EZA1_ARATH
ID EZA1_ARATH Reviewed; 856 AA.
AC Q9ZSM8; O04246;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Histone-lysine N-methyltransferase EZA1 {ECO:0000303|Ref.1};
DE EC=2.1.1.356 {ECO:0000255|PROSITE-ProRule:PRU00909};
DE AltName: Full=CURLY LEAF-like 1;
DE AltName: Full=Protein SET DOMAIN GROUP 10 {ECO:0000303|PubMed:12805620};
DE AltName: Full=Protein SWINGER {ECO:0000303|PubMed:14593172};
GN Name=EZA1 {ECO:0000303|Ref.1};
GN Synonyms=SDG10 {ECO:0000303|PubMed:12805620}, SET10,
GN SWN {ECO:0000303|PubMed:14593172};
GN OrderedLocusNames=At4g02020 {ECO:0000312|Araport:AT4G02020};
GN ORFNames=T10M13.3 {ECO:0000312|EMBL:AAC78694.1};
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 [MRNA].
RA Bilodeau P., Luo M., Dennis E.S., Peacock W.J., Chaudhury A.M.;
RT "EZA1, a novel polycomb group gene from Arabidopsis thaliana.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12805620; DOI=10.1104/pp.102.013722;
RA Springer N.M., Napoli C.A., Selinger D.A., Pandey R., Cone K.C.,
RA Chandler V.L., Kaeppler H.F., Kaeppler S.M.;
RT "Comparative analysis of SET domain proteins in maize and Arabidopsis
RT reveals multiple duplications preceding the divergence of monocots and
RT dicots.";
RL Plant Physiol. 132:907-925(2003).
RN [6]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18854416; DOI=10.1073/pnas.0808687105;
RA De Lucia F., Crevillen P., Jones A.M.E., Greb T., Dean C.;
RT "A PHD-polycomb repressive complex 2 triggers the epigenetic silencing of
RT FLC during vernalization.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:16831-16836(2008).
RN [7]
RP INTERACTION WITH TAF13.
RX PubMed=23506837; DOI=10.1016/j.ydbio.2013.03.005;
RA Lindner M., Simonini S., Kooiker M., Gagliardini V., Somssich M.,
RA Hohenstatt M., Simon R., Grossniklaus U., Kater M.M.;
RT "TAF13 interacts with PRC2 members and is essential for Arabidopsis seed
RT development.";
RL Dev. Biol. 379:28-37(2013).
RN [8]
RP INTERACTION WITH EOL1.
RC STRAIN=cv. Columbia;
RX PubMed=28428341; DOI=10.1073/pnas.1620955114;
RA Zhou Y., Tergemina E., Cui H., Foerderer A., Hartwig B.,
RA Velikkakam James G., Schneeberger K., Turck F.;
RT "Ctf4-related protein recruits LHP1-PRC2 to maintain H3K27me3 levels in
RT dividing cells in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:4833-4838(2017).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30307069; DOI=10.1111/tpj.14125;
RA Liu C., Cheng J., Zhuang Y., Ye L., Li Z., Wang Y., Qi M., Xu L., Zhang Y.;
RT "Polycomb repressive complex 2 attenuates ABA-induced senescence in
RT Arabidopsis.";
RL Plant J. 97:368-377(2019).
RN [10]
RP REVIEW.
RX PubMed=33170267; DOI=10.1042/bst20200660;
RA Shu J., Chen C., Li C., Cui Y.;
RT "The complexity of PRC2 catalysts CLF and SWN in plants.";
RL Biochem. Soc. Trans. 48:2779-2789(2020).
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, mainly
CC abscisic acid (ABA) responsive elements (PubMed:30307069). PcG proteins
CC act by forming multiprotein complexes, which are required to maintain
CC the transcriptionally repressive state of homeotic genes throughout
CC development. PcG proteins are not required to initiate repression, but
CC to maintain it during later stages of development (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:30307069}.
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: Component of the plant homeodomain / polycomb repressive
CC complex 2 (PHD-PRC2) large complex during prolonged cold, composed of
CC core PRC2 components (VRN2, EZA1, FIE and MSI1), and three related PHD
CC finger proteins (VIL1, VIL2 and VIN3) that mediates histone H3
CC trimethylation on 'Lys-27' H3K27me3. Interacts with TAF13. Interacts
CC with EOL1 (PubMed:28428341). {ECO:0000269|PubMed:18854416,
CC ECO:0000269|PubMed:23506837, ECO:0000269|PubMed:28428341}.
CC -!- INTERACTION:
CC Q9ZSM8; Q8W5B1: VRN2; NbExp=3; IntAct=EBI-1102047, EBI-2128880;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- DISRUPTION PHENOTYPE: The double mutant clf-50 swn-1 is hypersensitive
CC to abscisic acid (ABA) associated with reduced ABA-responsive genes
CC repression by histone H3 'Lys-27' methylation (H3K27me3).
