HDA8_ARATH
ID HDA8_ARATH Reviewed; 377 AA.
AC Q94EJ2; Q944J5; Q9SJE6;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Histone deacetylase 8 {ECO:0000303|PubMed:12466527};
DE EC=3.5.1.98 {ECO:0000250|UniProtKB:Q8RX28};
GN Name=HDA8 {ECO:0000303|PubMed:12466527};
GN OrderedLocusNames=At1g08460 {ECO:0000312|EMBL:AEE28294.1};
GN ORFNames=T27G7.14 {ECO:0000312|EMBL:AAF22892.1}, T27G7_7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12466527; DOI=10.1093/nar/gkf660;
RA Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S.,
RA Richards E.J., Bender J., Mount D.W., Jorgensen R.A.;
RT "Analysis of histone acetyltransferase and histone deacetylase families of
RT Arabidopsis thaliana suggests functional diversification of chromatin
RT modification among multicellular eukaryotes.";
RL Nucleic Acids Res. 30:5036-5055(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22363501; DOI=10.1371/journal.pone.0030846;
RA Alinsug M.V., Chen F.F., Luo M., Tai R., Jiang L., Wu K.;
RT "Subcellular localization of class II HDAs in Arabidopsis thaliana:
RT nucleocytoplasmic shuttling of HDA15 is driven by light.";
RL PLoS ONE 7:e30846-e30846(2012).
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. {ECO:0000250|UniProtKB:Q8RX28}.
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:Q8RX28};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC Evidence={ECO:0000250|UniProtKB:Q8RX28};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q8GXJ1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q8GXJ1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22363501}. Cytoplasm
CC {ECO:0000269|PubMed:22363501}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves, flowers, siliques and
CC mature seeds. {ECO:0000269|PubMed:22363501}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF22892.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAL16299.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF510167; AAM49769.1; -; mRNA.
DR EMBL; AC006932; AAF22892.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28294.1; -; Genomic_DNA.
DR EMBL; AF410272; AAK95258.1; -; mRNA.
DR EMBL; AF428369; AAL16299.1; ALT_INIT; mRNA.
DR EMBL; AY097371; AAM19887.1; -; mRNA.
DR PIR; G86217; G86217.
DR RefSeq; NP_563817.1; NM_100719.4.
DR AlphaFoldDB; Q94EJ2; -.
DR SMR; Q94EJ2; -.
DR BioGRID; 22607; 1.
DR STRING; 3702.AT1G08460.1; -.
DR PaxDb; Q94EJ2; -.
DR PRIDE; Q94EJ2; -.
DR ProteomicsDB; 230290; -.
DR EnsemblPlants; AT1G08460.1; AT1G08460.1; AT1G08460.
DR GeneID; 837366; -.
DR Gramene; AT1G08460.1; AT1G08460.1; AT1G08460.
DR KEGG; ath:AT1G08460; -.
DR Araport; AT1G08460; -.
DR TAIR; locus:2201826; AT1G08460.
DR eggNOG; KOG1343; Eukaryota.
DR HOGENOM; CLU_007727_8_2_1; -.
DR InParanoid; Q94EJ2; -.
DR OMA; GRAMGFC; -.
DR OrthoDB; 1484694at2759; -.
DR PhylomeDB; Q94EJ2; -.
DR PRO; PR:Q94EJ2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94EJ2; baseline and differential.
DR Genevisible; Q94EJ2; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR000286; His_deacetylse.
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 SUPFAM; SSF52768; SSF52768; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc.
FT CHAIN 1..377
FT /note="Histone deacetylase 8"
FT /id="PRO_0000280087"
FT REGION 5..336
FT /note="Histone deacetylase"
FT ACT_SITE 145
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT SITE 318
FT /note="Polarizes the scissile carbonyl of the substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
SQ SEQUENCE 377 AA; 41263 MW; 538E741343EC8CF3 CRC64;
MVTNRVDVFW HEGMLRHDAV EGVFDTGYDP GFLDVLEKHP ENADRVRNML SILRRGPIAP
HVNWFTGLPA IVSELLMFHT SEYIEKLVEA DKSGERCEIA AGTFMSPGSW EAALLAAGTT
LSAMQHILDC HGKIAYALVR PPGHHSQPTQ ADGYCFLNNA ALAVKLALNS GSCSRVAVID
IDVHYGNGTA EGFYTSDKVL TVSLHMNHGS WGSSHPQKGS IDELGEDVGL GYNLNVPLPN
GTGDRGYEYA MNELVVPAVR RFGPDMVVLV VGQDSSAFDP NGRQSLTMNG YRRIGQIMRG
VAEEHSHGRL LMVQEGGYHV TYAAYCLHAM LEGVLKIPEP HLSDPIAYYP EEEANAVAAV
ESIKTYHTEF VPFLRGT
