MTNA_MOUSE
ID MTNA_MOUSE Reviewed; 369 AA.
AC Q9CQT1; Q8BXF6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE Short=M1Pi {ECO:0000255|HAMAP-Rule:MF_03119};
DE Short=MTR-1-P isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE EC=5.3.1.23 {ECO:0000255|HAMAP-Rule:MF_03119};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE AltName: Full=Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein {ECO:0000255|HAMAP-Rule:MF_03119};
GN Name=Mri1;
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=Cerebellum, Head, and Lung;
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=Mammary tumor;
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, Heart, Kidney, Liver, Lung, Pancreas, 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).
RN [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-158, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC {ECO:0000255|HAMAP-Rule:MF_03119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-
CC D-ribulose 1-phosphate; Xref=Rhea:RHEA:19989, ChEBI:CHEBI:58533,
CC ChEBI:CHEBI:58548; EC=5.3.1.23; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03119};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 1/6. {ECO:0000255|HAMAP-Rule:MF_03119}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03119}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03119}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000255|HAMAP-Rule:MF_03119}.
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DR EMBL; AK010538; BAB27014.1; -; mRNA.
DR EMBL; AK013882; BAB29034.1; -; mRNA.
DR EMBL; AK164894; BAE37957.1; -; mRNA.
DR EMBL; AK047287; BAC33016.1; -; mRNA.
DR EMBL; BC025049; AAH25049.1; -; mRNA.
DR CCDS; CCDS22473.1; -.
DR RefSeq; NP_080699.3; NM_026423.4.
DR AlphaFoldDB; Q9CQT1; -.
DR SMR; Q9CQT1; -.
DR BioGRID; 212500; 2.
DR STRING; 10090.ENSMUSP00000122623; -.
DR iPTMnet; Q9CQT1; -.
DR PhosphoSitePlus; Q9CQT1; -.
DR EPD; Q9CQT1; -.
DR jPOST; Q9CQT1; -.
DR MaxQB; Q9CQT1; -.
DR PaxDb; Q9CQT1; -.
DR PeptideAtlas; Q9CQT1; -.
DR PRIDE; Q9CQT1; -.
DR ProteomicsDB; 290215; -.
DR Antibodypedia; 26489; 235 antibodies from 26 providers.
DR Ensembl; ENSMUST00000126435; ENSMUSP00000122623; ENSMUSG00000004996.
DR GeneID; 67873; -.
DR KEGG; mmu:67873; -.
DR UCSC; uc009mmi.2; mouse.
DR CTD; 84245; -.
DR MGI; MGI:1915123; Mri1.
DR VEuPathDB; HostDB:ENSMUSG00000004996; -.
DR eggNOG; KOG1468; Eukaryota.
DR GeneTree; ENSGT00390000013732; -.
DR HOGENOM; CLU_016218_1_3_1; -.
DR InParanoid; Q9CQT1; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 1410886at2759; -.
DR PhylomeDB; Q9CQT1; -.
DR TreeFam; TF300852; -.
DR Reactome; R-MMU-1237112; Methionine salvage pathway.
DR UniPathway; UPA00904; UER00874.
DR BioGRID-ORCS; 67873; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Mri1; mouse.
DR PRO; PR:Q9CQT1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9CQT1; protein.
DR Bgee; ENSMUSG00000004996; Expressed in right kidney and 229 other tissues.
DR ExpressionAtlas; Q9CQT1; baseline and differential.
DR Genevisible; Q9CQT1; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.420; -; 1.
DR Gene3D; 3.40.50.10470; -; 1.
DR HAMAP; MF_01678; Salvage_MtnA; 1.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR005251; IF-M1Pi.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR InterPro; IPR027363; M1Pi_N.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR TIGRFAMs; TIGR00512; salvage_mtnA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Cytoplasm; Isomerase;
KW Methionine biosynthesis; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..369
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000317326"
FT ACT_SITE 248
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT SITE 168
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV20"
FT MOD_RES 158
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5HZE4"
FT CONFLICT 168
FT /note="C -> L (in Ref. 1; BAC33016)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="E -> D (in Ref. 1; BAC33016)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="R -> Q (in Ref. 1; BAC33016)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="T -> S (in Ref. 1; BAC33016)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 39411 MW; 5DEA57F8E4AE99E0 CRC64;
MTLEAIRYSP GSLQILDQLQ LPEHCHYEAL SSVQQASEAI RAMKVRGAPA IALVGCLSLA
VELRAGAGGP GLAALVAFVR DQLRLLVAAR PTAVNMARAA RDLGQVAAQE AEREGATEET
VRERVIRFAE DMLEKDLKDN RSIGDLGARH LLEQTNPRGG KVTVLTHCNT GALATAGYGT
ALGVIRSLHE MGRLEHTFCT ETRPYNQGAR LTAFELVYEQ IPATLITDSM AAAAMAHRGV
SAVVVGADRV VANGDTANKI GTYQLAIVAK HHGVPFYVAA PSSSCDLHLE TGKEIVIEER
PSQELTDLNG VRIAAQGIRV WNPAFDVTPH ELITGGIITE LGVFAPEELR GALSASVFSE
GQTLDSPWV
