METL1_ARATH
ID METL1_ARATH Reviewed; 775 AA.
AC Q94AI4; F4JKV6; Q9T0F6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=N6-adenosine-methyltransferase non-catalytic subunit MTB {ECO:0000305};
DE AltName: Full=Methyltransferase-like protein 1 {ECO:0000305};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1691 {ECO:0000303|PubMed:15266054};
DE AltName: Full=Protein METTL14 homolog {ECO:0000303|PubMed:28503769};
GN Name=MTB {ECO:0000303|PubMed:28503769};
GN Synonyms=EMB1691 {ECO:0000303|PubMed:15266054};
GN OrderedLocusNames=At4g09980 {ECO:0000312|Araport:AT4G09980};
GN ORFNames=T5L19.110 {ECO:0000312|EMBL:CAB39622.1};
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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, IDENTIFICATION BY MASS SPECTROMETRY, HOMODIMERIZATION,
RP INTERACTION WITH HAKAI; MTA AND VIR, AND SUBCELLULAR LOCATION.
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: Probable non-catalytic subunit of the N6-methyltransferase
CC complex, a multiprotein complex that mediates N6-methyladenosine (m6A)
CC methylation at the 5'-[AG]GAC-3' consensus sites of some mRNAs
CC (PubMed:28503769). Associates with MTA, FIP37, VIR and HAKAI to form
CC the 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:28503769). {ECO:0000269|PubMed:28503769}.
CC -!- SUBUNIT: Forms homodimers (PubMed:28503769). Interacts with HAKAI, MTA
CC and VIR (PubMed:28503769). Associates with MTA, FIP37, VIR and HAKAI to
CC form the m6A writer complex which is essential for adenosine
CC methylation at specific mRNA sequences (PubMed:28503769).
CC {ECO:0000269|PubMed:28503769}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:28503769}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:28503769}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94AI4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94AI4-2; Sequence=VSP_059895;
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality: arrest at the globular stage
CC of embryo development. {ECO:0000269|PubMed:15266054}.
CC -!- SIMILARITY: Belongs to the MT-A70-like family. {ECO:0000255|PROSITE-
CC ProRule:PRU00489}.
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DR EMBL; AL049481; CAB39622.1; -; Genomic_DNA.
DR EMBL; AL161516; CAB78121.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82823.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82824.1; -; Genomic_DNA.
DR EMBL; AY046016; AAK76690.1; -; mRNA.
DR EMBL; BT000992; AAN41392.1; -; mRNA.
DR PIR; T04002; T04002.
DR RefSeq; NP_001078365.1; NM_001084896.2. [Q94AI4-1]
DR RefSeq; NP_567348.2; NM_117066.4. [Q94AI4-2]
DR AlphaFoldDB; Q94AI4; -.
DR SMR; Q94AI4; -.
DR BioGRID; 11888; 1.
DR IntAct; Q94AI4; 1.
DR STRING; 3702.AT4G09980.1; -.
DR iPTMnet; Q94AI4; -.
DR PaxDb; Q94AI4; -.
DR PRIDE; Q94AI4; -.
DR ProteomicsDB; 232275; -. [Q94AI4-1]
DR EnsemblPlants; AT4G09980.1; AT4G09980.1; AT4G09980. [Q94AI4-2]
DR EnsemblPlants; AT4G09980.2; AT4G09980.2; AT4G09980. [Q94AI4-1]
DR GeneID; 826589; -.
DR Gramene; AT4G09980.1; AT4G09980.1; AT4G09980. [Q94AI4-2]
DR Gramene; AT4G09980.2; AT4G09980.2; AT4G09980. [Q94AI4-1]
DR KEGG; ath:AT4G09980; -.
DR Araport; AT4G09980; -.
DR TAIR; locus:2140503; AT4G09980.
DR eggNOG; KOG2097; Eukaryota.
DR HOGENOM; CLU_006673_0_0_1; -.
DR InParanoid; Q94AI4; -.
DR OMA; WAYMQEN; -.
DR OrthoDB; 349671at2759; -.
DR PhylomeDB; Q94AI4; -.
DR PRO; PR:Q94AI4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94AI4; baseline and differential.
DR Genevisible; Q94AI4; AT.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; IMP:UniProtKB.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR045123; METTL14-like.
DR InterPro; IPR007757; MT-A70-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13107; PTHR13107; 1.
DR Pfam; PF05063; MT-A70; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51143; MT_A70; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..775
FT /note="N6-adenosine-methyltransferase non-catalytic subunit
FT MTB"
FT /id="PRO_0000260073"
FT REGION 1..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 775
FT /note="G -> GSTQKPEDMYRIIEHFALGRRRLELFGEDHNIRAGWLTVGKGLSSSN
FT FEPQAYVRNFADKEGKVWLGGGGRNPPPDAPHLVVTTPDIESLRPKSPMKNQQQQSYPS
FT SLASANSSNRRTTGNSPQANPNVVVLHQEASGSNFSVPTTPHWVPPTAPAAAGPPPMDS
FT FRVPEGGNNTRPPDDKSFDMYGFN (in isoform 2)"
FT /id="VSP_059895"
SQ SEQUENCE 775 AA; 85846 MW; C1A90C40B9DD86DE CRC64;
MKKKQEESSL EKLSTWYQDG EQDGGDRSEK RRMSLKASDF ESSSRSGGSK SKEDNKSVVD
VEHQDRDSKR ERDGRERTHG SSSDSSKRKR WDEAGGLVND GDHKSSKLSD SRHDSGGERV
SVSNEHGESR RDLKSDRSLK TSSRDEKSKS RGVKDDDRGS PLKKTSGKDG SEVVREVGRS
NRSKTPDADY EKEKYSRKDE RSRGRDDGWS DRDRDQEGLK DNWKRRHSSS GDKDQKDGDL
LYDRGREREF PRQGRERSEG ERSHGRLGGR KDGNRGEAVK ALSSGGVSNE NYDVIEIQTK
PHDYVRGESG PNFARMTESG QQPPKKPSNN EEEWAHNQEG RQRSETFGFG SYGEDSRDEA
GEASSDYSGA KARNQRGSTP GRTNFVQTPN RGYQTPQGTR GNRPLRGGKG RPAGGRENQQ
GAIPMPIMGS PFANLGMPPP SPIHSLTPGM SPIPGTSVTP VFMPPFAPTL IWPGARGVDG
NMLPVPPVLS PLPPGPSGPR FPSIGTPPNP NMFFTPPGSD RGGPPNFPGS NISGQMGRGM
PSDKTSGGWV PPRGGGPPGK APSRGEQNDY SQNFVDTGMR PQNFIRELEL TNVEDYPKLR
ELIQKKDEIV SNSASAPMYL KGDLHEVELS PELFGTKFDV ILVDPPWEEY VHRAPGVSDS
MEYWTFEDII NLKIEAIADT PSFLFLWVGD GVGLEQGRQC LKKWGFRRCE DICWVKTNKS
NAAPTLRHDS RTVFQRSKEH CLMGIKGTVR RSTDGHIIHA NIDTDVIIAE EPPYG
