MCES_MOUSE
ID MCES_MOUSE Reviewed; 465 AA.
AC Q9D0L8; Q3V3U9; Q6ZQC6; Q9D5F1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=mRNA cap guanine-N7 methyltransferase;
DE EC=2.1.1.56 {ECO:0000250|UniProtKB:O43148};
DE AltName: Full=RG7MT1;
DE AltName: Full=mRNA (guanine-N(7))-methyltransferase;
DE AltName: Full=mRNA cap methyltransferase;
GN Name=Rnmt; Synonyms=Kiaa0398;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-15, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15; SER-64 AND
RP SER-100, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalytic subunit of the mRNA-capping methyltransferase
CC RNMT:RAMAC complex that methylates the N7 position of the added
CC guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-
CC terminal GpppC. {ECO:0000250|UniProtKB:O43148}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; EC=2.1.1.56;
CC Evidence={ECO:0000250|UniProtKB:O43148, ECO:0000255|PROSITE-
CC ProRule:PRU00895};
CC -!- ACTIVITY REGULATION: Methyltransferase activity is activated by RAMAC.
CC {ECO:0000250|UniProtKB:O43148}.
CC -!- SUBUNIT: Interacts with importin alpha, leading to stimulate both RNA-
CC binding and methyltransferase activity. Interaction with importin alpha
CC and beta is required for its nuclear localization, importin beta
CC dissociating in response to RanGTP, allowing RNMT-importin alpha to
CC bind RNA substrates. Interacts with elongating form of polymerase II
CC and RNGTT. Interacts with RAMAC, this interaction significantly
CC enhances RNA-binding and cap methyltransferase activity.
CC {ECO:0000250|UniProtKB:O43148}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43148}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9D0L8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D0L8-2; Sequence=VSP_020243;
CC Name=3;
CC IsoId=Q9D0L8-3; Sequence=VSP_020242;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. mRNA cap 0 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00895}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97940.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129130; BAC97940.1; ALT_INIT; mRNA.
DR EMBL; AK011300; BAB27527.1; -; mRNA.
DR EMBL; AK015403; BAB29834.1; -; mRNA.
DR EMBL; AK031780; BAE43278.1; -; mRNA.
DR EMBL; BC021794; AAH21794.1; -; mRNA.
DR EMBL; AK082331; BAC38469.1; -; mRNA.
DR CCDS; CCDS37852.1; -. [Q9D0L8-1]
DR CCDS; CCDS50314.1; -. [Q9D0L8-3]
DR RefSeq; NP_001164424.1; NM_001170953.1. [Q9D0L8-3]
DR RefSeq; NP_080716.1; NM_026440.4. [Q9D0L8-1]
DR RefSeq; XP_006526256.1; XM_006526193.3. [Q9D0L8-1]
DR RefSeq; XP_006526257.1; XM_006526194.3.
DR RefSeq; XP_006526259.1; XM_006526196.3.
DR RefSeq; XP_006526260.1; XM_006526197.3. [Q9D0L8-1]
DR RefSeq; XP_011245293.1; XM_011246991.2. [Q9D0L8-1]
DR AlphaFoldDB; Q9D0L8; -.
DR SMR; Q9D0L8; -.
DR BioGRID; 212521; 11.
DR IntAct; Q9D0L8; 1.
DR STRING; 10090.ENSMUSP00000009679; -.
DR iPTMnet; Q9D0L8; -.
DR PhosphoSitePlus; Q9D0L8; -.
DR EPD; Q9D0L8; -.
DR jPOST; Q9D0L8; -.
DR MaxQB; Q9D0L8; -.
DR PaxDb; Q9D0L8; -.
DR PeptideAtlas; Q9D0L8; -.
DR PRIDE; Q9D0L8; -.
DR ProteomicsDB; 252743; -. [Q9D0L8-1]
DR ProteomicsDB; 252744; -. [Q9D0L8-2]
DR ProteomicsDB; 252745; -. [Q9D0L8-3]
DR Antibodypedia; 21962; 309 antibodies from 26 providers.
DR DNASU; 67897; -.
DR Ensembl; ENSMUST00000009679; ENSMUSP00000009679; ENSMUSG00000009535. [Q9D0L8-1]
DR Ensembl; ENSMUST00000025427; ENSMUSP00000025427; ENSMUSG00000009535. [Q9D0L8-3]
DR GeneID; 67897; -.
DR KEGG; mmu:67897; -.
DR UCSC; uc008fnj.2; mouse. [Q9D0L8-1]
DR UCSC; uc012bem.1; mouse. [Q9D0L8-3]
DR CTD; 8731; -.
DR MGI; MGI:1915147; Rnmt.
DR VEuPathDB; HostDB:ENSMUSG00000009535; -.
DR eggNOG; KOG1975; Eukaryota.
DR GeneTree; ENSGT00390000002368; -.
DR HOGENOM; CLU_020346_0_1_1; -.
DR InParanoid; Q9D0L8; -.
DR OMA; WDATSIY; -.
DR OrthoDB; 1390749at2759; -.
DR PhylomeDB; Q9D0L8; -.
DR TreeFam; TF314347; -.
DR Reactome; R-MMU-72086; mRNA Capping.
DR Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR BioGRID-ORCS; 67897; 26 hits in 71 CRISPR screens.
DR ChiTaRS; Rnmt; mouse.
DR PRO; PR:Q9D0L8; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9D0L8; protein.
DR Bgee; ENSMUSG00000009535; Expressed in secondary oocyte and 270 other tissues.
DR ExpressionAtlas; Q9D0L8; baseline and differential.
DR Genevisible; Q9D0L8; MM.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; ISS:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR InterPro; IPR016899; mRNA_G-N7_MeTrfase_euk.
DR InterPro; IPR039753; RG7MT1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12189; PTHR12189; 1.
DR Pfam; PF03291; Pox_MCEL; 1.
DR PIRSF; PIRSF028762; ABD1; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51562; RNA_CAP0_MT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; mRNA capping; mRNA processing;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..465
FT /note="mRNA cap guanine-N7 methyltransferase"
FT /id="PRO_0000248323"
FT DOMAIN 117..465
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 113..115
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 65..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 165..166
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 216
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 250
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 273
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 278
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT SITE 197
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 203
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 228
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 277
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 359
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 456
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2U7"
FT VAR_SEQ 315..369
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020242"
FT VAR_SEQ 370..465
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020243"
FT CONFLICT 32
FT /note="E -> K (in Ref. 2; BAB29834)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="L -> H (in Ref. 2; BAE43278)"
FT /evidence="ECO:0000305"
SQ 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
