HDA14_ARATH
ID HDA14_ARATH Reviewed; 423 AA.
AC Q941D6; Q9SZC4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Histone deacetylase 14, chloroplastic {ECO:0000303|PubMed:12466527};
DE EC=3.5.1.- {ECO:0000269|PubMed:29247559};
DE AltName: Full=N-acetylserotonin deacetylase {ECO:0000303|PubMed:29247559};
DE Flags: Precursor;
GN Name=HDA14 {ECO:0000303|PubMed:12466527};
GN Synonyms=ASDAC {ECO:0000303|PubMed:29247559};
GN OrderedLocusNames=At4g33470 {ECO:0000312|EMBL:AEE86231.1};
GN ORFNames=F17M5.230 {ECO:0000312|EMBL:CAB38805.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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 [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).
RN [5]
RP FUNCTION.
RX PubMed=16176989; DOI=10.1073/pnas.0503143102;
RA Xu C.-R., Liu C., Wang Y.-L., Li L.-C., Chen W.-Q., Xu Z.-H., Bai S.-N.;
RT "Histone acetylation affects expression of cellular patterning genes in the
RT Arabidopsis root epidermis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:14469-14474(2005).
RN [6]
RP FUNCTION, INTERACTION WITH PP2A2, AND SUBCELLULAR LOCATION.
RX PubMed=22404109; DOI=10.1111/j.1365-313x.2012.04984.x;
RA Tran H.T., Nimick M., Uhrig R.G., Templeton G., Morrice N., Gourlay R.,
RA DeLong A., Moorhead G.B.;
RT "Arabidopsis thaliana histone deacetylase 14 (HDA14) is an alpha-tubulin
RT deacetylase that associates with PP2A and enriches in the microtubule
RT fraction with the putative histone acetyltransferase ELP3.";
RL Plant J. 71:263-272(2012).
RN [7]
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).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=29061669; DOI=10.15252/msb.20177819;
RA Hartl M., Fuessl M., Boersema P.J., Jost J.O., Kramer K., Bakirbas A.,
RA Sindlinger J., Ploechinger M., Leister D., Uhrig G., Moorhead G.B., Cox J.,
RA Salvucci M.E., Schwarzer D., Mann M., Finkemeier I.;
RT "Lysine acetylome profiling uncovers novel histone deacetylase substrate
RT proteins in Arabidopsis.";
RL Mol. Syst. Biol. 13:949-949(2017).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=29247559; DOI=10.1111/jpi.12460;
RA Lee K., Lee H.Y., Back K.;
RT "Rice histone deacetylase 10 and Arabidopsis histone deacetylase 14 genes
RT encode N-acetylserotonin deacetylase, which catalyzes conversion of N-
RT acetylserotonin into serotonin, a reverse reaction for melatonin
RT biosynthesis in plants.";
RL J. Pineal Res. 64:0-0(2018).
CC -!- FUNCTION: Regulates lysine acetylation levels of plastid proteins
CC related to photosynthesis (PubMed:29061669). Involved in the regulation
CC of the activation state of RuBisCO, which is controlled by lysine
CC acetylation of RuBisCO activase under low-light conditions
CC (PubMed:29061669). Associates with alpha- and beta-tubulins and
CC deacetylate alpha-tubulin (PubMed:22404109). Does not seem to be
CC required for the cellular patterning in the root epidermis
CC (PubMed:16176989). Involved in the regulation of melatonin biosynthesis
CC by catalyzing the deacetylation of N-acetylserotonin to produce
CC serotonin (PubMed:29247559). N-acetylserotonin is methylated by
CC acetylserotonin O-methyltransferase (ASMT) to produce melatonin (N-
CC acetyl-5-methoxytryptamine) (Probable). Deacetylates melatonin to
CC produce 5-methoxytryptamine (PubMed:29247559). In vitro, deacetylates
CC N-acetyltyramine and N-acetyltryptamine to produce tyramine and
CC tryptamine, respectively (PubMed:29247559).
