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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: HDA6_ARATH B1PXB9_ARATH A0A178URK5_ARATH
LinkDB: HDA6_ARATH B1PXB9_ARATH A0A178URK5_ARATH
Original site: HDA6_ARATH B1PXB9_ARATH A0A178URK5_ARATH 
ID   HDA6_ARATH              Reviewed;         471 AA.
AC   Q9FML2; Q9FVE5;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   23-MAY-2018, entry version 120.
DE   RecName: Full=Histone deacetylase 6;
DE            EC=3.5.1.98;
GN   Name=HDA6; Synonyms=RPD3B; OrderedLocusNames=At5g63110;
GN   ORFNames=MDC12.7;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=11117260; DOI=10.1023/A:1006498413543;
RA   Wu K., Malik K., Tian L., Brown D., Miki B.;
RT   "Functional analysis of a RPD3 histone deacetylase homologue in
RT   Arabidopsis thaliana.";
RL   Plant Mol. Biol. 44:167-176(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III.
RT   Sequence features of the regions of 1,191,918 bp covered by seventeen
RT   physically assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF GLY-127; GLY-284 AND ALA-294.
RX   PubMed=11340181; DOI=10.1105/tpc.13.5.1047;
RA   Murfett J., Wang X.-J., Hagen G., Guilfoyle T.J.;
RT   "Identification of Arabidopsis histone deacetylase HDA6 mutants that
RT   affect transgene expression.";
RL   Plant Cell 13:1047-1061(2001).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF 459-ASP--SER-471.
RX   PubMed=12486004; DOI=10.1093/emboj/cdf663;
RA   Aufsatz W., Mette M.F., van der Winden J., Matzke M., Matzke A.J.M.;
RT   "HDA6, a putative histone deacetylase needed to enhance DNA
RT   methylation induced by double-stranded RNA.";
RL   EMBO J. 21:6832-6841(2002).
RN   [8]
RP   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
RT   families of Arabidopsis thaliana suggests functional diversification
RT   of chromatin modification among multicellular eukaryotes.";
RL   Nucleic Acids Res. 30:5036-5055(2002).
RN   [9]
RP   INTERACTION WITH COI1.
RX   PubMed=12445118; DOI=10.1046/j.1365-313X.2002.01432.x;
RA   Devoto A., Nieto-Rostro M., Xie D., Ellis C., Harmston R., Patrick E.,
RA   Davis J., Sherratt L., Coleman M., Turner J.G.;
RT   "COI1 links jasmonate signalling and fertility to the SCF ubiquitin-
RT   ligase complex in Arabidopsis.";
RL   Plant J. 32:457-466(2002).
RN   [10]
RP   FUNCTION, AND MUTAGENESIS OF GLY-16.
RX   PubMed=15037732; DOI=10.1105/tpc.018754;
RA   Probst A.V., Fagard M., Proux F., Mourrain P., Boutet S., Earley K.,
RA   Lawrence R.J., Pikaard C.S., Murfett J., Furner I., Vaucheret H.,
RA   Mittelsten Scheid O.;
RT   "Arabidopsis histone deacetylase HDA6 is required for maintenance of
RT   transcriptional gene silencing and determines nuclear organization of
RT   rDNA repeats.";
RL   Plant Cell 16:1021-1034(2004).
RN   [11]
RP   INDUCTION.
RX   PubMed=15749761; DOI=10.1105/tpc.104.028514;
RA   Zhou C., Zhang L., Duan J., Miki B., Wu K.;
RT   "HISTONE DEACETYLASE19 is involved in jasmonic acid and ethylene
RT   signaling of pathogen response in Arabidopsis.";
RL   Plant Cell 17:1196-1204(2005).
RN   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
RX   PubMed=16648464; DOI=10.1101/gad.1417706;
RA   Earley K., Lawrence R.J., Pontes O., Reuther R., Enciso A.J.,
RA   Silva M., Neves N., Gross M., Viegas W., Pikaard C.S.;
RT   "Erasure of histone acetylation by Arabidopsis HDA6 mediates large-
RT   scale gene silencing in nucleolar dominance.";
RL   Genes Dev. 20:1283-1293(2006).
RN   [13]
RP   INTERACTION WITH AHL22.
