TM10C_MOUSE
ID TM10C_MOUSE Reviewed; 414 AA.
AC Q3UFY8; Q8R588; Q9DBC1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=tRNA methyltransferase 10 homolog C {ECO:0000305};
DE AltName: Full=Mitochondrial ribonuclease P protein 1 {ECO:0000250|UniProtKB:Q7L0Y3};
DE Short=Mitochondrial RNase P protein 1 {ECO:0000250|UniProtKB:Q7L0Y3};
DE AltName: Full=RNA (guanine-9-)-methyltransferase domain-containing protein 1 {ECO:0000250|UniProtKB:Q7L0Y3};
DE AltName: Full=mRNA methyladenosine-N(1)-methyltransferase {ECO:0000250|UniProtKB:Q7L0Y3};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q7L0Y3};
DE AltName: Full=tRNA (adenine(9)-N(1))-methyltransferase {ECO:0000250|UniProtKB:Q7L0Y3};
DE EC=2.1.1.218 {ECO:0000250|UniProtKB:Q7L0Y3};
DE AltName: Full=tRNA (guanine(9)-N(1))-methyltransferase {ECO:0000250|UniProtKB:Q7L0Y3};
DE EC=2.1.1.221 {ECO:0000250|UniProtKB:Q7L0Y3};
DE Flags: Precursor;
GN Name=Trmt10c {ECO:0000312|MGI:MGI:1196261}; Synonyms=Mrpp1, Rg9mtd1;
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, and NOD; TISSUE=Liver, Muellerian duct, 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=FVB/N; TISSUE=Colon, and Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Spleen;
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: Mitochondrial tRNA N(1)-methyltransferase involved in
CC mitochondrial tRNA maturation. Component of mitochondrial ribonuclease
CC P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3,
CC which cleaves tRNA molecules in their 5'-ends. Together with
CC HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P,
CC named MRPP1-MRPP2 subcomplex, which displays functions that are
CC independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex
CC catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at
CC position 9 (m1G9 and m1A9, respectively) in tRNAs; TRMT10C/MRPP1 acting
CC as the catalytic N(1)-methyltransferase subunit. The MRPP1-MRPP2
CC subcomplex also acts as a tRNA maturation platform: following 5'-end
CC cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2
CC subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2,
CC retains the tRNA product after ELAC2 processing and presents the
CC nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1
CC enzyme. In addition to tRNA N(1)-methyltransferase activity,
CC TRMT10C/MRPP1 also acts as a mRNA N(1)-methyltransferase by mediating
CC methylation of adenosine residues at the N(1) position of MT-ND5 mRNA.
CC Associates with mitochondrial DNA complexes at the nucleoids to
CC initiate RNA processing and ribosome assembly.
CC {ECO:0000250|UniProtKB:Q7L0Y3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43148, Rhea:RHEA-COMP:10363, Rhea:RHEA-COMP:10364,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.218;
CC Evidence={ECO:0000250|UniProtKB:Q7L0Y3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221;
CC Evidence={ECO:0000250|UniProtKB:Q7L0Y3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(1)-
CC methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55392, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12415,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491;
CC Evidence={ECO:0000250|UniProtKB:Q7L0Y3};
CC -!- SUBUNIT: Component of mitochondrial ribonuclease P, a complex composed
CC of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3. Interacts with
CC HSD17B10/MRPP2; forming the MRPP1-MRPP2 subcomplex of the mitochondrial
CC ribonuclease P complex. Interacts with GRSF1.
CC {ECO:0000250|UniProtKB:Q7L0Y3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000250|UniProtKB:Q7L0Y3}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. TRM10 family. {ECO:0000255|PROSITE-ProRule:PRU01012}.
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DR EMBL; AK005047; BAB23773.1; -; mRNA.
DR EMBL; AK087991; BAC40080.1; -; mRNA.
DR EMBL; AK135426; BAE22529.1; -; mRNA.
DR EMBL; AK148219; BAE28421.1; -; mRNA.
DR EMBL; AK166781; BAE39015.1; -; mRNA.
DR EMBL; BC023147; AAH23147.1; -; mRNA.
DR EMBL; BC106131; AAI06132.1; -; mRNA.
DR CCDS; CCDS28220.1; -.
DR RefSeq; NP_083368.1; NM_029092.3.
DR AlphaFoldDB; Q3UFY8; -.
DR SMR; Q3UFY8; -.
DR BioGRID; 206672; 12.
