Reviewed, UniProtKB/Swiss-Prot Q9D0L8 (MCES_MOUSE)

Names and origin

Protein names

Recommended name:
    mRNA cap guanine-N7 methyltransferase
    EC=2.1.1.56
Alternative name(s):
    mRNA (guanine-N(7)-)-methyltransferase
    RG7MT1
    mRNA cap methyltransferase

Gene names

Name:	Rnmt
Synonyms:	Kiaa0398

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC By similarity.
Catalytic activity	S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.
Subunit structure	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 By similarity.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the mRNA cap methyltransferase family.

Ontologies

Keywords
Biological process	mRNA capping mRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	mRNA capping Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	RNA binding Inferred from sequence or structural similarity. Source: UniProtKB mRNA (guanine-N7-)-methyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9D0L8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9D0L8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     370-465: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9D0L8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     315-369: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 465	465	mRNA cap guanine-N7 methyltransferase		PRO_0000248323
Regions
	Region	165 – 166	2	mRNA cap binding By similarity
	Motif	113 – 115	3	Nuclear localization signal By similarity
Sites
	Binding site	169	1	S-adenosyl-L-methionine By similarity
	Binding site	194	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	197	1	mRNA cap By similarity
	Binding site	203	1	mRNA cap By similarity
	Binding site	216	1	S-adenosyl-L-methionine By similarity
	Binding site	228	1	mRNA cap By similarity
	Binding site	250	1	S-adenosyl-L-methionine By similarity
	Binding site	273	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	277	1	mRNA cap By similarity
	Binding site	359	1	mRNA cap By similarity
	Binding site	456	1	mRNA cap By similarity
Amino acid modifications
	Modified residue	11	1	Phosphoserine Ref.4
	Modified residue	15	1	Phosphoserine Ref.4 Ref.5
	Modified residue	64	1	Phosphoserine Ref.4
	Modified residue	100	1	Phosphoserine
Natural variations
	Alternative sequence	315 – 369	55	Missing in isoform 3.		VSP_020242
	Alternative sequence	370 – 465	96	Missing in isoform 2.		VSP_020243
Experimental info
	Sequence conflict	32	1	E → K in BAB29834. Ref.2
	Sequence conflict	53	1	L → H in BAE43278. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: D1422D9621EE2A1A	FASTA	465	53,291
	10 20 30 40 50 60 MEGSAKASVA SDPESPPGGN EPAAASGQRL PENTPPCQQV DQPKMQKEFG EDLVEQNSSY 70 80 90 100 110 120 VQDSPSKKRK LDVEIILEEK HSEDDGGSAK RSKLERGDVS EDEPSLGRLN QTKRKLQPQD 130 140 150 160 170 180 DEVPQKLQKL EEGHSSAVAA HYNELQEVGL AKRSQSRIFY LRNFNNWIKS ILIGEILEKV 190 200 210 220 230 240 RQRKTRDITV LDLGCGKGGD LLKWRKGRIS RLVCADIADI SMKQCQQRYE DMRCRRDNEH 250 260 270 280 290 300 IFSAEFITAD CSKELLVEKF RDPEMYFDVC SCQFACHYSF ESQVQADTML RNACGRLNPG 310 320 330 340 350 360 GYFIGTTPNS FELIRRLEAS ETESFGNEIY TVKFQKKGNY PLFGCKYDFN LEGVVDVPEF 370 380 390 400 410 420 LVYFPLLTEM AKKYNMKLIY KKTFLEFYEE KIKNNENKML LKRMQALEQY PAHENSKLAS 430 440 450 460 EKVGDYTHAA EYLKKSQVRL PLGTLSKSEW EATSIYLVFA FEKQQ
	Isoform 2. Checksum: CBC66ABB10D0F940	FASTA	369	41,908
	10 20 30 40 50 60 MEGSAKASVA SDPESPPGGN EPAAASGQRL PENTPPCQQV DQPKMQKEFG EDLVEQNSSY 70 80 90 100 110 120 VQDSPSKKRK LDVEIILEEK HSEDDGGSAK RSKLERGDVS EDEPSLGRLN QTKRKLQPQD 130 140 150 160 170 180 DEVPQKLQKL EEGHSSAVAA HYNELQEVGL AKRSQSRIFY LRNFNNWIKS ILIGEILEKV 190 200 210 220 230 240 RQRKTRDITV LDLGCGKGGD LLKWRKGRIS RLVCADIADI SMKQCQQRYE DMRCRRDNEH 250 260 270 280 290 300 IFSAEFITAD CSKELLVEKF RDPEMYFDVC SCQFACHYSF ESQVQADTML RNACGRLNPG 310 320 330 340 350 360 GYFIGTTPNS FELIRRLEAS ETESFGNEIY TVKFQKKGNY PLFGCKYDFN LEGVVDVPEF LVYFPLLTE
	Isoform 3. Checksum: 7654F2915B8EB905	FASTA	410	46,867
	10 20 30 40 50 60 MEGSAKASVA SDPESPPGGN EPAAASGQRL PENTPPCQQV DQPKMQKEFG EDLVEQNSSY 70 80 90 100 110 120 VQDSPSKKRK LDVEIILEEK HSEDDGGSAK RSKLERGDVS EDEPSLGRLN QTKRKLQPQD 130 140 150 160 170 180 DEVPQKLQKL EEGHSSAVAA HYNELQEVGL AKRSQSRIFY LRNFNNWIKS ILIGEILEKV 190 200 210 220 230 240 RQRKTRDITV LDLGCGKGGD LLKWRKGRIS RLVCADIADI SMKQCQQRYE DMRCRRDNEH 250 260 270 280 290 300 IFSAEFITAD CSKELLVEKF RDPEMYFDVC SCQFACHYSF ESQVQADTML RNACGRLNPG 310 320 330 340 350 360 GYFIGTTPNS FELIMAKKYN MKLIYKKTFL EFYEEKIKNN ENKMLLKRMQ ALEQYPAHEN 370 380 390 400 410 SKLASEKVGD YTHAAEYLKK SQVRLPLGTL SKSEWEATSI YLVFAFEKQQ