CC {ECO:0000269|PubMed:30307069}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAC78694.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80695.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF100163; AAD09108.1; -; mRNA.
DR EMBL; AF001308; AAC78694.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161493; CAB80695.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82112.1; -; Genomic_DNA.
DR EMBL; AY057477; AAL09711.1; -; mRNA.
DR EMBL; AY090293; AAL90954.1; -; mRNA.
DR PIR; T01503; T01503.
DR PIR; T52415; T52415.
DR RefSeq; NP_567221.1; NM_116433.3.
DR AlphaFoldDB; Q9ZSM8; -.
DR SMR; Q9ZSM8; -.
DR BioGRID; 13454; 6.
DR DIP; DIP-35029N; -.
DR IntAct; Q9ZSM8; 7.
DR STRING; 3702.AT4G02020.1; -.
DR iPTMnet; Q9ZSM8; -.
DR PaxDb; Q9ZSM8; -.
DR PRIDE; Q9ZSM8; -.
DR ProteomicsDB; 221823; -.
DR EnsemblPlants; AT4G02020.1; AT4G02020.1; AT4G02020.
DR GeneID; 828165; -.
DR Gramene; AT4G02020.1; AT4G02020.1; AT4G02020.
DR KEGG; ath:AT4G02020; -.
DR Araport; AT4G02020; -.
DR TAIR; locus:2132178; AT4G02020.
DR eggNOG; KOG1079; Eukaryota.
DR HOGENOM; CLU_011060_0_0_1; -.
DR InParanoid; Q9ZSM8; -.
DR OrthoDB; 875190at2759; -.
DR PhylomeDB; Q9ZSM8; -.
DR PRO; PR:Q9ZSM8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZSM8; baseline and differential.
DR Genevisible; Q9ZSM8; AT.
DR GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0031519; C:PcG protein complex; IEA:EnsemblPlants.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1990110; P:callus formation; IGI:TAIR.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
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; IMP:TAIR.
DR GO; GO:1900055; P:regulation of leaf senescence; IGI:TAIR.
DR GO; GO:0048587; P:regulation of short-day photoperiodism, flowering; IEA:EnsemblPlants.
DR GO; GO:0009737; P:response to abscisic acid; IGI:TAIR.
DR GO; GO:0010048; P:vernalization response; IMP:TAIR.
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; SM00717; SANT; 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 Abscisic acid signaling pathway; Chromatin regulator; Coiled coil;
KW Methyltransferase; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..856
FT /note="Histone-lysine N-methyltransferase EZA1"
FT /id="PRO_0000213996"
FT DOMAIN 489..539
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 594..693
FT /note="CXC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00970"
FT DOMAIN 707..822
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..49
FT /evidence="ECO:0000255"
FT MOTIF 838..845
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 68..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 821
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ SEQUENCE 856 AA; 95396 MW; DD4B099C936F197C CRC64;
MVTDDSNSSG RIKSHVDDDD DGEEEEDRLE GLENRLSELK RKIQGERVRS IKEKFEANRK
KVDAHVSPFS SAASSRATAE DNGNSNMLSS RMRMPLCKLN GFSHGVGDRD YVPTKDVISA
SVKLPIAERI PPYTTWIFLD RNQRMAEDQS VVGRRQIYYE QHGGETLICS DSEEEPEPEE
EKREFSEGED SIIWLIGQEY GMGEEVQDAL CQLLSVDASD ILERYNELKL KDKQNTEEFS
NSGFKLGISL EKGLGAALDS FDNLFCRRCL VFDCRLHGCS QPLISASEKQ PYWSDYEGDR
KPCSKHCYLQ LKAVREVPET CSNFASKAEE KASEEECSKA VSSDVPHAAA SGVSLQVEKT
DIGIKNVDSS SGVEQEHGIR GKREVPILKD SNDLPNLSNK KQKTAASDTK MSFVNSVPSL
DQALDSTKGD QGGTTDNKVN RDSEADAKEV GEPIPDNSVH DGGSSICQPH HGSGNGAIII
AEMSETSRPS TEWNPIEKDL YLKGVEIFGR NSCLIARNLL SGLKTCLDVS NYMRENEVSV
FRRSSTPNLL LDDGRTDPGN DNDEVPPRTR LFRRKGKTRK LKYSTKSAGH PSVWKRIAGG
KNQSCKQYTP CGCLSMCGKD CPCLTNETCC EKYCGCSKSC KNRFRGCHCA KSQCRSRQCP
CFAAGRECDP DVCRNCWVSC GDGSLGEAPR RGEGQCGNMR LLLRQQQRIL LGKSDVAGWG
AFLKNSVSKN EYLGEYTGEL ISHHEADKRG KIYDRANSSF LFDLNDQYVL DAQRKGDKLK
FANHSAKPNC YAKVMFVAGD HRVGIFANER IEASEELFYD YRYGPDQAPV WARKPEGSKK
DDSAITHRRA RKHQSH
