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Database: UniProt
Entry: O65312
LinkDB: O65312
Original site: O65312 
ID   MEDEA_ARATH             Reviewed;         689 AA.
AC   O65312;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JAN-2019, entry version 151.
DE   RecName: Full=Histone-lysine N-methyltransferase MEDEA;
DE            EC=2.1.1.43;
DE   AltName: Full=Maternal embryogenesis control protein;
DE   AltName: Full=Protein EMBRYO DEFECTIVE 173;
DE   AltName: Full=Protein FERTILIZATION-INDEPENDENT SEED 1;
DE   AltName: Full=Protein SET DOMAIN GROUP 5;
GN   Name=MEA; Synonyms=EMB173, FIS1, MEDEA, SDG5, SET5;
GN   OrderedLocusNames=At1g02580; ORFNames=T14P4.11;
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 bud;
RX   PubMed=9545225; DOI=10.1126/science.280.5362.446;
RA   Grossniklaus U., Vielle-Calzada J.-P., Hoeppner M.A., Gagliano W.B.;
RT   "Maternal control of embryogenesis by MEDEA, a polycomb group gene in
RT   Arabidopsis.";
RL   Science 280:446-450(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta; TISSUE=Silique;
RX   PubMed=9874812; DOI=10.1073/pnas.96.1.296;
RA   Luo M., Bilodeau P., Koltunow A., Dennis E.S., Peacock W.J.,
RA   Chaudhury A.;
RT   "Genes controlling fertilization-independent seed development in
RT   Arabidopsis thaliana.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:296-301(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [4]
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   [5]
RP   IMPRINTING.
RX   PubMed=10580004; DOI=10.1101/gad.13.22.2971;
RA   Vielle-Calzada J.-P., Thomas J., Spillane C., Coluccio A.,
RA   Hoeppner M.A., Grossniklaus U.;
RT   "Maintenance of genomic imprinting at the Arabidopsis medea locus
RT   requires zygotic DDM1 activity.";
RL   Genes Dev. 13:2971-2982(1999).
RN   [6]
RP   FUNCTION.
RX   PubMed=10097185; DOI=10.1073/pnas.96.7.4186;
RA   Kiyosue T., Ohad N., Yadegari R., Hannon M., Dinneny J., Wells D.,
RA   Katz A., Margossian L., Harada J.J., Goldberg R.B., Fischer R.L.;
RT   "Control of fertilization-independent endosperm development by the
RT   MEDEA polycomb gene in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:4186-4191(1999).
RN   [7]
RP   INTERACTION WITH FIE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11114524; DOI=10.1016/S0960-9822(00)00839-3;
RA   Spillane C., MacDougall C., Stock C., Koehler C.,
RA   Vielle-Calzada J.-P., Nunes S.M., Grossniklaus U., Goodrich J.;
RT   "Interaction of the Arabidopsis polycomb group proteins FIE and MEA
RT   mediates their common phenotypes.";
RL   Curr. Biol. 10:1535-1538(2000).
RN   [8]
RP   INTERACTION WITH FIE, AND TISSUE SPECIFICITY.
RX   PubMed=10962025; DOI=10.1073/pnas.170292997;
RA   Luo M., Bilodeau P., Dennis E.S., Peacock W.J., Chaudhury A.;
RT   "Expression and parent-of-origin effects for FIS2, MEA, and FIE in the
RT   endosperm and embryo of developing Arabidopsis seeds.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10637-10642(2000).
RN   [9]
RP   INTERACTION WITH FIE.
RX   PubMed=11148284; DOI=10.1105/tpc.12.12.2367;
RA   Yadegari R., Kinoshita T., Lotan O., Cohen G., Katz A., Choi Y.,
RA   Katz A., Nakashima K., Harada J.J., Goldberg R.B., Fischer R.L.,
RA   Ohad N.;
RT   "Mutations in the FIE and MEA genes that encode interacting polycomb
RT   proteins cause parent-of-origin effects on seed development by
RT   distinct mechanisms.";
RL   Plant Cell 12:2367-2382(2000).
RN   [10]
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   [11]
RP   INDUCTION.
RX   PubMed=14667411; DOI=10.1016/S1534-5807(03)00361-7;
RA   Xiao W., Gehring M., Choi Y., Margossian L., Pu H., Harada J.J.,
RA   Goldberg R.B., Pennell R.I., Fischer R.L.;
RT   "Imprinting of the MEA Polycomb gene is controlled by antagonism
RT   between MET1 methyltransferase and DME glycosylase.";
RL   Dev. Cell 5:891-901(2003).
