JMJ15_ARATH
ID JMJ15_ARATH Reviewed; 806 AA.
AC O64752;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Lysine-specific demethylase JMJ15 {ECO:0000303|PubMed:18713399};
DE EC=1.14.11.- {ECO:0000269|PubMed:22555401};
DE AltName: Full=Jumonji domain-containing protein 15 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ15 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 15 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Lysine-specific histone demethylase JMJ15 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 27 {ECO:0000303|PubMed:18713399};
DE AltName: Full=[histone H3]-trimethyl-L-lysine(4) monodemethylase JMJ15 {ECO:0000305};
GN Name=JMJ15 {ECO:0000303|PubMed:18713399};
GN Synonyms=MEE27 {ECO:0000303|PubMed:18713399},
GN PKDM7C {ECO:0000303|PubMed:20202164};
GN OrderedLocusNames=At2g34880 {ECO:0000312|Araport:AT2G34880};
GN ORFNames=F19I3 {ECO:0000312|EMBL:AAC12829.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=20202164; DOI=10.1111/j.1365-313x.2010.04182.x;
RA Yang W., Jiang D., Jiang J., He Y.;
RT "A plant-specific histone H3 lysine 4 demethylase represses the floral
RT transition in Arabidopsis.";
RL Plant J. 62:663-673(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22555401; DOI=10.1007/s00299-012-1249-5;
RA Yang H., Mo H., Fan D., Cao Y., Cui S., Ma L.;
RT "Overexpression of a histone H3K4 demethylase, JMJ15, accelerates flowering
RT time in Arabidopsis.";
RL Plant Cell Rep. 31:1297-1308(2012).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION BY SALT.
RC STRAIN=cv. Columbia;
RX PubMed=25009544; DOI=10.3389/fpls.2014.00290;
RA Shen Y., Conde E Silva N., Audonnet L., Servet C., Wei W., Zhou D.-X.;
RT "Over-expression of histone H3K4 demethylase gene JMJ15 enhances salt
RT tolerance in Arabidopsis.";
RL Front. Plant Sci. 5:290-290(2014).
CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-4' (H3K4me) of
CC histone H3 with a specific activity for H3K4me3 (PubMed:22555401). No
CC activity on H3K4me2, H3K4me1, H3K9me3/2, H3K27me3/2 and H3K36me3/2
CC (PubMed:22555401). Involved in the control of flowering time by
CC demethylating H3K4me3 at the FLC locus and repressing its expression
CC (PubMed:22555401). The repression of FLC level and reduction in H3K4me3
CC at the FLC locus results in induction of the flowering activator FT,
CC which is a downstream target of FLC (PubMed:22555401). Promotes salt
CC tolerance by down-regulating the expression of several transcriptions
CC factors involved in stress responses via H3K4me3 and H3K4me2
CC demethylation (PubMed:25009544). {ECO:0000269|PubMed:22555401,
CC ECO:0000269|PubMed:25009544}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone
CC H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(4)-
CC [histone H3] + succinate; Xref=Rhea:RHEA:60212, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15540, 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:22555401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60213;
CC Evidence={ECO:0000269|PubMed:22555401};
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:0000255|PROSITE-ProRule:PRU00537,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, shoot apex, rosette
CC and cauline leaves, stems, inflorescences and siliques
CC (PubMed:18713399). Expressed at low levels during vegetative growth but
CC to higher levels in young floral organs (PubMed:25009544).
CC {ECO:0000269|PubMed:18713399, ECO:0000269|PubMed:22555401,
CC ECO:0000269|PubMed:25009544}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, confined at the base of rosette
CC leaves and in root vascular tissues (PubMed:25009544). Accumulates in
CC pericycle cells precursors of lateral root meristems and remains at the
CC base of growing lateral roots, but not in tips (PubMed:25009544). In
CC the inflorescence, strongly expressed in young anthers and present in
CC carpels (PubMed:25009544). Fades out in mature flowers
CC (PubMed:25009544). {ECO:0000269|PubMed:25009544}.
CC -!- INDUCTION: Slightly induced by salt. {ECO:0000269|PubMed:25009544}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:20202164, PubMed:22555401, PubMed:25009544).
CC Increased sensitivity to salt (PubMed:25009544).
