ID   JMJ22_ARATH             Reviewed;         502 AA.
AC   Q67XX3; Q9FG15;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 119.
DE   RecName: Full=Arginine-specific demethylase JMJ22 {ECO:0000303|PubMed:18713399};
DE            EC=1.14.11.- {ECO:0000269|PubMed:22483719};
DE   AltName: Full=Arginine-specific histone demethylase JMJ22 {ECO:0000303|PubMed:18713399};
DE   AltName: Full=F-box protein JMJ22;
DE   AltName: Full=Jumonji domain-containing protein 22 {ECO:0000303|PubMed:18713399};
DE            Short=AtJMJ22 {ECO:0000303|PubMed:18713399};
DE            Short=Protein JUMONJI 22 {ECO:0000303|PubMed:18713399};
DE   AltName: Full=[histone H4]-dimethyl-L-arginine(3) monodemethylase JMJ22 {ECO:0000305};
GN   Name=JMJ22 {ECO:0000303|PubMed:18713399};
GN   OrderedLocusNames=At5g06550 {ECO:0000312|Araport:AT5G06550};
GN   ORFNames=F15M7.8 {ECO:0000312|EMBL:BAB11404.1};
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;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Carninci P., Hayashizaki Y.,
RA   Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA   Shinozaki K., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, INDUCTION BY RED LIGHT,
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Columbia;
RX   PubMed=22483719; DOI=10.1016/j.devcel.2012.01.024;
RA   Cho J.-N., Ryu J.-Y., Jeong Y.-M., Park J., Song J.-J., Amasino R.M.,
RA   Noh B., Noh Y.-S.;
RT   "Control of seed germination by light-induced histone arginine
RT   demethylation activity.";
RL   Dev. Cell 22:736-748(2012).
CC   -!- FUNCTION: Histone demethylase that demethylates 'Arg-3' (H4R3me) of
CC       histone H4 with a specific activity for H4R3me2 (PubMed:22483719).
CC       Involved in the positive regulation of gene expression
CC       (PubMed:22483719). Together with JMJ20, positively regulates seed
CC       germination by promoting the removal of repressive histone arginine
CC       methylations (e.g. H4R3me2) at GA3ox1 and GA3ox2 to trigger gibberellic
CC       acid (GA) biosynthesis (PubMed:22483719).
CC       {ECO:0000269|PubMed:22483719}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2-
CC         oxoglutarate + O2 = N(omega)-methyl-L-arginyl-[protein] +
CC         formaldehyde + succinate + CO2; Xref=Rhea:RHEA:58352, Rhea:RHEA-
CC         COMP:11990, Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:61897, ChEBI:CHEBI:65280;
CC         Evidence={ECO:0000269|PubMed:22483719};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58353;
CC         Evidence={ECO:0000269|PubMed:22483719};
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:22483719}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q67XX3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q67XX3-2; Sequence=VSP_024322;
CC   -!- TISSUE SPECIFICITY: Expressed in inflorescences, roots and siliques,
CC       and, at low levels, in leaves and stems. {ECO:0000269|PubMed:18713399}.
CC   -!- DEVELOPMENTAL STAGE: In far-red light (FR)-treated seeds, mainly
CC       observed in the radicle of the embryo (PubMed:22483719). Accumulates
CC       upon red light (R) in cotyledons (PubMed:22483719).
CC       {ECO:0000269|PubMed:22483719}.
CC   -!- INDUCTION: Repressed by the zinc-finger protein SOMNUS when PHYB is
CC       inactive in far-red (FR) conditions, but derepressed upon PHYB
CC       activation by red light (R). {ECO:0000269|PubMed:22483719}.
CC   -!- DISRUPTION PHENOTYPE: Plants missing both JMJ20 and JMJ22 exhibit
CC       reduced seed germination efficiency during PHYB activation after red
CC       light (R)-pulse treatment due to an impaired H4R3me2 removal-dependent
CC       derepression of GA3ox1 and GA3ox2 causing lower endogenous gibberellic
CC       acid (GA) biosynthesis. {ECO:0000269|PubMed:22483719}.
CC   -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC       {ECO:0000305}.
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DR   EMBL; AP002543; BAB11404.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91033.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7051292.1; -; Genomic_DNA.
