JMJ22_ARATH
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 03-AUG-2022, entry version 102.
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 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 [4]
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 [5]
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 [6]
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, regulates positively 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=2-oxoglutarate + N(omega),N(omega)-dimethyl-L-arginyl-
CC [protein] + O2 = CO2 + formaldehyde + N(omega)-methyl-L-arginyl-
CC [protein] + succinate; Xref=Rhea:RHEA:58352, Rhea:RHEA-COMP:11990,
CC Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031,
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP002543; BAB11404.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91033.1; -; 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 IntAct; Q67XX3; 3.
DR STRING; 3702.AT5G06550.1; -.
DR PaxDb; Q67XX3; -.
DR PRIDE; Q67XX3; -.
DR ProteomicsDB; 232056; -. [Q67XX3-1]
DR EnsemblPlants; AT5G06550.1; AT5G06550.1; AT5G06550. [Q67XX3-1]
DR GeneID; 830543; -.
DR Gramene; AT5G06550.1; AT5G06550.1; AT5G06550. [Q67XX3-1]
DR KEGG; ath:AT5G06550; -.
DR Araport; AT5G06550; -.
DR TAIR; locus:2144153; AT5G06550.
DR eggNOG; KOG2130; Eukaryota.
DR HOGENOM; CLU_016785_1_2_1; -.
DR InParanoid; Q67XX3; -.
DR OMA; QNFVPRK; -.
DR OrthoDB; 609279at2759; -.
DR PhylomeDB; Q67XX3; -.
DR PRO; PR:Q67XX3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q67XX3; baseline and differential.
DR Genevisible; Q67XX3; AT.
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:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0010476; P:gibberellin mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0070079; P:histone H4-R3 demethylation; IDA:UniProtKB.
DR GO; GO:0043985; P:histone H4-R3 methylation; IGI:TAIR.
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 InterPro; IPR041667; Cupin_8.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR Pfam; PF13621; Cupin_8; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF81383; SSF81383; 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 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.3"
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
