GenomeNet

Database: UniProt
Entry: P93831
LinkDB: P93831
Original site: P93831 
ID   CLF_ARATH               Reviewed;         902 AA.
AC   P93831; O80455;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   13-FEB-2019, entry version 153.
DE   RecName: Full=Histone-lysine N-methyltransferase CLF;
DE            EC=2.1.1.43;
DE   AltName: Full=Polycomb group protein CURLY LEAF;
DE   AltName: Full=Protein INCURVATA 1;
DE   AltName: Full=Protein SET DOMAIN GROUP 1;
DE   AltName: Full=Protein photoperiod insensitive flowering;
GN   Name=CLF; Synonyms=ICU1, PIF1, PIF2, SDG1, SET1;
GN   OrderedLocusNames=At2g23380; ORFNames=F26B6.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta; TISSUE=Flower;
RX   PubMed=9052779; DOI=10.1038/386044a0;
RA   Goodrich J., Puangsomlee P., Martin M., Long D., Meyerowitz E.M.,
RA   Coupland G.;
RT   "A Polycomb-group gene regulates homeotic gene expression in
RT   Arabidopsis.";
RL   Nature 386:44-51(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION.
RX   PubMed=9736998; DOI=10.1007/s004250050389;
RA   Kim G.-T., Tsukaya H., Uchimiya H.;
RT   "The CURLY LEAF gene controls both division and elongation of cells
RT   during the expansion of the leaf blade in Arabidopsis thaliana.";
RL   Planta 206:175-183(1998).
RN   [5]
RP   FUNCTION.
RX   PubMed=11063708;
RA   Serrano-Cartagena J., Candela H., Robles P., Ponce M.R.,
RA   Perez-Perez J.M., Piqueras P., Micol J.L.;
RT   "Genetic analysis of incurvata mutants reveals three independent
RT   genetic operations at work in Arabidopsis leaf morphogenesis.";
RL   Genetics 156:1363-1377(2000).
RN   [6]
RP   FUNCTION.
RX   PubMed=11250158; DOI=10.1016/S0960-9822(01)00072-0;
RA   Soerensen M.B., Chaudhury A.M., Robert H., Bancharel E., Berger F.;
RT   "Polycomb group genes control pattern formation in plant seed.";
RL   Curr. Biol. 11:277-281(2001).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11691919; DOI=10.1093/nar/29.21.4319;
RA   Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
RA   Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
RT   "The Arabidopsis thaliana genome contains at least 29 active genes
RT   encoding SET domain proteins that can be assigned to four
RT   evolutionarily conserved classes.";
RL   Nucleic Acids Res. 29:4319-4333(2001).
RN   [8]
RP   INTERACTION WITH FIE.
RX   PubMed=14871310; DOI=10.1111/j.1365-313X.2003.01996.x;
RA   Katz A., Oliva M., Mosquna A., Hakim O., Ohad N.;
RT   "FIE and CURLY LEAF polycomb proteins interact in the regulation of
RT   homeobox gene expression during sporophyte development.";
RL   Plant J. 37:707-719(2004).
RN   [9]
RP   INTERACTION WITH RING1A.
RX   PubMed=19097900; DOI=10.1016/j.cub.2008.11.019;
RA   Xu L., Shen W.H.;
RT   "Polycomb silencing of KNOX genes confines shoot stem cell niches in
RT   Arabidopsis.";
RL   Curr. Biol. 18:1966-1971(2008).
RN   [10]
RP   INTERACTION WITH BLI.
RX   PubMed=20647345; DOI=10.1105/tpc.109.073403;
RA   Schatlowski N., Stahl Y., Hohenstatt M.L., Goodrich J., Schubert D.;
RT   "The CURLY LEAF interacting protein BLISTER controls expression of
RT   polycomb-group target genes and cellular differentiation of
RT   Arabidopsis thaliana.";
RL   Plant Cell 22:2291-2305(2010).
RN   [11]
RP   INTERACTION WITH ALP1.
RX   PubMed=26642436; DOI=10.1371/journal.pgen.1005660;
RA   Liang S.C., Hartwig B., Perera P., Mora-Garcia S., de Leau E.,
RA   Thornton H., de Lima Alves F., de Alves F.L., Rappsilber J.,
RA   Rapsilber J., Yang S., James G.V., Schneeberger K., Finnegan E.J.,
RA   Turck F., Goodrich J.;
RT   "Kicking against the PRCs - A domesticated transposase antagonises
RT   silencing mediated by polycomb group proteins and is an accessory
RT   component of polycomb repressive complex 2.";
RL   PLoS Genet. 11:E1005660-E1005660(2015).
