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Protein

Peptide methionine sulfoxide reductase B2, chloroplastic

Gene

MSRB2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Specifically reduces the MetSO R-enantiomer. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. May play an essential function in association with MSRB1 in maintaining vegetative growth during environmental constraints, through the preservation of photosynthetic antennae. MSRB1 and MSRB2 account for most of the leaf peptide MSR capacity.4 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

Kineticsi

  1. KM=54 µM for dabsyl methionine sulfoxide1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi116 – 1161ZincPROSITE-ProRule annotation
    Metal bindingi119 – 1191ZincPROSITE-ProRule annotation
    Metal bindingi162 – 1621ZincPROSITE-ProRule annotation
    Metal bindingi165 – 1651ZincPROSITE-ProRule annotation
    Active sitei187 – 1871NucleophilePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciARA:AT4G21860-MONOMER.
    ARA:GQT-564-MONOMER.
    ARA:GQT-565-MONOMER.
    ReactomeiR-ATH-5676934. Protein repair.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptide methionine sulfoxide reductase B2, chloroplastic (EC:1.8.4.12)
    Short name:
    AtMSRB2
    Alternative name(s):
    Peptide-methionine (R)-S-oxide reductase
    Gene namesi
    Name:MSRB2
    Ordered Locus Names:At4g21860
    ORF Names:T8O5.70
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G21860.

    Subcellular locationi

    • Plastidchloroplast 1 Publication

    GO - Cellular componenti

    • chloroplast Source: UniProtKB
    • chloroplast stroma Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi134 – 1341C → S or T: Increases activity 2-fold. Abolishes reduction by thioredoxin h. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6363ChloroplastSequence analysisAdd
    BLAST
    Chaini64 – 202139Peptide methionine sulfoxide reductase B2, chloroplasticPRO_0000395520Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi134 ↔ 187Redox-active

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiQ9C5C8.
    PRIDEiQ9C5C8.

    PTM databases

    iPTMnetiQ9C5C8.

    Expressioni

    Tissue specificityi

    Expressed in stems, young leaves, floral buds and flowers. Expressed at low levels in roots, mature leaves and siliques (at protein level).1 Publication

    Inductioni

    By photooxidative stress.1 Publication

    Gene expression databases

    GenevisibleiQ9C5C8. AT.

    Interactioni

    Protein-protein interaction databases

    BioGridi13563. 1 interaction.
    IntActiQ9C5C8. 1 interaction.
    STRINGi3702.AT4G21860.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9C5C8.
    SMRiQ9C5C8. Positions 82-202.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini77 – 198122MsrBPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Redox-active center, Transit peptide

    Phylogenomic databases

    eggNOGiKOG0856. Eukaryota.
    COG0229. LUCA.
    HOGENOMiHOG000243424.
    InParanoidiQ9C5C8.
    KOiK07305.
    OMAiTIELISY.
    PhylomeDBiQ9C5C8.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9C5C8-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MAFNIITPGR VYSATSLTFV STIKAAFVKP PLASPSRRNL LRFSSSPLSF
    60 70 80 90 100
    PSLRRGFHGG RIVAMGSSAP ESVNKPEEEW RAILSPEQFR ILRQKGTEYP
    110 120 130 140 150
    GTGEYNKVFD DGIYCCAGCG TPLYKSTTKF DSGCGWPAFF DGLPGAITRT
    160 170 180 190 200
    PDPDGRRIEI TCAACGGHLG HVFKGEGFPT PTDERHCVNS ISLKFTPENP

    TL
    Length:202
    Mass (Da):21,968
    Last modified:June 1, 2001 - v1
    Checksum:i53B85798B1E94D68
    GO
    Isoform 2 (identifier: Q9C5C8-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         151-184: PDPDGRRIEITCAACGGHLGHVFKGEGFPTPTDE → MGDESRSHVLLVEDILVTFLKEKVSLLLPMSDTV
         185-202: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:184
    Mass (Da):20,164
    Checksum:i1CFC2A20A3CAEF9A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 377PLASPSR → SFASRSH in AAM62876 (Ref. 5) Curated
    Sequence conflicti64 – 641A → S in AAM62876 (Ref. 5) Curated
    Sequence conflicti79 – 791E → G in BAH19668 (PubMed:19423640).Curated
    Sequence conflicti82 – 821A → T in AAM62876 (Ref. 5) Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei151 – 18434PDPDG…TPTDE → MGDESRSHVLLVEDILVTFL KEKVSLLLPMSDTV in isoform 2. 1 PublicationVSP_039510Add
    BLAST
    Alternative sequencei185 – 20218Missing in isoform 2. 1 PublicationVSP_039511Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL021890 Genomic DNA. No translation available.
    AL161556 Genomic DNA. No translation available.
    CP002687 Genomic DNA. Translation: AEE84513.1.
    CP002687 Genomic DNA. Translation: AEE84514.1.
    CP002687 Genomic DNA. Translation: AEE84515.1.
    AF360341 mRNA. Translation: AAK28638.1.
    AY051078 mRNA. Translation: AAK93755.1.
    AK316971 mRNA. Translation: BAH19668.1.
    AY085655 mRNA. Translation: AAM62876.1.
    RefSeqiNP_001078423.1. NM_001084954.2. [Q9C5C8-2]
    NP_001190791.1. NM_001203862.1. [Q9C5C8-1]
    NP_567639.1. NM_118306.6. [Q9C5C8-1]
    UniGeneiAt.24358.

