Reviewed, UniProtKB/Swiss-Prot O82486 (MTA70_ARATH)

Names and origin

Protein names

Recommended name:
    N6-adenosine-methyltransferase MT-A70-like
    EC=2.1.1.62
Alternative name(s):
    Protein EMBRYO DEFECTIVE 1706

Gene names

Name:	EMB1706
Ordered Locus Names:	At4g10760
ORF Names:	T12H20.6

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	685 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probable N6-methyltransferase that methylates adenosine residues of some mRNAs. N6-methyladenosine (m6A), which is present at internal sites of some mRNAs, may play a role in the efficiency of mRNA splicing, transport or translation By similarity.
Catalytic activity	S-adenosyl-L-methionine + m7G(5')pppAm = S-adenosyl-L-homocysteine + m7G(5')pppm6Am.
Subcellular location	Nucleus Ref.3.
Sequence similarities	Belongs to the MT-A70-like family.
Sequence caution	The sequence AAC35526.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AK227385 differs from that shown. Reason: Frameshift at position 206.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	RNA-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	mRNA methylation Inferred from mutant phenotype. Source: TAIR
Cellular component	chloroplast Inferred from direct assay. Source: TAIR nuclear speck Inferred from direct assay. Source: TAIR
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FIP37	Q9ZSZ8	3	EBI-1797380,EBI-1641243

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 685	685	N6-adenosine-methyltransferase MT-A70-like		PRO_0000207632
Regions
	Compositional bias	259 – 290	32	Met-rich
Amino acid modifications
	Modified residue	664	1	Phosphoserine Ref.3 Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O82486-1 [UniParc]. Last modified August 16, 2005. Version 2. Checksum: 1DBB54FBE7C5034D	FASTA	685	76,645
	10 20 30 40 50 60 METESDDATI TVVKDMRVRL ENRIRTQHDA HLDLLSSLQS IVPDIVPSLD LSLKLISSFT 70 80 90 100 110 120 NRPFVATPPL PEPKVEKKHH PIVKLGTQLQ QLHGHDSKSM LVDSNQRDAE ADGSSGSPMA 130 140 150 160 170 180 LVRAMVAECL LQRVPFSPTD SSTVLRKLEN DQNARPAEKA ALRDLGGECG PILAVETALK 190 200 210 220 230 240 SMAEENGSVE LEEFEVSGKP RIMVLAIDRT RLLKELPESF QGNNESNRVV ETPNSIENAT 250 260 270 280 290 300 VSGGGFGVSG SGNFPRPEMW GGDPNMGFRP MMNAPRGMQM MGMHHPMGIM GRPPPFPLPL 310 320 330 340 350 360 PLPVPSNQKL RSEEEDLKDV EALLSKKSFK EKQQSRTGEE LLDLIHRPTA KEAATAAKFK 370 380 390 400 410 420 SKGGSQVKYY CRYLTKEDCR LQSGSHIACN KRHFRRLIAS HTDVSLGDCS FLDTCRHMKT 430 440 450 460 470 480 CKYVHYELDM ADAMMAGPDK ALKPLRADYC SEAELGEAQW INCDIRSFRM DILGTFGVVM 490 500 510 520 530 540 ADPPWDIHME LPYGTMADDE MRTLNVPSLQ TDGLIFLWVT GRAMELGREC LELWGYKRVE 550 560 570 580 590 600 EIIWVKTNQL QRIIRTGRTG HWLNHSKEHC LVGIKGNPEV NRNIDTDVIV AEVRETSRKP 610 620 630 640 650 660 DEMYAMLERI MPRARKLELF ARMHNAHAGW LSLGNQLNGV RLINEGLRAR FKASYPEIDV 670 680 QPPSPPRASA METDNEPMAI DSITA

References

[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana." Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C. J. Proteomics 72:439-451(2009) [PubMed: 19245862] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[4]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, MASS SPECTROMETRY. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF080119 Genomic DNA. Translation: AAC35526.1. Sequence problems. AL161518 Genomic DNA. Translation: CAB81177.1. AK227385 mRNA. No translation available.
IPI	IPI00534419.
PIR	E85112. T01901.
RefSeq	NP_192814.1.
UniGene	At.20163 At.63691
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O82486. 1 interaction.
STRING	O82486.
Proteomic databases
PRIDE	O82486.
Genome annotation databases
GeneID	826670.
GenomeReviews	Gene locus AT4G10760 in contig CT486007_GR.
KEGG	ath:AT4G10760.
NMPDR	fig|3702.1.peg.18737.
Organism-specific databases
GeneFarm	4529. 449.
TAIR	At4g10760.
Phylogenomic databases
eggNOG	KOG2098.
HOGENOM	HBG318286.
InParanoid	O82486.
OMA	MADDEMR.
PhylomeDB	O82486.
Enzyme and pathway databases
BRENDA	2.1.1.62. 302.
Gene expression databases
Genevestigator	O82486.
GermOnline	AT4G10760. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR007757. MT-A70. [Graphical view]
Pfam	PF05063. MT-A70. 1 hit. [Graphical view]
PROSITE	PS51143. MT_A70. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MTA70_ARATH

Accession

Primary (citable) accession number: O82486
Secondary accession number(s): Q9M0N2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2003
Last sequence update:	August 16, 2005
Last modified:	February 9, 2010
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)