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Methionine-R-sulfoxide reductase B1 (MsrB1) (EC 1.8.4.-) (Selenoprotein X) (SelX)

 MSRB1_RAT               Reviewed;         116 AA.
Q52KJ8;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 2.
22-NOV-2017, entry version 84.
RecName: Full=Methionine-R-sulfoxide reductase B1;
Short=MsrB1;
EC=1.8.4.12 {ECO:0000250|UniProtKB:Q9JLC3};
EC=1.8.4.14 {ECO:0000250|UniProtKB:Q9JLC3};
AltName: Full=Selenoprotein X;
Short=SelX;
Name=Msrb1; Synonyms=Sepx1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Methionine-sulfoxide reductase that specifically reduces
methionine (R)-sulfoxide back to methionine. While in many cases,
methionine oxidation is the result of random oxidation following
oxidative stress, methionine oxidation is also a post-
translational modification that takes place on specific residue.
Acts as a regulator of actin assembly by reducing methionine (R)-
sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin,
thereby promoting filament repolymerization. Plays a role in
innate immunity by reducing oxidized actin, leading to actin
repolymerization in macrophages. {ECO:0000250|UniProtKB:Q9JLC3}.
-!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin.
{ECO:0000250|UniProtKB:Q9JLC3}.
-!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O =
L-methionine (R)-S-oxide + thioredoxin.
{ECO:0000250|UniProtKB:Q9JLC3}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q9JLC3};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9JLC3};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JLC3}.
Nucleus {ECO:0000250|UniProtKB:Q9JLC3}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q9JLC3}.
-!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH94309.1; Type=Erroneous termination; Positions=95; Note=Translated as Sec.; Evidence={ECO:0000305};
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EMBL; BC094309; AAH94309.1; ALT_SEQ; mRNA.
RefSeq; NP_001037750.2; NM_001044285.3.
UniGene; Rn.198860; -.
ChEMBL; CHEMBL3509600; -.
GeneID; 685059; -.
KEGG; rno:685059; -.
UCSC; RGD:1583243; rat.
CTD; 51734; -.
RGD; 1583243; Msrb1.
HOGENOM; HOG000243424; -.
HOVERGEN; HBG002192; -.
InParanoid; Q52KJ8; -.
KO; K07305; -.
PhylomeDB; Q52KJ8; -.
TreeFam; TF329147; -.
PRO; PR:Q52KJ8; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0003779; F:actin binding; ISS:UniProtKB.
GO; GO:0033745; F:L-methionine-(R)-S-oxide reductase activity; IEA:UniProtKB-EC.
GO; GO:0070191; F:methionine-R-sulfoxide reductase activity; ISO:RGD.
GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISO:RGD.
GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; ISO:RGD.
GO; GO:0030091; P:protein repair; ISO:RGD.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
InterPro; IPR028427; Met_Sox_Rdtase.
InterPro; IPR002579; Met_Sox_Rdtase_MsrB.
InterPro; IPR011057; Mss4-like_sf.
PANTHER; PTHR10173; PTHR10173; 1.
Pfam; PF01641; SelR; 1.
SUPFAM; SSF51316; SSF51316; 1.
PROSITE; PS51790; MSRB; 1.
3: Inferred from homology;
Complete proteome; Cytoplasm; Cytoskeleton; Immunity; Innate immunity;
Metal-binding; Nucleus; Oxidoreductase; Reference proteome;
Selenocysteine; Zinc.
CHAIN 1 116 Methionine-R-sulfoxide reductase B1.
/FTId=PRO_0000318612.
DOMAIN 1 106 MsrB. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
ACT_SITE 95 95 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
METAL 23 23 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
METAL 26 26 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
METAL 71 71 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
METAL 74 74 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
NON_STD 95 95 Selenocysteine. {ECO:0000250}.
SEQUENCE 116 AA; 12797 MW; 2CADD12D1C32CCC8 CRC64;
MSFCSFFGGE VFQNHFEPGV YVCAKCGYEL FSSRSKYAHS SPWPAFTETI HEDSVAKCPE
KNRPEALKVS CGKCGNGLGH EFLNDGPKRG QSRFUIFSSS LKFIPKGKEA PASQGD


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EIAAB25532 Methionine-R-sulfoxide reductase B1,Mouse,MsrB1,Msrb1,Mus musculus,Selenoprotein R,Selenoprotein X,SelR,SelX,Sepr,Sepx1
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EIAAB25533 Homo sapiens,HSPC270,Human,Methionine-R-sulfoxide reductase B1,MsrB1,MSRB1,Selenoprotein X,SelX,SEPX1
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