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CLF_ORYSJ
ID   CLF_ORYSJ               Reviewed;         896 AA.
AC   Q5VN06;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Histone-lysine N-methyltransferase CLF {ECO:0000305};
DE            Short=OsCLF {ECO:0000303|PubMed:19825651};
DE            EC=2.1.1.356 {ECO:0000255|PROSITE-ProRule:PRU00909};
DE   AltName: Full=Protein SET DOMAIN GROUP 711 {ECO:0000305};
DE   AltName: Full=SET family protein 24 {ECO:0000305};
DE            Short=OsSET24 {ECO:0000303|PubMed:23762371};
GN   Name=CLF {ECO:0000303|PubMed:19825651};
GN   Synonyms=SDG711 {ECO:0000303|PubMed:25400654};
GN   OrderedLocusNames=Os06g0275500 {ECO:0000312|EMBL:BAF19293.1},
GN   LOC_Os06g16390 {ECO:0000305};
GN   ORFNames=P0038C05.29 {ECO:0000312|EMBL:BAD68028.1},
GN   P0676F10.40 {ECO:0000312|EMBL:BAD69169.1};
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 [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   [2]
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   [3]
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   [4]
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   [5]
RP   INTERACTION WITH FIE1.
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
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   [7]
RP   TISSUE SPECIFICITY, 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   [8]
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. Represses
CC       flowering under long day (LD) conditions. Regulates the trimethylation
CC       on histone H3 'Lys-27' (H3K27me3) of the flowering regulators MADS14,
CC       MADS15, RFT1, EHD1, HD3A and LF (PubMed:25400654).
CC       {ECO:0000269|PubMed:25400654, 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). Component of the
CC       polycomb repressive complex 2 (PRC2), composed of the core PRC2
CC       components FIE2, EMF2B and EZ1. PRC2 methylates 'Lys-27' residues of
CC       histone H3 (H3K27me3), leading to transcriptional repression of the
CC       affected target gene (PubMed:23505380). {ECO:0000269|PubMed:23150632,
CC       ECO:0000269|PubMed:23505380}.
CC   -!- TISSUE SPECIFICITY: Widely expressed (PubMed:19825651). Highly
CC       expressed in young panicle (PubMed:23762371).
CC       {ECO:0000269|PubMed:19825651, ECO:0000269|PubMed:23762371}.
CC   -!- MISCELLANEOUS: Over-expression and down-regulation of CLF respectively,
CC       represses and promotes flowering in long day (LD), but has no effect in
CC       short day (SD). {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}.
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DR   EMBL; AP003044; BAD68028.1; -; Genomic_DNA.
DR   EMBL; AP005813; BAD69169.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF19293.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS97226.1; -; Genomic_DNA.
DR   RefSeq; XP_015644234.1; XM_015788748.1.
DR   AlphaFoldDB; Q5VN06; -.
DR   SMR; Q5VN06; -.
DR   STRING; 4530.OS06T0275500-01; -.
DR   PaxDb; Q5VN06; -.
DR   PRIDE; Q5VN06; -.
DR   EnsemblPlants; Os06t0275500-01; Os06t0275500-01; Os06g0275500.
DR   GeneID; 4340748; -.
DR   Gramene; Os06t0275500-01; Os06t0275500-01; Os06g0275500.
DR   KEGG; osa:4340748; -.
DR   eggNOG; KOG1079; Eukaryota.
DR   HOGENOM; CLU_011060_0_0_1; -.
DR   InParanoid; Q5VN06; -.
DR   OMA; DESICRQ; -.
DR   OrthoDB; 875190at2759; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
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:0009294; P:DNA-mediated transformation; IEA:EnsemblPlants.
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:0009965; P:leaf morphogenesis; IEA:EnsemblPlants.
DR   GO; GO:0009909; P:regulation of flower development; IEA:EnsemblPlants.
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:0048586; P:regulation of long-day photoperiodism, flowering; IMP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:EnsemblPlants.
DR   GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IEA:EnsemblPlants.
DR   GO; GO:0010048; P:vernalization response; IEA:EnsemblPlants.
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; 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; Reference proteome; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..896
FT                   /note="Histone-lysine N-methyltransferase CLF"
FT                   /id="PRO_0000444465"
FT   DOMAIN          633..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          344..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..896
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..514
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"
SQ   SEQUENCE   896 AA;  100296 MW;  7DCE38E04E7505DF CRC64;
     MAGDSRNEPM FCEEGSSESG YVLCVIDSLK KKITSDRFVY IQKRVEENSI KLSPITLHSH
     NLSKNRQTST SNSTDLVSNL LTKRKEDALC AVNSRESSPD ESEGANCQDE CSSTVIVGGN
     LSARNSVRPI RLPEVATLPP YTTWIFLDRN QRMQEDQSVL GRRRIYYDTN CGEALICSDS
     EDEAVEDEEE KKEFKDSEDC IIRMTIQECG MSDAVLETLA RDIERAPDDI KARYEILQGE
     KPEGSSKKVS ELNVKMEDVY GDKDLDAALD SFDNLFCRRC LVFDCKLHGC SQDLVFPTEK
     QAPLCSSDEG TPCGIHCYKL VSKPDAIMEI DSHLLVDVEE PTSDNLKDQI GSNKKKLGSS
     GQKTKSQQSE SSSTARVSSE SSESEVQLLS NKSPQHSPGL SKNKLGAKGG IKKSTNRRIA
     ERILMSVKKG QQEMSPDSNS IVNGCHWPRD MKLRSDTRSG IKDSVVSSQC NSPSTRSFRK
     KGTLQMENNS SFVDAQSDSM EDTNNEHSAT DGCDSSRKEE CVDESICRQE AHGRSWKVIE
     QGLLLKGLEI FGKNSCLIAR NLLGGMKTCT DVFQYMNYIE NSSASGALSG VDSLVKGYMK
     GNELRTRSRF VRRRGRVRRL KYTWKTAGYH FIRKRITERK DQPCRQYTPC GCQSACGKQC
     PCLTNGTCCE KYCGCPKMCK NRFRGCHCAK SQCRSRQCPC FAADRECDPD VCRNCWVGCG
     DGTLGVPNQR GDNYECRNMK LLLKQQQRVL LGRSDVSGWG AFLKNSVGKH EYLGEYTGEL
     ISHKEADKRG KIYDRENSSF LFNLNNEYVL DAYRMGDKLK FANHSPDPNC YAKVIMVAGD
     HRVGIFAKER ISAGEELFYD YRYEPDRAPA WARKPEGPGA KDDAQPSTGR AKKLAH
 
 
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