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   04-NOV-2026, entry version 163.
DE   RecName: Full=Histone deacetylase 6 {ECO:0000303|PubMed:11340181, ECO:0000303|PubMed:28229965};
DE            Short=AtHDA6 {ECO:0000303|PubMed:11340181, ECO:0000303|PubMed:28229965};
DE            EC=3.5.1.98 {ECO:0000269|PubMed:21398257};
GN   Name=HDA6 {ECO:0000303|PubMed:11340181, ECO:0000303|PubMed:28229965};
GN   Synonyms=RPD3B {ECO:0000303|PubMed:11117260};
GN   OrderedLocusNames=At5g63110 {ECO:0000312|Araport:AT5G63110};
GN   ORFNames=MDC12.7 {ECO:0000312|EMBL:BAB10553.1};
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], 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 Arabidopsis
RT   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. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   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 reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
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   [7]
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 affect
RT   transgene expression.";
RL   Plant Cell 13:1047-1061(2001).
RN   [8]
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 methylation
RT   induced by double-stranded RNA.";
RL   EMBO J. 21:6832-6841(2002).
RN   [9]
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 families of
RT   Arabidopsis thaliana suggests functional diversification of chromatin
RT   modification among multicellular eukaryotes.";
RL   Nucleic Acids Res. 30:5036-5055(2002).
RN   [10]
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-ligase
RT   complex in Arabidopsis.";
RL   Plant J. 32:457-466(2002).
RN   [11]
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 rDNA
RT   repeats.";
RL   Plant Cell 16:1021-1034(2004).
RN   [12]
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 signaling
RT   of pathogen response in Arabidopsis.";
RL   Plant Cell 17:1196-1204(2005).
RN   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX   PubMed=16648464; DOI=10.1101/gad.1417706;
RA   Earley K., Lawrence R.J., Pontes O., Reuther R., Enciso A.J., Silva M.,
RA   Neves N., Gross M., Viegas W., Pikaard C.S.;
RT   "Erasure of histone acetylation by Arabidopsis HDA6 mediates large-scale
RT   gene silencing in nucleolar dominance.";
RL   Genes Dev. 20:1283-1293(2006).
RN   [14]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH FLD.
RX   PubMed=21398257; DOI=10.1104/pp.111.174417;
RA   Yu C.-W., Liu X., Luo M., Chen C., Lin X., Tian G., Lu Q., Cui Y., Wu K.;
RT   "HISTONE DEACETYLASE6 interacts with FLOWERING LOCUS D and regulates
RT   flowering in Arabidopsis.";
RL   Plant Physiol. 156:173-184(2011).
RN   [15]
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 initiation
RT   by modifying FLOWERING LOCUS T chromatin in Arabidopsis.";
RL   J. Biol. Chem. 287:15307-15316(2012).
RN   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   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., Meinnel T.,
RA   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   [17]
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., Yang J.Y.,
RA   Wu K.;
RT   "Histone deacetylase HDA6 is functionally associated with AS1 in repression
RT   of KNOX genes in arabidopsis.";
RL   PLoS Genet. 8:E1003114-E1003114(2012).
RN   [18]
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 genes
RT   involves plant specific PHD-containing proteins.";
RL   Plant Cell 26:3922-3938(2014).
RN   [19]
RP   FUNCTION, AND INTERACTION WITH HDA5.
RX   PubMed=25922987; DOI=10.1111/tpj.12868;
RA   Luo M., Tai R., Yu C.W., Yang S., Chen C.Y., Lin W.D., Schmidt W., Wu K.;
RT   "Regulation of flowering time by the histone deacetylase HDA5 in
RT   Arabidopsis.";
RL   Plant J. 82:925-936(2015).
RN   [20]
RP   INTERACTION WITH MBD6.
RX   PubMed=28229965; DOI=10.1007/s12038-016-9658-1;
RA   Parida A.P., Sharma A., Sharma A.K.;
RT   "AtMBD6, a methyl CpG binding domain protein, maintains gene silencing in
RT   Arabidopsis by interacting with RNA binding proteins.";
RL   J. Biosci. 42:57-68(2017).