DR   EMBL; BT012560; AAS99704.1; -; mRNA.
DR   EMBL; AK175402; BAD43165.1; -; mRNA.
DR   EMBL; AK176695; BAD44458.1; -; mRNA.
DR   RefSeq; NP_196273.3; NM_120738.5. [Q67XX3-1]
DR   AlphaFoldDB; Q67XX3; -.
DR   SMR; Q67XX3; -.
DR   BioGRID; 15822; 3.
DR   FunCoup; Q67XX3; 860.
DR   IntAct; Q67XX3; 3.
DR   STRING; 3702.Q67XX3; -.
DR   PaxDb; 3702-Q67XX3; -.
DR   ProteomicsDB; 232056; -. [Q67XX3-1]
DR   GeneID; 830543; -.
DR   KEGG; ath:AT5G06550; -.
DR   Araport; AT5G06550; -.
DR   TAIR; AT5G06550; JMJ22.
DR   eggNOG; KOG2130; Eukaryota.
DR   HOGENOM; CLU_016785_1_2_1; -.
DR   InParanoid; Q67XX3; -.
DR   OMA; WPAYKNW; -.
DR   PhylomeDB; Q67XX3; -.
DR   PRO; PR:Q67XX3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:TAIR.
DR   GO; GO:0032452; F:histone demethylase activity; IGI:TAIR.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0040029; P:epigenetic regulation of gene expression; IDA:UniProtKB.
DR   GO; GO:0010476; P:gibberellin mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0010030; P:positive regulation of seed germination; IMP:UniProtKB.
DR   GO; GO:0010099; P:regulation of photomorphogenesis; IMP:UniProtKB.
DR   GO; GO:0010114; P:response to red light; IMP:UniProtKB.
DR   FunFam; 2.60.120.650:FF:000045; F-box protein At1g78280; 1.
DR   Gene3D; 1.20.1280.50; -; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   InterPro; IPR041667; Cupin_8.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR050910; JMJD6_ArgDemeth/LysHydrox.
DR   PANTHER; PTHR12480; ARGININE DEMETHYLASE AND LYSYL-HYDROXYLASE JMJD; 1.
DR   PANTHER; PTHR12480:SF21; JMJC DOMAIN-CONTAINING PROTEIN 8; 1.
DR   Pfam; PF13621; Cupin_8; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Gibberellin signaling pathway; Iron; Metal-binding;
KW   Nucleus; Oxidoreductase; Reference proteome.
FT   CHAIN           1..502
FT                   /note="Arginine-specific demethylase JMJ22"
FT                   /id="PRO_0000283519"
FT   DOMAIN          80..126
FT                   /note="F-box"
FT   DOMAIN          279..439
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   REGION          15..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         324
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
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         407
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   VAR_SEQ         427..502
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_024322"
SQ   SEQUENCE   502 AA;  57419 MW;  79E0EF14743219E6 CRC64;
     MPKCKNLLLT SKRRKSKSKR LKLHQHEPES LFPEKEVEEE DEDEGGFKLK IAAPSQEHGV
     QPLGNLYFNP GAVNVRNTGL GNLQILSDEL VLDILGLLGA NHLGVLATVT KSFYIFANHE
     PLWRNLVLEE LKGDFLFNGS WRSTYVAAYH PKFKFAGDGE SNLKIIDFYS DYLFQSWLCA
     NLEMKPKWLR RDNITRVRGI SVEDFITKFE EPNKPVLLEG CLDGWPAIEK WSRDYLTKVV
     GDVEFAVGPV EMKLEKYFRY SDGAREERPL YLFDPKFAEK VPVLDSEYDV PVYFREDLFG
     VLGNERPDYR WIIIGPAGSG SSFHIDPNST SAWNAVITGS KKWVLFPPDV VPPGVHPSPD
     GAEVACPVSI IEWFMNFYDD TKDWEKKPIE CICKAGEVMF VPNGWWHLVI NLEESIAITQ
     NYASRSNLLN VLEFLKKPNA KELVSGTTDR ENLHDKFKKA IEEAYPGTIQ ELEKKAEEAK
     RAEEQRVSFW DSAKTDTFKF SF
//