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Protein

Peptide methionine sulfoxide reductase 2

Gene

MXR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Methionine-R-sulfoxide reductase which catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. Protects iron-sulfur clusters from oxidative inactivation along with MXR1. Involved in the regulation of lifespan.2 Publications

Catalytic activityi

Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791ZincPROSITE-ProRule annotation
Metal bindingi82 – 821ZincPROSITE-ProRule annotation
Metal bindingi128 – 1281ZincPROSITE-ProRule annotation
Metal bindingi131 – 1311ZincPROSITE-ProRule annotation
Active sitei157 – 1571NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • peptide-methionine (R)-S-oxide reductase activity Source: SGD

GO - Biological processi

  • cellular response to oxidative stress Source: SGD
  • protein repair Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29293-MONOMER.
ReactomeiR-SCE-5676934. Protein repair.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide methionine sulfoxide reductase 2 (EC:1.8.4.12)
Gene namesi
Name:MXR2
Synonyms:MSRB
Ordered Locus Names:YCL033C
ORF Names:YCL33C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCL033C.
SGDiS000000538. MXR2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 168168Peptide methionine sulfoxide reductase 2PRO_0000140326Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi97 ↔ 157Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP25566.

Interactioni

Protein-protein interaction databases

BioGridi30950. 18 interactions.
DIPiDIP-4861N.
IntActiP25566. 2 interactions.
MINTiMINT-507745.

Structurei

3D structure databases

ProteinModelPortaliP25566.
SMRiP25566. Positions 54-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 168129MsrBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 MsrB (methionine-R-sulfoxide reductase) domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

GeneTreeiENSGT00510000046802.
InParanoidiP25566.
KOiK07305.
OMAiSFFETVR.
OrthoDBiEOG751NSN.

Family and domain databases

Gene3Di2.170.150.20. 1 hit.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002579. Met_Sox_Rdtase_MsrB.
IPR011057. Mss4-like.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 1 hit.
PfamiPF01641. SelR. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
TIGRFAMsiTIGR00357. TIGR00357. 1 hit.
PROSITEiPS51790. MSRB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25566-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKWSRLYVI TVRRTFPGRR NIVLTQYWNK SKKMSDESND VKWNDALTPL
60 70 80 90 100
QLMVLRDKAT ERPNTGAYLH TNESGVYHCA NCDRPLYSSK AKFDARCGWP
110 120 130 140 150
AFYEEVSPGA ITYHRDNSLM PARVEICCAR CGGHLGHVFE GEGWKQLLNL
160
PKDTRHCVNS ASLNLKKD
Length:168
Mass (Da):19,279
Last modified:May 1, 1992 - v1
Checksum:iC79BE75DC35D82F4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42383.1.
BK006937 Genomic DNA. Translation: DAA07451.1.
PIRiS19361.
RefSeqiNP_009897.1. NM_001178678.1.

Genome annotation databases

EnsemblFungiiCAA42383; CAA42383; CAA42383.
YCL033C; YCL033C; YCL033C.
GeneIDi850324.
KEGGisce:YCL033C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42383.1.
BK006937 Genomic DNA. Translation: DAA07451.1.
PIRiS19361.
RefSeqiNP_009897.1. NM_001178678.1.

3D structure databases

ProteinModelPortaliP25566.
SMRiP25566. Positions 54-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi30950. 18 interactions.
DIPiDIP-4861N.
IntActiP25566. 2 interactions.
MINTiMINT-507745.

Proteomic databases

MaxQBiP25566.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42383; CAA42383; CAA42383.
YCL033C; YCL033C; YCL033C.
GeneIDi850324.
KEGGisce:YCL033C.

Organism-specific databases

EuPathDBiFungiDB:YCL033C.
SGDiS000000538. MXR2.

Phylogenomic databases

GeneTreeiENSGT00510000046802.
InParanoidiP25566.
KOiK07305.
OMAiSFFETVR.
OrthoDBiEOG751NSN.

Enzyme and pathway databases

BioCyciYEAST:G3O-29293-MONOMER.
ReactomeiR-SCE-5676934. Protein repair.

Miscellaneous databases

PROiP25566.

Family and domain databases

Gene3Di2.170.150.20. 1 hit.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002579. Met_Sox_Rdtase_MsrB.
IPR011057. Mss4-like.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 1 hit.
PfamiPF01641. SelR. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
TIGRFAMsiTIGR00357. TIGR00357. 1 hit.
PROSITEiPS51790. MSRB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  4. "Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and -independent components of aging."
    Koc A., Gasch A.P., Rutherford J.C., Kim H.Y., Gladyshev V.N.
    Proc. Natl. Acad. Sci. U.S.A. 101:7999-8004(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Methionine sulphoxide reductases protect iron-sulphur clusters from oxidative inactivation in yeast."
    Sideri T.C., Willetts S.A., Avery S.V.
    Microbiology 155:612-623(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMXR2_YEAST
AccessioniPrimary (citable) accession number: P25566
Secondary accession number(s): D6VQY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 6, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 799 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.