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Database: UniProt
Entry: Q10MI4
LinkDB: Q10MI4
Original site: Q10MI4 
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   10-APR-2019, entry version 108.
DE   RecName: Full=Histone-lysine N-methyltransferase EZ1 {ECO:0000305};
DE            EC=2.1.1.43 {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; Magnoliophyta; 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.,
RA   Xu Z.H., 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.,
RA   Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L.,
RA   Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S., Johri S.,
RA   Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S.,
RA   Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J.,
RA   de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H.,
RA   Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F.,
RA   Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A.,
RA   Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J.,
RA   Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L.,
RA   Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A.,
RA   Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W.,
RA   Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome
RT   3 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.,
RA   McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
RA   Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
RA   Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
RA   Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using
RT   next 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.,
RA   Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
RA   Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
RA   Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
RA   Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
RA   Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
RA   Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
RA   Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
RA   Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
RA   Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
RA   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
RT   polycomb 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.,
RA   Zhang X., 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
RT   a 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
RP   FIE2.
RX   PubMed=23505380; DOI=10.1371/journal.pgen.1003322;
RA   Nallamilli B.R., Zhang J., Mujahid H., Malone B.M., Bridges S.M.,
RA   Peng Z.;
RT   "Polycomb group gene OsFIE2 regulates rice (Oryza sativa) seed
RT   development and grain filling via a mechanism distinct from
RT   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
RT   of 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
RT   respectively involved in long day and short day signaling to mediate
RT   the accurate photoperiod control of flowering time.";
RL   Front. Plant Sci. 5:591-591(2014).
CC   -!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of some
CC       PcG multiprotein complex, which methylates 'Lys-27' of histone H3,
CC       leading to transcriptional repression of the affected target
CC       genes. PcG proteins act by forming multiprotein complexes, which
CC       are required to maintain the transcriptionally repressive state of
CC       homeotic genes throughout development. PcG proteins are not
CC       required to initiate repression, but to maintain it during later
CC       stages of development (Probable). Involved in the regulation of
CC       flowering. Promotes flowering under short day (SD) conditions.
CC       Regulates the trimethylation on histone H3 'Lys-27' (H3K27me3) of
CC       the flowering regulator LF (PubMed:25400654).
CC       {ECO:0000269|PubMed:25400654, ECO:0000305|PubMed:25400654}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00909};
CC   -!- SUBUNIT: Interacts with FIE1 (PubMed:23150632). Interacts with
CC       FIE2 (Ref.9, PubMed:23150632, PubMed:23505380). Component of the
CC       polycomb repressive complex 2 (PRC2), composed of the core PRC2
CC       components FIE2, EMF2B and CLF. PRC2 methylates 'Lys-27' residues
CC       of histone H3 (H3K27me3), leading to transcriptional repression of
CC       the affected target gene. {ECO:0000269|PubMed:23150632,
CC       ECO:0000269|PubMed:23505380, ECO:0000269|Ref.9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12815033}.
CC   -!- TISSUE SPECIFICITY: Widely expressed (PubMed:19825651). Expressed
CC       in leaves and stems. Expressed a low levels in roots, anthers,
CC       ovaries and ovules (Ref.9). {ECO:0000269|PubMed:19825651,
CC       ECO:0000269|Ref.9}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in seed endosperm 7 days
CC       after pollination. {ECO:0000269|PubMed:23762371}.
CC   -!- MISCELLANEOUS: Down-regulation of EZ1 delays flowering in short
CC       day (SD), but has no effect in long day (LD).
CC       {ECO:0000269|PubMed:25400654}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. EZ subfamily. {ECO:0000255|PROSITE-ProRule:PRU00909}.
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   UniGene; Os.21566; -.
DR   STRING; 4530.OS03T0307800-01; -.
DR   PaxDb; 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   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000083511; -.
DR   InParanoid; Q10MI4; -.
DR   KO; K11430; -.
DR   OMA; RIGDGKQ; -.
DR   OrthoDB; 875190at2759; -.
DR   Reactome; R-OSA-8953750; Transcriptional Regulation by E2F6.
DR   Proteomes; UP000059680; Chromosome 3.
DR   GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
DR   GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006342; P:chromatin silencing; IMP:UniProtKB.
DR   GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR   GO; GO:0070734; P:histone H3-K27 methylation; IMP:UniProtKB.
DR   GO; GO:0048587; P:regulation of short-day photoperiodism, flowering; IMP:UniProtKB.
DR   CDD; cd00167; SANT; 1.
DR   InterPro; IPR026489; CXC_dom.
DR   InterPro; IPR025778; Hist-Lys_N-MeTrfase_EZ.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR   PANTHER; PTHR22884:SF237; PTHR22884:SF237; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01114; CXC; 1.
DR   SMART; SM00317; SET; 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; Complete proteome; Developmental protein;
KW   Differentiation; Flowering; Methyltransferase; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    895       Histone-lysine N-methyltransferase EZ1.
FT                                /FTId=PRO_0000444467.
FT   DOMAIN      628    732       CXC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00970}.
FT   DOMAIN      747    862       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   BINDING     861    861       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   CONFLICT    572    572       M -> V (in Ref. 1; AAN01115 and 2;
FT                                AEJ08686). {ECO:0000305}.
FT   CONFLICT    728    728       L -> P (in Ref. 1; AAN01115 and 2;
FT                                AEJ08686). {ECO:0000305}.
FT   CONFLICT    818    818       K -> N (in Ref. 1; AAN01115 and 2;
FT                                AEJ08686). {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
//
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