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. Required to regulate floral development by repressing the
CC       AGAMOUS homeotic gene in leaves, influorescence stems and flowers.
CC       Regulates the antero-posterior organization of the endosperm, as
CC       well as the division and elongation rates of leaf cells. PcG
CC       proteins act by forming multiprotein complexes, which are required
CC       to maintain the transcriptionally repressive state of homeotic
CC       genes throughout development. PcG proteins are not required to
CC       initiate repression, but to maintain it during later stages of
CC       development. {ECO:0000269|PubMed:11063708,
CC       ECO:0000269|PubMed:11250158, ECO:0000269|PubMed:9052779,
CC       ECO:0000269|PubMed:9736998}.
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: Probable component of a PcG complex. In plants, PcG
CC       complexes are probably composed of a member of the EZ family (CLF
CC       or MEA), FIE, and a member of the VEFS family (FIS2, VRN2 or EMF2)
CC       (By similarity). Interacts with FIE (PubMed:14871310). Interacts
CC       with RING1A (PubMed:19097900). Binds to ALP1 (PubMed:26642436).
CC       Interacts with BLI (PubMed:20647345). {ECO:0000250,
CC       ECO:0000269|PubMed:14871310, ECO:0000269|PubMed:19097900,
CC       ECO:0000269|PubMed:20647345, ECO:0000269|PubMed:26642436}.
CC   -!- INTERACTION:
CC       Q9SHY1:At1g65740; NbExp=2; IntAct=EBI-307155, EBI-15923123;
CC       Q8L6Y4:EMF2; NbExp=4; IntAct=EBI-307155, EBI-2128696;
CC       Q9LT47:FIE; NbExp=4; IntAct=EBI-307155, EBI-307146;
CC       O22607:MSI4; NbExp=3; IntAct=EBI-307155, EBI-9661079;
CC       Q8W5B1:VRN2; NbExp=3; IntAct=EBI-307155, EBI-2128880;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11691919}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed throughout the apical
CC       meristem, leaf primordia, and leaves of 7-8 day-old seedling.
CC       Weakly expressed in the vasculature of hypocotyl. Strongly
CC       expressed throughout the young stages 1 and 2 floral meristems
CC       that arose on the flanks of the apex. In stage 3 and 4 flowers, it
CC       is expressed in the emerging sepal primordia and in the dome of
CC       the floral meristem. During stages 6 and 7, it is strongly
CC       expressed in developing petal and stamen, and weakly expressed in
CC       the sepals. Late in floral development, at stage 12, it is weakly
CC       expressed in all floral whorls, and expressed at intermediate
CC       level in petals and ovules. {ECO:0000269|PubMed:9052779}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in all four whorls throughout
CC       flower development.
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; Y10580; CAA71599.1; -; mRNA.
DR   EMBL; AC003040; AAC23781.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07449.1; -; Genomic_DNA.
DR   PIR; T01127; T01127.
DR   RefSeq; NP_179919.1; NM_127902.6.
DR   UniGene; At.22; -.
DR   ProteinModelPortal; P93831; -.
DR   BioGrid; 2222; 17.
DR   DIP; DIP-31377N; -.
DR   IntAct; P93831; 14.
DR   STRING; 3702.AT2G23380.1; -.
DR   iPTMnet; P93831; -.
DR   PaxDb; P93831; -.
DR   PRIDE; P93831; -.
DR   EnsemblPlants; AT2G23380.1; AT2G23380.1; AT2G23380.
DR   GeneID; 816870; -.
DR   Gramene; AT2G23380.1; AT2G23380.1; AT2G23380.
DR   KEGG; ath:AT2G23380; -.
DR   Araport; AT2G23380; -.
DR   TAIR; locus:2005501; AT2G23380.
DR   eggNOG; KOG1079; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000083511; -.
DR   InParanoid; P93831; -.
DR   KO; K11430; -.
DR   OMA; CAVNSRE; -.
DR   OrthoDB; 875190at2759; -.
DR   PhylomeDB; P93831; -.
DR   Reactome; R-ATH-212300; PRC2 methylates histones and DNA.
DR   Reactome; R-ATH-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-ATH-8953750; Transcriptional Regulation by E2F6.
DR   PRO; PR:P93831; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P93831; baseline and differential.
DR   Genevisible; P93831; AT.