RX   PubMed=22442143; DOI=10.1074/jbc.M111.318477;
RA   Yun J., Kim Y.S., Jung J.H., Seo P.J., Park C.M.;
RT   "The AT-hook motif-containing protein AHL22 regulates flowering
RT   initiation by modifying FLOWERING LOCUS T chromatin in Arabidopsis.";
RL   J. Biol. Chem. 287:15307-15316(2012).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [15]
RP   FUNCTION, INTERACTION WITH AS1, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=23271976; DOI=10.1371/journal.pgen.1003114;
RA   Luo M., Yu C.W., Chen F.F., Zhao L., Tian G., Liu X., Cui Y.,
RA   Yang J.Y., Wu K.;
RT   "Histone deacetylase HDA6 is functionally associated with AS1 in
RT   repression of KNOX genes in arabidopsis.";
RL   PLoS Genet. 8:E1003114-E1003114(2012).
RN   [16]
RP   INTERACTION WITH EBS AND SHL.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=25281686; DOI=10.1105/tpc.114.130781;
RA   Lopez-Gonzalez L., Mouriz A., Narro-Diego L., Bustos R.,
RA   Martinez-Zapater J.M., Jarillo J.A., Pineiro M.;
RT   "Chromatin-dependent repression of the Arabidopsis floral integrator
RT   genes involves plant specific PHD-containing proteins.";
RL   Plant Cell 26:3922-3938(2014).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Might remove acetyl residues only from specific targets, such as
CC       rDNA repeats or complex transgenes. Histone deacetylation gives a
CC       tag for epigenetic repression and plays an important role in
CC       transcriptional regulation, cell cycle progression and
CC       developmental events. Histone deacetylases act via the formation
CC       of large multiprotein complexes. Required for rRNA gene silencing
CC       in nucleolar dominance. Plays a role in transgene silencing, but
CC       this effect seems to bee independent of the histone deacetylase
CC       activity (PubMed:11340181, PubMed:12486004, PubMed:15037732,
CC       PubMed:16648464). Part of the AS1 repressor complex to regulate
CC       the KNOX expression in leaf development (PubMed:23271976). Binds
CC       to KNAT1, KNAT2, and KNATM chromatin (PubMed:23271976).
CC       {ECO:0000269|PubMed:11340181, ECO:0000269|PubMed:12486004,
CC       ECO:0000269|PubMed:15037732, ECO:0000269|PubMed:16648464,
CC       ECO:0000269|PubMed:23271976}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- ENZYME REGULATION: Inhibited by trichostatin A.
CC       {ECO:0000269|PubMed:16648464}.
CC   -!- SUBUNIT: Interacts with Coi1, which functions in an SCF complex
CC       that recruits regulators for ubiquitination. Interacts with AHL22
CC       (PubMed:12445118, PubMed:22442143). Interacts with AS1
CC       (PubMed:23271976). Part of the AS1 repressor complex composed of
CC       AS1, LBD6/AS2 and HDA6 (PubMed:23271976). Binds to EBS and SHL
CC       (PubMed:25281686). {ECO:0000269|PubMed:12445118,
CC       ECO:0000269|PubMed:22442143, ECO:0000269|PubMed:23271976,
CC       ECO:0000269|PubMed:25281686}.
CC   -!- INTERACTION:
CC       O04197:COI1; NbExp=3; IntAct=EBI-639608, EBI-401159;
CC       O24606:EIN3; NbExp=2; IntAct=EBI-639608, EBI-593576;
CC       Q9LMA8:TIFY10A; NbExp=4; IntAct=EBI-639608, EBI-1388539;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000269|PubMed:16648464}. Nucleus
CC       {ECO:0000269|PubMed:23271976}.
CC   -!- TISSUE SPECIFICITY: Not detected in leaves, stems, flowers and
CC       young siliques. {ECO:0000269|PubMed:11117260}.
CC   -!- INDUCTION: By jasmonic acid and ethylene.
CC       {ECO:0000269|PubMed:15749761}.
CC   -!- DISRUPTION PHENOTYPE: Curling and serrated leaves. Down curling
CC       phenotype on both the distal and lateral axis.
CC       {ECO:0000269|PubMed:23271976}.
