MSRB1_PONAB
ID MSRB1_PONAB Reviewed; 116 AA.
AC Q5R869;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 77.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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}. Nucleus {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}.
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; CR859820; CAH91977.1; -; mRNA.
DR EMBL; CR859885; CAH92041.1; -; mRNA.
DR RefSeq; NP_001126146.1; NM_001132674.1.
DR STRING; 9601.ENSPPYP00000007893; -.
DR GeneID; 100173105; -.
DR KEGG; pon:100173105; -.
DR CTD; 51734; -.
DR eggNOG; KOG0856; Eukaryota.
DR InParanoid; Q5R869; -.
DR OrthoDB; 1549489at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
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_0000249713"
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; 12744 MW; 032B033BFFCB7C11 CRC64;
MSFCSFFGGE VFQNHFEPGV YVCAKCGYEL FSSRSKYAHS SPWPAFTETI HADSVAKRPE
HNRAEALKVS CGKCGNGLGH EFLNDGPKPG QSRFUIFSSS LKFVPKGKET SASQGH
