MCES_RAT
ID MCES_RAT Reviewed; 461 AA.
AC Q5U2U7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-16; SER-94 AND
RP SER-99, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. mRNA cap 0 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00895}.
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; BC085858; AAH85858.1; -; mRNA.
DR RefSeq; NP_001008300.1; NM_001008299.2.
DR RefSeq; XP_006254956.1; XM_006254894.1.
DR RefSeq; XP_006254957.1; XM_006254895.3.
DR AlphaFoldDB; Q5U2U7; -.
DR SMR; Q5U2U7; -.
DR BioGRID; 253542; 2.
DR STRING; 10116.ENSRNOP00000022410; -.
DR iPTMnet; Q5U2U7; -.
DR PhosphoSitePlus; Q5U2U7; -.
DR jPOST; Q5U2U7; -.
DR PaxDb; Q5U2U7; -.
DR PRIDE; Q5U2U7; -.
DR Ensembl; ENSRNOT00000022410; ENSRNOP00000022410; ENSRNOG00000016698.
DR GeneID; 291534; -.
DR KEGG; rno:291534; -.
DR UCSC; RGD:1309242; rat.
DR CTD; 8731; -.
DR RGD; 1309242; Rnmt.
DR eggNOG; KOG1975; Eukaryota.
DR GeneTree; ENSGT00390000002368; -.
DR HOGENOM; CLU_020346_0_1_1; -.
DR InParanoid; Q5U2U7; -.
DR OMA; WDATSIY; -.
DR OrthoDB; 1390749at2759; -.
DR PhylomeDB; Q5U2U7; -.
DR TreeFam; TF314347; -.
DR Reactome; R-RNO-72086; mRNA Capping.
DR Reactome; R-RNO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:Q5U2U7; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000016698; Expressed in thymus and 20 other tissues.
DR Genevisible; Q5U2U7; RN.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
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; ISO:RGD.
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 Methyltransferase; mRNA capping; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..461
FT /note="mRNA cap guanine-N7 methyltransferase"
FT /id="PRO_0000248324"
FT DOMAIN 113..461
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 107..109
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161..162
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 269
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 274
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT SITE 193
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 199
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 224
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 273
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 355
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 452
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0L8"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0L8"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 461 AA; 52817 MW; 6AF6C1B59C829C1E CRC64;
MESSVKASVD SETESSPGVN ETAAASGQRL SEKTRQQADQ PKTQDDLVEQ NSSYVQDSPS
KKRKLDVEII LDEKHSEDDG GASKRSKLER GGGSEDEPSP GGLTERKRKL QPQDALETQT
RKFQKLEEGH SSAVAAHYNE LQEVGLVKRS QSRIFYLRNF NNWIKSILIG EILEKVRQRK
NRDITVLDLG CGKGGDLLKW RKGRISRLVC ADIADISMKQ CQQRYEDMKC RRDNEYIFSA
EFITADCSKE LLVEKFHDPE MYFDICSCQF ACHYSFESLE QADMMLRNAC GRLNPGGYFI
GTTPNSFELI RRLEASETES FGNEIYTVKF QKKGNYPLFG CKYDFNLEGV VDVPEFLVYF
PLLTEMAKKY NMKLIYKKTF LEFYEEKIKN NENKMLLKRM QALESYPANE NSKLASEKAG
DYAHAAEYMK NSQVRLPLGT LSKSEWEATS IYLVFAFEKQ Q
