NSUN3_MOUSE
ID NSUN3_MOUSE Reviewed; 348 AA.
AC Q8CCT7; Q3TE43;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=tRNA (cytosine(34)-C(5))-methyltransferase, mitochondrial {ECO:0000250|UniProtKB:Q9H649};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9H649};
DE AltName: Full=NOL1/NOP2/Sun domain family member 3 {ECO:0000312|MGI:MGI:2146565};
GN Name=Nsun3 {ECO:0000312|MGI:MGI:2146565};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Medulla oblongata, 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] (ISOFORM 1).
RC TISSUE=Brain;
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: Mitochondrial tRNA methyltransferase that mediates
CC methylation of cytosine to 5-methylcytosine (m5C) at position 34 of mt-
CC tRNA(Met). mt-tRNA(Met) methylation at cytosine(34) takes place at the
CC wobble position of the anticodon and initiates the formation of 5-
CC formylcytosine (f(5)c) at this position. mt-tRNA(Met) containing the
CC f(5)c modification at the wobble position enables recognition of the
CC AUA codon in addition to the AUG codon, expanding codon recognition in
CC mitochondrial translation. {ECO:0000250|UniProtKB:Q9H649}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(34) in mitochondrial tRNA + S-adenosyl-L-methionine =
CC 5-methylcytidine(34) in mitochondrial tRNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:53076, Rhea:RHEA-COMP:13451, Rhea:RHEA-
CC COMP:13453, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:Q9H649};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53077;
CC Evidence={ECO:0000250|UniProtKB:Q9H649};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9H649}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CCT7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CCT7-2; Sequence=VSP_025970;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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DR EMBL; AK032127; BAC27717.1; -; mRNA.
DR EMBL; AK153942; BAE32268.1; -; mRNA.
DR EMBL; AK169841; BAE41405.1; -; mRNA.
DR EMBL; BC125628; AAI25629.1; -; mRNA.
DR EMBL; BC125630; AAI25631.1; -; mRNA.
DR CCDS; CCDS37373.1; -. [Q8CCT7-1]
DR RefSeq; NP_849256.1; NM_178925.3. [Q8CCT7-1]
DR AlphaFoldDB; Q8CCT7; -.
DR SMR; Q8CCT7; -.
DR STRING; 10090.ENSMUSP00000059720; -.
DR PhosphoSitePlus; Q8CCT7; -.
DR EPD; Q8CCT7; -.
DR PaxDb; Q8CCT7; -.
DR PRIDE; Q8CCT7; -.
DR ProteomicsDB; 252858; -. [Q8CCT7-1]
DR ProteomicsDB; 252859; -. [Q8CCT7-2]
DR Antibodypedia; 32087; 126 antibodies from 20 providers.
DR DNASU; 106338; -.
DR Ensembl; ENSMUST00000063089; ENSMUSP00000059720; ENSMUSG00000050312. [Q8CCT7-1]
DR GeneID; 106338; -.
DR KEGG; mmu:106338; -.
DR UCSC; uc007zps.1; mouse. [Q8CCT7-1]
DR UCSC; uc007zpt.2; mouse. [Q8CCT7-2]
DR CTD; 63899; -.
DR MGI; MGI:2146565; Nsun3.
DR VEuPathDB; HostDB:ENSMUSG00000050312; -.
DR eggNOG; KOG2198; Eukaryota.
DR GeneTree; ENSGT00940000153665; -.
DR HOGENOM; CLU_041061_1_0_1; -.
DR InParanoid; Q8CCT7; -.
DR OMA; KAWGPMF; -.
DR OrthoDB; 1239772at2759; -.
DR PhylomeDB; Q8CCT7; -.
DR TreeFam; TF321304; -.
DR BioGRID-ORCS; 106338; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Nsun3; mouse.
DR PRO; PR:Q8CCT7; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8CCT7; protein.
DR Bgee; ENSMUSG00000050312; Expressed in animal zygote and 233 other tissues.
DR ExpressionAtlas; Q8CCT7; baseline and differential.
DR Genevisible; Q8CCT7; MM.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070129; P:regulation of mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR GO; GO:0002127; P:tRNA wobble base cytosine methylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; PTHR22808; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Methyltransferase; Mitochondrion; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA-binding.
FT CHAIN 1..348
FT /note="tRNA (cytosine(34)-C(5))-methyltransferase,
FT mitochondrial"
FT /id="PRO_0000289231"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 139..145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 193
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT VAR_SEQ 1..196
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025970"
SQ SEQUENCE 348 AA; 39182 MW; 0018E6C33BCFE145 CRC64;
MLTRLKAKSE GKLAKQLCRV VLDQFDKQYS KELGDSWSTV RDVLISPSLW QYAILFNRFN
YPFELEKALH LRGYHTVLQG ALPHYPKSMK CYLSRTPDRM PSERHQTGSL KKYYLLNAAS
LLPVLALELR DGEAVLDLCA APGGKSVALL QCAYPGYLLC NEYDRPRGRW LRQTLESFIP
QPLINVIKVS ELDGREMGDA QPATFDKVLV DAPCSNDRSW LFSSDSQKAA YRIHQRKNLP
VLQVELVRSA IKALRPGGLL VYSTCTLSKA ENQDVISEVL TSDSNIVPVD ISGIARTFSQ
DFTFAPTDQK CSLLVIPEKG KAWGPMYIAK LKKGMSTRKR QGEFCKPC
