MEDEA_ARATH
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 03-AUG-2022, entry version 165.
DE RecName: Full=Histone-lysine N-methyltransferase MEDEA;
DE EC=2.1.1.356;
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., 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., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis 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 reference
RT 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., Hoeppner M.A.,
RA Grossniklaus U.;
RT "Maintenance of genomic imprinting at the Arabidopsis medea locus requires
RT 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., Katz A.,
RA Margossian L., Harada J.J., Goldberg R.B., Fischer R.L.;
RT "Control of fertilization-independent endosperm development by the MEDEA
RT 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., Vielle-Calzada J.-P.,
RA 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=10.2307/3871235;
RA Yadegari R., Kinoshita T., Lotan O., Cohen G., Katz A., Choi Y., Katz A.,
RA Nakashima K., Harada J.J., Goldberg R.B., Fischer R.L., 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 distinct
RT 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 between
RT 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., Grossniklaus U.;
RT "The Polycomb-group protein MEDEA regulates seed development by controlling
RT 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 Polycomb
RT group pathway involved in the control of seed development in Arabidopsis
RT 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 is
RT necessary for transcriptional activation of the imprinted MEDEA 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 expression
RT 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 seed
RT development.";
RL Dev. Biol. 379:28-37(2013).
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. Required to
CC prevent the proliferation of the central cell of the female gametophyte
CC by repressing target genes before fertilization. After fertilization,
CC it probably also regulates the embryo and endosperm proliferation and
CC anteroposterior organization during seed development. PcG proteins act
CC by forming 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, but
CC to maintain it during later stages of development. Interacts with the
CC promoter and repress the transcription of genes such as PHE1 and PHE2,
CC that are paternally active and maternally silenced genes.
CC {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(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 directly with FIE via its N-terminal domain. These
CC two proteins are probably indirectly associated with FIS2. In plants,
CC PcG 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 Interacts with TAF13. {ECO:0000269|PubMed:10962025,
CC ECO:0000269|PubMed:11114524, ECO:0000269|PubMed:11148284,
CC ECO:0000269|PubMed:23506837}.
CC -!- INTERACTION:
CC O65312; 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 contain
CC maturing gametophytes. Not expressed at early stages of floral
CC 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 by
CC MET1 in the central cell of the female gametophyte, the progenitor of
CC the endosperm. {ECO:0000269|PubMed:14667411}.
CC -!- MISCELLANEOUS: The MEA locus is imprinted. Maternal inherited gene is
CC expressed in the ovule (the egg and the central cell), while the
CC paternal inherited gene is silenced in the pollen. After fertilization,
CC only the maternal inherited allele is expressed. The paternal
CC repression is dependent on DDM1 protein, which may methylate the
CC paternal locus, while the maternal inherited allele is allowed by the
CC DME protein, which may antagonize or suppress DDM1 dependent
CC methylation, and activates its transcription.
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; 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 AlphaFoldDB; 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 HOGENOM; CLU_011060_0_0_1; -.
DR OMA; HFNENDD; -.
DR OrthoDB; 875190at2759; -.
DR PhylomeDB; O65312; -.
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:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
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 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 genomic 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 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 Developmental protein; Methyltransferase; Nucleus; Reference proteome;
KW Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..689
FT /note="Histone-lysine N-methyltransferase MEDEA"
FT /id="PRO_0000213997"
FT DOMAIN 339..389
FT /note="SANT"
FT DOMAIN 428..532
FT /note="CXC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00970"
FT DOMAIN 544..659
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..109
FT /note="Interaction with FIE"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
