JMJ30_ARATH
ID JMJ30_ARATH Reviewed; 429 AA.
AC Q8RWR1; Q9LT40;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Lysine-specific demethylase JMJ30 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ30 {ECO:0000303|PubMed:18713399};
DE EC=1.14.11.27 {ECO:0000269|PubMed:25132385};
DE EC=1.14.11.68 {ECO:0000269|PubMed:25267112};
DE EC=1.14.11.69 {ECO:0000269|PubMed:25132385};
DE AltName: Full=JmjC domain-containing protein 30 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Jumonji domain-containing protein 5 {ECO:0000303|PubMed:21115819};
DE Short=AtJMJD5 {ECO:0000303|PubMed:21115819};
DE AltName: Full=[histone H3]-trimethyl-L-lysine(36) monodemethylase JMJ30 {ECO:0000305};
GN Name=JMJ30 {ECO:0000303|PubMed:18713399};
GN Synonyms=JMJD5 {ECO:0000303|PubMed:21115819};
GN OrderedLocusNames=At3g20810 {ECO:0000312|Araport:AT3G20810};
GN ORFNames=MOE17.12 {ECO:0000312|EMBL:BAB02489.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18713399; DOI=10.1111/j.1744-7909.2008.00692.x;
RA Lu F., Li G., Cui X., Liu C., Wang X.-J., Cao X.;
RT "Comparative analysis of JmjC domain-containing proteins reveals the
RT potential histone demethylases in Arabidopsis and rice.";
RL J. Integr. Plant Biol. 50:886-896(2008).
RN [6]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21115819; DOI=10.1073/pnas.1014204108;
RA Jones M.A., Covington M.F., DiTacchio L., Vollmers C., Panda S.,
RA Harmer S.L.;
RT "Jumonji domain protein JMJD5 functions in both the plant and human
RT circadian systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:21623-21628(2010).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21139085; DOI=10.1104/pp.110.167015;
RA Lu S.X., Knowles S.M., Webb C.J., Celaya R.B., Cha C., Siu J.P.,
RA Tobin E.M.;
RT "The Jumonji C domain-containing protein JMJ30 regulates period length in
RT the Arabidopsis circadian clock.";
RL Plant Physiol. 155:906-915(2011).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21358285; DOI=10.4161/psb.6.3.14654;
RA Jones M.A., Harmer S.L.;
RT "JMJD5 functions in concert with TOC1 in the Arabidopsis circadian
RT system.";
RL Plant Signal. Behav. 6:445-448(2011).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH EFM, AND INDUCTION.
RX PubMed=25132385; DOI=10.1016/j.devcel.2014.07.004;
RA Yan Y., Shen L., Chen Y., Bao S., Thong Z., Yu H.;
RT "A MYB-domain protein EFM mediates flowering responses to environmental
RT cues in Arabidopsis.";
RL Dev. Cell 30:437-448(2014).
RN [10]
RP FUNCTION, MUTAGENESIS OF HIS-326, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY,
RP INDUCTION BY ELEVATED TEMPERATURES, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25267112; DOI=10.1038/ncomms6098;
RA Gan E.-S., Xu Y., Wong J.-Y., Goh J.G., Sun B., Wee W.-Y., Huang J.,
RA Ito T.;
RT "Jumonji demethylases moderate precocious flowering at elevated temperature
RT via regulation of FLC in Arabidopsis.";
RL Nat. Commun. 5:5098-5098(2014).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INTERACTION WITH ATXR2; ARF7 AND ARF19.
RC STRAIN=cv. Columbia;
RX PubMed=29923261; DOI=10.1111/tpj.14002;
RA Lee K., Park O.-S., Seo P.J.;
RT "JMJ30-mediated demethylation of H3K9me3 drives tissue identity changes to
RT promote callus formation in Arabidopsis.";
RL Plant J. 95:961-975(2018).
RN [12]
RP FUNCTION, MUTAGENESIS OF HIS-326, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=30774641; DOI=10.3389/fpls.2019.00057;
RA Jones M.A., Morohashi K., Grotewold E., Harmer S.L.;
RT "Arabidopsis JMJD5/JMJ30 acts independently of LUX ARRHYTHMO within the
RT plant circadian clock to enable temperature compensation.";
RL Front. Plant Sci. 10:57-57(2019).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY
RP ABSCISIC ACID.