RN   [21]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH GYRB3.
RC   STRAIN=cv. Columbia;
RX   PubMed=41036628; DOI=10.1093/nar/gkaf985;
RA   Gy I., Beaubiat S., Bouche N.;
RT   "The arabidopsis GyraseB3 contributes to transposon silencing by promoting
RT   histone deacetylation.";
RL   Nucleic Acids Res. 53:0-0(2025).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC       N-terminal part of the core histones (H2A, H2B, H3 and H4). Might
CC       remove acetyl residues only from specific targets, such as rDNA repeats
CC       or complex transgenes. Histone deacetylation gives a tag for epigenetic
CC       repression and plays an important role in transcriptional regulation,
CC       cell cycle progression and developmental events. Together with GYRB3,
CC       contributes to transposable elements (TEs) silencing by promoting
CC       histone deacetylation (PubMed:41036628). Histone deacetylases act via
CC       the formation of large multiprotein complexes. Required for rRNA gene
CC       silencing in nucleolar dominance. Plays a role in transgene silencing,
CC       but 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 the
CC       KNOX expression in leaf development (PubMed:23271976). Binds to KNAT1,
CC       KNAT2, and KNATM chromatin (PubMed:23271976). Involved in the
CC       regulation of flowering time (PubMed:21398257, PubMed:25922987). Forms
CC       a histone deacetylase complex with HDA5, FLD and MSI4/FVE that
CC       represses FLC gene expression to control flowering time
CC       (PubMed:21398257, PubMed:25922987). {ECO:0000269|PubMed:11340181,
CC       ECO:0000269|PubMed:12486004, ECO:0000269|PubMed:15037732,
CC       ECO:0000269|PubMed:16648464, ECO:0000269|PubMed:21398257,
CC       ECO:0000269|PubMed:23271976, ECO:0000269|PubMed:25922987,
CC       ECO:0000269|PubMed:41036628}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] +
CC         acetate; 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:21398257};
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   -!- ACTIVITY REGULATION: Inhibited by trichostatin A.
CC       {ECO:0000269|PubMed:16648464}.
CC   -!- SUBUNIT: Interacts with Coi1, which functions in an SCF complex that
CC       recruits regulators for ubiquitination (PubMed:12445118). Interacts
CC       with AHL22 (PubMed:12445118, PubMed:22442143). Interacts with AS1
CC       (PubMed:23271976). Part of the AS1 repressor complex composed of AS1,
CC       LBD6/AS2 and HDA6 (PubMed:23271976). Binds to EBS and SHL
CC       (PubMed:25281686). Interacts with MBD6 (PubMed:28229965). Interacts
CC       with HDA5 (PubMed:25922987). Interacts with FLD (PubMed:21398257).
CC       Associates with HDA6; this interaction is likely mediating transposable
CC       elements (TEs) silencing (PubMed:41036628).
CC       {ECO:0000269|PubMed:12445118, ECO:0000269|PubMed:21398257,
CC       ECO:0000269|PubMed:22442143, ECO:0000269|PubMed:23271976,
CC       ECO:0000269|PubMed:25281686, ECO:0000269|PubMed:25922987,
CC       ECO:0000269|PubMed:28229965, ECO:0000269|PubMed:41036628}.
CC   -!- INTERACTION:
CC       Q9FML2; O04197: COI1; NbExp=3; IntAct=EBI-639608, EBI-401159;
CC       Q9FML2; O24606: EIN3; NbExp=2; IntAct=EBI-639608, EBI-593576;
CC       Q9FML2; Q9LMA8: TIFY10A; NbExp=4; IntAct=EBI-639608, EBI-1388539;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16648464}.
CC       Nucleus {ECO:0000269|PubMed:23271976}.
CC   -!- TISSUE SPECIFICITY: Not detected in leaves, stems, flowers and young
CC       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 (PubMed:23271976).
