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 22-JUL-2008, entry version 40. 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; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; 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 MEDLINE=98162728; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; 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 [4] 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 [5] 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 [6] 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 [7] RP GENE FAMILY, AND NOMENCLATURE. RX MEDLINE=22354691; 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 [8] RP INTERACTION WITH COI1. RX MEDLINE=22337574; PubMed=12445118; RX 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 [9] 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 [10] 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 [11] 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). 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. 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 -!- SUBUNIT: Interacts with Coi1, which functions in an SCF complex CC that recruits regulators for ubiquitination. CC -!- INTERACTION: CC O04197:COI1; NbExp=3; IntAct=EBI-639608, EBI-401159; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. CC -!- TISSUE SPECIFICITY: Not detected in leaves, stems, flowers and CC young siliques. CC -!- INDUCTION: By jasmonic acid and ethylene. 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. Type 1 CC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF195548; AAG28475.1; -; mRNA. DR EMBL; AB008265; BAB10553.1; -; 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; -. DR UniGene; At.8834; -. DR HSSP; O67135; 1C3P. DR IntAct; Q9FML2; -. DR GeneID; 836431; -. DR GenomeReviews; BA000015_GR; AT5G63110. DR KEGG; ath:AT5G63110; -. DR NMPDR; fig|3702.1.peg.28357; -. DR TAIR; At5g63110; -. DR ArrayExpress; Q9FML2; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR000286; His_deacetylse. DR InterPro; IPR003084; His_deacetylse_1. DR Gene3D; G3DSA:3.40.800.20; His_deacetylse; 1. DR PANTHER; PTHR10625; His_deacetylse; 1. DR PANTHER; PTHR10625:SF28; His_deacetylse_1; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PIRSF; PIRSF037913; His_deacetylse_1; 1. DR PRINTS; PR01270; HDASUPER. DR PRINTS; PR01271; HISDACETLASE. PE 1: Evidence at protein level; KW Chromatin regulator; Complete proteome; Hydrolase; Nucleus; Repressor; KW Transcription; 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 By similarity. FT MUTAGEN 16 16 G->R: In sil1; suppression of transgene FT silencing. FT MUTAGEN 127 127 G->R: In axe1-1; suppression of transgene FT silencing. FT MUTAGEN 284 284 G->D: In axe1-2; suppression of transgene FT silencing. FT MUTAGEN 294 294 A->V: In axe1-3; suppression of transgene FT silencing. FT MUTAGEN 459 471 Missing: In rts1-2; suppression of FT transgene silencing. FT CONFLICT 313 313 G -> E (in Ref. 1; AAG28475). 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 //