ID MSRA_BOVIN Reviewed; 233 AA. AC P54149; Q3ZC16; Q5E976; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 2. DT 02-SEP-2026, entry version 153. DE RecName: Full=Mitochondrial peptide methionine sulfoxide reductase; DE EC=1.8.4.11 {ECO:0000269|PubMed:8700890}; DE AltName: Full=Peptide-methionine (S)-S-oxide reductase; DE Short=Peptide Met(O) reductase; DE AltName: Full=Protein-methionine-S-oxide reductase; DE Flags: Precursor; GN Name=MSRA; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY. RC TISSUE=Adrenal medulla; RX PubMed=8700890; DOI=10.1073/pnas.93.5.2095; RA Moskovitz J., Weissbach H., Brot N.; RT "Cloning the expression of a mammalian gene involved in the reduction of RT methionine sulfoxide residues in proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 93:2095-2099(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Hypothalamus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). RX PubMed=11063566; DOI=10.1021/bi0020269; RA Lowther W.T., Brot N., Weissbach H., Matthews B.W.; RT "Structure and mechanism of peptide methionine sulfoxide reductase, an RT 'anti-oxidation' enzyme."; RL Biochemistry 39:13307-13312(2000). CC -!- FUNCTION: Catalyzes the reversible oxidation-reduction of methionine CC sulfoxide in proteins to methionine. Has an important function as a CC repair enzyme for proteins that have been inactivated by oxidation CC (PubMed:8700890). Plays a crucial role in repairing oxidized methionine CC residues in key lens proteins, such as alpha-crystallin (CRYAA/CRYAB) CC and cytochrome c (CYCS), thereby restoring their function and CC maintaining lens transparency (By similarity). CC {ECO:0000250|UniProtKB:Q9D6Y7, ECO:0000269|PubMed:8700890}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L- CC methionyl-(S)-S-oxide-[protein] + [thioredoxin]-dithiol; 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:8700890}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-disulfide + L-methionine + H2O = L-methionine CC (S)-S-oxide + [thioredoxin]-dithiol; 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:8700890}; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9UJ68}. CC Cytoplasm {ECO:0000250|UniProtKB:Q9UJ68}. 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; U37150; AAC48539.1; -; mRNA. DR EMBL; BT021044; AAX09061.1; -; mRNA. DR EMBL; BC102980; AAI02981.1; -; mRNA. DR RefSeq; NP_776539.1; NM_174114.2. DR PDB; 1FVA; X-ray; 1.70 A; A/B=13-229. DR PDB; 1FVG; X-ray; 1.60 A; A=21-219. DR AlphaFoldDB; P54149; -. DR SMR; P54149; -. DR BioGRID; 158665; 1. DR FunCoup; P54149; 1576. DR STRING; 9913.ENSBTAP00000065414; -. DR BindingDB; P54149; -. DR ChEMBL; CHEMBL2007622; -. DR GlyGen; P54149; 1 site. DR PaxDb; 9913-ENSBTAP00000065414; -. DR PeptideAtlas; P54149; -. DR Ensembl; ENSBTAT00000028825.7; ENSBTAP00000028825.5; ENSBTAG00000021632.7. DR Ensembl; ENSBTAT00085037316; ENSBTAP00085048482; ENSBTAG00085014474. DR Ensembl; ENSBTAT00090068779; ENSBTAP00090037806; ENSBTAG00090032483. DR GeneID; 281312; -. DR KEGG; bta:281312; -. DR CTD; 4482; -. DR VEuPathDB; HostDB:ENSBTAG00000021632; -. DR VGNC; VGNC:31705; MSRA. DR eggNOG; KOG1635; Eukaryota. DR GeneTree; ENSGT00390000003823; -. DR HOGENOM; CLU_031040_10_3_1; -. DR InParanoid; P54149; -. DR OMA; LFWESHD; -. DR OrthoDB; 77405at2759; -. DR BRENDA; 1.8.4.11; 908. DR Reactome; R-BTA-5676934; Protein repair. DR EvolutionaryTrace; P54149; -. DR Proteomes; UP000009136; Chromosome 8. DR Bgee; ENSBTAG00000021632; Expressed in metanephros cortex and 105 other cell types or tissues. DR ExpressionAtlas; P54149; baseline. