MTA70_ARATH
ID MTA70_ARATH Reviewed; 685 AA.
AC O82486; Q9M0N2;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=N6-adenosine-methyltransferase MT-A70-like {ECO:0000305};
DE EC=2.1.1.348 {ECO:0000305|PubMed:18505803};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1706 {ECO:0000303|PubMed:15266054};
DE AltName: Full=Protein METTL3 homolog {ECO:0000303|PubMed:28503769};
GN Name=MTA {ECO:0000303|PubMed:28503769};
GN Synonyms=EMB1706 {ECO:0000303|PubMed:15266054};
GN OrderedLocusNames=At4g10760 {ECO:0000312|Araport:AT4G10760};
GN ORFNames=T12H20.6 {ECO:0000312|EMBL:AAC35526.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DISRUPTION PHENOTYPE [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=15266054; DOI=10.1104/pp.104.045179;
RA Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT "Identification of genes required for embryo development in Arabidopsis.";
RL Plant Physiol. 135:1206-1220(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH FIP37, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18505803; DOI=10.1105/tpc.108.058883;
RA Zhong S., Li H., Bodi Z., Button J., Vespa L., Herzog M., Fray R.G.;
RT "MTA is an Arabidopsis messenger RNA adenosine methylase and interacts with
RT a homolog of a sex-specific splicing factor.";
RL Plant Cell 20:1278-1288(2008).
RN [6]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP FUNCTION, AND INTERACTION WITH FIP37 AND MTB.
RX PubMed=28503769; DOI=10.1111/nph.14586;
RA Ruzicka K., Zhang M., Campilho A., Bodi Z., Kashif M., Saleh M.,
RA Eeckhout D., El-Showk S., Li H., Zhong S., De Jaeger G., Mongan N.P.,
RA Hejatko J., Helariutta Y., Fray R.G.;
RT "A mRNA methylation in Arabidopsis reveals a role for the conserved E3
RT ubiquitin ligase HAKAI.";
RL New Phytol. 215:157-172(2017).
CC -!- FUNCTION: Catalytic subunit of the N6-methyltransferase complex, a
CC multiprotein complex that mediates N6-methyladenosine (m6A) methylation
CC at the 5'-[AG]GAC-3' consensus sites of some mRNAs (PubMed:18505803,
CC PubMed:28503769). Associates with MTB, FIP37, VIR and HAKAI to form the
CC m6A writer complex which is essential for adenosine methylation at
CC specific mRNA sequences (PubMed:28503769). N6-methyladenosine (m6A)
CC plays a role in mRNA stability, processing, translation efficiency and
CC editing (PubMed:18505803, PubMed:28503769).
CC {ECO:0000269|PubMed:18505803, ECO:0000269|PubMed:28503769}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(6)-
CC methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55584, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.348;
CC Evidence={ECO:0000305|PubMed:18505803};
CC -!- SUBUNIT: Interacts with FIP37 (PubMed:18505803, PubMed:28503769).
CC Interacts with MTB (PubMed:28503769). Associates with MTB, FIP37, VIR
CC and HAKAI to form the m6A writer complex which is essential for
CC adenosine methylation at specific mRNA sequences (PubMed:28503769).
CC {ECO:0000269|PubMed:18505803, ECO:0000269|PubMed:28503769}.
CC -!- INTERACTION:
CC O82486; Q9ZSZ8: FIP37; NbExp=5; IntAct=EBI-1797380, EBI-1641243;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19245862}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality: arrest at the globular stage
CC of embryo development (PubMed:15266054, PubMed:18505803). Arrested
CC seeds are deficient in mRNAs containing N6-methyladenosine (m6A)
CC (PubMed:18505803). {ECO:0000269|PubMed:15266054,
CC ECO:0000269|PubMed:18505803}.
