JM705_ORYSJ
ID JM705_ORYSJ Reviewed; 1286 AA.
AC Q5N712; A0A0P0VBR2; Q8LIW4;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Lysine-specific demethylase JMJ705;
DE EC=1.14.11.68 {ECO:0000269|PubMed:24280387};
DE AltName: Full=Jumonji domain-containing protein 705;
DE AltName: Full=Lysine-specific histone demethylase JMJ705;
DE AltName: Full=Protein JUMONJI 705;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(27) demethylase JMJ705 {ECO:0000305};
GN Name=JMJ705; OrderedLocusNames=Os01g0907400, LOC_Os01g67970;
GN ORFNames=B1417F08.20, OsJ_04472, P0497A05.7;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-244.
RC STRAIN=cv. Hwayoung, and cv. Zhonghua 11;
RX PubMed=24280387; DOI=10.1105/tpc.113.118802;
RA Li T., Chen X., Zhong X., Zhao Y., Liu X., Zhou S., Cheng S., Zhou D.X.;
RT "Jumonji C domain protein JMJ705-mediated removal of histone H3 lysine 27
RT trimethylation is involved in defense-related gene activation in rice.";
RL Plant Cell 25:4725-4736(2013).
CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-27' (H3K27me) of
CC histone H3 with a specific activity for H3K27me3 and H3K27me2. No
CC activity on H3K4me3, H3K9me3, H3K27me1 and H3K36me3. Involved in biotic
CC stress response. May demethylate H3K27me3-marked defense-related genes
CC and increase their basal and induced expression levels during pathogen
CC infection. {ECO:0000269|PubMed:24280387}.
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:24280387};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60225;
CC Evidence={ECO:0000269|PubMed:24280387};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q53WJ1};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q53WJ1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537,
CC ECO:0000269|PubMed:24280387}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flag leaves. Expressed at
CC low levels in roots, shoots, stems and panicles.
CC {ECO:0000269|PubMed:24280387}.
CC -!- INDUCTION: By salt stress, abscisic acid (ABA), jasmonic acid (JA), the
CC ethylene precursor ACC and infection by the bacterial pathogen
CC Xanthomonas oryzae pv. oryzae. {ECO:0000269|PubMed:24280387}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant height, panicle length, spikelets
CC per panicle and spikelet fertility. Increased susceptibility to the
CC bacterial pathogen Xanthomonas oryzae pv. oryzae.
CC {ECO:0000269|PubMed:24280387}.
CC -!- MISCELLANEOUS: Plants over-expressing JMJ705 display a leaf lesion-
CC mimic phenotype in mature leaves, have high levels of biotic stress-
CC responsive and defense-related genes leading to enhanced plant
CC resistance to the bacterial pathogen Xanthomonas oryzae pv. oryzae.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB92564.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003380; BAB92564.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP006531; BAD82744.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF07051.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS75802.1; -; Genomic_DNA.
DR EMBL; CM000138; EEE55852.1; -; Genomic_DNA.
DR EMBL; AK068952; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015621377.1; XM_015765891.1.
DR AlphaFoldDB; Q5N712; -.
DR SMR; Q5N712; -.
DR STRING; 4530.OS01T0907400-01; -.
DR PaxDb; Q5N712; -.
DR PRIDE; Q5N712; -.
DR EnsemblPlants; Os01t0907400-01; Os01t0907400-01; Os01g0907400.
DR GeneID; 4324980; -.
DR Gramene; Os01t0907400-01; Os01t0907400-01; Os01g0907400.
DR KEGG; osa:4324980; -.
DR eggNOG; KOG1246; Eukaryota.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_001687_1_0_1; -.
DR InParanoid; Q5N712; -.
DR OMA; MRFREPS; -.
DR OrthoDB; 664180at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q5N712; OS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0071558; F:histone H3-tri/di-methyl-lysine-27 demethylase activity; IDA:UniProtKB.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; IDA:UniProtKB.
