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mRNA cap guanine-N7 methyltransferase (EC 2.1.1.56) (RG7MT1) (mRNA (guanine-N(7)-)-methyltransferase) (mRNA cap methyltransferase)

 MCES_MOUSE              Reviewed;         465 AA.
Q9D0L8; Q3V3U9; Q6ZQC6; Q9D5F1;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 124.
RecName: Full=mRNA cap guanine-N7 methyltransferase;
EC=2.1.1.56 {ECO:0000250|UniProtKB:O43148};
AltName: Full=RG7MT1;
AltName: Full=mRNA (guanine-N(7)-)-methyltransferase;
AltName: Full=mRNA cap methyltransferase;
Name=Rnmt; Synonyms=Kiaa0398;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-15, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15; SER-64 AND
SER-100, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Catalytic subunit of the mRNA-capping methyltransferase
RNMT:RAM/FAM103A1 complex that methylates the N7 position of the
added guanosine to the 5'-cap structure of mRNAs. Binds RNA
containing 5'-terminal GpppC. {ECO:0000250|UniProtKB:O43148}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
{ECO:0000250|UniProtKB:O43148, ECO:0000255|PROSITE-
ProRule:PRU00895}.
-!- ENZYME REGULATION: Methyltransferase activity is activated by
RAM/FAM103A1. {ECO:0000250|UniProtKB:O43148}.
-!- SUBUNIT: Interacts with importin alpha, leading to stimulate both
RNA-binding and methyltransferase activity. Interaction with
importin alpha and beta is required for its nuclear localization,
importin beta dissociating in response to RanGTP, allowing RNMT-
importin alpha to bind RNA substrates. Interacts with elongating
form of polymerase II and RNGTT. Interacts with RAM/FAM103A1, this
interaction significantly enhances RNA-binding and cap
methyltransferase activity. {ECO:0000250|UniProtKB:O43148}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43148}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9D0L8-1; Sequence=Displayed;
Name=2;
IsoId=Q9D0L8-2; Sequence=VSP_020243;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9D0L8-3; Sequence=VSP_020242;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. mRNA cap 0 methyltransferase
family. {ECO:0000255|PROSITE-ProRule:PRU00895}.
-!- SEQUENCE CAUTION:
Sequence=BAC97940.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK129130; BAC97940.1; ALT_INIT; mRNA.
EMBL; AK011300; BAB27527.1; -; mRNA.
EMBL; AK015403; BAB29834.1; -; mRNA.
EMBL; AK031780; BAE43278.1; -; mRNA.
EMBL; BC021794; AAH21794.1; -; mRNA.
EMBL; AK082331; BAC38469.1; -; mRNA.
CCDS; CCDS37852.1; -. [Q9D0L8-1]
CCDS; CCDS50314.1; -. [Q9D0L8-3]
RefSeq; NP_001164424.1; NM_001170953.1. [Q9D0L8-3]
RefSeq; NP_080716.1; NM_026440.4. [Q9D0L8-1]
RefSeq; XP_006526256.1; XM_006526193.3. [Q9D0L8-1]
RefSeq; XP_006526257.1; XM_006526194.3. [Q9D0L8-1]
RefSeq; XP_006526259.1; XM_006526196.3. [Q9D0L8-1]
RefSeq; XP_006526260.1; XM_006526197.3. [Q9D0L8-1]
RefSeq; XP_011245293.1; XM_011246991.2. [Q9D0L8-1]
UniGene; Mm.27544; -.
ProteinModelPortal; Q9D0L8; -.
SMR; Q9D0L8; -.
STRING; 10090.ENSMUSP00000009679; -.
iPTMnet; Q9D0L8; -.
PhosphoSitePlus; Q9D0L8; -.
EPD; Q9D0L8; -.
PaxDb; Q9D0L8; -.
PeptideAtlas; Q9D0L8; -.
PRIDE; Q9D0L8; -.
Ensembl; ENSMUST00000009679; ENSMUSP00000009679; ENSMUSG00000009535. [Q9D0L8-1]
Ensembl; ENSMUST00000025427; ENSMUSP00000025427; ENSMUSG00000009535. [Q9D0L8-3]
GeneID; 67897; -.
