JMJ20_ARATH
ID JMJ20_ARATH Reviewed; 462 AA.
AC Q67ZB6; Q680P2; Q9FML5;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Arginine-specific demethylase JMJ20 {ECO:0000303|PubMed:18713399};
DE EC=1.14.11.- {ECO:0000269|PubMed:22483719};
DE AltName: Full=Arginine-specific histone demethylase JMJ20 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Jumonji domain-containing protein 20 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ20 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 20 {ECO:0000303|PubMed:18713399};
DE AltName: Full=[histone H4]-dimethyl-L-arginine(3) monodemethylase JMJ20 {ECO:0000305};
GN Name=JMJ20 {ECO:0000303|PubMed:18713399};
GN OrderedLocusNames=At5g63080 {ECO:0000312|Araport:AT5G63080};
GN ORFNames=MDC12.4 {ECO:0000312|EMBL:BAB10550.1};
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) 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 JMJ22, 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 -!- TISSUE SPECIFICITY: Mostly expressed in leaves, and, to a lower extent,
CC in inflorescences, roots, siliques and stems.
CC {ECO:0000269|PubMed:18713399}.
CC -!- DEVELOPMENTAL STAGE: In far-red light (FR)-treated seeds, present in
CC the whole embryo (PubMed:22483719). Accumulates upon red light (R)
CC (PubMed:22483719). {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 -!- SEQUENCE CAUTION:
CC Sequence=BAB10550.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB008265; BAB10550.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97697.1; -; Genomic_DNA.
DR EMBL; AK175825; BAD43588.1; -; mRNA.
DR EMBL; AK176202; BAD43965.1; -; mRNA.
DR EMBL; BT023460; AAY56451.1; -; mRNA.
DR RefSeq; NP_201113.2; NM_125702.4.
DR STRING; 3702.AT5G63080.1; -.
DR PRIDE; Q67ZB6; -.
DR ProteomicsDB; 180951; -.
DR EnsemblPlants; AT5G63080.1; AT5G63080.1; AT5G63080.
DR GeneID; 836428; -.
DR Gramene; AT5G63080.1; AT5G63080.1; AT5G63080.
DR KEGG; ath:AT5G63080; -.
DR Araport; AT5G63080; -.
DR TAIR; locus:2161967; AT5G63080.
DR eggNOG; KOG2131; Eukaryota.
DR HOGENOM; CLU_016785_2_1_1; -.
DR OMA; HPCMFSR; -.
DR OrthoDB; 609279at2759; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q67ZB6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0033746; F:histone H3-methyl-arginine-2 demethylase activity; IDA:TAIR.
DR GO; GO:0033749; F:histone H3-methyl-arginine-3 demethylase activity; IDA:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
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:0010629; P:negative regulation of gene expression; IBA:GO_Central.
DR GO; GO:0010030; P:positive regulation of seed germination; IMP:UniProtKB.
DR GO; GO:0045905; P:positive regulation of translational termination; IBA:GO_Central.
DR GO; GO:0018126; P:protein hydroxylation; IBA:GO_Central.
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; 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 Gibberellin signaling pathway; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..462
FT /note="Arginine-specific demethylase JMJ20"
FT /id="PRO_0000456190"
FT DOMAIN 115..287
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 177
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 179
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 255
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 462 AA; 54358 MW; D6D79E33AE4821B2 CRC64;
MGIQIIGQIE RINGKELSYG DFAERYLAKN QPVVISDLTE DWRAREDWVS ENGNPNLHVF
ATHFGKSRVQ VADCDTREFT DQKRLEMSVT EFVEQWTNKD SIEESVLYLK DWHFVKEYPD
YTAYQTPPLF SDDWLNVYLD NYQMHEDRDS FQKYDQISCS DYRFVYMGGK GSWTPLHADV
FRSYSWSANV CGKKRWLFLP PPQSHLVYDR YMKNCVYDIF EEVNETKFPG FKKTTWLECI
QEPGEIIFVP SGWHHQVYNL EDTISINHNW LNAYNLSWVW DLLWKDYKDT EESIEDIRDI
CDDFEAICQR NLAANTGMNL NDFFLFMSRF SLGNMVLLQS YSDKHKNLNS CSLAMAQNLL
MNLSTILKVM MKMISAGGVT AEEVYLDLRE TLEDPQFLRF VRDMGRTYAR IHMEEEDQFL
SSKELLQKLS GLAGPNMQIC SPKDLVEMIN HHNTFSSQIY FI
