MSRA_MOUSE
ID MSRA_MOUSE Reviewed; 233 AA.
AC Q9D6Y7; Q5EBQ7; Q91WK9; Q9DCY2;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Mitochondrial peptide methionine sulfoxide reductase;
DE EC=1.8.4.11 {ECO:0000269|PubMed:30529269};
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE Short=Peptide Met(O) reductase;
DE AltName: Full=Protein-methionine-S-oxide reductase;
DE Short=PMSR;
DE Flags: Precursor;
GN Name=Msra;
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 4).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord, and 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Kidney;
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 PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, ALTERNATIVE
RP SPLICING, AND SUBCELLULAR LOCATION.
RX PubMed=15924425; DOI=10.1021/bi0501131;
RA Kim H.Y., Gladyshev V.N.;
RT "Role of structural and functional elements of mouse methionine-S-sulfoxide
RT reductase in its subcellular distribution.";
RL Biochemistry 44:8059-8067(2005).
RN [5]
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).
RN [6]
RP MYRISTOYLATION AT GLY-2 (ISOFORM 2), AND ALTERNATIVE INITIATION.
RX PubMed=20368336; DOI=10.1074/jbc.m110.119701;
RA Kim G., Cole N.B., Lim J.C., Zhao H., Levine R.L.;
RT "Dual sites of protein initiation control the localization and
RT myristoylation of methionine sulfoxide reductase A.";
RL J. Biol. Chem. 285:18085-18094(2010).
RN [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-104 AND LYS-183, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104 AND LYS-183, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30529269; DOI=10.1016/j.freeradbiomed.2018.12.001;
RA Tarafdar S., Kim G., Levine R.L.;
RT "Drosophila methionine sulfoxide reductase A (MSRA) lacks methionine
RT oxidase activity.";
RL Free Radic. Biol. Med. 131:154-161(2019).
CC -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC that have been inactivated by oxidation. Catalyzes the reversible
CC oxidation-reduction of methionine sulfoxide in proteins to methionine.
CC {ECO:0000269|PubMed:30529269}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC ChEBI:CHEBI:50058; EC=1.8.4.11;
CC Evidence={ECO:0000269|PubMed:30529269};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58772; EC=1.8.4.11;
CC Evidence={ECO:0000269|PubMed:30529269};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus. Membrane; Lipid-
CC anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Comment=Only about 25% of mRNAs are initiated at the mitochondrial
CC isoform 1 codon. According to PubMed:15924425, differential
CC subcellular targeting is not due alternative initiation.
CC {ECO:0000269|PubMed:20368336};
CC Name=1;
CC IsoId=Q9D6Y7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D6Y7-2; Sequence=VSP_042133;
CC Name=3;
CC IsoId=Q9D6Y7-3; Sequence=VSP_041409;
CC Name=4;
CC IsoId=Q9D6Y7-4; Sequence=VSP_041408;
CC -!- MISCELLANEOUS: [Isoform 1]: Mitochondrial.
CC -!- MISCELLANEOUS: [Isoform 2]: Cytoplasmic. Produced by alternative
CC initiation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK002356; BAB22035.1; -; mRNA.
DR EMBL; AK009822; BAB26522.1; -; mRNA.
DR EMBL; AK049714; BAC33889.1; -; mRNA.
DR EMBL; AK018338; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH466535; EDL36048.1; -; Genomic_DNA.
DR EMBL; BC014738; AAH14738.1; -; mRNA.
DR EMBL; BC089311; AAH89311.1; -; mRNA.
DR CCDS; CCDS27209.1; -. [Q9D6Y7-1]
DR CCDS; CCDS84147.1; -. [Q9D6Y7-4]
DR RefSeq; NP_001240641.1; NM_001253712.1. [Q9D6Y7-1]
DR RefSeq; NP_001240643.1; NM_001253714.1.
DR RefSeq; NP_001240644.1; NM_001253715.1. [Q9D6Y7-3]
DR RefSeq; NP_001240645.1; NM_001253716.1. [Q9D6Y7-4]
DR RefSeq; NP_080598.2; NM_026322.4. [Q9D6Y7-1]
DR PDB; 2L90; NMR; -; A=22-233.
DR PDB; 6AGV; X-ray; 1.62 A; A=1-233.
DR PDBsum; 2L90; -.
DR PDBsum; 6AGV; -.
DR AlphaFoldDB; Q9D6Y7; -.
DR BMRB; Q9D6Y7; -.
DR SMR; Q9D6Y7; -.
DR IntAct; Q9D6Y7; 1.
DR MINT; Q9D6Y7; -.
DR STRING; 10090.ENSMUSP00000065754; -.
DR iPTMnet; Q9D6Y7; -.
