ID MSRB2_MOUSE Reviewed; 175 AA. AC Q78J03; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 22-JUL-2015, entry version 84. DE RecName: Full=Methionine-R-sulfoxide reductase B2, mitochondrial; DE Short=MsrB2; DE EC=1.8.4.-; DE Flags: Precursor; GN Name=Msrb2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, AND COFACTOR. RX PubMed=14699060; DOI=10.1091/mbc.E03-08-0629; RA Kim H.-Y., Gladyshev V.N.; RT "Methionine sulfoxide reduction in mammals: characterization of RT methionine-R-sulfoxide reductases."; RL Mol. Biol. Cell 15:1055-1064(2004). RN [4] RP FUNCTION. RX PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019; RA Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., RA Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., RA Gladyshev V.N.; RT "MsrB1 and MICALs regulate actin assembly and macrophage function via RT reversible stereoselective methionine oxidation."; RL Mol. Cell 51:397-404(2013). CC -!- FUNCTION: Methionine-sulfoxide reductase that specifically reduces CC methionine (R)-sulfoxide back to methionine. While in many cases, CC methionine oxidation is the result of random oxidation following CC oxidative stress, methionine oxidation is also a post- CC translational modification that takes place on specific residue. CC Upon oxidative stress, may play a role in the preservation of CC mitochondrial integrity by decreasing the intracellular reactive CC oxygen species build-up through its scavenging role, hence CC contributing to cell survival and protein maintenance. CC {ECO:0000269|PubMed:14699060, ECO:0000269|PubMed:23911929}. CC -!- CATALYTIC ACTIVITY: L-methionine + oxidized thioredoxin = L- CC methionine R-oxide + reduced thioredoxin. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:14699060}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14699060}; CC -!- ENZYME REGULATION: Inhibited by high concentrations of substrate. CC {ECO:0000269|PubMed:14699060}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14699060}. CC -!- SIMILARITY: Belongs to the MsrB 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; AL928806; CAM21786.1; -; Genomic_DNA. DR EMBL; BC021619; AAH21619.1; -; mRNA. DR CCDS; CCDS15714.1; -. DR RefSeq; NP_083895.1; NM_029619.2. DR UniGene; Mm.27166; -. DR PDB; 2L1U; NMR; -; A=45-175. DR PDBsum; 2L1U; -. DR ProteinModelPortal; Q78J03; -. DR SMR; Q78J03; 45-175. DR IntAct; Q78J03; 1. DR STRING; 10090.ENSMUSP00000023856; -. DR PhosphoSite; Q78J03; -. DR MaxQB; Q78J03; -. DR PaxDb; Q78J03; -. DR PRIDE; Q78J03; -. DR Ensembl; ENSMUST00000023856; ENSMUSP00000023856; ENSMUSG00000023094. DR GeneID; 76467; -. DR KEGG; mmu:76467; -. DR UCSC; uc008imf.2; mouse. DR CTD; 22921; -. DR MGI; MGI:1923717; Msrb2. DR eggNOG; COG0229; -. DR GeneTree; ENSGT00510000046802; -. DR HOGENOM; HOG000243424; -. DR HOVERGEN; HBG002192; -. DR InParanoid; Q78J03; -. DR KO; K07305; -. DR OMA; TRYNKTT; -. DR OrthoDB; EOG7VHSZD; -. DR PhylomeDB; Q78J03; -. DR TreeFam; TF329147; -. DR BRENDA; 1.8.4.12; 3474. DR NextBio; 345204; -. DR PRO; PR:Q78J03; -. DR Proteomes; UP000000589; Chromosome 2. DR Bgee; Q78J03; -. DR Genevisible; Q78J03; MM. DR GO; GO:0005739; C:mitochondrion; IDA:HGNC. DR GO; GO:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:HGNC. DR GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB. DR GO; GO:0030091; P:protein repair; IDA:HGNC. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 2.170.150.20; -; 1. DR InterPro; IPR028427; Met_Sox_Rdtase. DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB. DR InterPro; IPR011057; Mss4-like. DR PANTHER; PTHR10173; PTHR10173; 1. DR Pfam; PF01641; SelR; 1. DR SUPFAM; SSF51316; SSF51316; 1. DR TIGRFAMs; TIGR00357; TIGR00357; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Metal-binding; Mitochondrion; KW Oxidoreductase; Reference proteome; Transit peptide; Zinc. FT TRANSIT 1 42 Mitochondrion. {ECO:0000255}. FT CHAIN 43 175 Methionine-R-sulfoxide reductase B2, FT mitochondrial. FT /FTId=PRO_0000327243. FT ACT_SITE 162 162 Nucleophile. {ECO:0000250}. FT METAL 83 83 Zinc. {ECO:0000250}. FT METAL 86 86 Zinc. {ECO:0000250}. FT METAL 139 139 Zinc. {ECO:0000250}. FT METAL 142 142 Zinc. {ECO:0000250}. FT HELIX 48 51 {ECO:0000244|PDB:2L1U}. FT HELIX 55 61 {ECO:0000244|PDB:2L1U}. FT HELIX 70 72 {ECO:0000244|PDB:2L1U}. FT STRAND 79 87 {ECO:0000244|PDB:2L1U}. FT STRAND 89 92 {ECO:0000244|PDB:2L1U}. FT HELIX 93 95 {ECO:0000244|PDB:2L1U}. FT TURN 98 101 {ECO:0000244|PDB:2L1U}. FT STRAND 104 108 {ECO:0000244|PDB:2L1U}. FT HELIX 116 119 {ECO:0000244|PDB:2L1U}. FT STRAND 122 127 {ECO:0000244|PDB:2L1U}. FT STRAND 134 142 {ECO:0000244|PDB:2L1U}. FT STRAND 147 150 {ECO:0000244|PDB:2L1U}. FT HELIX 156 158 {ECO:0000244|PDB:2L1U}. FT STRAND 160 163 {ECO:0000244|PDB:2L1U}. FT STRAND 168 175 {ECO:0000244|PDB:2L1U}. SQ SEQUENCE 175 AA; 19157 MW; 916771737762C6A6 CRC64; MARLLRALRG LPLLQAPGRL ARGCAGSGSK DTGSLTKSKR SLSEADWQKK LTPEQFYVTR EKGTEAPFSG MYLNNKETGM YHCVCCDSPL FSSEKKYCSG TGWPSFSEAY GSKGSDESHT GILRRLDTSL GCPRMEVVCK QCEAHLGHVF PDGPKPTGQR FCINSVALKF KPSKP //