LOCUS       NP_001037750             116 aa            linear   ROD 01-JUN-2024
DEFINITION  methionine-R-sulfoxide reductase B1 [Rattus norvegicus].
ACCESSION   NP_001037750 XP_001062118
VERSION     NP_001037750.2
DBSOURCE    REFSEQ: accession NM_001044285.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Dai,J., Zhou,J., Liu,H. and Huang,K.
  TITLE     Selenite and ebselen supplementation attenuates D-galactose-induced
            oxidative stress and increases expression of SELR and SEP15 in rat
            lens
  JOURNAL   J Biol Inorg Chem 21 (8), 1037-1046 (2016)
   PUBMED   27752786
  REMARK    GeneRIF: Data show that 15kD selenoprotein (SEP15) protein and
            selenoprotein R (SELR) protein expression was decreased in the
            lenses of galactose induced cataract.
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Lee,B.C., Peterfi,Z., Hoffmann,F.W., Moore,R.E., Kaya,A.,
            Avanesov,A., Tarrago,L., Zhou,Y., Weerapana,E., Fomenko,D.E.,
            Hoffmann,P.R. and Gladyshev,V.N.
  TITLE     MsrB1 and MICALs regulate actin assembly and macrophage function
            via reversible stereoselective methionine oxidation
  JOURNAL   Mol Cell 51 (3), 397-404 (2013)
   PUBMED   23911929
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Mariotti,M., Ridge,P.G., Zhang,Y., Lobanov,A.V., Pringle,T.H.,
            Guigo,R., Hatfield,D.L. and Gladyshev,V.N.
  TITLE     Composition and evolution of the vertebrate and mammalian
            selenoproteomes
  JOURNAL   PLoS One 7 (3), e33066 (2012)
   PUBMED   22479358
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    Publication Status: Online-Only
REFERENCE   5  (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   6  (residues 1 to 116)
  AUTHORS   Kryukov,G.V., Castellano,S., Novoselov,S.V., Lobanov,A.V.,
            Zehtab,O., Guigo,R. and Gladyshev,V.N.
  TITLE     Characterization of mammalian selenoproteomes
  JOURNAL   Science 300 (5624), 1439-1443 (2003)
   PUBMED   12775843
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FQ220312.1, BC094309.1 and
            AI044339.1.
            
            On May 3, 2007 this sequence version replaced NP_001037750.1.
            
            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.
            [provided by RefSeq, Oct 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ220312.1, BC094309.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            protein contains selenocysteine :: inferred from conservation
            RefSeq Select criteria          :: based on single protein-coding
                                               transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     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=12666
     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="selX; Sepx1"
                     /coded_by="NM_001044285.3:82..432"
                     /note="UGA stop codon recoded as selenocysteine"
                     /db_xref="GeneID:685059"
                     /db_xref="RGD:1583243"
ORIGIN      
        1 msfcsffgge vfqnhfepgv yvcakcgyel fssrskyahs spwpafteti hedsvakcpe
       61 knrpealkvs cgkcgnglgh eflndgpkrg qsrfuifsss lkfipkgkea pasqgd
//