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0033744; F:L-methionine (S)-S-oxide reductase activity; EXP:UniProtKB. DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IDA:UniProtKB. DR FunFam; 3.30.1060.10:FF:000001; Peptide methionine sulfoxide reductase MsrA; 1. DR Gene3D; 3.30.1060.10; Peptide methionine sulphoxide reductase MsrA; 1. DR HAMAP; MF_01401; MsrA; 1. DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom. DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf. DR InterPro; IPR050162; MsrA_MetSO_reductase. DR NCBIfam; TIGR00401; msrA; 1. DR PANTHER; PTHR42799; MITOCHONDRIAL PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1. DR PANTHER; PTHR42799:SF2; MITOCHONDRIAL PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1. DR Pfam; PF01625; PMSR; 1. DR SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1. DR PDBsum; 1FVA; -. DR PDBsum; 1FVG; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Disulfide bond; Mitochondrion; KW Oxidoreductase; Redox-active center; Reference proteome; Transit peptide. FT TRANSIT 1..20 FT /note="Mitochondrion" FT /evidence="ECO:0000250|UniProtKB:Q9UJ68" FT CHAIN 21..233 FT /note="Mitochondrial peptide methionine sulfoxide FT reductase" FT /id="PRO_0000138625" 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:0000250|UniProtKB:Q9D6Y7" FT MOD_RES 104 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9D6Y7" 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 CONFLICT 4 FT /note="A -> V (in Ref. 1; AAC48539)" FT /evidence="ECO:0000305" FT CONFLICT 125 FT /note="H -> R (in Ref. 2; AAX09061)" FT /evidence="ECO:0000305" FT HELIX 28..30 FT /evidence="ECO:0007829|PDB:1FVG" FT TURN 31..33 FT /evidence="ECO:0007829|PDB:1FVG" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:1FVG" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:1FVG" FT STRAND 64..72 FT /evidence="ECO:0007829|PDB:1FVG" FT HELIX 73..81 FT /evidence="ECO:0007829|PDB:1FVG" FT STRAND 86..97 FT /evidence="ECO:0007829|PDB:1FVG" FT HELIX 103..108 FT /evidence="ECO:0007829|PDB:1FVG" FT STRAND 114..121 FT /evidence="ECO:0007829|PDB:1FVG" FT TURN 123..125 FT /evidence="ECO:0007829|PDB:1FVG" FT HELIX 128..137 FT /evidence="ECO:0007829|PDB:1FVG" FT STRAND 144..147 FT /evidence="ECO:0007829|PDB:1FVG" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:1FVG" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:1FVG" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:1FVG" FT HELIX 164..183 FT /evidence="ECO:0007829|PDB:1FVG" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:1FVG" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:1FVG" FT HELIX 209..212 FT /evidence="ECO:0007829|PDB:1FVG" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:1FVA" SQ SEQUENCE 233 AA; 25818 MW; DA09151E42FB6C08 CRC64; MLSATRRALQ LFHSLFPIPR MGDSAAKIVS PQEALPGRKE PLVVAAKHHV NGNRTVEPFP EGTQMAVFGM GCFWGAERKF WTLKGVYSTQ VGFAGGYTPN PTYKEVCSGK TGHAEVVRVV FQPEHISFEE LLKVFWENHD PTQGMRQGND HGSQYRSAIY PTSAEHVGAA LKSKEDYQKV LSEHGFGLIT TDIREGQTFY YAEDYHQQYL SKDPDGYCGL GGTGVSCPLG IKK //