MRM2_MOUSE
ID MRM2_MOUSE Reviewed; 246 AA.
AC Q9CPY0;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=rRNA methyltransferase 2, mitochondrial {ECO:0000303|PubMed:24036117};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9UI43};
DE AltName: Full=16S rRNA (uridine(1369)-2'-O)-methyltransferase {ECO:0000250|UniProtKB:Q9UI43};
DE AltName: Full=16S rRNA [Um1369] 2'-O-methyltransferase {ECO:0000250|UniProtKB:Q9UI43};
DE AltName: Full=Protein ftsJ homolog 2 {ECO:0000250|UniProtKB:Q9UI43};
DE Flags: Precursor;
GN Name=Mrm2 {ECO:0000303|PubMed:24036117};
GN Synonyms=Ftsj2 {ECO:0000312|MGI:MGI:1915267};
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=Head, Testis, and Tongue;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CD-1; TISSUE=Neural stem cell;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
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).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=24036117; DOI=10.1074/jbc.m113.515692;
RA Lee K.W., Okot-Kotber C., LaComb J.F., Bogenhagen D.F.;
RT "Mitochondrial ribosomal RNA (rRNA) methyltransferase family members are
RT positioned to modify nascent rRNA in foci near the mitochondrial DNA
RT nucleoid.";
RL J. Biol. Chem. 288:31386-31399(2013).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose
CC methyltransferase that catalyzes the formation of 2'-O-methyluridine at
CC position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal
CC RNA (mtLSU rRNA), a universally conserved modification in the peptidyl
CC transferase domain of the mtLSU rRNA. {ECO:0000250|UniProtKB:Q9UI43}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(1369) in 16S rRNA = 2'-O-
CC methyluridine(1369) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47764, Rhea:RHEA-COMP:11903, Rhea:RHEA-COMP:11904,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478;
CC Evidence={ECO:0000250|UniProtKB:Q9UI43};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24036117}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. {ECO:0000305}.
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DR EMBL; AK009656; BAB26420.1; -; mRNA.
DR EMBL; AK017300; BAB30680.1; -; mRNA.
DR EMBL; AK077929; BAC37070.1; -; mRNA.
DR EMBL; AK145808; BAE26662.1; -; mRNA.
DR EMBL; CH466529; EDL19124.1; -; Genomic_DNA.
DR EMBL; BC064776; AAH64776.1; -; mRNA.
DR CCDS; CCDS39355.1; -.
DR RefSeq; NP_080786.1; NM_026510.1.
DR AlphaFoldDB; Q9CPY0; -.
DR SMR; Q9CPY0; -.
DR BioGRID; 212599; 1.
DR STRING; 10090.ENSMUSP00000031536; -.
DR PhosphoSitePlus; Q9CPY0; -.
DR EPD; Q9CPY0; -.
DR MaxQB; Q9CPY0; -.
DR PaxDb; Q9CPY0; -.
DR PeptideAtlas; Q9CPY0; -.
DR PRIDE; Q9CPY0; -.
DR ProteomicsDB; 291444; -.
DR Antibodypedia; 24314; 67 antibodies from 16 providers.
DR Ensembl; ENSMUST00000031536; ENSMUSP00000031536; ENSMUSG00000029557.
DR GeneID; 68017; -.
DR KEGG; mmu:68017; -.
DR UCSC; uc009ahm.1; mouse.
DR CTD; 29960; -.
DR MGI; MGI:1915267; Mrm2.
DR VEuPathDB; HostDB:ENSMUSG00000029557; -.
DR eggNOG; KOG4589; Eukaryota.
DR GeneTree; ENSGT00730000111241; -.
DR HOGENOM; CLU_009422_4_2_1; -.
DR InParanoid; Q9CPY0; -.
DR OMA; HRQTDHL; -.
DR OrthoDB; 1039414at2759; -.
DR PhylomeDB; Q9CPY0; -.
DR TreeFam; TF316701; -.
DR BioGRID-ORCS; 68017; 19 hits in 73 CRISPR screens.
DR PRO; PR:Q9CPY0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CPY0; protein.
DR Bgee; ENSMUSG00000029557; Expressed in right kidney and 205 other tissues.
DR Genevisible; Q9CPY0; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; ISO:MGI.
DR GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; ISO:MGI.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; NAS:BHF-UCL.
DR GO; GO:0006364; P:rRNA processing; NAS:BHF-UCL.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01728; FtsJ; 1.
DR PIRSF; PIRSF005461; 23S_rRNA_mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Mitochondrion; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..246
FT /note="rRNA methyltransferase 2, mitochondrial"
FT /id="PRO_0000391771"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0C0R7"
FT BINDING 83..86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 129..130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
SQ SEQUENCE 246 AA; 27145 MW; EAC621A13628FE1A CRC64;
MAGHLKLVGV PLKVRRLHTA VCHYRGRTGA EHLWLTRHLK DPFVKAAKVE SYRCRSAFKL
LEMNEKHQIL RPGLRVLDCG AAPGAWSQVA VQRVNATGAD SSSPVGFVLG VDLLHIFPLA
GATFLCPADV TDPRTFQKIL ELLPSRRADV ILSDMAPNAT GIRDLDHDKL ISLCLTLVDM
AVDILHPGGT LLCKTWAGSK SHLLQKRLTQ EFQSTRVVKP EASRKESSEV YLLATQYRGG
KGTRRP