RC STRAIN=cv. Columbia;
RX PubMed=30859592; DOI=10.1111/pce.13547;
RA Wu J., Ichihashi Y., Suzuki T., Shibata A., Shirasu K., Yamaguchi N.,
RA Ito T.;
RT "Abscisic acid-dependent histone demethylation during postgermination
RT growth arrest in Arabidopsis.";
RL Plant Cell Environ. 42:2198-2214(2019).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=30983495; DOI=10.1080/15592324.2019.1604019;
RA Wu J., Yamaguchi N., Ito T.;
RT "Histone demethylases control root elongation in response to stress-
RT signaling hormone abscisic acid.";
RL Plant Signal. Behav. 14:1604019-1604019(2019).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, REPRESSION BY BRASSINOSTEROIDS, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=33324437; DOI=10.3389/fpls.2020.596835;
RA Wu J., Yan M., Zhang D., Zhou D., Yamaguchi N., Ito T.;
RT "Histone demethylases coordinate the antagonistic interaction between
RT abscisic acid and brassinosteroid signaling in Arabidopsis.";
RL Front. Plant Sci. 11:596835-596835(2020).
CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-36' (H3K36me) of
CC histone H3 with a specific activity for H3K36me3 and H3K36me2
CC (PubMed:25132385, PubMed:30774641). Also active on 'Lys-27' (H3K27me)
CC of histone H3 with a specific activity for H3K27me3 and H3K27me2
CC (PubMed:25267112, PubMed:33324437, PubMed:30774641). No activity on
CC H3K36me1 and H3K27me1 (PubMed:25132385, PubMed:25267112). Involved in
CC the control of flowering time by demethylating H3K36me2 at the FT locus
CC and repressing its expression (PubMed:25132385). Acts within the
CC central clock and contributes, in parallel with LUX, to temperature
CC compensation, probably as a component of the evening complex, to
CC maintain circadian period at increasing temperatures; this mechanism
CC involves binding to and regulation of CCA1 and PRR7 promoters
CC (PubMed:21358285, PubMed:30774641). Works in concert with TOC1 to
CC promote the morning-phased clock genes CCA1 and LHY which function as
CC components of the central oscillator (PubMed:21358285). Together with
CC JMJ32, regulates the flowering-repressor FLOWERING LOCUS C (FLC) locus
CC by removing the repressive histone modification H3 lysine 27
CC trimethylation (H3K27me3), especially at elevated temperatures (e.g. 29
CC degrees Celsius), thus preventing extreme precocious flowering
CC (PubMed:25267112). JMJ30 and JMJ32 are regulators involved in the
CC integration of abscisic acid (ABA) and brassinosteroids (BR) signaling
CC pathways (PubMed:33324437). Together with JMJ32, controls ABA-mediated
CC growth arrest during the post-germination stage in unfavorable
CC conditions, and responses to ABA during root development, via the
CC removal of repressive histone mark (H3K27me3) from the SnRK2.8
CC promoter, thus promoting SnRK2.8 expression and subsequent kinase-
CC dependent ABI3 activation (PubMed:30983495, PubMed:30859592). In
CC addition, removes the repressive histone marks (H3K27me3) from the BZR1
CC locus in response to stress and ABA, thus activating the BR signaling
CC pathway which, in turn, inhibits the ABA signaling pathway
CC (PubMed:33324437). Able to drive tissue identity changes to promote
CC callus formation form somatic cells via a massive genome-wide chromatin
CC remodeling (e.g. H3K9me3 demethylation) leading to the induction of
CC Lateral organ Boundaries-Domain (LBD) genes (e.g. LBD16 and LBD29) that
CC establish root primordia; when in complex with ARF proteins (e.g. ARF7
CC and ARF19), recruits ATXR2 which promotes the deposition of H3K36me3 at
CC LBD genes promoters, thus ensuring their stable activation during
CC callus formation (PubMed:29923261). {ECO:0000269|PubMed:21115819,
CC ECO:0000269|PubMed:21139085, ECO:0000269|PubMed:21358285,
CC ECO:0000269|PubMed:25132385, ECO:0000269|PubMed:25267112,
CC ECO:0000269|PubMed:29923261, ECO:0000269|PubMed:30774641,
CC ECO:0000269|PubMed:30859592, ECO:0000269|PubMed:30983495,
CC ECO:0000269|PubMed:33324437}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(36)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60236,
CC Rhea:RHEA-COMP:9786, Rhea:RHEA-COMP:15536, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.69; Evidence={ECO:0000269|PubMed:25132385};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60237;
CC Evidence={ECO:0000269|PubMed:25132385};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224,
CC Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.68; Evidence={ECO:0000269|PubMed:25267112};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60225;
CC Evidence={ECO:0000269|PubMed:25267112};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.27;
CC Evidence={ECO:0000269|PubMed:25132385};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42033;
CC Evidence={ECO:0000269|PubMed:25132385};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q8GUI6};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8GUI6};
CC -!- SUBUNIT: Interacts with EFM (PubMed:25132385). Binds to ATXR2, ARF7 and
CC ARF19 (PubMed:29923261). {ECO:0000269|PubMed:25132385,
CC ECO:0000269|PubMed:29923261}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25267112,
CC ECO:0000305|PubMed:21139085}. Cytoplasm {ECO:0000269|PubMed:25267112,
CC ECO:0000305|PubMed:21139085}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:25267112}. Note=Predominantly localized in the
CC nucleus, especially in euchromatin. {ECO:0000269|PubMed:25267112}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RWR1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RWR1-2; Sequence=VSP_055399;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in vasculatures, roots,
CC rosette leaves, stems, inflorescences and siliques (PubMed:18713399,
CC PubMed:25267112). Mainly present in the root meristem and root
CC differentiation area (PubMed:30859592, PubMed:33324437). Observed at
CC high level in callus (PubMed:29923261). {ECO:0000269|PubMed:18713399,
CC ECO:0000269|PubMed:25267112, ECO:0000269|PubMed:29923261,
CC ECO:0000269|PubMed:30859592, ECO:0000269|PubMed:33324437}.
