EZ1_ORYSJ
ID EZ1_ORYSJ Reviewed; 895 AA.
AC Q10MI4; Q8LLD6;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Histone-lysine N-methyltransferase EZ1 {ECO:0000305};
DE EC=2.1.1.356 {ECO:0000255|PROSITE-ProRule:PRU00909};
DE AltName: Full=Protein SET DOMAIN GROUP 718 {ECO:0000305};
DE AltName: Full=SET family protein 1 {ECO:0000305};
DE Short=OsSET1 {ECO:0000303|PubMed:12815033};
DE AltName: Full=SET family protein 15 {ECO:0000305};
DE Short=OsSET15 {ECO:0000303|PubMed:23762371};
GN Name=EZ1 {ECO:0000303|Ref.9};
GN Synonyms=SDG718 {ECO:0000303|PubMed:25400654},
GN SET1 {ECO:0000303|PubMed:12815033};
GN OrderedLocusNames=Os03g0307800 {ECO:0000312|EMBL:BAF11813.1},
GN LOC_Os03g19480 {ECO:0000312|EMBL:ABF95544.1};
GN ORFNames=OsJ_10569 {ECO:0000312|EMBL:EEE58920.1};
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 [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=12815033; DOI=10.1093/jxb/erg201;
RA Liang Y.K., Wang Y., Zhang Y., Li S.G., Lu X.C., Li H., Zou C., Xu Z.H.,
RA Bai S.N.;
RT "OsSET1, a novel SET-domain-containing gene from rice.";
RL J. Exp. Bot. 54:1995-1996(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim D.Y., Yoon I.S.;
RT "Functional analysis of gene related to development in rice.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=19825651; DOI=10.1093/mp/ssp036;
RA Luo M., Platten D., Chaudhury A., Peacock W.J., Dennis E.S.;
RT "Expression, imprinting, and evolution of rice homologs of the polycomb
RT group genes.";
RL Mol. Plant 2:711-723(2009).
RN [9]
RP INTERACTION WITH FIE2, AND TISSUE SPECIFICITY.
RX DOI=10.1007/s11816-012-0229-0;
RA Na J.K., Seo M.H., Yoon I.S., Lee Y.H., Lee K.O., Kim D.Y.;
RT "Involvement of rice polycomb protein OsFIE2 in plant growth and seed
RT size.";
RL Plant Biotechnol. Rep. 6:339-346(2012).
RN [10]
RP INTERACTION WITH FIE1 AND FIE2.
RX PubMed=23150632; DOI=10.1105/tpc.112.102269;
RA Zhang L., Cheng Z., Qin R., Qiu Y., Wang J.L., Cui X., Gu L., Zhang X.,
RA Guo X., Wang D., Jiang L., Wu C.Y., Wang H., Cao X., Wan J.;
RT "Identification and characterization of an epi-allele of FIE1 reveals a
RT regulatory linkage between two epigenetic marks in rice.";
RL Plant Cell 24:4407-4421(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND INTERACTION WITH FIE2.
RX PubMed=23505380; DOI=10.1371/journal.pgen.1003322;
RA Nallamilli B.R., Zhang J., Mujahid H., Malone B.M., Bridges S.M., Peng Z.;
RT "Polycomb group gene OsFIE2 regulates rice (Oryza sativa) seed development
RT and grain filling via a mechanism distinct from Arabidopsis.";
RL PLoS Genet. 9:E1003322-E1003322(2013).
RN [12]
RP DEVELOPMENTAL STAGE, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=23762371; DOI=10.1371/journal.pone.0065426;
RA Lu Z., Huang X., Ouyang Y., Yao J.;
RT "Genome-wide identification, phylogenetic and co-expression analysis of
RT OsSET gene family in rice.";
RL PLoS ONE 8:E65426-E65426(2013).
RN [13]
RP FUNCTION.
RX PubMed=25400654; DOI=10.3389/fpls.2014.00591;
RA Liu X., Zhou C., Zhao Y., Zhou S., Wang W., Zhou D.X.;
RT "The rice enhancer of zeste [E(z)] genes SDG711 and SDG718 are respectively
RT involved in long day and short day signaling to mediate the accurate
RT photoperiod control of flowering time.";
RL Front. Plant Sci. 5:591-591(2014).
CC -!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of some PcG
CC multiprotein complex, which methylates 'Lys-27' of histone H3, leading
CC to transcriptional repression of the affected target genes. PcG
CC proteins act by forming multiprotein complexes, which are required to
CC maintain the transcriptionally repressive state of homeotic genes
CC throughout development. PcG proteins are not required to initiate
CC repression, but to maintain it during later stages of development
CC (Probable). Involved in the regulation of flowering. Promotes flowering
CC under short day (SD) conditions. Regulates the trimethylation on
CC histone H3 'Lys-27' (H3K27me3) of the flowering regulator LF
CC (PubMed:25400654). {ECO:0000269|PubMed:25400654,
CC ECO:0000305|PubMed:25400654}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-
CC COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.356;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00909};
CC -!- SUBUNIT: Interacts with FIE1 (PubMed:23150632). Interacts with FIE2
CC (Ref.9, PubMed:23150632, PubMed:23505380). Component of the polycomb
CC repressive complex 2 (PRC2), composed of the core PRC2 components FIE2,
CC EMF2B and CLF. PRC2 methylates 'Lys-27' residues of histone H3
CC (H3K27me3), leading to transcriptional repression of the affected
CC target gene. {ECO:0000269|PubMed:23150632, ECO:0000269|PubMed:23505380,
CC ECO:0000269|Ref.9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12815033}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:19825651). Expressed in
CC leaves and stems. Expressed a low levels in roots, anthers, ovaries and
CC ovules (Ref.9). {ECO:0000269|PubMed:19825651, ECO:0000269|Ref.9}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in seed endosperm 7 days after
CC pollination. {ECO:0000269|PubMed:23762371}.
