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 30-NOV-2016, entry version 137.
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;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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: S-adenosyl-L-methionine + L-lysine-[histone] =
CC S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC {ECO:0000255|PROSITE-ProRule:PRU00909}.
CC -!- SUBUNIT: Interacts directly with FIE via its N-terminal domain.
CC These two proteins are probably inderectly 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}.
CC -!- SIMILARITY: Contains 1 CXC domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00970}.
CC -!- SIMILARITY: Contains 1 SANT domain. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 SET domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00190}.
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 EnsemblPlants; AT1G02580.1; AT1G02580.1; AT1G02580.
DR GeneID; 839422; -.
DR Gramene; AT1G02580.1; AT1G02580.1; AT1G02580.
DR KEGG; ath:AT1G02580; -.
DR TAIR; AT1G02580; -.
DR eggNOG; KOG1079; Eukaryota.
DR eggNOG; COG2940; LUCA.
DR HOGENOM; HOG000083511; -.
DR KO; K11430; -.
DR OMA; NCYAKLM; -.
DR OrthoDB; EOG09360260; -.
DR PhylomeDB; O65312; -.
DR PRO; PR:O65312; -.
DR Proteomes; UP000006548; Chromosome 1.
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:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS: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 GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR InterPro; IPR026489; CXC_dom.
DR InterPro; IPR025778; Hist-Lys_N-MeTrfase_EZ.
DR InterPro; IPR033498; MEDEA.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR PANTHER; PTHR22884:SF326; PTHR22884:SF326; 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 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.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 544 665 ismart:SET [T]
FT MYHIT 481 519 ismart:CXC [T]
FT MYHIT 428 532 iprf:CXC [T]
FT MYHIT 1 689 iprf:SAM_MT43_EZ [T]
FT MYHIT 544 659 iprf:SET [T]
FT MYHIT 555 658 ipfam:SET [T]
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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