DR STRING; 10090.ENSMUSP00000058954; -.
DR iPTMnet; Q3UFY8; -.
DR PhosphoSitePlus; Q3UFY8; -.
DR EPD; Q3UFY8; -.
DR jPOST; Q3UFY8; -.
DR MaxQB; Q3UFY8; -.
DR PaxDb; Q3UFY8; -.
DR PeptideAtlas; Q3UFY8; -.
DR PRIDE; Q3UFY8; -.
DR ProteomicsDB; 259459; -.
DR Antibodypedia; 32284; 83 antibodies from 18 providers.
DR DNASU; 52575; -.
DR Ensembl; ENSMUST00000059052; ENSMUSP00000058954; ENSMUSG00000044763.
DR GeneID; 52575; -.
DR KEGG; mmu:52575; -.
DR UCSC; uc007zmd.1; mouse.
DR CTD; 54931; -.
DR MGI; MGI:1196261; Trmt10c.
DR VEuPathDB; HostDB:ENSMUSG00000044763; -.
DR eggNOG; KOG2967; Eukaryota.
DR GeneTree; ENSGT00530000063169; -.
DR HOGENOM; CLU_034384_3_1_1; -.
DR InParanoid; Q3UFY8; -.
DR OMA; IDPFHIY; -.
DR OrthoDB; 1569668at2759; -.
DR PhylomeDB; Q3UFY8; -.
DR TreeFam; TF319795; -.
DR BioGRID-ORCS; 52575; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Trmt10c; mouse.
DR PRO; PR:Q3UFY8; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q3UFY8; protein.
DR Bgee; ENSMUSG00000044763; Expressed in basal plate medulla oblongata and 111 other tissues.
DR Genevisible; Q3UFY8; MM.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0030678; C:mitochondrial ribonuclease P complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043527; C:tRNA methyltransferase complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0061953; F:mRNA (adenine-N1-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; ISO:MGI.
DR GO; GO:0052905; F:tRNA (guanine(9)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; ISO:MGI.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0000964; P:mitochondrial RNA 5'-end processing; ISS:UniProtKB.
DR GO; GO:1990180; P:mitochondrial tRNA 3'-end processing; ISO:MGI.
DR GO; GO:0097745; P:mitochondrial tRNA 5'-end processing; ISS:UniProtKB.
DR GO; GO:0070901; P:mitochondrial tRNA methylation; ISO:MGI.
DR GO; GO:0090646; P:mitochondrial tRNA processing; ISS:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR025812; TRM10C.
DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR13563; PTHR13563; 1.
DR PANTHER; PTHR13563:SF5; PTHR13563:SF5; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Methyltransferase; Mitochondrion; Mitochondrion nucleoid;
KW Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase;
KW Transit peptide; tRNA processing.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..414
FT /note="tRNA methyltransferase 10 homolog C"
FT /id="PRO_0000311310"
FT DOMAIN 186..378
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT COILED 133..171
FT /evidence="ECO:0000255"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 40
FT /note="A -> T (in Ref. 1; BAE28421)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="D -> E (in Ref. 1; BAE28421)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="A -> V (in Ref. 1; BAE28421)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="E -> G (in Ref. 1; BAE28421)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="I -> L (in Ref. 1; BAE28421)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="N -> S (in Ref. 2; AAI06132/AAH23147)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="N -> S (in Ref. 1; BAE28421)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="V -> A (in Ref. 1; BAE28421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 48386 MW; A48979421D1E7038 CRC64;
MNVTVRFLRP FARCLVPYTF HRKRSHLYSG VLQRYMSSKA PSLSCHNKDS ASPPEQLELD
GWKATMKSSI QEDGVSEVSD KDEDSLASTR ELIEMWRLLG KEVPEHITEE DLKTLMECAS
KSAKKKYLRY LYGKEKAKKA KQVKKEMKAE AREEAKRARL LETTAEEQQQ DFMFLRLWDR
QINIALGWKG VQAMQFGQPL VFDMAYDNYM KPSELQNTVS QLLESEGWNR RNVDPFHIYF
CNLKIDSAYH RELVKRYREK WDKLLLTATE KSPVDLFPKD SIIYLTADSP NVMTTFKHDK
IYIIGSFVDK NTQTGTSLAK AKRLNIATEC LPLDKYLQWE IGNKNLTLDQ MIRILLCLKN
TGNWEEALKF VPRRKHTGYL EVSEQSQELV RKLKKTKTLN SFRKGSLNVR TWKR
