LOCUS       NM_013759                953 bp    mRNA    linear   ROD 07-FEB-2025
DEFINITION  Mus musculus methionine sulfoxide reductase B1 (Msrb1), transcript
            variant 1, mRNA.
ACCESSION   NM_013759
VERSION     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  (bases 1 to 953)
  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  (bases 1 to 953)
  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  (bases 1 to 953)
  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  (bases 1 to 953)
  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  (bases 1 to 953)
  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  (bases 1 to 953)
  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  (bases 1 to 953)
  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  (bases 1 to 953)
  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  (bases 1 to 953)
  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 (bases 1 to 953)
  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.
            
            On Oct 24, 2016 this sequence version replaced NM_013759.2.
            
            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##
            COMPLETENESS: complete on the 3' end.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-49                BY034747.1         2-50
            50-929              BC090646.1         1-880
            930-953             BI133579.1         1-24                c
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Mus musculus"
                     /mol_type="mRNA"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 12.53 cM"
     gene            1..953
                     /gene="Msrb1"
                     /gene_synonym="D17Wsu82e; SelR; SELX; Sepr; Sepx1"
                     /note="methionine sulfoxide reductase B1"
                     /db_xref="GeneID:27361"
                     /db_xref="MGI:MGI:1351642"
     exon            1..170
                     /gene="Msrb1"
                     /gene_synonym="D17Wsu82e; SelR; SELX; Sepr; Sepx1"
                     /inference="alignment:Splign:2.1.0"
     exon            171..319
                     /gene="Msrb1"
                     /gene_synonym="D17Wsu82e; SelR; SELX; Sepr; Sepx1"
                     /inference="alignment:Splign:2.1.0"
     exon            320..434
                     /gene="Msrb1"
                     /gene_synonym="D17Wsu82e; SelR; SELX; Sepr; Sepx1"
                     /inference="alignment:Splign:2.1.0"
     exon            435..466
                     /gene="Msrb1"
                     /gene_synonym="D17Wsu82e; SelR; SELX; Sepr; Sepx1"
                     /inference="alignment:Splign:2.1.0"
     exon            467..935
                     /gene="Msrb1"
                     /gene_synonym="D17Wsu82e; SelR; SELX; Sepr; Sepx1"
                     /inference="alignment:Splign:2.1.0"
     regulatory      531..602
                     /regulatory_class="recoding_stimulatory_region"
                     /gene="Msrb1"
                     /gene_synonym="D17Wsu82e; SelR; SELX; Sepr; Sepx1"
                     /note="SECIS_element"
                     /function="essential for recoding UGA to specify
                     selenocysteine"
     regulatory      912..917
                     /regulatory_class="polyA_signal_sequence"
                     /gene="Msrb1"
                     /gene_synonym="D17Wsu82e; SelR; SELX; Sepr; Sepx1"
                     /note="hexamer: AATAAA"
     polyA_site      929
                     /gene="Msrb1"
                     /gene_synonym="D17Wsu82e; SelR; SELX; Sepr; Sepx1"
                     /note="major polyA site"
ORIGIN      
        1 ggggcttatg gcgaatcgga aagtgattgg ttattgggac tgggtcgggt ttgagtccag
       61 atcttagggt tttacccgga cctggctggg agcttttgcc tgtcccgtcg cgaccatgtc
      121 gttctgcagc ttcttcggag gcgaggtttt ccagaatcac ttcgagccag gtgtctacgt
      181 gtgtgccaag tgcagctatg agctgttctc cagtcactcg aagtacgcac actcatcccc
      241 gtggccagcg ttcactgaaa ccatccaccc agacagtgtg accaagtgcc ctgagaaaaa
      301 ccgaccagaa gctttaaagg tgtcctgtgg caagtgtggc aatgggttgg gccacgagtt
      361 cctgaatgat ggccccaagc ggggacaatc aagattctga atatttagca gctcactgaa
      421 gttcgtccct aaaggcaaag aagctgctgc ctcccagggg cactaggaca tggactgcga
      481 atggcctgcc ccctgccccc tgccccctgt cccctgccaa ccgctccagc ctcagtcacc
      541 gaatgatctg ctctggtcaa atccttctat gccagccagg gtggtgatga cccgtgacct
      601 ttgaggaggg gagtaggctg ataccgggaa ctcttggatc cttgccttct ggcagagaaa
      661 acaaaactcc gtttcataat ctgcaaactc atcttgcctc actctagctt ggggaagtga
      721 cagttgttgc cccattagct ggccagcgtg gcagggaccc tcttctcacc actttgtcca
      781 gcgtgtacct cccaagagaa agccactgta ccttattggt gtgtttggaa gctcttgaca
      841 cctgggagag tggctgaagc tgagacccac tccccccctt gattgctctc tgggatgatc
      901 aagtagaagt caataaacat gcagcctgag ccgttaaaaa aaaaaaaaaa aaa
//
