MSRB2_ARATH
ID MSRB2_ARATH Reviewed; 202 AA.
AC Q9C5C8; A8MQE9; B9DG01; Q8LE28;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Peptide methionine sulfoxide reductase B2, chloroplastic {ECO:0000303|PubMed:15923321, ECO:0000303|PubMed:17031545};
DE Short=AtMSRB2 {ECO:0000303|PubMed:15923321, ECO:0000303|PubMed:17031545};
DE EC=1.8.4.12 {ECO:0000269|PubMed:15923321, ECO:0000269|PubMed:17761174, ECO:0000269|PubMed:19457862};
DE AltName: Full=Peptide-methionine (R)-S-oxide reductasemethionine;
DE Flags: Precursor;
GN Name=MSRB2 {ECO:0000303|PubMed:15923321, ECO:0000303|PubMed:17031545};
GN OrderedLocusNames=At4g21860 {ECO:0000312|Araport:AT4G21860};
GN ORFNames=T8O5.70 {ECO:0000312|EMBL:AL021890};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15923321; DOI=10.1104/pp.105.062430;
RA Vieira Dos Santos C., Cuine S., Rouhier N., Rey P.;
RT "The Arabidopsis plastidic methionine sulfoxide reductase B proteins.
RT Sequence and activity characteristics, comparison of the expression with
RT plastidic methionine sulfoxide reductase A, and induction by photooxidative
RT stress.";
RL Plant Physiol. 138:909-922(2005).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17031545; DOI=10.1007/s11120-006-9097-1;
RA Rouhier N., Vieira Dos Santos C., Tarrago L., Rey P.;
RT "Plant methionine sulfoxide reductase A and B multigenic families.";
RL Photosyn. Res. 89:247-262(2006).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17761174; DOI=10.1016/j.febslet.2007.07.081;
RA Vieira Dos Santos C., Laugier E., Tarrago L., Massot V.,
RA Issakidis-Bourguet E., Rouhier N., Rey P.;
RT "Specificity of thioredoxins and glutaredoxins as electron donors to two
RT distinct classes of Arabidopsis plastidial methionine sulfoxide reductases
RT B.";
RL FEBS Lett. 581:4371-4376(2007).
RN [9]
RP FUNCTION, MUTAGENESIS OF CYS-134, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19457862; DOI=10.1074/jbc.m109.015487;
RA Tarrago L., Laugier E., Zaffagnini M., Marchand C., Le Marechal P.,
RA Rouhier N., Lemaire S.D., Rey P.;
RT "Regeneration mechanisms of Arabidopsis thaliana methionine sulfoxide
RT reductases B by glutaredoxins and thioredoxins.";
RL J. Biol. Chem. 284:18963-18971(2009).
RN [10]
RP FUNCTION.
RX PubMed=19874542; DOI=10.1111/j.1365-313x.2009.04053.x;
RA Laugier E., Tarrago L., Vieira Dos Santos C., Eymery F., Havaux M., Rey P.;
RT "Arabidopsis thaliana plastidial methionine sulfoxide reductases B, MSRBs,
RT account for most leaf peptide MSR activity and are essential for growth
RT under environmental constraints through a role in the preservation of
RT photosystem antennas.";
RL Plant J. 61:271-282(2010).
CC -!- FUNCTION: Catalyzes the reduction of methionine sulfoxide (MetSO) to
CC methionine in proteins. Specifically reduces the MetSO R-enantiomer.
CC Plays a protective role against oxidative stress by restoring activity
CC to proteins that have been inactivated by methionine oxidation. May
CC play an essential function in association with MSRB1 in maintaining
CC vegetative growth during environmental constraints, through the
CC preservation of photosynthetic antennae. MSRB1 and MSRB2 account for
CC most of the leaf peptide MSR capacity. {ECO:0000269|PubMed:15923321,
CC ECO:0000269|PubMed:17761174, ECO:0000269|PubMed:19457862,
CC ECO:0000269|PubMed:19874542}.
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:0000269|PubMed:15923321, ECO:0000269|PubMed:17761174,
CC ECO:0000269|PubMed:19457862};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0A746};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P0A746};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=54 uM for dabsyl methionine sulfoxide
CC {ECO:0000269|PubMed:15923321};
CC Note=kcat is 0.028 sec(-1) with dabsyl-MetSO as substrate.
CC {ECO:0000269|PubMed:19457862};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15923321}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C5C8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C5C8-2; Sequence=VSP_039510, VSP_039511;
CC -!- TISSUE SPECIFICITY: Expressed in stems, young leaves, floral buds and
CC flowers. Expressed at low levels in roots, mature leaves and siliques
CC (at protein level). {ECO:0000269|PubMed:15923321}.
CC -!- INDUCTION: By photooxidative stress. {ECO:0000269|PubMed:15923321}.