CC -!- SIMILARITY: Belongs to the MT-A70-like family. {ECO:0000255|PROSITE-
CC ProRule:PRU00489}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC35526.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AK227385; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF080119; AAC35526.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161518; CAB81177.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82925.1; -; Genomic_DNA.
DR EMBL; AK227385; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; E85112; E85112.
DR PIR; T01901; T01901.
DR RefSeq; NP_192814.1; NM_117144.4.
DR AlphaFoldDB; O82486; -.
DR SMR; O82486; -.
DR BioGRID; 11969; 1.
DR IntAct; O82486; 1.
DR STRING; 3702.AT4G10760.1; -.
DR iPTMnet; O82486; -.
DR PaxDb; O82486; -.
DR PRIDE; O82486; -.
DR ProteomicsDB; 238940; -.
DR EnsemblPlants; AT4G10760.1; AT4G10760.1; AT4G10760.
DR GeneID; 826670; -.
DR Gramene; AT4G10760.1; AT4G10760.1; AT4G10760.
DR KEGG; ath:AT4G10760; -.
DR Araport; AT4G10760; -.
DR TAIR; locus:2132731; AT4G10760.
DR eggNOG; KOG2098; Eukaryota.
DR HOGENOM; CLU_018702_3_0_1; -.
DR InParanoid; O82486; -.
DR OMA; PESAQYQ; -.
DR OrthoDB; 349671at2759; -.
DR PhylomeDB; O82486; -.
DR PRO; PR:O82486; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O82486; baseline and differential.
DR Genevisible; O82486; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0001734; F:mRNA (N6-adenosine)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; IMP:TAIR.
DR GO; GO:0001510; P:RNA methylation; ISS:UniProtKB.
DR InterPro; IPR007757; MT-A70-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF05063; MT-A70; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51143; MT_A70; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..685
FT /note="N6-adenosine-methyltransferase MT-A70-like"
FT /id="PRO_0000207632"
FT REGION 552..565
FT /note="Positively charged region required for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q86U44"
FT REGION 657..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 464..465
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86U44"
FT BINDING 482
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86U44"
FT BINDING 599
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86U44"
FT BINDING 622..625
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86U44"
FT BINDING 635..636
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86U44"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
SQ SEQUENCE 685 AA; 76645 MW; 1DBB54FBE7C5034D CRC64;
METESDDATI TVVKDMRVRL ENRIRTQHDA HLDLLSSLQS IVPDIVPSLD LSLKLISSFT
NRPFVATPPL PEPKVEKKHH PIVKLGTQLQ QLHGHDSKSM LVDSNQRDAE ADGSSGSPMA
LVRAMVAECL LQRVPFSPTD SSTVLRKLEN DQNARPAEKA ALRDLGGECG PILAVETALK
SMAEENGSVE LEEFEVSGKP RIMVLAIDRT RLLKELPESF QGNNESNRVV ETPNSIENAT
VSGGGFGVSG SGNFPRPEMW GGDPNMGFRP MMNAPRGMQM MGMHHPMGIM GRPPPFPLPL
PLPVPSNQKL RSEEEDLKDV EALLSKKSFK EKQQSRTGEE LLDLIHRPTA KEAATAAKFK
SKGGSQVKYY CRYLTKEDCR LQSGSHIACN KRHFRRLIAS HTDVSLGDCS FLDTCRHMKT
CKYVHYELDM ADAMMAGPDK ALKPLRADYC SEAELGEAQW INCDIRSFRM DILGTFGVVM
ADPPWDIHME LPYGTMADDE MRTLNVPSLQ TDGLIFLWVT GRAMELGREC LELWGYKRVE
EIIWVKTNQL QRIIRTGRTG HWLNHSKEHC LVGIKGNPEV NRNIDTDVIV AEVRETSRKP
DEMYAMLERI MPRARKLELF ARMHNAHAGW LSLGNQLNGV RLINEGLRAR FKASYPEIDV
QPPSPPRASA METDNEPMAI DSITA