CC -!- MISCELLANEOUS: Down-regulation of EZ1 delays flowering in short day
CC (SD), but has no effect in long day (LD).
CC {ECO:0000269|PubMed:25400654}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. EZ subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00909}.
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; AF407010; AAN01115.1; -; mRNA.
DR EMBL; HQ881586; AEJ08686.1; -; mRNA.
DR EMBL; DP000009; ABF95544.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11813.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83828.1; -; Genomic_DNA.
DR EMBL; CM000140; EEE58920.1; -; Genomic_DNA.
DR RefSeq; XP_015630972.1; XM_015775486.1.
DR AlphaFoldDB; Q10MI4; -.
DR SMR; Q10MI4; -.
DR STRING; 4530.OS03T0307800-01; -.
DR PaxDb; Q10MI4; -.
DR PRIDE; Q10MI4; -.
DR EnsemblPlants; Os03t0307800-01; Os03t0307800-01; Os03g0307800.
DR GeneID; 4332612; -.
DR Gramene; Os03t0307800-01; Os03t0307800-01; Os03g0307800.
DR KEGG; osa:4332612; -.
DR eggNOG; KOG1079; Eukaryota.
DR HOGENOM; CLU_011060_0_0_1; -.
DR InParanoid; Q10MI4; -.
DR OMA; NEQYVLD; -.
DR OrthoDB; 875190at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0005677; C:chromatin silencing complex; IEA:EnsemblPlants.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:EnsemblPlants.
DR GO; GO:1990110; P:callus formation; IEA:EnsemblPlants.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:0070734; P:histone H3-K27 methylation; IMP:UniProtKB.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IBA:GO_Central.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IEA:EnsemblPlants.
DR GO; GO:1900055; P:regulation of leaf senescence; IEA:EnsemblPlants.
DR GO; GO:0048587; P:regulation of short-day photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0010048; P:vernalization response; IEA:EnsemblPlants.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR026489; CXC_dom.
DR InterPro; IPR045318; EZH1/2-like.
DR InterPro; IPR025778; Hist-Lys_N-MeTrfase_plant.
DR InterPro; IPR041355; Pre-SET_CXC.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR PANTHER; PTHR45747; PTHR45747; 1.
DR Pfam; PF18264; preSET_CXC; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM01114; CXC; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51633; CXC; 1.
DR PROSITE; PS51576; SAM_MT43_EZ; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Developmental protein; Differentiation; Flowering;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..895
FT /note="Histone-lysine N-methyltransferase EZ1"
FT /id="PRO_0000444467"
FT DOMAIN 628..732
FT /note="CXC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00970"
FT DOMAIN 747..862
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 861
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT CONFLICT 572
FT /note="M -> V (in Ref. 1; AAN01115 and 2; AEJ08686)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="L -> P (in Ref. 1; AAN01115 and 2; AEJ08686)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="K -> N (in Ref. 1; AAN01115 and 2; AEJ08686)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 895 AA; 99863 MW; 8820777FE1F85325 CRC64;
MASSSSKASD SSSQRPKRPD QGPSGKDAAG LVALHGKLAQ LKRQVQSTRL AAIKERVEAN
RKALQVHTCA LFDVAAAAEV ASRGAEGGNA LSRGAAEGHR RFVGWDSASG PGERELVHVQ
EENLVAGTLV LSSSGGSGAS HRTVVQLVKL PVVDKIPPYT TWIFLDKNQR MADDQSVGRR
RIYYDPIVNE ALICSESDDD VPEPEEEKHV FTEGEDQLIW KATQDHGLSR EVLNVLCQFV
DATPSEIEER SEVLFEKYEK QSQSSYKTDL QLFLDKTMDV ALDSFDNLFC RRCLVFDCRL
HGCSQNLVFP SEKQPYGHEL DENKRPCGDQ CYLRRREVYQ DTCNDDRNAC TTYNMDSRSS
SLKVSATILS ESEDSNRDED NIKSTSIVET SRSKITNSEY ADKSVTPPPG DASETENVSP
DMPLRTLGRR KISKHASKSN DHSPDKRQKI YSSPFPFAMS VLNKQSVPEI GETCPDSIES
AVDQLPSLDD PNKKISTKDM CAGSTTNTTE NTLRDNNNNL FISNKEHSIS HWSALERDLY
LKGIEIFGKN SCLIARNLLS GLKTCMEVAS YMYNNGAAMA KRPLSGKSIL GDFAEAEQGY
MEQDLVARTR ICRRKGRARK LKYTWKSAGH PTVRKRIGDG KQWYTQYNPC GCQQMCGKDC
ACVENGTCCE KYCGCSKSCK NRFRGCHCAK SQCRSRQCPC FAASRECDPD VCRNCWVSCG
DGSLGEPLAR GDGYQCGNMK LLLKQQQRIL LGKSDVAGWG AFIKNPVNRN DYLGEYTGEL
ISHREADKRG KIYDRANSSF LFDLNEQYVL DAYRKGDKLK FANHSSNPNC YAKVMLVAGD
HRVGIYAKDR IEASEELFYD YRYGPDQAPA WARRPEGSKK DEASVSHHRA HKVAR
