JMJ32_ARATH
ID JMJ32_ARATH Reviewed; 345 AA.
AC Q0WVR4; Q9LZU2;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Lysine-specific demethylase JMJ32 {ECO:0000303|PubMed:18713399};
DE EC=1.14.11.68 {ECO:0000269|PubMed:25267112};
DE AltName: Full=Jumonji domain-containing protein 32 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ32 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 32 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Lysine-specific histone demethylase JMJ32 {ECO:0000303|PubMed:18713399};
DE AltName: Full=[histone H3]-trimethyl-L-lysine(27) monodemethylase JMJ32 {ECO:0000305};
GN Name=JMJ32 {ECO:0000303|PubMed:18713399};
GN OrderedLocusNames=At3g45880 {ECO:0000312|Araport:AT3G45880};
GN ORFNames=F16L2.90 {ECO:0000312|EMBL:CAB82812.1};
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=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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP SUBCELLULAR 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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
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 [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
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-27' (H3K27me) of
CC histone H3 with a specific activity for H3K27me3 and H3K27me2, and
CC involved in the regulation of gene expression (PubMed:25267112,
CC PubMed:33324437). No activity on H3K27me1 (PubMed:25267112). Together
CC with JMJ30, regulates the flowering-repressor FLOWERING LOCUS C (FLC)
CC locus 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 JMJ30, 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:30859592, PubMed:30983495). 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). {ECO:0000269|PubMed:25267112,
CC ECO:0000269|PubMed:30859592, ECO:0000269|PubMed:30983495,
CC ECO:0000269|PubMed:33324437}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone
CC H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(27)-
CC [histone H3] + succinate; Xref=Rhea:RHEA:60228, Rhea:RHEA-COMP:15535,
CC Rhea:RHEA-COMP:15539, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61961, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000269|PubMed:25267112};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60229;
CC Evidence={ECO:0000269|PubMed:25267112};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(27)-[histone H3] +
CC O2 = CO2 + formaldehyde + N(6)-methyl-L-lysyl(27)-[histone H3] +
CC succinate; Xref=Rhea:RHEA:60232, Rhea:RHEA-COMP:15539, Rhea:RHEA-
CC COMP:15544, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:25267112};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60233;
CC Evidence={ECO:0000269|PubMed:25267112};
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 -!- 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25267112}. Cytoplasm
CC {ECO:0000269|PubMed:25267112}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:25267112}. Note=Predominantly localized in the
CC nucleus. {ECO:0000269|PubMed:25267112}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously including in vasculatures,
CC leaves, siliques, roots and inflorescences (PubMed:25267112,
CC PubMed:18713399). Present in the root meristem (PubMed:30859592).
CC Accumulates in cotyledons and root tips of young seedlings
CC (PubMed:33324437). {ECO:0000269|PubMed:18713399,
CC ECO:0000269|PubMed:25267112, ECO:0000269|PubMed:30859592,
CC ECO:0000269|PubMed:33324437}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:30859592). Reduced abscisic acid (ABA)-mediated
CC growth arrest during the post-germination stage, with stronger effect
CC in plants lacking both JMJ30 and JMJ32 (PubMed:30859592). The double
CC mutant missing JMJ30 and JMJ32 exhibits an early-flowering phenotype at
CC elevated temperatures (e.g. 29 degrees Celsius), associated with
CC increased H3K27me3 levels at the FLC locus and decreased FLC expression
CC (PubMed:25267112). The double mutant jmj30 jmj32 has longer primary
CC roots (PubMed:30983495). In jmj30-2 jmj32-1 double mutants, reduced
CC brassinosteroids (BR) mediated repression of ABA-inducible genes (e.g.
CC ABI5, ABF2, ABF3 and ABF4) (PubMed:33324437).
CC {ECO:0000269|PubMed:25267112, ECO:0000269|PubMed:30859592,
CC ECO:0000269|PubMed:30983495, ECO:0000269|PubMed:33324437}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB82812.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162459; CAB82812.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78086.1; -; Genomic_DNA.
DR EMBL; AK226677; BAE98784.1; -; mRNA.
DR PIR; T47528; T47528.
DR RefSeq; NP_190174.2; NM_114457.3.
DR SMR; Q0WVR4; -.
DR IntAct; Q0WVR4; 7.
DR STRING; 3702.AT3G45880.1; -.
DR PRIDE; Q0WVR4; -.
DR ProteomicsDB; 185660; -.
DR EnsemblPlants; AT3G45880.1; AT3G45880.1; AT3G45880.
DR GeneID; 823731; -.
DR Gramene; AT3G45880.1; AT3G45880.1; AT3G45880.
DR Araport; AT3G45880; -.
DR TAIR; locus:2077172; AT3G45880.
DR eggNOG; KOG2508; Eukaryota.
DR HOGENOM; CLU_016785_6_0_1; -.
DR OMA; PLEFMRY; -.
DR OrthoDB; 1385616at2759; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WVR4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; 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:0071558; F:histone H3-tri/di-methyl-lysine-27 demethylase activity; IDA:UniProtKB.
DR GO; GO:0071557; P:histone H3-K27 demethylation; IDA: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: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:0009266; P:response to temperature stimulus; IMP:UniProtKB.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
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; Brassinosteroid signaling pathway;
KW Cytoplasm; Endoplasmic reticulum; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..345
FT /note="Lysine-specific demethylase JMJ32"
FT /id="PRO_0000456197"
FT DOMAIN 122..315
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 174
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 281
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 345 AA; 39123 MW; 1577985D3C279BCA CRC64;
MAKEIENLWR EVRELSLGTK IDRFDSQPSP VKFLRNYVSQ SKPCVISKAI THWPALKLWS
DPAYLTGALS DDVVSLHLTP NGCADAVTGD SDLCFASAHV EKVLFPEALK VVQSSCKGLK
VGYLQQQNDC FRTEYSTVAL DCDGDIEWAT EAFGCSPEAV NLWIGTDDSV TSFHKDHYEN
LYAVVSGEKH FLLLPPTDVH RLYIEQYPAA NYSYHRDTDA FKLEVEEPVR HVPWSSVDPY
PSPEKEASER LKFPLFFDGP KPFHCTVKAG EVLYLPSMWF HHVSQTPGDG GYTIAVNYWY
DMQFDIKYAY FNFLQSLLYK SSSLNPVLSW REDEDSESSD AEIAP
