MTU1_MOUSE
ID MTU1_MOUSE Reviewed; 417 AA.
AC Q9DAT5;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Mitochondrial tRNA-specific 2-thiouridylase 1;
DE EC=2.8.1.14 {ECO:0000250|UniProtKB:Q12093};
GN Name=Trmu; Synonyms=Mtu1, Trmt1;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14746906; DOI=10.1016/j.bbaexp.2003.11.010;
RA Yan Q., Guan M.-X.;
RT "Identification and characterization of mouse TRMU gene encoding the
RT mitochondrial 5-methylaminomethyl-2-thiouridylate-methyltransferase.";
RL Biochim. Biophys. Acta 1676:119-126(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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, Heart, Liver, Pancreas, 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: Catalyzes the 2-thiolation of uridine at the wobble position
CC (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for
CC the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of
CC mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble
CC position. ATP is required to activate the C2 atom of the wobble base.
CC {ECO:0000250|UniProtKB:O75648}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-
CC cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A +
CC AMP + diphosphate + H(+) + L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:47040, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11726,
CC Rhea:RHEA-COMP:11732, Rhea:RHEA-COMP:11733, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:61963,
CC ChEBI:CHEBI:87171, ChEBI:CHEBI:87172, ChEBI:CHEBI:456215;
CC EC=2.8.1.14; Evidence={ECO:0000250|UniProtKB:Q12093};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14746906}.
CC -!- TISSUE SPECIFICITY: Widely expressed but most abundant in tissues with
CC high metabolic rate including heart, liver and brain. Expression is low
CC in spleen, testis, lung and skeletal muscle. Also expressed in inner
CC ear. {ECO:0000269|PubMed:14746906}.
CC -!- MISCELLANEOUS: During the reaction, ATP is used to activate the C2 atom
CC of U34 by adenylation. After this, the persulfide sulfur on the
CC catalytic cysteine is transferred to the C2 atom of the wobble base
CC (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). The reaction
CC probably involves hydrogen sulfide that is generated from the
CC persulfide intermediate and that acts as nucleophile towards the
CC activated C2 atom on U34. Subsequently, a transient disulfide bond is
CC formed between the two active site cysteine residues (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a 5-methylaminomethyl-2-
CC methyltransferase involved in tRNA modification.
CC {ECO:0000305|PubMed:14746906}.
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DR EMBL; AY349617; AAQ55218.1; -; mRNA.
DR EMBL; AK005541; BAB24110.1; -; mRNA.
DR EMBL; AK043532; BAC31570.1; -; mRNA.
DR EMBL; AK044059; BAC31758.1; -; mRNA.
DR EMBL; BC061026; AAH61026.1; -; mRNA.
DR CCDS; CCDS27726.1; -.
DR RefSeq; NP_082339.1; NM_028063.2.
DR AlphaFoldDB; Q9DAT5; -.
DR SMR; Q9DAT5; -.
DR STRING; 10090.ENSMUSP00000023019; -.
DR iPTMnet; Q9DAT5; -.
DR PhosphoSitePlus; Q9DAT5; -.
DR EPD; Q9DAT5; -.
DR MaxQB; Q9DAT5; -.
DR PaxDb; Q9DAT5; -.
DR PeptideAtlas; Q9DAT5; -.
DR PRIDE; Q9DAT5; -.
DR ProteomicsDB; 290220; -.
DR Antibodypedia; 28061; 187 antibodies from 18 providers.
DR Ensembl; ENSMUST00000023019; ENSMUSP00000023019; ENSMUSG00000022386.
DR GeneID; 72026; -.
DR KEGG; mmu:72026; -.
DR UCSC; uc007xdr.1; mouse.
DR CTD; 55687; -.
DR MGI; MGI:1919276; Trmu.
DR VEuPathDB; HostDB:ENSMUSG00000022386; -.
DR eggNOG; KOG2805; Eukaryota.
DR GeneTree; ENSGT00390000014323; -.
DR HOGENOM; CLU_035188_1_1_1; -.
DR InParanoid; Q9DAT5; -.
DR OMA; AVCTGHY; -.
DR OrthoDB; 697006at2759; -.
DR PhylomeDB; Q9DAT5; -.
DR TreeFam; TF105611; -.
DR BRENDA; 2.1.1.61; 3474.
DR BioGRID-ORCS; 72026; 25 hits in 74 CRISPR screens.
DR PRO; PR:Q9DAT5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9DAT5; protein.
DR Bgee; ENSMUSG00000022386; Expressed in retinal neural layer and 224 other tissues.
DR ExpressionAtlas; Q9DAT5; baseline and differential.
DR Genevisible; Q9DAT5; MM.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061708; F:tRNA-5-taurinomethyluridine 2-sulfurtransferase; IEA:RHEA.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
DR CDD; cd01998; tRNA_Me_trans; 1.
DR Gene3D; 2.30.30.280; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1.
DR InterPro; IPR023382; Adenine_a_hdrlase_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR TIGRFAMs; TIGR00420; trmU; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; Mitochondrion; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..417
FT /note="Mitochondrial tRNA-specific 2-thiouridylase 1"
FT /id="PRO_0000121709"
FT REGION 96..98
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000250"
FT REGION 171..173
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 334..335
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 397..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 222
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 127
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 267
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 367
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT DISULFID 101..222
FT /evidence="ECO:0000250"
SQ SEQUENCE 417 AA; 47240 MW; 8B4F0E6F461953CE CRC64;
MSALRHVVCA LSGGVDSAVA ALLLRRRGYQ VTGVFMKNWD SLDEQGVCAA DKDCEDAYKV
CQILDIPFHQ VSYVKEYWND VFSDFLNEYE KGRTPNPDIN CNKHIKFSCF YHYAVDNLGA
DAVATGHYAR TSLEDEEVFE QKHTKKPDGL FRNRFEVRNP VKLLQAADSF KDQTFFLSQV
SQDALRRTIF PLGELTKDFV KKIAAENSLH HVLQKRESMG ICFIGKRNLE HFLLQYLQPR
PGKFVSIEDN TVLGTHKGWF LYTLGQRAKI SGLREPWYVV EKDGTKGDVL VAPRVDHPAL
YRDLLRTNRV HWIAEEPPAA LVRDKMMECH FRFRHQMALV PCVLTLNQDG TVWVTAVKAV
RGLALGQFAV FYKGEECLGS GKILRLGPSA YTLQKGKNRT RVAPEASSDS PGLHPTS