CC -!- DEVELOPMENTAL STAGE: Accumulates progressively during seedling growth
CC (PubMed:33324437). Expressed during callus formation (PubMed:29923261).
CC {ECO:0000269|PubMed:29923261, ECO:0000269|PubMed:33324437}.
CC -!- INDUCTION: Circadian-regulation with a broad peak in the late day and
CC early night (PubMed:21115819, PubMed:21139085, PubMed:25132385).
CC Stabilized at elevated temperatures (at protein level)
CC (PubMed:25267112). Induced by abscisic acid (ABA) specifically during
CC the post-germination stage in an ABI3-dependent manner
CC (PubMed:30859592). Repressed by brassinosteroids (BR) during the post-
CC germination stage (PubMed:33324437). {ECO:0000269|PubMed:21115819,
CC ECO:0000269|PubMed:21139085, ECO:0000269|PubMed:25132385,
CC ECO:0000269|PubMed:25267112, ECO:0000269|PubMed:30859592,
CC ECO:0000269|PubMed:33324437}.
CC -!- DISRUPTION PHENOTYPE: Altered overall H3K36me3 modifications
CC (PubMed:30774641). No visible phenotype under normal growth conditions,
CC but mutant plants have a short-period circadian phenotype
CC (PubMed:21115819, PubMed:21139085, PubMed:30859592, PubMed:21358285,
CC PubMed:30774641). Defective temperature compensation leading to shorter
CC circadian period at increasing temperatures with altered expression
CC levels of clock genes at 27 degrees Celsius (PubMed:30774641). Reduced
CC callus formation from somatic cells associated with low Lateral organ
CC Boundaries-Domain (LBD) transcript levels (e.g. LBD16, LBD17, LBD18 and
CC LBD29) associated with an impaired reduction of H3K9me3 deposition and
CC altered H3K36me3 accumulation at their loci during leaf-to-callus
CC transition (PubMed:29923261). The double mutant jmj30-2 atxr2-1 is
CC strongly impaired in callus formation (PubMed:29923261). Reduced
CC abscisic acid (ABA)-mediated growth arrest during the post-germination
CC stage, with stronger effect in plants lacking both JMJ30 and JMJ32
CC (PubMed:30859592). The double mutant missing JMJ30 and JMJ32 exhibits
CC an early-flowering phenotype at elevated temperatures (e.g. 29 degrees
CC Celsius), associated with increased H3K27me3 levels at the FLC locus
CC and decreased FLC expression (PubMed:25267112). The double mutant jmj30
CC jmj32 has longer primary roots (PubMed:30983495). In jmj30-2 jmj32-1
CC double mutants, reduced brassinosteroids (BR) mediated repression of
CC ABA-inducible genes (e.g. ABI5, ABF2, ABF3 and ABF4) (PubMed:33324437).
CC {ECO:0000269|PubMed:21115819, ECO:0000269|PubMed:21139085,
CC ECO:0000269|PubMed:21358285, ECO:0000269|PubMed:25267112,
CC ECO:0000269|PubMed:29923261, ECO:0000269|PubMed:30774641,
CC ECO:0000269|PubMed:30859592, ECO:0000269|PubMed:30983495,
CC ECO:0000269|PubMed:33324437}.
CC -!- MISCELLANEOUS: Plants over-expressing JMJD5 show delayed flowering.
CC {ECO:0000305|PubMed:21139085}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
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DR EMBL; AB025629; BAB02489.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76425.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76426.1; -; Genomic_DNA.
DR EMBL; AY091769; AAM10317.1; -; mRNA.
DR EMBL; AY125538; AAM78048.1; -; mRNA.
DR EMBL; AY084468; AAM61040.1; -; mRNA.
