RAMAC_MOUSE
ID RAMAC_MOUSE Reviewed; 119 AA.
AC Q9CQY2; Q3TV69; Q9CWI1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=RNA guanine-N7 methyltransferase activating subunit {ECO:0000250|UniProtKB:Q9BTL3};
DE AltName: Full=Protein FAM103A1;
DE AltName: Full=RNA guanine-7 methyltransferase activating subunit {ECO:0000250|UniProtKB:Q9BTL3};
DE AltName: Full=RNMT-activating mRNA cap methylating subunit {ECO:0000250|UniProtKB:Q9BTL3};
DE AltName: Full=RNMT-activating mRNA cap methyltransferase subunit;
DE AltName: Full=RNMT-activating mini protein {ECO:0000250|UniProtKB:Q9BTL3};
DE Short=RAM {ECO:0000250|UniProtKB:Q9BTL3};
GN Name=Ramac; Synonyms=Fam103a1, Rammet {ECO:0000312|MGI:MGI:1914398};
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].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Cecum, Head, Stomach, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Kidney, and Mammary gland;
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).
CC -!- FUNCTION: Regulatory 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. Promotes the recruitment of
CC the methyl donor, S-adenosyl-L-methionine, to RNMT. Regulates RNMT
CC expression by a post-transcriptional stabilizing mechanism. Binds RNA.
CC {ECO:0000250|UniProtKB:Q9BTL3}.
CC -!- SUBUNIT: Interacts with RNMT; this interaction enhances mRNA binding
CC and cap methyltransferase activity. {ECO:0000250|UniProtKB:Q9BTL3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BTL3}.
CC -!- SIMILARITY: Belongs to the RAM family. {ECO:0000305}.
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DR EMBL; AK010694; BAB27126.1; -; mRNA.
DR EMBL; AK011881; BAB27895.1; -; mRNA.
DR EMBL; AK018614; BAB31308.1; -; mRNA.
DR EMBL; AK079819; BAC37755.1; -; mRNA.
DR EMBL; AK081301; BAC38188.1; -; mRNA.
DR EMBL; AK085230; BAC39395.1; -; mRNA.
DR EMBL; AK150938; BAE29973.1; -; mRNA.
DR EMBL; AK160347; BAE35751.1; -; mRNA.
DR EMBL; AK169392; BAE41139.1; -; mRNA.
DR EMBL; BC058367; AAH58367.1; -; mRNA.
DR EMBL; BC091760; AAH91760.1; -; mRNA.
DR EMBL; BC096399; AAH96399.1; -; mRNA.
DR CCDS; CCDS21406.1; -.
DR RefSeq; NP_080273.1; NM_025997.2.
DR AlphaFoldDB; Q9CQY2; -.
DR SMR; Q9CQY2; -.
DR BioGRID; 211976; 6.
DR STRING; 10090.ENSMUSP00000039065; -.
DR iPTMnet; Q9CQY2; -.
DR PhosphoSitePlus; Q9CQY2; -.
DR EPD; Q9CQY2; -.
DR jPOST; Q9CQY2; -.
DR MaxQB; Q9CQY2; -.
DR PaxDb; Q9CQY2; -.
DR PeptideAtlas; Q9CQY2; -.
DR PRIDE; Q9CQY2; -.
DR ProteomicsDB; 254979; -.
DR DNASU; 67148; -.
DR Ensembl; ENSMUST00000042166; ENSMUSP00000039065; ENSMUSG00000038646.
DR Ensembl; ENSMUST00000118190; ENSMUSP00000113339; ENSMUSG00000038646.
DR GeneID; 67148; -.
DR KEGG; mmu:67148; -.
DR UCSC; uc009icl.1; mouse.
DR CTD; 83640; -.
DR MGI; MGI:1914398; Ramac.
DR VEuPathDB; HostDB:ENSMUSG00000038646; -.
DR eggNOG; ENOG502S60Q; Eukaryota.
DR GeneTree; ENSGT00390000011190; -.
DR HOGENOM; CLU_144253_0_0_1; -.
DR InParanoid; Q9CQY2; -.
DR OMA; PPIIEEW; -.
DR OrthoDB; 1548572at2759; -.
DR PhylomeDB; Q9CQY2; -.
DR TreeFam; TF335880; -.
DR BioGRID-ORCS; 67148; 8 hits in 36 CRISPR screens.
DR ChiTaRS; Ramac; mouse.
DR PRO; PR:Q9CQY2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CQY2; protein.
DR Bgee; ENSMUSG00000038646; Expressed in animal zygote and 63 other tissues.
DR ExpressionAtlas; Q9CQY2; baseline and differential.
DR Genevisible; Q9CQY2; MM.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008047; F:enzyme activator 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:0032259; P:methylation; ISS:UniProtKB.
DR GO; GO:0036031; P:recruitment of mRNA capping enzyme to RNA polymerase II holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0106005; P:RNA 5'-cap (guanine-N7)-methylation; IEA:InterPro.
DR InterPro; IPR028271; RAMAC.
DR Pfam; PF15320; RAM; 1.
PE 3: Inferred from homology;
KW Methylation; mRNA capping; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..119
FT /note="RNA guanine-N7 methyltransferase activating subunit"
FT /id="PRO_0000089984"
FT REGION 1..55
FT /note="Interaction with RNMT"
FT /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT REGION 30..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..119
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT MOTIF 36..42
FT /note="RNMT-activating domain"
FT /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT MOD_RES 85
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT CONFLICT 95
FT /note="Q -> E (in Ref. 1; BAB27126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 119 AA; 14556 MW; 43C7E1C68E14011C CRC64;
MSDTSEEIPN FEEMFASRFT KDDKEYQEYL KRPPESPPIV EEWNSRAGGN QRNRGNWLQD
NRQFRGRDNR RGWPSDNRSN QWHGRSWGNN NYPQQRPEPY YQQQYTQYGH NQRPPYGYY