RN   [12]
RP   FUNCTION.
RX   PubMed=12815071; DOI=10.1101/gad.257403;
RA   Koehler C., Hennig L., Spillane C., Pien S., Gruissem W.,
RA   Grossniklaus U.;
RT   "The Polycomb-group protein MEDEA regulates seed development by
RT   controlling expression of the MADS-box gene PHERES1.";
RL   Genes Dev. 17:1540-1553(2003).
RN   [13]
RP   FUNCTION.
RX   PubMed=15151989; DOI=10.1242/dev.01168;
RA   Guitton A.-E., Page D.R., Chambrier P., Lionnet C., Faure J.-E.,
RA   Grossniklaus U., Berger F.;
RT   "Identification of new members of fertilisation independent seed
RT   Polycomb group pathway involved in the control of seed development in
RT   Arabidopsis thaliana.";
RL   Development 131:2971-2981(2004).
RN   [14]
RP   REGULATION OF IMPRINTING BY DME.
RX   PubMed=15128940; DOI=10.1073/pnas.0402328101;
RA   Choi Y., Harada J.J., Goldberg R.B., Fischer R.L.;
RT   "An invariant aspartic acid in the DNA glycosylase domain of DEMETER
RT   is necessary for transcriptional activation of the imprinted MEDEA
RT   gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7481-7486(2004).
RN   [15]
RP   REVIEW.
RX   PubMed=15653395; DOI=10.1016/j.pbi.2004.11.011;
RA   Autran D., Huanca-Mamani W., Vielle-Calzada J.-P.;
RT   "Genomic imprinting in plants: the epigenetic version of an Oedipus
RT   complex.";
RL   Curr. Opin. Plant Biol. 8:19-25(2005).
RN   [16]
RP   FUNCTION.
RX   PubMed=15619622; DOI=10.1038/ng1495;
RA   Koehler C., Page D.R., Gagliardini V., Grossniklaus U.;
RT   "The Arabidopsis thaliana MEDEA Polycomb group protein controls
RT   expression of PHERES1 by parental imprinting.";
RL   Nat. Genet. 37:28-30(2005).
RN   [17]
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
RT   seed development.";
RL   Dev. Biol. 379:28-37(2013).
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 prevent the proliferation of the central cell
CC       of the female gametophyte by repressing target genes before
CC       fertilization. After fertilization, it probably also regulates the
CC       embryo and endosperm proliferation and anteroposterior
CC       organization during seed development. PcG proteins act by forming
CC       multiprotein complexes, which are required to maintain the
CC       transcriptionally repressive state of homeotic genes throughout
CC       development. PcG proteins are not required to initiate repression,
CC       but to maintain it during later stages of development. Interacts
CC       with the promoter and repress the transcription of genes such as
CC       PHE1 and PHE2, that are paternally active and maternally silenced
CC       genes. {ECO:0000269|PubMed:10097185, ECO:0000269|PubMed:11250158,
CC       ECO:0000269|PubMed:12815071, ECO:0000269|PubMed:15151989,
CC       ECO:0000269|PubMed:15619622, ECO:0000269|PubMed:9545225}.
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 directly with FIE via its N-terminal domain.
CC       These two proteins are probably indirectly associated with FIS2.
CC       In plants, PcG complexes are probably composed of a member of the
CC       EZ family (CLF or MEA), FIE, and a member of the VEFS family
CC       (FIS2, VRN2 or EMF2). Interacts with TAF13.
CC       {ECO:0000269|PubMed:10962025, ECO:0000269|PubMed:11114524,
CC       ECO:0000269|PubMed:11148284, ECO:0000269|PubMed:23506837}.
CC   -!- INTERACTION:
CC       Q9LT47:FIE; NbExp=12; IntAct=EBI-632832, EBI-307146;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11114524}.
CC       Note=Excluded from the nucleolus.
CC   -!- TISSUE SPECIFICITY: Expressed in unpollinated siliques that
CC       contain maturing gametophytes. Not expressed at early stages of
CC       floral development during early megagametogenesis.
CC       {ECO:0000269|PubMed:10962025, ECO:0000269|PubMed:11114524,
CC       ECO:0000269|PubMed:9545225}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed in both egg and central cell before fertilization. After
CC       fertilization, it is expressed in the embryo and endosperm, then
CC       decreases during seed maturation.
CC   -!- INDUCTION: Maternal MEA allele is activated by DME but repressed
CC       by MET1 in the central cell of the female gametophyte, the
CC       progenitor of the endosperm. {ECO:0000269|PubMed:14667411}.
