MRES1_MOUSE
ID MRES1_MOUSE Reviewed; 240 AA.
AC Q9CQF4; Q3TQU4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Mitochondrial transcription rescue factor 1;
DE Flags: Precursor;
GN Name=Mtres1;
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=Egg, Pancreas, Stomach, and Testis;
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].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-116, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Mitochondrial RNA-binding protein involved in mitochondrial
CC transcription regulation. Functions as a protective factor to maintain
CC proper mitochondrial RNA level during stress. Acts at the transcription
CC level and its protective function depends on its RNA binding ability.
CC Part of a mitoribosome-associated quality control pathway that prevents
CC aberrant translation by responding to interruptions during elongation.
CC As heterodimer with MTRF, ejects the unfinished nascent chain and
CC peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes.
CC Recruitment of mitoribosome biogenesis factors to these quality control
CC intermediates suggests additional roles for MTRES1 and MTRF during
CC mitoribosome rescue. {ECO:0000250|UniProtKB:Q9P0P8}.
CC -!- SUBUNIT: Monomer. Interacts with POLRMT. Interacts (via S4 domain) with
CC MTRFR (via C-terminus). Associates with mitoribosomal S39 large
CC subunit, peptidyl tRNA and nascent chain.
CC {ECO:0000250|UniProtKB:Q9P0P8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9P0P8}.
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DR EMBL; AK006199; BAB24454.1; -; mRNA.
DR EMBL; AK007370; BAB24992.1; -; mRNA.
DR EMBL; AK008795; BAB25900.1; -; mRNA.
DR EMBL; AK163304; BAE37288.1; -; mRNA.
DR EMBL; BC013506; AAH13506.1; -; mRNA.
DR CCDS; CCDS23820.1; -.
DR RefSeq; NP_080687.1; NM_026411.1.
DR RefSeq; XP_006512896.1; XM_006512833.3.
DR RefSeq; XP_006512897.1; XM_006512834.3.
DR RefSeq; XP_017169558.1; XM_017314069.1.
DR AlphaFoldDB; Q9CQF4; -.
DR SMR; Q9CQF4; -.
DR BioGRID; 212481; 3.
DR STRING; 10090.ENSMUSP00000019932; -.
DR iPTMnet; Q9CQF4; -.
DR PhosphoSitePlus; Q9CQF4; -.
DR EPD; Q9CQF4; -.
DR jPOST; Q9CQF4; -.
DR MaxQB; Q9CQF4; -.
DR PaxDb; Q9CQF4; -.
DR PeptideAtlas; Q9CQF4; -.
DR PRIDE; Q9CQF4; -.
DR Antibodypedia; 55873; 84 antibodies from 15 providers.
DR DNASU; 67851; -.
DR Ensembl; ENSMUST00000147196; ENSMUSP00000119053; ENSMUSG00000019797.
DR GeneID; 67851; -.
DR KEGG; mmu:67851; -.
DR UCSC; uc007ezk.1; mouse.
DR CTD; 51250; -.
DR MGI; MGI:1915101; Mtres1.
DR VEuPathDB; HostDB:ENSMUSG00000019797; -.
DR eggNOG; KOG4837; Eukaryota.
DR GeneTree; ENSGT00390000009366; -.
DR HOGENOM; CLU_076117_0_0_1; -.
DR InParanoid; Q9CQF4; -.
DR OMA; VHHLRFK; -.
DR OrthoDB; 1440120at2759; -.
DR PhylomeDB; Q9CQF4; -.
DR TreeFam; TF323798; -.
DR BioGRID-ORCS; 67851; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9CQF4; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CQF4; protein.
DR Bgee; ENSMUSG00000019797; Expressed in motor neuron and 261 other tissues.
DR Genevisible; Q9CQF4; MM.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043023; F:ribosomal large subunit binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:1903108; P:regulation of mitochondrial transcription; ISS:UniProtKB.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR InterPro; IPR039167; MTRES1.
DR PANTHER; PTHR13633; PTHR13633; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transit peptide.
FT TRANSIT 1..83
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q9P0P8"
FT CHAIN 84..240
FT /note="Mitochondrial transcription rescue factor 1"
FT /id="PRO_0000089560"
FT DOMAIN 142..217
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9P0P8,
FT ECO:0000255|PROSITE-ProRule:PRU00182"
FT REGION 92..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..121
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 240 AA; 27847 MW; 92A79152831F27BB CRC64;
MAVPGVRLLT GALRKPDAWT RLWGVIQGTS SHKLCASWNR YLYFSSTKLN TSNYKTLFRN
IFSLRLPELL VSPECYFPFS IRLKSNINSK KSTKKTLQKE ADEEDSDEET SYPERSEQEE
ELESEPGVAK DYKDLEKVVQ SFRYDVILKT GLDVGRNKVE DAFYKGELRL NGEKLWKKSR
TVKVGDTLDL ITGENKETGT EVVMRILLKK VYEEKTENDK HRVVLRRWKS LKLPKKTLSK
