MSRB2_MOUSE
ID MSRB2_MOUSE Reviewed; 175 AA.
AC Q78J03;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND COFACTOR.
RX PubMed=14699060; DOI=10.1091/mbc.e03-08-0629;
RA Kim H.-Y., Gladyshev V.N.;
RT "Methionine sulfoxide reduction in mammals: characterization of methionine-
RT R-sulfoxide reductases.";
RL Mol. Biol. Cell 15:1055-1064(2004).
RN [4]
RP FUNCTION.
RX PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019;
RA Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A.,
RA Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R.,
RA Gladyshev V.N.;
RT "MsrB1 and MICALs regulate actin assembly and macrophage function via
RT reversible stereoselective methionine oxidation.";
RL Mol. Cell 51:397-404(2013).
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:0000269|PubMed:14699060,
CC ECO:0000269|PubMed:23911929}.
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:0000269|PubMed:14699060};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14699060};
CC -!- ACTIVITY REGULATION: Inhibited by high concentrations of substrate.
CC {ECO:0000269|PubMed:14699060}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14699060}.
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; AL928806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021619; AAH21619.1; -; mRNA.
DR CCDS; CCDS15714.1; -.
DR RefSeq; NP_083895.1; NM_029619.2.
DR PDB; 2L1U; NMR; -; A=45-175.
DR PDBsum; 2L1U; -.
DR AlphaFoldDB; Q78J03; -.
DR BMRB; Q78J03; -.
DR SMR; Q78J03; -.
DR IntAct; Q78J03; 1.
DR STRING; 10090.ENSMUSP00000023856; -.
DR iPTMnet; Q78J03; -.
DR PhosphoSitePlus; Q78J03; -.
DR SwissPalm; Q78J03; -.
DR EPD; Q78J03; -.
DR MaxQB; Q78J03; -.
DR PaxDb; Q78J03; -.
DR PeptideAtlas; Q78J03; -.
DR PRIDE; Q78J03; -.
DR ProteomicsDB; 291526; -.
DR Antibodypedia; 25752; 185 antibodies from 28 providers.
DR DNASU; 76467; -.
DR Ensembl; ENSMUST00000023856; ENSMUSP00000023856; ENSMUSG00000023094.
DR GeneID; 76467; -.
DR KEGG; mmu:76467; -.
DR UCSC; uc008imf.2; mouse.
DR CTD; 22921; -.
DR MGI; MGI:1923717; Msrb2.
DR VEuPathDB; HostDB:ENSMUSG00000023094; -.
DR eggNOG; KOG0856; Eukaryota.
DR GeneTree; ENSGT00940000161673; -.
DR HOGENOM; CLU_031040_8_2_1; -.
DR InParanoid; Q78J03; -.
DR OMA; RTEEHCA; -.
DR OrthoDB; 1549489at2759; -.
DR PhylomeDB; Q78J03; -.
DR TreeFam; TF329147; -.
DR BRENDA; 1.8.4.12; 3474.
DR Reactome; R-MMU-5676934; Protein repair.
DR BioGRID-ORCS; 76467; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Msrb2; mouse.
DR PRO; PR:Q78J03; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q78J03; protein.
DR Bgee; ENSMUSG00000023094; Expressed in interventricular septum and 204 other tissues.
DR Genevisible; Q78J03; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:HGNC-UCL.
DR GO; GO:0003779; F:actin binding; IDA: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; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:HGNC-UCL.
DR GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0030091; P:protein repair; IDA:HGNC-UCL.
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 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Mitochondrion; Oxidoreductase;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..175
FT /note="Methionine-R-sulfoxide reductase B2, mitochondrial"
FT /id="PRO_0000327243"
FT DOMAIN 44..173
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT REGION 22..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 162
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:2L1U"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:2L1U"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2L1U"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:2L1U"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:2L1U"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2L1U"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:2L1U"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:2L1U"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:2L1U"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2L1U"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:2L1U"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:2L1U"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2L1U"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2L1U"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:2L1U"
SQ SEQUENCE 175 AA; 19157 MW; 916771737762C6A6 CRC64;
MARLLRALRG LPLLQAPGRL ARGCAGSGSK DTGSLTKSKR SLSEADWQKK LTPEQFYVTR
EKGTEAPFSG MYLNNKETGM YHCVCCDSPL FSSEKKYCSG TGWPSFSEAY GSKGSDESHT
GILRRLDTSL GCPRMEVVCK QCEAHLGHVF PDGPKPTGQR FCINSVALKF KPSKP