CC {ECO:0000269|PubMed:20202164, ECO:0000269|PubMed:22555401,
CC ECO:0000269|PubMed:25009544}.
CC -!- MISCELLANEOUS: Plants over-expressing JMJ15 show early flowering
CC phenotype. {ECO:0000305|PubMed:22555401}.
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; AC004238; AAC12829.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09034.1; -; Genomic_DNA.
DR PIR; T00470; T00470.
DR RefSeq; NP_181034.1; NM_129041.1.
DR AlphaFoldDB; O64752; -.
DR SMR; O64752; -.
DR STRING; 3702.AT2G34880.1; -.
DR PaxDb; O64752; -.
DR PRIDE; O64752; -.
DR ProteomicsDB; 232268; -.
DR EnsemblPlants; AT2G34880.1; AT2G34880.1; AT2G34880.
DR GeneID; 818053; -.
DR Gramene; AT2G34880.1; AT2G34880.1; AT2G34880.
DR KEGG; ath:AT2G34880; -.
DR Araport; AT2G34880; -.
DR TAIR; locus:2044697; AT2G34880.
DR eggNOG; KOG1246; Eukaryota.
DR HOGENOM; CLU_000991_8_1_1; -.
DR InParanoid; O64752; -.
DR OMA; DARHDAY; -.
DR OrthoDB; 664180at2759; -.
DR PhylomeDB; O64752; -.
DR BRENDA; 1.14.11.67; 399.
DR PRO; PR:O64752; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64752; baseline and differential.
DR Genevisible; O64752; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0044648; P:histone H3-K4 dimethylation; IMP:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0009909; P:regulation of flower development; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR004198; Znf_C5HC2.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..806
FT /note="Lysine-specific demethylase JMJ15"
FT /id="PRO_0000429994"
FT DOMAIN 61..102
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 261..427
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT DOMAIN 629..687
FT /note="FYR N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00875"
FT DOMAIN 689..775
FT /note="FYR C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00876"
FT ZN_FING 514..566
FT /note="C5HC2"
FT /evidence="ECO:0000255"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 132..139
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..151
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 307
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 309
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 395
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 514
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 528
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 531
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 539
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 542
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 545
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
SQ SEQUENCE 806 AA; 91718 MW; FB6A98F150776E48 CRC64;
MEPFSAAQNK EDKDTSVEPP RRRCHRKNKG TNVEPPSSPY HPKVLARWDP ANEKRPDIGE
APVFHPTSEE FEDTLAYIEK IRPLAESFGI CRIVPPSNWS PPCRLKGDSI WKNKNFPTRV
QFVDLLQNRG PVKKKTPKGR KRKRGKYSRT VAPKKRNGSV SKSVSTPKAT EEENFGFESG
PEFTLEKFEK YAQDFKDSYF ERKDNVGDPS VEEIEGEYWR IIEKETNEVK VLYGTDLENP
ILGSGFSKGV KIPTRRNDMD KYISSGWNLN NLARLQGSLL SFEDCEISGV QVPWLYVGMC
FSTFCWHVED NHLYSLNYHH FGEPKVWYGV PGSHATGLEK AMRKHLPDLF DEQPDLLHEL
VTQFSPTILK NEGVPVYRAV QNAGEYVLTF PRAYHSGFNC GFNCAEAVNV APVDWLAHGQ
NAVEIYSQET RKTSLSHDKI LLGAAFEAVK SLSAHGEDNT KRFSWKRFCG KDGIITKAIE
ARLRMEEKRI EALGNGFSLV KMDKDFDSNC ERECISCFSD LHLSATGCKN CSSLEEYGCT
KHDICSCEGK DRFIFLRYTI DELSSLVRAL EGESDDLKAW LSKVMEGCSE TQKGESSGII
VKEKQVQEEC FDLNGECNKS SEICEDASIM DLAAYHVEPI NLGFLVVGKL WCNKHAIFPK
GFKSRVKFYN VQDPMRISYY VSEIVDAGLL GPLFKVTLEE SQDESFSYAS PQKCWEMVLL
RVKEEIMRRS NQKQDVHMLE SIDGLKMFGF RSPFIVQATE ALDPNHGQVE YWNHKNEKDS
LEMKDCFMSN SSQSLSKARL FGVDLN
