ID   HDA17_ARATH             Reviewed;         158 AA.
AC   Q9LXN8;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Histone deacetylase 17;
DE            EC=3.5.1.98;
GN   Name=HDA17; OrderedLocusNames=At3g44490; ORFNames=F14L2.40;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-158.
RC   STRAIN=cv. Columbia;
RG   Center for eukaryotic structural genomics (CESG);
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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).
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:O22446}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. {ECO:0000305}.
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DR   EMBL; AL353818; CAB88531.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77907.1; -; Genomic_DNA.
DR   EMBL; BT014712; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; T48929; T48929.
DR   RefSeq; NP_190035.1; NM_114317.2.
DR   AlphaFoldDB; Q9LXN8; -.
DR   SMR; Q9LXN8; -.
DR   STRING; 3702.AT3G44490.1; -.
DR   PaxDb; Q9LXN8; -.
DR   PRIDE; Q9LXN8; -.
DR   ProteomicsDB; 230309; -.
DR   EnsemblPlants; AT3G44490.1; AT3G44490.1; AT3G44490.
DR   GeneID; 823574; -.
DR   Gramene; AT3G44490.1; AT3G44490.1; AT3G44490.
DR   KEGG; ath:AT3G44490; -.
DR   Araport; AT3G44490; -.
DR   TAIR; locus:2076053; AT3G44490.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_3_2_1; -.
DR   InParanoid; Q9LXN8; -.
DR   OMA; CLNVPLW; -.
DR   OrthoDB; 1818114at2759; -.
DR   PhylomeDB; Q9LXN8; -.
DR   PRO; PR:Q9LXN8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LXN8; baseline and differential.
DR   Genevisible; Q9LXN8; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   SUPFAM; SSF52768; SSF52768; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Hydrolase; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..158
FT                   /note="Histone deacetylase 17"
FT                   /id="PRO_0000280092"
FT   REGION          3..50
FT                   /note="Histone deacetylase"
FT   REGION          120..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        58
FT                   /note="S -> P (in Ref. 3; BT014712)"
FT   CONFLICT        94
FT                   /note="Q -> R (in Ref. 3; BT014712)"
FT   CONFLICT        133
FT                   /note="V -> A (in Ref. 3; BT014712)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   158 AA;  18116 MW;  B4C29ACF84F232E0 CRC64;
     MAFSMLFTGH AECVKFVKKF NLPLLVTGGG GYTKENVARC WTVETGILLD TELPNEISEN
     DYIKYFAPDF SLKIPGGHIE NLNTKSYISS IKVQILENLR YIQHAPSVQM QEVPPDFYIP
     DFDEDEQNPD VRVDQRSRDK QIQRDDEYFD GDNDNDAS