CC       Suppression of the developmental phenotypes of ibm2 or ibm1 by
CC       preventing the accumulation of heterochromatic marks (e.g.
CC       hypermethylation) on a large range of target genes (PubMed:41036628).
CC       {ECO:0000269|PubMed:23271976, ECO:0000269|PubMed:41036628}.
CC   -!- MISCELLANEOUS: HDA6 mutations induce high acetylation of histone H4,
CC       increased methylation of histone H3 'Lys-4' and hypomethylation of DNA
CC       at particular loci, such as the rDNA repeats.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF195548; AAG28475.1; -; mRNA.
DR   EMBL; AB008265; BAB10553.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97705.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7057572.1; -; 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   AlphaFoldDB; Q9FML2; -.
DR   SMR; Q9FML2; -.
DR   BioGRID; 21674; 20.
DR   DIP; DIP-33452N; -.
DR   FunCoup; Q9FML2; 3244.
DR   IntAct; Q9FML2; 7.
DR   STRING; 3702.Q9FML2; -.
DR   iPTMnet; Q9FML2; -.
DR   PaxDb; 3702-Q9FML2; -.
DR   ProteomicsDB; 230310; -.
DR   GeneID; 836431; -.
DR   KEGG; ath:AT5G63110; -.
DR   Araport; AT5G63110; -.
DR   TAIR; AT5G63110; HDA6.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_7_12_1; -.
DR   InParanoid; Q9FML2; -.
DR   OMA; AAGHPMK; -.
DR   OrthoDB; 1918432at2759; -.
DR   PhylomeDB; Q9FML2; -.
DR   PRO; PR:Q9FML2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Proteomes; UP001984100; Chromosome 5.
DR   ExpressionAtlas; Q9FML2; baseline and differential.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0070822; C:Sin3-type complex; IDA:TAIR.
DR   GO; GO:0004407; F:histone deacetylase activity; IMP:TAIR.
DR   GO; GO:0141221; F:histone deacetylase activity, hydrolytic mechanism; EXP:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0040029; P:epigenetic regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0016441; P:post-transcriptional gene silencing; IMP:TAIR.
DR   GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:UniProtKB.
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:0141005; P:transposable element silencing by heterochromatin formation; IMP:UniProtKB.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR   CDD; cd09991; HDAC_classI; 1.
DR   FunFam; 3.40.800.20:FF:000001; Histone deacetylase; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR003084; HDAC_I/II.
DR   InterPro; IPR000286; HDACs.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625:SF10; HISTONE DEACETYLASE HDAC1; 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   Acetylation; Chromatin regulator; Hydrolase; Metal-binding; Nucleus;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Zinc.
FT   CHAIN           1..471
FT                   /note="Histone deacetylase 6"
FT                   /id="PRO_0000280085"
FT   REGION          20..333
FT                   /note="Histone deacetylase"
FT   REGION          389..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..463
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        153
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT   BINDING         188
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT   SITE            315
FT                   /note="Polarizes the scissile carbonyl of the substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00004"
FT   MUTAGEN         16
FT                   /note="G->R: In sil1; suppression of transgene silencing."
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         127
FT                   /note="G->R: In axe1-1; suppression of transgene
FT                   silencing."
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MUTAGEN         284
FT                   /note="G->D: In axe1-2; suppression of transgene
FT                   silencing."
FT                   /evidence="ECO:0000269|PubMed:15037732"
FT   MUTAGEN         294
FT                   /note="A->V: In axe1-3; suppression of transgene
FT                   silencing."
FT                   /evidence="ECO:0000269|PubMed:11340181"
FT   MUTAGEN         459..471
FT                   /note="Missing: In rts1-2; suppression of transgene
FT                   silencing."
FT                   /evidence="ECO:0000269|PubMed:11340181"
FT   CONFLICT        313
FT                   /note="G -> E (in Ref. 1; AAG28475)"
FT                   /evidence="ECO:0000269|PubMed:11340181"
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
//