MSRB1_PIG
ID MSRB1_PIG Reviewed; 116 AA.
AC A1E952;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Methionine-R-sulfoxide reductase B1;
DE Short=MsrB1;
DE EC=1.8.4.12 {ECO:0000250|UniProtKB:Q9JLC3};
DE EC=1.8.4.14 {ECO:0000250|UniProtKB:Q9JLC3};
DE AltName: Full=Selenoprotein X;
DE Short=SelX;
GN Name=MSRB1; Synonyms=SEPX1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RG sus scrofa;
RA Zhao H., Zhou J.C., Wang K.N., Xia X.J., Zhao Y., Lei X.G.;
RT "Cloning of selenoprotein X from Sus scrofa.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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-translational
CC modification that takes place on specific residue. Acts as a regulator
CC of actin assembly by reducing methionine (R)-sulfoxide mediated by
CC MICALs (MICAL1, MICAL2 or MICAL3) on actin, thereby promoting filament
CC repolymerization. Plays a role in innate immunity by reducing oxidized
CC actin, leading to actin repolymerization in macrophages.
CC {ECO:0000250|UniProtKB:Q9JLC3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
CC Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764,
CC ChEBI:CHEBI:50058; EC=1.8.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q9JLC3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (R)-S-oxide; Xref=Rhea:RHEA:21260, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58773; EC=1.8.4.14;
CC Evidence={ECO:0000250|UniProtKB:Q9JLC3};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9JLC3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9JLC3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JLC3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9JLC3}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9JLC3}.
CC -!- PTM: Truncated MSRB1/SEPX1 proteins produced by failed UGA/Sec decoding
CC are ubiquitinated by the CRL2(FEM1C) E3 ubiquitin-protein ligase
CC complex. {ECO:0000250|UniProtKB:Q9NZV6}.
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; EF113597; ABL61085.1; -; mRNA.
DR RefSeq; NP_001090929.1; NM_001097460.1.
DR GeneID; 100037965; -.
DR KEGG; ssc:100037965; -.
DR CTD; 51734; -.
DR InParanoid; A1E952; -.
DR OrthoDB; 1549489at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0033745; F:L-methionine-(R)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0070191; F:methionine-R-sulfoxide reductase activity; IBA:GO_Central.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0030091; P:protein repair; IBA:GO_Central.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; Immunity; Innate immunity; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Selenocysteine; Ubl conjugation; Zinc.
FT CHAIN 1..116
FT /note="Methionine-R-sulfoxide reductase B1"
FT /id="PRO_0000318613"
FT DOMAIN 1..106
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT NON_STD 95
FT /note="Selenocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZV6"
SQ SEQUENCE 116 AA; 12783 MW; 13E913EE38ABEAF0 CRC64;
MSFCSFFGGE VFQNHFEPGV YVCAKCGYEL FSSHSKYAHS SPWPAFTETI HADSVAKRPE
HNRPGALKVS CGRCGNGLGH EFLNDGPKRG QSRFUIFSSS LKFIPKGQES SPSQGQ