CC {ECO:0000269|PubMed:16176989, ECO:0000269|PubMed:22404109,
CC ECO:0000269|PubMed:29061669, ECO:0000269|PubMed:29247559,
CC ECO:0000305|PubMed:29247559}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetylserotonin = acetate + serotonin;
CC Xref=Rhea:RHEA:67196, ChEBI:CHEBI:15377, ChEBI:CHEBI:17697,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:350546;
CC Evidence={ECO:0000269|PubMed:29247559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67197;
CC Evidence={ECO:0000269|PubMed:29247559};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyltyramine = acetate + tyramine;
CC Xref=Rhea:RHEA:67200, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:125610, ChEBI:CHEBI:327995;
CC Evidence={ECO:0000269|PubMed:29247559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67201;
CC Evidence={ECO:0000269|PubMed:29247559};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyltryptamine = acetate + tryptamine;
CC Xref=Rhea:RHEA:67204, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:55515, ChEBI:CHEBI:57887;
CC Evidence={ECO:0000269|PubMed:29247559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67205;
CC Evidence={ECO:0000269|PubMed:29247559};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + melatonin = 5-methoxytryptamine + acetate;
CC Xref=Rhea:RHEA:67208, ChEBI:CHEBI:15377, ChEBI:CHEBI:16796,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:166874;
CC Evidence={ECO:0000269|PubMed:29247559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67209;
CC Evidence={ECO:0000269|PubMed:29247559};
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: Its activity is inhibited by trichostatin A (TSA),
CC a known histone deacetylase inhibitor. {ECO:0000269|PubMed:29061669}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=701 uM for N-acetylserotonin {ECO:0000269|PubMed:29247559};
CC Vmax=1.2 pmol/sec/mg enzyme with N-acetylserotonin as substrate
CC {ECO:0000269|PubMed:29247559};
CC -!- SUBUNIT: Interacts with PP2A2. {ECO:0000269|PubMed:22404109}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22404109}. Cytoplasm
CC {ECO:0000269|PubMed:22363501, ECO:0000269|PubMed:22404109}. Plastid,
CC chloroplast stroma {ECO:0000269|PubMed:29061669,
CC ECO:0000269|PubMed:29247559}. Mitochondrion
CC {ECO:0000269|PubMed:29061669}.
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=CAB38805.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80064.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035678; CAB38805.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161583; CAB80064.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86231.1; -; Genomic_DNA.
DR EMBL; AY052234; AAK97704.1; -; mRNA.
DR EMBL; AY113069; AAM47377.1; -; mRNA.
DR PIR; T05998; T05998.
DR RefSeq; NP_567921.1; NM_119501.4.
DR AlphaFoldDB; Q941D6; -.
DR SMR; Q941D6; -.
DR BioGRID; 14768; 2.
DR STRING; 3702.AT4G33470.1; -.
DR PaxDb; Q941D6; -.
DR PRIDE; Q941D6; -.
DR ProteomicsDB; 230374; -.
DR EnsemblPlants; AT4G33470.1; AT4G33470.1; AT4G33470.
DR GeneID; 829484; -.
DR Gramene; AT4G33470.1; AT4G33470.1; AT4G33470.
DR KEGG; ath:AT4G33470; -.
DR Araport; AT4G33470; -.
DR TAIR; locus:2119201; AT4G33470.
DR eggNOG; KOG1343; Eukaryota.
DR HOGENOM; CLU_007727_8_2_1; -.
DR InParanoid; Q941D6; -.
DR OMA; CTSPAMG; -.
DR OrthoDB; 1484694at2759; -.
DR PhylomeDB; Q941D6; -.
DR PRO; PR:Q941D6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q941D6; baseline and differential.
DR Genevisible; Q941D6; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:TAIR.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:TAIR.
DR GO; GO:0019213; F:deacetylase activity; IDA:UniProtKB.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0033558; F:protein lysine deacetylase activity; IDA:UniProtKB.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0042903; F:tubulin deacetylase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0030186; P:melatonin metabolic process; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006476; P:protein deacetylation; IDA:UniProtKB.
DR GO; GO:0042548; P:regulation of photosynthesis, light reaction; IMP:UniProtKB.
DR GO; GO:0090042; P:tubulin deacetylation; IDA:TAIR.
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 1: Evidence at protein level;
KW Chloroplast; Chromatin regulator; Cytoplasm; Hydrolase; Metal-binding;
KW Mitochondrion; Nucleus; Plastid; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Transit peptide; Zinc.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..423
FT /note="Histone deacetylase 14, chloroplastic"
FT /id="PRO_0000280090"
FT REGION 62..392
FT /note="Histone deacetylase"
FT ACT_SITE 202
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT SITE 370
FT /note="Polarizes the scissile carbonyl of the substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
SQ SEQUENCE 423 AA; 45577 MW; EA56909AFC9672E0 CRC64;
MSMALIVRPF FVPGSAGISG SRNICKKNQW RKYLLKPSGS SINCSFSTEK NPLLPSIQQL
ADARLIYSVS AALGHNKESH PECSARVPAI VNALEMNELT PKFRGSQILE LANFKTATVE
DIANVHDKAY VFGLEKAMDE ASDSGLIFIE GSGPTYATST TFQDSLIAAG AGMALVDSVI
AASRNSVDPP IGFALIRPPG HHAVPKGPMG FCVFGNVAIA ARHAQRTHGL KRIFIIDFDV
HHGNGTNDAF TEDPDIFFLS THQDGSYPGT GKISDIGKGK GEGTTLNLPL PGGSGDIAMR
TVFEEIIVPC AQRFKPDIIL VSAGYDAHVL DPLANLQFTT ATYYSLAKDI KRLAKEVCGG
RCVFFLEGGY NLESLSSSVA DSFRALLGED SLASEFDNPA YLYDEPMRKV RDAIQRAKSI
HCL