    Genome annotation databases

    EnsemblPlantsiAT4G21860.1; AT4G21860.1; AT4G21860. [Q9C5C8-1]
    AT4G21860.3; AT4G21860.3; AT4G21860. [Q9C5C8-1]
    GeneIDi828274.
    KEGGiath:AT4G21860.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL021890 Genomic DNA. No translation available.
    AL161556 Genomic DNA. No translation available.
    CP002687 Genomic DNA. Translation: AEE84513.1.
    CP002687 Genomic DNA. Translation: AEE84514.1.
    CP002687 Genomic DNA. Translation: AEE84515.1.
    AF360341 mRNA. Translation: AAK28638.1.
    AY051078 mRNA. Translation: AAK93755.1.
    AK316971 mRNA. Translation: BAH19668.1.
    AY085655 mRNA. Translation: AAM62876.1.
    RefSeqiNP_001078423.1. NM_001084954.2. [Q9C5C8-2]
    NP_001190791.1. NM_001203862.1. [Q9C5C8-1]
    NP_567639.1. NM_118306.6. [Q9C5C8-1]
    UniGeneiAt.24358.

    3D structure databases

    ProteinModelPortaliQ9C5C8.
    SMRiQ9C5C8. Positions 82-202.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi13563. 1 interaction.
    IntActiQ9C5C8. 1 interaction.
    STRINGi3702.AT4G21860.1.

    PTM databases

    iPTMnetiQ9C5C8.

    Proteomic databases

    PaxDbiQ9C5C8.
    PRIDEiQ9C5C8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G21860.1; AT4G21860.1; AT4G21860. [Q9C5C8-1]
    AT4G21860.3; AT4G21860.3; AT4G21860. [Q9C5C8-1]
    GeneIDi828274.
    KEGGiath:AT4G21860.

    Organism-specific databases

    TAIRiAT4G21860.

    Phylogenomic databases

    eggNOGiKOG0856. Eukaryota.
    COG0229. LUCA.
    HOGENOMiHOG000243424.
    InParanoidiQ9C5C8.
    KOiK07305.
    OMAiTIELISY.
    PhylomeDBiQ9C5C8.

    Enzyme and pathway databases

    BioCyciARA:AT4G21860-MONOMER.
    ARA:GQT-564-MONOMER.
    ARA:GQT-565-MONOMER.
    ReactomeiR-ATH-5676934. Protein repair.

    Miscellaneous databases

    PROiQ9C5C8.

    Gene expression databases

    GenevisibleiQ9C5C8. AT.

    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. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: cv. Columbia.
    4. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
      Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
      DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: cv. Columbia.
    5. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "The Arabidopsis plastidic methionine sulfoxide reductase B proteins. Sequence and activity characteristics, comparison of the expression with plastidic methionine sulfoxide reductase A, and induction by photooxidative stress."
      Vieira Dos Santos C., Cuine S., Rouhier N., Rey P.
      Plant Physiol. 138:909-922(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    7. "Plant methionine sulfoxide reductase A and B multigenic families."
      Rouhier N., Vieira Dos Santos C., Tarrago L., Rey P.
      Photosyn. Res. 89:247-262(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.
    8. "Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B."
      Vieira Dos Santos C., Laugier E., Tarrago L., Massot V., Issakidis-Bourguet E., Rouhier N., Rey P.
      FEBS Lett. 581:4371-4376(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Regeneration mechanisms of Arabidopsis thaliana methionine sulfoxide reductases B by glutaredoxins and thioredoxins."
      Tarrago L., Laugier E., Zaffagnini M., Marchand C., Le Marechal P., Rouhier N., Lemaire S.D., Rey P.
      J. Biol. Chem. 284:18963-18971(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-134.
    10. "Arabidopsis thaliana plastidial methionine sulfoxide reductases B, MSRBs, account for most leaf peptide MSR activity and are essential for growth under environmental constraints through a role in the preservation of photosystem antennas."
      Laugier E., Tarrago L., Vieira Dos Santos C., Eymery F., Havaux M., Rey P.
      Plant J. 61:271-282(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiMSRB2_ARATH
    AccessioniPrimary (citable) accession number: Q9C5C8
    Secondary accession number(s): A8MQE9, B9DG01, Q8LE28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: June 1, 2001
    Last modified: June 8, 2016
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Reduced by thioredoxins f, m, x and y through a dithiol-disulfide exchange involving both redox-active Cys of the two partners.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    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.