ID   MTO1_MOUSE              Reviewed;         669 AA.
AC   Q923Z3; Q9D2Q5;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Protein MTO1 homolog, mitochondrial;
DE   Flags: Precursor;
GN   Name=Mto1;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=14522080; DOI=10.1016/s0167-4781(03)00160-x;
RA   Li R.-H., Li X.-M., Yan Q.-F., Mo J.Q., Guan M.-X.;
RT   "Identification and characterization of mouse MTO1 gene related to
RT   mitochondrial tRNA modification.";
RL   Biochim. Biophys. Acta 1629:53-59(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=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).
CC   -!- FUNCTION: Involved in the 5-carboxymethylaminomethyl modification
CC       (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
CC       {ECO:0000269|PubMed:14522080}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14522080}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in various tissues, but with
CC       markedly elevated expression in tissues of high metabolic rates.
CC       {ECO:0000269|PubMed:14522080}.
CC   -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000305}.
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DR   EMBL; AF369902; AAK63070.1; -; mRNA.
DR   EMBL; AK019088; BAB31540.1; -; mRNA.
DR   CCDS; CCDS23363.1; -.
DR   RefSeq; NP_080934.2; NM_026658.2.
DR   AlphaFoldDB; Q923Z3; -.
DR   SMR; Q923Z3; -.
DR   BioGRID; 212787; 1.
DR   STRING; 10090.ENSMUSP00000034896; -.
DR   iPTMnet; Q923Z3; -.
DR   PhosphoSitePlus; Q923Z3; -.
DR   MaxQB; Q923Z3; -.
DR   PaxDb; Q923Z3; -.
DR   PRIDE; Q923Z3; -.
DR   ProteomicsDB; 290113; -.
DR   DNASU; 68291; -.
DR   GeneID; 68291; -.
DR   KEGG; mmu:68291; -.
DR   CTD; 25821; -.
DR   MGI; MGI:1915541; Mto1.
DR   eggNOG; KOG2311; Eukaryota.
DR   InParanoid; Q923Z3; -.
DR   OrthoDB; 1437708at2759; -.
DR   PhylomeDB; Q923Z3; -.
DR   BioGRID-ORCS; 68291; 13 hits in 70 CRISPR screens.
DR   ChiTaRS; Mto1; mouse.
DR   PRO; PR:Q923Z3; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q923Z3; protein.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0070899; P:mitochondrial tRNA wobble uridine modification; IGI:MGI.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IGI:MGI.
DR   Gene3D; 1.10.150.570; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_00129; MnmG_GidA; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004416; MnmG.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   InterPro; IPR026904; MnmG_C.
DR   InterPro; IPR044920; MnmG_C_subdom.
DR   InterPro; IPR040131; MnmG_N.
DR   PANTHER; PTHR11806; PTHR11806; 1.
DR   PANTHER; PTHR11806:SF0; PTHR11806:SF0; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00136; gidA; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Methylation; Mitochondrion; Reference proteome;
KW   Transit peptide; tRNA processing.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..669
FT                   /note="Protein MTO1 homolog, mitochondrial"
FT                   /id="PRO_0000042690"
FT   BINDING         42..47
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         507
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Z2"
FT   CONFLICT        602
FT                   /note="Q -> H (in Ref. 2; BAB31540)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   669 AA;  74332 MW;  4DE2FFD8DE754FF7 CRC64;
     MFLLRGRGHW AAASLGRRLP LRRLRSDSAA PCTPHFDVVV IGGGHAGTEA AAAAARCGSR
     TLLLTHRVDT IGQMSCNPSF GGIGKGHLMR EVDALDGLCS RICDQSGIHY KVLNRRKGPA
     VWGLRAQIDR KLYKQNMQKE ILSTPLLTVQ KGAVEDLVLA EPEPGYPGKS RVRGVVLADG
     STIYAESVIL TTGTFLRGMI IIGLEMHPAG RLGDQPSIGL AQTLEKLGFM VGRLKTGTPP
     RLGKESINFS ILNKHTPDDP SIPFSFLSDS VWIKPEDQLP CYLTHTNPRV DAIVLENLHL
     NSHVQETTKG PRYCPSIESK VLRFPNRLHQ VWLEPEGMDS DLIYPQGLSV TLPAELQEKM
     ITCIRGLEKA KMVHPGYGVQ YDYLDPRQIS PSLETHLVQR LFFAGQINGT TGYEEAAAQG
     VIAGINASLR VSRKPPFVVS RTEGYIGVLI DDLTTLGTSE PYRMFTSRVE FRLSLRPDNA
     DTRLTFRAHK EAGCVSSQRF ERALWMKSSL EEGISVLKSI KFSSSKWKKL IPQIPISINR
     SLPVSALDVL KYEEVDMESL VGVLPEPLEK YTACRELARR LKIEASYESV LSYQLQEIKE
     VQQDEALQLP HELDYLTIRD VSLSQEVREK LHLSRPQTIG AASRIPGVTP AAIINLLRFV
     RSTRQSRQQ