CC -!- MISCELLANEOUS: Reduced by thioredoxins f, m, x and y through a dithiol-
CC disulfide exchange involving both redox-active Cys of the two partners.
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; AL021890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE84513.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84514.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84515.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67853.1; -; Genomic_DNA.
DR EMBL; AF360341; AAK28638.1; -; mRNA.
DR EMBL; AY051078; AAK93755.1; -; mRNA.
DR EMBL; AK316971; BAH19668.1; -; mRNA.
DR EMBL; AY085655; AAM62876.1; -; mRNA.
DR RefSeq; NP_001078423.1; NM_001084954.2. [Q9C5C8-2]
DR RefSeq; NP_001190791.1; NM_001203862.1. [Q9C5C8-1]
DR RefSeq; NP_001320026.1; NM_001341518.1. [Q9C5C8-1]
DR RefSeq; NP_567639.1; NM_118306.7. [Q9C5C8-1]
DR AlphaFoldDB; Q9C5C8; -.
DR SMR; Q9C5C8; -.
DR BioGRID; 13563; 1.
DR IntAct; Q9C5C8; 1.
DR STRING; 3702.AT4G21860.1; -.
DR iPTMnet; Q9C5C8; -.
DR PaxDb; Q9C5C8; -.
DR PRIDE; Q9C5C8; -.
DR ProteomicsDB; 239015; -. [Q9C5C8-1]
DR EnsemblPlants; AT4G21860.1; AT4G21860.1; AT4G21860. [Q9C5C8-1]
DR EnsemblPlants; AT4G21860.2; AT4G21860.2; AT4G21860. [Q9C5C8-2]
DR EnsemblPlants; AT4G21860.3; AT4G21860.3; AT4G21860. [Q9C5C8-1]
DR EnsemblPlants; AT4G21860.4; AT4G21860.4; AT4G21860. [Q9C5C8-1]
DR GeneID; 828274; -.
DR Gramene; AT4G21860.1; AT4G21860.1; AT4G21860. [Q9C5C8-1]
DR Gramene; AT4G21860.2; AT4G21860.2; AT4G21860. [Q9C5C8-2]
DR Gramene; AT4G21860.3; AT4G21860.3; AT4G21860. [Q9C5C8-1]
DR Gramene; AT4G21860.4; AT4G21860.4; AT4G21860. [Q9C5C8-1]
DR KEGG; ath:AT4G21860; -.
DR Araport; AT4G21860; -.
DR TAIR; locus:2141702; AT4G21860.
DR eggNOG; KOG0856; Eukaryota.
DR HOGENOM; CLU_031040_8_1_1; -.
DR InParanoid; Q9C5C8; -.
DR OMA; SXCGAHL; -.
DR OrthoDB; 1549489at2759; -.
DR PhylomeDB; Q9C5C8; -.
DR SABIO-RK; Q9C5C8; -.
DR PRO; PR:Q9C5C8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9C5C8; baseline and differential.
DR Genevisible; Q9C5C8; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IDA:UniProtKB.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEP:UniProtKB.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR PANTHER; PTHR46081; PTHR46081; 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 Alternative splicing; Chloroplast; Disulfide bond; Electron transport;
KW Metal-binding; Oxidoreductase; Plastid; Redox-active center;
KW Reference proteome; Transit peptide; Transport; Zinc.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..202
FT /note="Peptide methionine sulfoxide reductase B2,
FT chloroplastic"
FT /id="PRO_0000395520"
FT DOMAIN 77..198
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 187
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT DISULFID 134..187
FT /note="Redox-active"
FT VAR_SEQ 151..184
FT /note="PDPDGRRIEITCAACGGHLGHVFKGEGFPTPTDE -> MGDESRSHVLLVED
FT ILVTFLKEKVSLLLPMSDTV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039510"
FT VAR_SEQ 185..202
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039511"
FT MUTAGEN 134
FT /note="C->S,T: Increases activity 2-fold. Abolishes
FT reduction by thioredoxin h."
FT /evidence="ECO:0000269|PubMed:19457862"
FT CONFLICT 31..37
FT /note="PLASPSR -> SFASRSH (in Ref. 5; AAM62876)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="A -> S (in Ref. 5; AAM62876)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="E -> G (in Ref. 4; BAH19668)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="A -> T (in Ref. 5; AAM62876)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 21968 MW; 53B85798B1E94D68 CRC64;
MAFNIITPGR VYSATSLTFV STIKAAFVKP PLASPSRRNL LRFSSSPLSF PSLRRGFHGG
RIVAMGSSAP ESVNKPEEEW RAILSPEQFR ILRQKGTEYP GTGEYNKVFD DGIYCCAGCG
TPLYKSTTKF DSGCGWPAFF DGLPGAITRT PDPDGRRIEI TCAACGGHLG HVFKGEGFPT
PTDERHCVNS ISLKFTPENP TL