DR GO; GO:0040010; P:positive regulation of growth rate; IMP:UniProtKB.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Plant defense; Reference proteome; Repeat; Stress response;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1286
FT /note="Lysine-specific demethylase JMJ705"
FT /id="PRO_0000430001"
FT DOMAIN 25..66
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 201..367
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 1167..1189
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1190..1214
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1220..1244
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1250..1276
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 82..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 244
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 335
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MUTAGEN 244
FT /note="H->A: Loss of activity on H3K27me3/2."
FT /evidence="ECO:0000269|PubMed:24280387"
FT CONFLICT 726
FT /note="K -> R (in Ref. 6; AK068952)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1286 AA; 142049 MW; 6B8376844FED8058 CRC64;
MRPSPPPAAP AAEPVPPWLR SLPVAPEFRP TAAEFADPVS YILKIEPAAA PYGICKVVPP
LPPPPKKATF SNLSRSFAAL HPDDRSPSFP TRHQQVGLCP RRTRPGLKPV WRSSHRYTLP
QFESKAGATR KSLLAGLNFP ASRQLTPLDH EVLFWRASAD RPIVVEYGSD MSGSGFSPCA
AQPQPPPQQQ PTARAAAHLG ETAWNMRGVA RSPGSLLRFM PEDVPGVTTP MLYVGMMFSW
FAWHVEDHDL HSLNYMHLGA AKTWYGVPRD AALAFEDVVR EHGYGGEVNP LETFATLGQK
TTVMSPEVLV ESGIPCCRLV QNAGEFVVTF PGSYHCGFSH GFNCGEASNI ATPEWLRIAK
EAAIRRASIN RPPMVSHYQL LYDLALSMRF REPSNGEMET RSSRIKEKKK CEGEQLVKKM
FIQNVIEDNE LLSHLLNDGS SCIILPANAH DGPGLSTLRS TDQSNMNSRI SHNLCSREEA
PEASGCLSPN RNGDTRNCIS SDTHNMEGDK GDIMSATGLL DQGLLSCVTC GILSFSCVAV
LKPRDSTARY LMSADSNSIN NQLSISGGSI LADAPTNERN GVISRPYSEH CCNEIMADDA
EIDKNSALDL LAFAHGGQPD PEEDPLEKIL KIAHGINKSQ PNSSNNVGCV GTKLSSSSTE
RQERPSSQNA HCNGSSVISN GPKGVRTRNK YQLKMVLSEG FQAKDIYSAK EKKVQSEPSS
SKGDVKETID VSGTENDVGC KSTTISVSEH RGSTKNMYSV KEKKVQSKPS SLKGTVKETV
DVSGTENDAR CKSITISVSE HRGSTPMTNS LAASIVKPDK DSSRMHVFCL EHAIEVEKQL
HAIGGSNIML ICRPEYPKIE AEARLLGEEM GLVYDWKGIH FKEANMEDRQ KIQEVLRDEE
AIPTSSDWAV KLGINLYYSA NLAKSPLYNK QMPYNRVIYR AFGCDSPNDS PVMFNTCERK
QSHQKKIVVA GRWCGKVWMS KQVHPYLAHR VESQEAEEAD RICSYHFDEK HKAEPVGNSS
RVEASKRKSS SLTDVTESSN RRGEIPGEET NTKRPKHSQE NNLRALETAA EVVVPSPAGT
GLRVSSRIAN RANKLKSKME KEDVPSSRPK SNIKEKSSHA SGQKSNVQEA NANSASHLRA
MPPKQKAEAE AKKQIRTPKP PKQAVEYSCD IEGCSMSFRT KRDLSLHKSD ICPVKGCGKK
FFSHKYLLQH RKVHTDDRPL TCPWKGCNMA FKWPWARTEH LRVHTGDRPY VCHEPGCAQT
FRFVSDFSRH KRKTGHSVKK KKKAKS
