MRM3_MOUSE
ID MRM3_MOUSE Reviewed; 418 AA.
AC Q5ND52; A4FUR4; Q3UGQ7; Q5U5W2; Q8C1J9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=rRNA methyltransferase 3, mitochondrial {ECO:0000250|UniProtKB:Q9HC36};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9HC36};
DE AltName: Full=16S rRNA (guanosine(1370)-2'-O)-methyltransferase {ECO:0000250|UniProtKB:Q9HC36};
DE AltName: Full=16S rRNA [Gm1370] 2'-O-methyltransferase {ECO:0000250|UniProtKB:Q9HC36};
DE AltName: Full=RNA methyltransferase-like protein 1 {ECO:0000250|UniProtKB:Q9HC36};
DE Flags: Precursor;
GN Name=Mrm3 {ECO:0000250|UniProtKB:Q9HC36};
GN Synonyms=Rnmtl1 {ECO:0000312|MGI:MGI:1914640};
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;
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 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-methylguanosine
CC at position 1370 (Gm1370) in the 16S mitochondrial large subunit
CC ribosomal RNA (mtLSU rRNA), a conserved modification in the peptidyl
CC transferase domain of the mtLSU rRNA. {ECO:0000250|UniProtKB:Q9HC36}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(1370) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-
CC methylguanosine(1370) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47756, Rhea:RHEA-COMP:11899, Rhea:RHEA-COMP:11900,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74445;
CC Evidence={ECO:0000250|UniProtKB:Q9HC36};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24036117}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH38288.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH90975.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI15623.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI15624.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC25446.1; Type=Frameshift; Evidence={ECO:0000305};
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; AK014739; BAC25446.1; ALT_FRAME; mRNA.
DR EMBL; AK147805; BAE28150.1; -; mRNA.
DR EMBL; AL591129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038288; AAH38288.1; ALT_INIT; mRNA.
DR EMBL; BC090975; AAH90975.2; ALT_INIT; mRNA.
DR EMBL; BC115622; AAI15623.1; ALT_INIT; mRNA.
DR EMBL; BC115623; AAI15624.1; ALT_INIT; mRNA.
DR CCDS; CCDS48852.1; -.
DR RefSeq; NP_899086.2; NM_183263.5.
DR AlphaFoldDB; Q5ND52; -.
DR SMR; Q5ND52; -.
DR BioGRID; 212154; 3.
DR STRING; 10090.ENSMUSP00000042882; -.
DR iPTMnet; Q5ND52; -.
DR PhosphoSitePlus; Q5ND52; -.
DR EPD; Q5ND52; -.
DR MaxQB; Q5ND52; -.
DR PaxDb; Q5ND52; -.
DR PeptideAtlas; Q5ND52; -.
DR PRIDE; Q5ND52; -.
DR ProteomicsDB; 291510; -.
DR Antibodypedia; 10311; 108 antibodies from 21 providers.
DR DNASU; 67390; -.
DR Ensembl; ENSMUST00000040577; ENSMUSP00000042882; ENSMUSG00000038046.
DR GeneID; 67390; -.
DR KEGG; mmu:67390; -.
DR UCSC; uc007kfn.2; mouse.
DR CTD; 55178; -.
DR MGI; MGI:1914640; Mrm3.
DR VEuPathDB; HostDB:ENSMUSG00000038046; -.
DR eggNOG; KOG2506; Eukaryota.
DR GeneTree; ENSGT00390000017317; -.
DR HOGENOM; CLU_021322_1_0_1; -.
DR InParanoid; Q5ND52; -.
DR OMA; ERKRAPG; -.
DR OrthoDB; 1183644at2759; -.
DR PhylomeDB; Q5ND52; -.
DR TreeFam; TF323420; -.
DR BioGRID-ORCS; 67390; 8 hits in 72 CRISPR screens.
DR PRO; PR:Q5ND52; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5ND52; protein.
DR Bgee; ENSMUSG00000038046; Expressed in digastric muscle group and 250 other tissues.
DR Genevisible; Q5ND52; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; ISO:MGI.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR013123; SpoU_subst-bd.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR Pfam; PF00588; SpoU_methylase; 1.
DR SMART; SM00967; SpoU_sub_bind; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Mitochondrion; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 41..418
FT /note="rRNA methyltransferase 3, mitochondrial"
FT /id="PRO_0000311302"
FT REGION 41..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT CONFLICT 102
FT /note="R -> K (in Ref. 3; AAH38288/AAI15624/AAI15623)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="P -> L (in Ref. 3; AAH38288/AAI15624/AAI15623)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="A -> V (in Ref. 1; BAE28150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46796 MW; 54E4A589B436141B CRC64;
MAAPAKGMWC SLGSLLRVVQ TRDLNARRWV RALRRSPVRV LSPSGQVEER KRAPDQQPRK
AVPKASSQGQ RQKQPLETSP SQTPHTWEEA GLRYDKAFPG DRRLSSVMTI VKSRPFREKQ
GKILLEGRRL IADALKAGAV PKAFFFSRLE YVKELPVDKL KDVSLIKVKF EDIKDWSDLV
TPQGIMGIFA KPDPVKMTYP ETPLHHTLPL VLICDNLRDP GNLGTILRSA AGAGCSKVLL
TKGCVDAWEP KVLRAGMGAH FQVPIVNNVE WETVPNHLPP DTRVYVADNC GHYAQVQMSD
KTGDRDWACD RRFLKFHKYE EDLDTKTRKD WLPKLEVQSY DLDWTGAPAA VVIGGETHGV
SLESLQLAES TGGKRLLIPV VPGVDSLNSA MAASILLFEG KRQLRIKVED LSRDRSYH
