHSDEYMTFL KSANPDNLKS FNKQMLKFNV GEDCPLFDGL YEFCQLSSGG
SLAAATKLNK QKVDIAINWM GGLHHAKKSE ASGFCYTNDI VLGILELLKY HKRVLYVDID
VHHGDGVEEA FYTTDRVMTV SFHKYGDFFP GTGDLKDIGA GKGKLYSVNV PLRDGITDVS
YQSIFKPIMT KVMERFDPCA VVLQCGADSL NGDRLGPFNL TLKGHGECAR FFRSYNVPLM
MVGGGGYTPR NVARCWTYET SIAVDKEVPN ELPYNDYFEY FGPNYRLHIE SSNAANENSS
DMLAKLQTDV IANLEQLTFV PSVQMRPIPE DALSALNDDS LIADQANPDK RLPPQITDGM
IQDDGDFYDG EREGDDRRNE SDAKRAAQFE SEGGEKRQKT E