DR   GO; GO:0005677; C:chromatin silencing complex; IEA:EnsemblPlants.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0031519; C:PcG protein complex; IEA:EnsemblPlants.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:TAIR.
DR   GO; GO:0003727; F:single-stranded RNA binding; IDA:TAIR.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006342; P:chromatin silencing; IEA:EnsemblPlants.
DR   GO; GO:0009294; P:DNA mediated transformation; IMP:TAIR.
DR   GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR   GO; GO:0070734; P:histone H3-K27 methylation; IEA:EnsemblPlants.
DR   GO; GO:0016571; P:histone methylation; IMP:TAIR.
DR   GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR   GO; GO:0045857; P:negative regulation of molecular function, epigenetic; IMP:TAIR.
DR   GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IMP:TAIR.
DR   GO; GO:0048586; P:regulation of long-day photoperiodism, flowering; IEA:EnsemblPlants.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR   InterPro; IPR026489; CXC_dom.
DR   InterPro; IPR025778; Hist-Lys_N-MeTrfase_EZ.
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; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    902       Histone-lysine N-methyltransferase CLF.
FT                                /FTId=PRO_0000213995.
FT   DOMAIN      531    581       SANT.
FT   DOMAIN      638    737       CXC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00970}.
FT   DOMAIN      752    867       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   COMPBIAS    649    720       Cys-rich.
FT   CONFLICT    225    225       S -> N (in Ref. 2; CAA71599).
FT                                {ECO:0000305}.
FT   CONFLICT    332    332       T -> P (in Ref. 2; CAA71599).
FT                                {ECO:0000305}.
FT   CONFLICT    415    415       K -> N (in Ref. 2; CAA71599).
FT                                {ECO:0000305}.
FT   CONFLICT    658    658       K -> Q (in Ref. 2; CAA71599).
FT                                {ECO:0000305}.
FT   CONFLICT    674    674       C -> Y (in Ref. 2; CAA71599).
FT                                {ECO:0000305}.
FT   CONFLICT    761    761       V -> I (in Ref. 2; CAA71599).
FT                                {ECO:0000305}.
SQ   SEQUENCE   902 AA;  100370 MW;  90B45ED27D219D64 CRC64;
     MASEASPSSS ATRSEPPKDS PAEERGPASK EVSEVIESLK KKLAADRCIS IKKRIDENKK
     NLFAITQSFM RSSMERGGSC KDGSDLLVKR QRDSPGMKSG IDESNNNRYV EDGPASSGMV
     QGSSVPVKIS LRPIKMPDIK RLSPYTTWVF LDRNQRMTED QSVVGRRRIY YDQTGGEALI
     CSDSEEEAID DEEEKRDFLE PEDYIIRMTL EQLGLSDSVL AELASFLSRS TSEIKARHGV
     LMKEKEVSES GDNQAESSLL NKDMEGALDS FDNLFCRRCL VFDCRLHGCS QDLIFPAEKP
     APWCPPVDEN LTCGANCYKT LLKSGRFPGY GTIEGKTGTS SDGAGTKTTP TKFSSKLNGR
     KPKTFPSESA SSNEKCALET SDSENGLQQD TNSDKVSSSP KVKGSGRRVG RKRNKNRVAE
     RVPRKTQKRQ KKTEASDSDS IASGSCSPSD AKHKDNEDAT SSSQKHVKSG NSGKSRKNGT
     PAEVSNNSVK DDVPVCQSNE VASELDAPGS DESLRKEEFM GETVSRGRLA TNKLWRPLEK
     SLFDKGVEIF GMNSCLIARN LLSGFKSCWE VFQYMTCSEN KASFFGGDGL NPDGSSKFDI
     NGNMVNNQVR RRSRFLRRRG KVRRLKYTWK SAAYHSIRKR ITEKKDQPCR QFNPCNCKIA
     CGKECPCLLN GTCCEKYCGC PKSCKNRFRG CHCAKSQCRS RQCPCFAADR ECDPDVCRNC
     WVIGGDGSLG VPSQRGDNYE CRNMKLLLKQ QQRVLLGISD VSGWGAFLKN SVSKHEYLGE
     YTGELISHKE ADKRGKIYDR ENCSFLFNLN DQFVLDAYRK GDKLKFANHS PEPNCYAKVI
     MVAGDHRVGI FAKERILAGE ELFYDYRYEP DRAPAWAKKP EAPGSKKDEN VTPSVGRPKK
     LA
//
DBGET integrated database retrieval system