DR RefSeq; NP_566667.1; NM_112972.4. [Q8RWR1-2]
DR RefSeq; NP_850617.1; NM_180286.1. [Q8RWR1-1]
DR AlphaFoldDB; Q8RWR1; -.
DR SMR; Q8RWR1; -.
DR BioGRID; 6961; 9.
DR IntAct; Q8RWR1; 8.
DR STRING; 3702.AT3G20810.2; -.
DR iPTMnet; Q8RWR1; -.
DR PaxDb; Q8RWR1; -.
DR ProteomicsDB; 238990; -. [Q8RWR1-1]
DR EnsemblPlants; AT3G20810.1; AT3G20810.1; AT3G20810. [Q8RWR1-2]
DR EnsemblPlants; AT3G20810.2; AT3G20810.2; AT3G20810. [Q8RWR1-1]
DR GeneID; 821629; -.
DR Gramene; AT3G20810.1; AT3G20810.1; AT3G20810. [Q8RWR1-2]
DR Gramene; AT3G20810.2; AT3G20810.2; AT3G20810. [Q8RWR1-1]
DR KEGG; ath:AT3G20810; -.
DR Araport; AT3G20810; -.
DR TAIR; locus:2091861; AT3G20810.
DR eggNOG; KOG2132; Eukaryota.
DR InParanoid; Q8RWR1; -.
DR OrthoDB; 1385616at2759; -.
DR PhylomeDB; Q8RWR1; -.
DR PRO; PR:Q8RWR1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RWR1; baseline and differential.
DR Genevisible; Q8RWR1; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IPI:TAIR.
DR GO; GO:0061628; F:H3K27me3 modified histone binding; IDA:UniProtKB.
DR GO; GO:0071558; F:histone H3-tri/di-methyl-lysine-27 demethylase activity; IDA:UniProtKB.
DR GO; GO:0140681; F:histone H3-tri/dimethyl-lysine-36 demethylase activity; IEA:RHEA.
DR GO; GO:0140684; F:histone H3-tri/dimethyl-lysine-9 demethylase activity; IMP:UniProtKB.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990110; P:callus formation; IMP:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0071557; P:histone H3-K27 demethylation; IDA:UniProtKB.
DR GO; GO:0070544; P:histone H3-K36 demethylation; IDA:TAIR.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IMP:UniProtKB.
DR GO; GO:0036124; P:histone H3-K9 trimethylation; IMP:UniProtKB.
DR GO; GO:0080022; P:primary root development; IMP:UniProtKB.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:1900457; P:regulation of brassinosteroid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IDA:UniProtKB.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:1900140; P:regulation of seedling development; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0009741; P:response to brassinosteroid; IEP:UniProtKB.
DR GO; GO:0009266; P:response to temperature stimulus; IDA:UniProtKB.
DR GO; GO:0010378; P:temperature compensation of the circadian clock; IMP:UniProtKB.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR003347; JmjC_dom.
DR Pfam; PF13621; Cupin_8; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing;
KW Brassinosteroid signaling pathway; Cytoplasm; Dioxygenase;
KW Endoplasmic reticulum; Flowering; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..429
FT /note="Lysine-specific demethylase JMJ30"
FT /id="PRO_0000429999"
FT DOMAIN 272..429
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 326
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 328
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 405
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT VAR_SEQ 163..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_055399"
FT MUTAGEN 326
FT /note="H->A: Abolished ability to demethylate H3K27me3 and
FT H3K27me2. Impaired temperature compensation of the
FT circadian period in response to increasing temperatures."
FT /evidence="ECO:0000269|PubMed:25267112,
FT ECO:0000269|PubMed:30774641"
SQ SEQUENCE 429 AA; 48075 MW; 94FC0D3735DF344B CRC64;
MSGATTASSG DHNNLRLPTP TLDAESQTLL QSISAEGGYA YARMAVLAVA GDQSAAEAAR
DMAWEQLHSG PWHSVLPVWR DAYSMACLHV AKIHFAAGEF GEALGALDMG LIMGGMLLRK
DLHDSVLLVS SEARKMTKSL EEASGDFKGE RLVPEVPVDV NEVRHVLANL QLLVLKILPC
RSLTCKRVEK RSGLSLEGFL RDYYLPGTPV VITNSMAHWP ARTKWNHLDY LNAVAGNRTV
PVEVGKNYLC SDWKQELVTF SKFLERMRTN KSSPMEPTYL AQHPLFDQIN ELRDDICIPD
YCFVGGGELQ SLNAWFGPAG TVTPLHHDPH HNILAQVVGK KYIRLYPSFL QDELYPYSET
MLCNSSQVDL DNIDETEFPK AMELEFMDCI LEEGEMLYIP PKWWHYVRSL TMSLSVSFWW
SNEAESSSS
