EZ2_MAIZE
ID EZ2_MAIZE Reviewed; 894 AA.
AC Q8S4P5;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Histone-lysine N-methyltransferase EZ2;
DE EC=2.1.1.356;
DE AltName: Full=Enhancer of zeste protein 2;
GN Name=EZ2; Synonyms=MEZ2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, AND
RP ALTERNATIVE SPLICING.
RC TISSUE=Seed;
RX PubMed=11950982; DOI=10.1104/pp.010742;
RA Springer N.M., Danilevskaya O.N., Hermon P., Helentjaris T.G.,
RA Phillips R.L., Kaeppler H.F., Kaeppler S.M.;
RT "Sequence relationships, conserved domains, and expression patterns for
RT maize homologs of the Polycomb group genes E(z), esc, and E(Pc).";
RL Plant Physiol. 128:1332-1345(2002).
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 are not required to initiate repression, but to maintain it
CC during later stages of development (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8S4P5-1; Sequence=Displayed;
CC Name=2; Synonyms=as1;
CC IsoId=Q8S4P5-2; Sequence=VSP_007783;
CC Name=3; Synonyms=as2;
CC IsoId=Q8S4P5-3; Sequence=VSP_007784;
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}.
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DR EMBL; AF443597; AAM13421.1; -; mRNA.
DR RefSeq; NP_001105650.1; NM_001112180.1. [Q8S4P5-1]
DR AlphaFoldDB; Q8S4P5; -.
DR SMR; Q8S4P5; -.
DR STRING; 4577.GRMZM5G875502_P02; -.
DR PaxDb; Q8S4P5; -.
DR PRIDE; Q8S4P5; -.
DR EnsemblPlants; Zm00001eb396070_T002; Zm00001eb396070_P002; Zm00001eb396070. [Q8S4P5-1]
DR GeneID; 542659; -.
DR Gramene; Zm00001eb396070_T002; Zm00001eb396070_P002; Zm00001eb396070. [Q8S4P5-1]
DR KEGG; zma:542659; -.
DR MaizeGDB; 754843; -.
DR eggNOG; KOG1079; Eukaryota.
DR OrthoDB; 875190at2759; -.
DR Proteomes; UP000007305; Chromosome 9.
DR ExpressionAtlas; Q8S4P5; baseline and differential.
DR Genevisible; Q8S4P5; ZM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031519; C:PcG protein complex; IEA:InterPro.
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:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Methyltransferase; Nucleus; Reference proteome;
KW Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..894
FT /note="Histone-lysine N-methyltransferase EZ2"
FT /id="PRO_0000213999"
FT DOMAIN 527..577
FT /note="SANT"
FT DOMAIN 627..731
FT /note="CXC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00970"
FT DOMAIN 746..861
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 342..894
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11950982"
FT /id="VSP_007783"
FT VAR_SEQ 625..894
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11950982"
FT /id="VSP_007784"
SQ SEQUENCE 894 AA; 99979 MW; 9C2B04E6F80BA113 CRC64;
MASSSKASDS SQRSKRSDQG MGKDAAAASV VPIHANLTQL IRQVQSGRLA YIKEKLEVNR
KTLQRHSCSL FDVAAAAEVA SRGTDGGNAL SQRAAERQCG SDLANGIGER DVVSVQEENL
ATGTLALSSS GATAQRTIVR FVKLPLVEKI PPYTTWIFLD KNQRMADDQS VVGRRRIYYD
TVGNEALICS DSDEEIPEPE EEKHFFTKGE DHLIWRATQD HGLNQEVVNV LCQFIGATPS
EIEERSEVLF EKNEKHSGSS DKIESRLSLD KTMDAVLDSF DNLFCRRCLV FDCRLHGCSQ
NLVFPCEKQP YSFDPDENKK PCGHLCYLRF PQWREGFKEM HDDGLAGGAT YTMESGTASQ
RVDVNVMYES EDSNRQKGNI RSMTLVGTSG SKIISSVSAE ESTTTPSADI SETENVSSDL
PPSSLRKHKI SKHGPRYREH SPGKRQKVFT SDISFEGNIM NKLSIPEIRD TRLESRESGG
DKLRILDEST KKTSRKDMCG ESPATTMENV GRQSNKVSST KNFLESTLSC WSALERDLYL
KGIEIFGKNS CLIARNLLSG LKTCIEVANY MYNNGAAMAK RPLLNKSISG DFAENEQDYM
EQDMAARTRI YRRRGRNRKL KYTWKSAGHP TVRKRTDDGK QCYTQYSPCA CQQMCGKDCP
CADKGTCCEK YCGCSKSCKN KFRGCHCAKS QCRSRQCPCF AASRECDPDV CRNCWVSCGD
GSLGEPLARG DGYQCGNMKL LLKQQQRILL GRSDVAGWGA FIKNPVNKND YLGEYTGELI
SHKEADKRGK IYDRANSSFL FDLNDQYVLD AYRKGDKLKF ANHSSNPNCY AKVMLVAGDH
RVGIYAKEHI EASEELFYDY RYGPDQAPAW ARRPEGSKKD EASVSHRRAH KVAR