CC   -!- MISCELLANEOUS: HDA6 mutations induce high acetylation of histone
CC       H4, increased methylation of histone H3 'Lys-4' and
CC       hypomethylation of DNA at particular loci, such as the rDNA
CC       repeats.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
DR   EMBL; AF195548; AAG28475.1; -; mRNA.
DR   EMBL; AB008265; BAB10553.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97705.1; -; Genomic_DNA.
DR   EMBL; AY142660; AAN13198.1; -; mRNA.
DR   EMBL; AY072201; AAL60022.1; -; mRNA.
DR   EMBL; AY088314; AAM65853.1; -; mRNA.
DR   RefSeq; NP_201116.1; NM_125705.4.
DR   UniGene; At.8834; -.
DR   ProteinModelPortal; Q9FML2; -.
DR   SMR; Q9FML2; -.
DR   BioGrid; 21674; 20.
DR   DIP; DIP-33452N; -.
DR   IntAct; Q9FML2; 7.
DR   STRING; 3702.AT5G63110.1; -.
DR   iPTMnet; Q9FML2; -.
DR   PaxDb; Q9FML2; -.
DR   EnsemblPlants; AT5G63110.1; AT5G63110.1; AT5G63110.
DR   GeneID; 836431; -.
DR   Gramene; AT5G63110.1; AT5G63110.1; AT5G63110.
DR   KEGG; ath:AT5G63110; -.
DR   Araport; AT5G63110; -.
DR   TAIR; locus:2162017; AT5G63110.
DR   eggNOG; KOG1342; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   HOGENOM; HOG000225180; -.
DR   InParanoid; Q9FML2; -.
DR   KO; K06067; -.
DR   OMA; MDTSKPK; -.
DR   OrthoDB; EOG093609CH; -.
DR   PhylomeDB; Q9FML2; -.
DR   Reactome; R-ATH-1538133; G0 and Early G1.
DR   Reactome; R-ATH-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-ATH-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   PRO; PR:Q9FML2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FML2; baseline and differential.
DR   Genevisible; Q9FML2; AT.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0004407; F:histone deacetylase activity; IMP:TAIR.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0016458; P:gene silencing; IMP:TAIR.
DR   GO; GO:0016575; P:histone deacetylation; IMP:TAIR.
DR   GO; GO:0016441; P:posttranscriptional gene silencing; IMP:TAIR.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   GO; GO:0010431; P:seed maturation; IMP:TAIR.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
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   PANTHER; PTHR10625; PTHR10625; 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; SSF52768; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromatin regulator; Complete proteome; Hydrolase;
KW   Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    471       Histone deacetylase 6.
FT                                /FTId=PRO_0000280085.
FT   REGION       20    333       Histone deacetylase.
FT   COMPBIAS    311    314       Poly-Gly.
FT   COMPBIAS    428    465       Asp-rich.
FT   ACT_SITE    153    153       {ECO:0000250}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000244|PubMed:22223895}.
FT   MUTAGEN      16     16       G->R: In sil1; suppression of transgene
FT                                silencing. {ECO:0000269|PubMed:15037732}.
FT   MUTAGEN     127    127       G->R: In axe1-1; suppression of transgene
FT                                silencing. {ECO:0000269|PubMed:11340181}.
FT   MUTAGEN     284    284       G->D: In axe1-2; suppression of transgene
FT                                silencing. {ECO:0000269|PubMed:11340181}.
FT   MUTAGEN     294    294       A->V: In axe1-3; suppression of transgene
FT                                silencing. {ECO:0000269|PubMed:11340181}.
FT   MUTAGEN     459    471       Missing: In rts1-2; suppression of
FT                                transgene silencing.
FT                                {ECO:0000269|PubMed:12486004}.
FT   CONFLICT    313    313       G -> E (in Ref. 1; AAG28475).
FT                                {ECO:0000305}.