KEGG; mmu:67897; -.
UCSC; uc008fnj.2; mouse. [Q9D0L8-1]
UCSC; uc012bem.1; mouse. [Q9D0L8-3]
CTD; 8731; -.
MGI; MGI:1915147; Rnmt.
eggNOG; KOG1975; Eukaryota.
eggNOG; ENOG410Y7HG; LUCA.
GeneTree; ENSGT00390000002368; -.
HOGENOM; HOG000242614; -.
HOVERGEN; HBG081963; -.
InParanoid; Q9D0L8; -.
KO; K00565; -.
OMA; LNLVSCQ; -.
OrthoDB; EOG091G0C9Y; -.
PhylomeDB; Q9D0L8; -.
TreeFam; TF314347; -.
Reactome; R-MMU-72086; mRNA Capping.
Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE.
ChiTaRS; Rnmt; mouse.
PRO; PR:Q9D0L8; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000009535; -.
CleanEx; MM_RNMT; -.
ExpressionAtlas; Q9D0L8; baseline and differential.
Genevisible; Q9D0L8; MM.
GO; GO:0001650; C:fibrillar center; ISO:MGI.
GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
GO; GO:0031533; C:mRNA cap methyltransferase complex; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
GO; GO:0006370; P:7-methylguanosine mRNA capping; ISS:UniProtKB.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0036265; P:RNA (guanine-N7)-methylation; IBA:GO_Central.
InterPro; IPR016899; mRNA_G-N7_MeTrfase.
InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF03291; Pox_MCEL; 1.
PIRSF; PIRSF028762; ABD1; 1.
SUPFAM; SSF53335; SSF53335; 2.
PROSITE; PS51562; RNA_CAP0_MT; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Methyltransferase;
mRNA capping; mRNA processing; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
CHAIN 1 465 mRNA cap guanine-N7 methyltransferase.
/FTId=PRO_0000248323.
DOMAIN 117 465 mRNA cap 0 methyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00895}.
REGION 165 166 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
MOTIF 113 115 Nuclear localization signal.
{ECO:0000250}.
BINDING 169 169 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00895}.
BINDING 194 194 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
BINDING 216 216 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00895}.
BINDING 250 250 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000250|UniProtKB:O43148}.
BINDING 273 273 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:O43148}.
BINDING 277 277 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
BINDING 278 278 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:O43148}.
BINDING 359 359 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
BINDING 456 456 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
SITE 197 197 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
SITE 203 203 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
SITE 228 228 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:21183079}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000250|UniProtKB:Q5U2U7}.
VAR_SEQ 315 369 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020242.
VAR_SEQ 370 465 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020243.
CONFLICT 32 32 E -> K (in Ref. 2; BAB29834).
{ECO:0000305}.
CONFLICT 53 53 L -> H (in Ref. 2; BAE43278).
{ECO:0000305}.
SEQUENCE 465 AA; 53291 MW; D1422D9621EE2A1A CRC64;
MEGSAKASVA SDPESPPGGN EPAAASGQRL PENTPPCQQV DQPKMQKEFG EDLVEQNSSY
VQDSPSKKRK LDVEIILEEK HSEDDGGSAK RSKLERGDVS EDEPSLGRLN QTKRKLQPQD
DEVPQKLQKL EEGHSSAVAA HYNELQEVGL AKRSQSRIFY LRNFNNWIKS ILIGEILEKV
RQRKTRDITV LDLGCGKGGD LLKWRKGRIS RLVCADIADI SMKQCQQRYE DMRCRRDNEH
IFSAEFITAD CSKELLVEKF RDPEMYFDVC SCQFACHYSF ESQVQADTML RNACGRLNPG
GYFIGTTPNS FELIRRLEAS ETESFGNEIY TVKFQKKGNY PLFGCKYDFN LEGVVDVPEF
LVYFPLLTEM AKKYNMKLIY KKTFLEFYEE KIKNNENKML LKRMQALEQY PAHENSKLAS
EKVGDYTHAA EYLKKSQVRL PLGTLSKSEW EATSIYLVFA FEKQQ


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