DR PhosphoSitePlus; Q9D6Y7; -.
DR SwissPalm; Q9D6Y7; -.
DR EPD; Q9D6Y7; -.
DR jPOST; Q9D6Y7; -.
DR MaxQB; Q9D6Y7; -.
DR PaxDb; Q9D6Y7; -.
DR PeptideAtlas; Q9D6Y7; -.
DR PRIDE; Q9D6Y7; -.
DR ProteomicsDB; 291521; -. [Q9D6Y7-1]
DR ProteomicsDB; 291522; -. [Q9D6Y7-2]
DR ProteomicsDB; 291523; -. [Q9D6Y7-3]
DR ProteomicsDB; 291524; -. [Q9D6Y7-4]
DR Antibodypedia; 8418; 247 antibodies from 33 providers.
DR DNASU; 110265; -.
DR Ensembl; ENSMUST00000067927; ENSMUSP00000065754; ENSMUSG00000054733. [Q9D6Y7-1]
DR Ensembl; ENSMUST00000210428; ENSMUSP00000147689; ENSMUSG00000054733. [Q9D6Y7-4]
DR GeneID; 110265; -.
DR KEGG; mmu:110265; -.
DR UCSC; uc007uig.2; mouse. [Q9D6Y7-4]
DR UCSC; uc007uih.2; mouse. [Q9D6Y7-3]
DR UCSC; uc007uii.2; mouse. [Q9D6Y7-1]
DR CTD; 4482; -.
DR MGI; MGI:106916; Msra.
DR VEuPathDB; HostDB:ENSMUSG00000054733; -.
DR eggNOG; KOG1635; Eukaryota.
DR GeneTree; ENSGT00390000003823; -.
DR HOGENOM; CLU_031040_10_3_1; -.
DR InParanoid; Q9D6Y7; -.
DR OMA; AGPFYYA; -.
DR OrthoDB; 1383773at2759; -.
DR PhylomeDB; Q9D6Y7; -.
DR TreeFam; TF353884; -.
DR BRENDA; 1.8.4.11; 3474.
DR Reactome; R-MMU-5676934; Protein repair.
DR BioGRID-ORCS; 110265; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Msra; mouse.
DR PRO; PR:Q9D6Y7; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9D6Y7; protein.
DR Bgee; ENSMUSG00000054733; Expressed in right kidney and 245 other tissues.
DR ExpressionAtlas; Q9D6Y7; baseline and differential.
DR Genevisible; Q9D6Y7; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR Gene3D; 3.30.1060.10; -; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR Pfam; PF01625; PMSR; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; Lipoprotein;
KW Membrane; Mitochondrion; Myristate; Nucleus; Oxidoreductase;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 21..233
FT /note="Mitochondrial peptide methionine sulfoxide
FT reductase"
FT /id="PRO_0000138627"
FT ACT_SITE 72
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A744"
FT MOD_RES 104
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 104
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 183
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 183
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT DISULFID 72..218
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0A744"
FT DISULFID 218..227
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0A744"
FT VAR_SEQ 1..45
FT /note="MLSASRRALQLLSSANPVRRMGDSASKVISAEEALPGRTEPIPVT -> MSK
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041408"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042133"
FT VAR_SEQ 69..108
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041409"
FT CONFLICT 20
FT /note="R -> G (in Ref. 1; BAB22035)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="R -> P (in Ref. 1; AK018338)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="G -> V (in Ref. 1; BAB22035)"
FT /evidence="ECO:0000305"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:2L90"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:6AGV"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6AGV"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6AGV"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:6AGV"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:6AGV"
FT STRAND 86..97
FT /evidence="ECO:0007829|PDB:6AGV"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:6AGV"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:6AGV"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:6AGV"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:6AGV"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:6AGV"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6AGV"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:6AGV"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6AGV"
FT HELIX 164..183
FT /evidence="ECO:0007829|PDB:6AGV"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6AGV"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:6AGV"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2L90"
FT LIPID Q9D6Y7-2:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:20368336"
SQ SEQUENCE 233 AA; 25988 MW; B16EFE01BE751242 CRC64;
MLSASRRALQ LLSSANPVRR MGDSASKVIS AEEALPGRTE PIPVTAKHHV SGNRTVEPFP
EGTQMAVFGM GCFWGAERKF WVLKGVYSTQ VGFAGGHTRN PTYKEVCSEK TGHAEVVRVV
YRPEHISFEE LLKVFWENHD PTQGMRQGND FGTQYRSAVY PTSAVQMEAA LRSKEEYQKV
LSKHNFGPIT TDIREGQVFY YAEDYHQQYL SKNPDGYCGL GGTGVSCPMA IKK
