LOCUS NP_038787 116 aa linear ROD 07-FEB-2025 DEFINITION methionine-R-sulfoxide reductase B1 [Mus musculus]. ACCESSION NP_038787 VERSION NP_038787.1 DBSOURCE REFSEQ: accession NM_013759.3 KEYWORDS RefSeq; RefSeq Select. SOURCE Mus musculus (house mouse) ORGANISM Mus musculus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus. REFERENCE 1 (residues 1 to 116) AUTHORS Yoo,H.J., Choi,D.W., Roh,Y.J., Lee,Y.M., Lim,J.H., Eo,S., Lee,H.J., Kim,N.Y., Kim,S., Cho,S., Im,G., Lee,B.C. and Kim,J.H. TITLE MsrB1-regulated GAPDH oxidation plays programmatic roles in shaping metabolic and inflammatory signatures during macrophage activation JOURNAL Cell Rep 41 (6), 111598 (2022) PUBMED 36351405 REMARK GeneRIF: MsrB1-regulated GAPDH oxidation plays programmatic roles in shaping metabolic and inflammatory signatures during macrophage activation. REFERENCE 2 (residues 1 to 116) AUTHORS Shi,T., Yang,Y., Zhang,Z., Zhang,L., Song,J., Ping,Y., Du,X., Song,G., Liu,Q. and Li,N. TITLE Loss of MsrB1 perturbs spatial learning and long-term potentiation/long-term depression in mice JOURNAL Neurobiol Learn Mem 166, 107104 (2019) PUBMED 31672630 REMARK GeneRIF: these results suggest that MsrB1 is essential for mice spatial learning and LTP/LTD induction, and the MsrB1 related redox homeostasis may be involved in regulating the phosphorylation of CaMKIIs. REFERENCE 3 (residues 1 to 116) AUTHORS Lai,L., Sun,J., Tarafdar,S., Liu,C., Murphy,E., Kim,G. and Levine,R.L. TITLE Loss of methionine sulfoxide reductases increases resistance to oxidative stress JOURNAL Free Radic Biol Med 145, 374-384 (2019) PUBMED 31606431 REMARK Erratum:[Free Radic Biol Med. 2024 Aug 1;220:166. doi: 10.1016/j.freeradbiomed.2024.05.002.. PMID: 38718559] REFERENCE 4 (residues 1 to 116) AUTHORS Liang,X., Fomenko,D.E., Hua,D., Kaya,A. and Gladyshev,V.N. TITLE Diversity of protein and mRNA forms of mammalian methionine sulfoxide reductase B1 due to intronization and protein processing JOURNAL PLoS One 5 (7), e11497 (2010) PUBMED 20634897 REMARK GeneRIF: Study characterized unexpected diversity of protein and mRNA forms of mammalian selenoprotein MsrB1. Publication Status: Online-Only REFERENCE 5 (residues 1 to 116) AUTHORS Fomenko,D.E., Novoselov,S.V., Natarajan,S.K., Lee,B.C., Koc,A., Carlson,B.A., Lee,T.H., Kim,H.Y., Hatfield,D.L. and Gladyshev,V.N. TITLE MsrB1 (methionine-R-sulfoxide reductase 1) knock-out mice: roles of MsrB1 in redox regulation and identification of a novel selenoprotein form JOURNAL J Biol Chem 284 (9), 5986-5993 (2009) PUBMED 18990697 REFERENCE 6 (residues 1 to 116) AUTHORS Sal,L.S., Aachmann,F.L., Kim,H.Y., Gladyshev,V.N. and Dikiy,A. TITLE NMR assignments of 1H, 13C and 15N spectra of methionine sulfoxide reductase B1 from Mus musculus JOURNAL Biomol NMR Assign 1 (1), 131-133 (2007) PUBMED 19636847 REMARK GeneRIF: The chemical shift index for MsrB1 indicates that the beta-sheets are the main element for the protein secondary structure. REFERENCE 7 (residues 1 to 116) AUTHORS Kim,H.Y. and Gladyshev,V.N. TITLE Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductases JOURNAL PLoS Biol 3 (12), e375 (2005) PUBMED 16262444 REFERENCE 8 (residues 1 to 116) AUTHORS Kim,H.Y. and Gladyshev,V.N. TITLE Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases JOURNAL Mol Biol Cell 15 (3), 1055-1064 (2004) PUBMED 14699060 REFERENCE 9 (residues 1 to 116) AUTHORS Kryukov,G.V., Kumar,R.A., Koc,A., Sun,Z. and Gladyshev,V.N. TITLE Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase JOURNAL Proc Natl Acad Sci U S A 99 (7), 4245-4250 (2002) PUBMED 11929995 REFERENCE 10 (residues 1 to 116) AUTHORS Kryukov,G.V., Kryukov,V.M. and Gladyshev,V.N. TITLE New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements JOURNAL J Biol Chem 274 (48), 33888-33897 (1999) PUBMED 10567350 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from BY034747.1, BC090646.1 and BI133579.1. Summary: The protein encoded by this gene belongs to the methionine-R-sulfoxide reductase B (MsrB) family. Members of this family function as repair enzymes that protect proteins from oxidative stress by catalyzing the reduction of methionine-R-sulfoxides to methionines. This protein is highly expressed in liver and kidney, and is localized to the nucleus and cytosol. It is the only member of the MsrB family that is a selenoprotein, containing a selenocysteine (Sec) residue at its active site. It also has the highest methionine-R-sulfoxide reductase activity compared to other members containing cysteine in place of Sec. Sec is encoded by the UGA codon, which normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, that is necessary for the recognition of UGA as a Sec codon, rather than as a stop signal. Alternatively spliced transcript variants have been described for this gene. [provided by RefSeq, Oct 2016]. Transcript Variant: This variant (1) represents the predominant 5-exon transcript. Variants 1 and 2 encode the same protein. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF195142.1, BC090646.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMN00849374, SAMN00849375 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## protein contains selenocysteine :: PMID: 10567350 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## FEATURES Location/Qualifiers source 1..116 /organism="Mus musculus" /strain="C57BL/6" /db_xref="taxon:10090" /chromosome="17" /map="17 12.53 cM" Protein 1..116 /product="methionine-R-sulfoxide reductase B1" /EC_number="1.8.4.12" /EC_number="1.8.4.14" /note="selenoprotein R; selenoprotein X 1" /calculated_mol_wt=12657 Region <14..108 /region_name="SelR" /note="SelR domain; cl15841" /db_xref="CDD:472838" Site 95 /site_type="other" /note="Selenocysteine" CDS 1..116 /gene="Msrb1" /gene_synonym="D17Wsu82e; SelR; SELX; Sepr; Sepx1" /coded_by="NM_013759.3:116..466" /note="UGA stop codon recoded as selenocysteine" /db_xref="CCDS:CCDS28495.1" /db_xref="GeneID:27361" /db_xref="MGI:MGI:1351642" ORIGIN 1 msfcsffgge vfqnhfepgv yvcakcsyel fsshskyahs spwpafteti hpdsvtkcpe 61 knrpealkvs cgkcgnglgh eflndgpkrg qsrfuifsss lkfvpkgkea aasqgh //