CC   -!- MISCELLANEOUS: The MEA locus is imprinted. Maternal inherited gene
CC       is expressed in the ovule (the egg and the central cell), while
CC       the paternal inherited gene is silenced in the pollen. After
CC       fertilization, only the maternal inherited allele is expressed.
CC       The paternal repression is dependent on DDM1 protein, which may
CC       methylate the paternal locus, while the maternal inherited allele
CC       is allowed by the DME protein, which may antagonize or suppress
CC       DDM1 dependent methylation, and activates its transcription.
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; AF060485; AAC39446.1; -; mRNA.
DR   EMBL; AF096094; AAD09103.1; -; Genomic_DNA.
DR   EMBL; AC022521; AAG10636.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27447.1; -; Genomic_DNA.
DR   PIR; T52060; T52060.
DR   RefSeq; NP_563658.1; NM_100139.4.
DR   UniGene; At.10786; -.
DR   ProteinModelPortal; O65312; -.
DR   SMR; O65312; -.
DR   BioGrid; 24657; 5.
DR   IntAct; O65312; 4.
DR   STRING; 3702.AT1G02580.1; -.
DR   PaxDb; O65312; -.
DR   PRIDE; O65312; -.
DR   EnsemblPlants; AT1G02580.1; AT1G02580.1; AT1G02580.
DR   GeneID; 839422; -.
DR   Gramene; AT1G02580.1; AT1G02580.1; AT1G02580.
DR   KEGG; ath:AT1G02580; -.
DR   Araport; AT1G02580; -.
DR   TAIR; locus:2196110; AT1G02580.
DR   eggNOG; KOG1079; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000083511; -.
DR   KO; K11430; -.
DR   OMA; HFNENDD; -.
DR   OrthoDB; 875190at2759; -.
DR   PhylomeDB; O65312; -.
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:O65312; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O65312; baseline and differential.
DR   Genevisible; O65312; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0031519; C:PcG protein complex; IEA:InterPro.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:TAIR.
DR   GO; GO:2000014; P:regulation of endosperm development; IMP:TAIR.
DR   GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IMP:TAIR.
DR   GO; GO:0009646; P:response to absence of light; IEP:TAIR.
DR   GO; GO:0048317; P:seed morphogenesis; IGI: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; 2.
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   Complete proteome; Developmental protein; Methyltransferase; Nucleus;
KW   Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    689       Histone-lysine N-methyltransferase MEDEA.
FT                                /FTId=PRO_0000213997.
FT   DOMAIN      339    389       SANT.
FT   DOMAIN      428    532       CXC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00970}.
FT   DOMAIN      544    659       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION        1    109       Interaction with FIE.
FT   COMPBIAS    450    519       Cys-rich.
SQ   SEQUENCE   689 AA;  79310 MW;  2103D06ACD589CDF CRC64;
     MEKENHEDDG EGLPPELNQI KEQIEKERFL HIKRKFELRY IPSVATHASH HQSFDLNQPA
     AEDDNGGDNK SLLSRMQNPL RHFSASSDYN SYEDQGYVLD EDQDYALEED VPLFLDEDVP
     LLPSVKLPIV EKLPRSITWV FTKSSQLMAE SDSVIGKRQI YYLNGEALEL SSEEDEEDEE
     EDEEEIKKEK CEFSEDVDRF IWTVGQDYGL DDLVVRRALA KYLEVDVSDI LERYNELKLK
     NDGTAGEASD LTSKTITTAF QDFADRRHCR RCMIFDCHMH EKYEPESRSS EDKSSLFEDE
     DRQPCSEHCY LKVRSVTEAD HVMDNDNSIS NKIVVSDPNN TMWTPVEKDL YLKGIEIFGR
     NSCDVALNIL RGLKTCLEIY NYMREQDQCT MSLDLNKTTQ RHNQVTKKVS RKSSRSVRKK
     SRLRKYARYP PALKKTTSGE AKFYKHYTPC TCKSKCGQQC PCLTHENCCE KYCGCSKDCN
     NRFGGCNCAI GQCTNRQCPC FAANRECDPD LCRSCPLSCG DGTLGETPVQ IQCKNMQFLL
     QTNKKILIGK SDVHGWGAFT WDSLKKNEYL GEYTGELITH DEANERGRIE DRIGSSYLFT
     LNDQLEIDAR RKGNEFKFLN HSARPNCYAK LMIVRGDQRI GLFAERAIEE GEELFFDYCY
     GPEHADWSRG REPRKTGASK RSKEARPAR
//
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