References

[1]	"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." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H. DNA Res. 10:167-180(2003) [PubMed: 14621295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Strain: C57BL/6J. Tissue: Cerebellum, Head and Testis.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: FVB/N. Tissue: Colon.
[4]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed: 15345747] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15 AND SER-64, MASS SPECTROMETRY. Tissue: Brain.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY. Tissue: Liver.
[6]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-100, MASS SPECTROMETRY. Tissue: Macrophage.
[7]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK129130 mRNA. Translation: BAC97940.1. Different initiation. AK011300 mRNA. Translation: BAB27527.1. AK015403 mRNA. Translation: BAB29834.1. AK031780 mRNA. Translation: BAE43278.1. BC021794 mRNA. Translation: AAH21794.1. AK082331 mRNA. Translation: BAC38469.1.
IPI	IPI00317422. IPI00453849. IPI00785256.
RefSeq	NP_080716.1.
UniGene	Mm.27544
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q9D0L8.
Proteomic databases
PRIDE	Q9D0L8.
Genome annotation databases
Ensembl	ENSMUSG00000009535. Mus musculus. [Contig view]
GeneID	67897.
KEGG	mmu:67897.
Organism-specific databases
MGI	MGI:1915147. Rnmt.
Rouge	Search...
Phylogenomic databases
HOVERGEN	Q9D0L8.
OMA	Q9D0L8. KYMKNSQ.
Enzyme and pathway databases
BRENDA	2.1.1.56. 244.
Gene expression databases
ArrayExpress	Q9D0L8.
Bgee	Q9D0L8.
CleanEx	MM_RNMT.
GermOnline	ENSMUSG00000009535. Mus musculus.
Family and domain databases
InterPro	IPR016899. mRNA_G-N7_MeTrfase. IPR004971. Pox_MCEL. [Graphical view]
Pfam	PF03291. Pox_MCEL. 1 hit. [Graphical view]
PIRSF	PIRSF028762. ABD1. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	325886.
SOURCE	Search...

Entry information

Entry name

MCES_MOUSE

Accession

Primary (citable) accession number: Q9D0L8
Secondary accession number(s): Q3V3U9, Q6ZQC6, Q9D5F1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)