MSRB2_RAT
ID MSRB2_RAT Reviewed; 174 AA.
AC Q4FZX5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Methionine-R-sulfoxide reductase B2, mitochondrial;
DE Short=MsrB2;
DE EC=1.8.4.12 {ECO:0000250|UniProtKB:Q9JLC3};
DE EC=1.8.4.14 {ECO:0000250|UniProtKB:Q9JLC3};
DE Flags: Precursor;
GN Name=Msrb2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. Upon oxidative
CC stress, may play a role in the preservation of mitochondrial integrity
CC by decreasing the intracellular reactive oxygen species build-up
CC through its scavenging role, hence contributing to cell survival and
CC protein maintenance. {ECO:0000250|UniProtKB:Q9Y3D2}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; BC098953; AAH98953.1; -; mRNA.
DR RefSeq; NP_001026830.1; NM_001031660.1.
DR AlphaFoldDB; Q4FZX5; -.
DR BMRB; Q4FZX5; -.
DR SMR; Q4FZX5; -.
DR STRING; 10116.ENSRNOP00000022661; -.
DR PhosphoSitePlus; Q4FZX5; -.
DR PaxDb; Q4FZX5; -.
DR PRIDE; Q4FZX5; -.
DR Ensembl; ENSRNOT00000022661; ENSRNOP00000022661; ENSRNOG00000016873.
DR GeneID; 361286; -.
DR KEGG; rno:361286; -.
DR UCSC; RGD:1306026; rat.
DR CTD; 22921; -.
DR RGD; 1306026; Msrb2.
DR eggNOG; KOG0856; Eukaryota.
DR GeneTree; ENSGT00940000161673; -.
DR HOGENOM; CLU_031040_8_2_1; -.
DR InParanoid; Q4FZX5; -.
DR OMA; CDVPLFS; -.
DR OrthoDB; 1549489at2759; -.
DR PhylomeDB; Q4FZX5; -.
DR TreeFam; TF329147; -.
DR Reactome; R-RNO-5676934; Protein repair.
DR PRO; PR:Q4FZX5; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000016873; Expressed in kidney and 20 other tissues.
DR Genevisible; Q4FZX5; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
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:0033743; F:peptide-methionine (R)-S-oxide reductase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0030091; P:protein repair; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR PANTHER; PTHR10173; PTHR10173; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR TIGRFAMs; TIGR00357; TIGR00357; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Mitochondrion; Oxidoreductase; Reference proteome;
KW Transit peptide; Zinc.
FT TRANSIT 1..61
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 62..174
FT /note="Methionine-R-sulfoxide reductase B2, mitochondrial"
FT /id="PRO_0000327244"
FT DOMAIN 62..172
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
SQ SEQUENCE 174 AA; 19073 MW; AE44A32C8AD71A6A CRC64;
MARLLRALRG LPWLEAPGRA RGCAGSGRGD TGSLIKSKLS LSKADWQKKL TPEQFYVTRE
KGTEAPFSGM YLKNKETGMY HCVCCDSPLF SSEKKYCSGT GWPSFSEAHG TKGSDESHTG
ILRRLDTSLG CPRMEVVCKQ CEAHLGHVFP DGPDPTGQRF CINSVALKFK PSKP