SQ   SEQUENCE   471 AA;  52652 MW;  CA16C2640D1B1732 CRC64;
     MEADESGISL PSGPDGRKRR VSYFYEPTIG DYYYGQGHPM KPHRIRMAHS LIIHYHLHRR
     LEISRPSLAD ASDIGRFHSP EYVDFLASVS PESMGDPSAA RNLRRFNVGE DCPVFDGLFD
     FCRASAGGSI GAAVKLNRQD ADIAINWGGG LHHAKKSEAS GFCYVNDIVL GILELLKMFK
     RVLYIDIDVH HGDGVEEAFY TTDRVMTVSF HKFGDFFPGT GHIRDVGAEK GKYYALNVPL
     NDGMDDESFR SLFRPLIQKV MEVYQPEAVV LQCGADSLSG DRLGCFNLSV KGHADCLRFL
     RSYNVPLMVL GGGGYTIRNV ARCWCYETAV AVGVEPDNKL PYNEYFEYFG PDYTLHVDPS
     PMENLNTPKD MERIRNTLLE QLSGLIHAPS VQFQHTPPVN RVLDEPEDDM ETRPKPRIWS
     GTATYESDSD DDDKPLHGYS CRGGATTDRD STGEDEMDDD NPEPDVNPPS S
//
ID   B1PXB9_ARATH            Unreviewed;       471 AA.
AC   B1PXB9;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   20-JUN-2018, entry version 89.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894283};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894283};
GN   Name=HDA6 {ECO:0000313|EMBL:ACA97992.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:ACA97992.1};
RN   [1] {ECO:0000313|EMBL:ACA97992.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Clifton R.S., Tessadori F., van Zanten M., Pavlova P., Snoek L.B.,
RA   Millenaar F.F., Schulkes R.K., van Driel R., Voesenek L.A.C.J.,
RA   Spillane C., Fransz P., Peeters A.J.M.;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACA97992.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19730687; DOI=10.1371/journal.pgen.1000638;
RA   Tessadori F., van Zanten M., Pavlova P., Clifton R., Pontvianne F.,
RA   Snoek L.B., Millenaar F.F., Schulkes R.K., van Driel R.,
RA   Voesenek L.A., Spillane C., Pikaard C.S., Fransz P., Peeters A.J.;
RT   "Phytochrome B and histone deacetylase 6 control light-induced
RT   chromatin compaction in Arabidopsis thaliana.";
RL   PLoS Genet. 5:E1000638-E1000638(2009).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC       {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894227}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037913,
CC       ECO:0000256|SAAS:SAAS00894298}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
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DR   EMBL; EU502909; ACA97992.1; -; Genomic_DNA.
DR   EMBL; EU502910; ACA97993.1; -; Genomic_DNA.
DR   RefSeq; NP_201116.1; NM_125705.4.
DR   UniGene; At.8834; -.
DR   EnsemblPlants; AT5G63110.1; AT5G63110.1; AT5G63110.
DR   GeneID; 836431; -.
DR   Gramene; AT5G63110.1; AT5G63110.1; AT5G63110.
DR   KEGG; ath:AT5G63110; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   KO; K06067; -.
DR   OMA; MDTSKPK; -.
DR   OrthoDB; EOG093609CH; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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   PANTHER; PTHR10625; PTHR10625; 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; SSF52768; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894233};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00870288};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894277};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894309};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894290}.
FT   DOMAIN       38    329       Hist_deacetyl. {ECO:0000259|Pfam:
FT                                PF00850}.
FT   ACT_SITE    153    153       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR037913-1}.
FT   METAL       188    188       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   METAL       190    190       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   METAL       276    276       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   BINDING     111    111       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR037913-2}.
FT   BINDING     161    161       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR037913-2}.
FT   BINDING     315    315       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR037913-2}.
SQ   SEQUENCE   471 AA;  52652 MW;  CA16C2640D1B1732 CRC64;
     MEADESGISL PSGPDGRKRR VSYFYEPTIG DYYYGQGHPM KPHRIRMAHS LIIHYHLHRR
     LEISRPSLAD ASDIGRFHSP EYVDFLASVS PESMGDPSAA RNLRRFNVGE DCPVFDGLFD
     FCRASAGGSI GAAVKLNRQD ADIAINWGGG LHHAKKSEAS GFCYVNDIVL GILELLKMFK
     RVLYIDIDVH HGDGVEEAFY TTDRVMTVSF HKFGDFFPGT GHIRDVGAEK GKYYALNVPL
     NDGMDDESFR SLFRPLIQKV MEVYQPEAVV LQCGADSLSG DRLGCFNLSV KGHADCLRFL
     RSYNVPLMVL GGGGYTIRNV ARCWCYETAV AVGVEPDNKL PYNEYFEYFG PDYTLHVDPS
     PMENLNTPKD MERIRNTLLE QLSGLIHAPS VQFQHTPPVN RVLDEPEDDM ETRPKPRIWS
     GTATYESDSD DDDKPLHGYS CRGGATTDRD STGEDEMDDD NPEPDVNPPS S
//
ID   A0A178URK5_ARATH        Unreviewed;       471 AA.
AC   A0A178URK5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   28-MAR-2018, entry version 9.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894283};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894283};
GN   OrderedLocusNames=AXX17_At5g62680 {ECO:0000313|EMBL:OAO96110.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:OAO96110.1, ECO:0000313|Proteomes:UP000078284};
RN   [1] {ECO:0000313|Proteomes:UP000078284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta {ECO:0000313|Proteomes:UP000078284};
RX   PubMed=27354520; DOI=10.1073/pnas.1607532113;
RA   Zapata L., Ding J., Willing E.M., Hartwig B., Bezdan D., Jiao W.B.,
RA   Patel V., Velikkakam James G., Koornneef M., Ossowski S.,
RA   Schneeberger K.;
RT   "Chromosome-level assembly of Arabidopsis thaliana Ler reveals the
RT   extent of translocation and inversion polymorphisms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:E4052-E4060(2016).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC       {ECO:0000256|PIRNR:PIRNR037913, ECO:0000256|SAAS:SAAS00894227}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037913,
CC       ECO:0000256|SAAS:SAAS00894298}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAO96110.1}.
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DR   EMBL; LUHQ01000005; OAO96110.1; -; Genomic_DNA.
DR   RefSeq; NP_201116.1; NM_125705.4.
DR   UniGene; At.8834; -.
DR   SMR; A0A178URK5; -.
DR   EnsemblPlants; AT5G63110.1; AT5G63110.1; AT5G63110.
DR   GeneID; 836431; -.
DR   Gramene; AT5G63110.1; AT5G63110.1; AT5G63110.
DR   KEGG; ath:AT5G63110; -.
DR   KO; K06067; -.
DR   OMA; MDTSKPK; -.
DR   Proteomes; UP000078284; Chromosome 5.
DR   ExpressionAtlas; A0A178URK5; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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   PANTHER; PTHR10625; PTHR10625; 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; SSF52768; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894233};
KW   Complete proteome {ECO:0000313|Proteomes:UP000078284};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00870288};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894277};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894309};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037913,
KW   ECO:0000256|SAAS:SAAS00894290}.
FT   DOMAIN       38    329       Hist_deacetyl. {ECO:0000259|Pfam:
FT                                PF00850}.
FT   ACT_SITE    153    153       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR037913-1}.
FT   METAL       188    188       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   METAL       190    190       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   METAL       276    276       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR037913-3}.
FT   BINDING     111    111       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR037913-2}.
FT   BINDING     161    161       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR037913-2}.
FT   BINDING     315    315       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR037913-2}.
SQ   SEQUENCE   471 AA;  52652 MW;  CA16C2640D1B1732 CRC64;
     MEADESGISL PSGPDGRKRR VSYFYEPTIG DYYYGQGHPM KPHRIRMAHS LIIHYHLHRR
     LEISRPSLAD ASDIGRFHSP EYVDFLASVS PESMGDPSAA RNLRRFNVGE DCPVFDGLFD
     FCRASAGGSI GAAVKLNRQD ADIAINWGGG LHHAKKSEAS GFCYVNDIVL GILELLKMFK
     RVLYIDIDVH HGDGVEEAFY TTDRVMTVSF HKFGDFFPGT GHIRDVGAEK GKYYALNVPL
     NDGMDDESFR SLFRPLIQKV MEVYQPEAVV LQCGADSLSG DRLGCFNLSV KGHADCLRFL
     RSYNVPLMVL GGGGYTIRNV ARCWCYETAV AVGVEPDNKL PYNEYFEYFG PDYTLHVDPS
     PMENLNTPKD MERIRNTLLE QLSGLIHAPS VQFQHTPPVN RVLDEPEDDM ETRPKPRIWS
     GTATYESDSD DDDKPLHGYS CRGGATTDRD STGEDEMDDD NPEPDVNPPS S
//
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