MSRB1_ARATH
ID MSRB1_ARATH Reviewed; 202 AA.
AC Q9C8M2; A6QRB3; Q8LAR2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Peptide methionine sulfoxide reductase B1, chloroplastic {ECO:0000303|PubMed:15923321, ECO:0000303|PubMed:17031545};
DE Short=AtMSRB1 {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 reductase;
DE Flags: Precursor;
GN Name=MSRB1 {ECO:0000303|PubMed:15923321, ECO:0000303|PubMed:17031545};
GN OrderedLocusNames=At1g53670 {ECO:0000312|Araport:AT1G53670};
GN ORFNames=F22G10.17 {ECO:0000312|EMBL:AAG51964.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 2).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quan R., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-202 (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-202 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP 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-116; THR-132 AND CYS-186, CATALYTIC ACTIVITY,
RP AND 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, AND MUTAGENESIS OF CYS-186.
RX PubMed=20236937; DOI=10.1074/jbc.m110.108373;
RA Tarrago L., Laugier E., Zaffagnini M., Marchand C.H., Le Marechal P.,
RA Lemaire S.D., Rey P.;
RT "Plant thioredoxin CDSP32 regenerates 1-Cys methionine sulfoxide reductase
RT B activity through the direct reduction of sulfenic acid.";
RL J. Biol. Chem. 285:14964-14972(2010).
RN [11]
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 MSRB2 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, ECO:0000269|PubMed:20236937}.
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=78.5 uM for dabsyl methionine sulfoxide
CC {ECO:0000269|PubMed:15923321};
CC Note=kcat is 0.075 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=Q9C8M2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C8M2-2; Sequence=VSP_039509;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in stems, leaves, floral
CC buds, flowers and siliques (at protein level).
CC {ECO:0000269|PubMed:15923321}.
CC -!- INDUCTION: By photooxidative stress. {ECO:0000269|PubMed:15923321}.
CC -!- MISCELLANEOUS: Lacks the conserved cysteine (here Thr-132) required for
CC the reduction by thioredoxins (TRX) through a dithiol-disulfide
CC exchange involving both redox-active Cys of TRX and MSRB. Reduced by
CC thioredoxin CDSP32 which regenerates MSRB1 through the direct reduction
CC of the sulfenic acid formed on the catalytic Cys, without the help of
CC any other thiol compound. Also reduced by the glutahione/glutaredoxin
CC (GSH/GRX) system via a glutathionylation step of the sulfenic acid and
CC then by GRX reduction of the GSH-MSR adduct.
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65202.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC41985.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC024260; AAG51964.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32979.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32980.1; -; Genomic_DNA.
DR EMBL; BT030636; ABR46216.1; -; mRNA.
DR EMBL; AY087664; AAM65202.1; ALT_INIT; mRNA.
DR EMBL; AK117314; BAC41985.1; ALT_INIT; mRNA.
DR PIR; H96576; H96576.
DR RefSeq; NP_001117484.1; NM_001124012.1. [Q9C8M2-2]
DR RefSeq; NP_564640.2; NM_104245.4. [Q9C8M2-1]
DR AlphaFoldDB; Q9C8M2; -.
DR SMR; Q9C8M2; -.
DR BioGRID; 27029; 1.
DR STRING; 3702.AT1G53670.1; -.
DR PaxDb; Q9C8M2; -.
DR PRIDE; Q9C8M2; -.
DR ProteomicsDB; 250793; -. [Q9C8M2-1]
DR EnsemblPlants; AT1G53670.1; AT1G53670.1; AT1G53670. [Q9C8M2-1]
DR EnsemblPlants; AT1G53670.2; AT1G53670.2; AT1G53670. [Q9C8M2-2]
DR GeneID; 841804; -.
DR Gramene; AT1G53670.1; AT1G53670.1; AT1G53670. [Q9C8M2-1]
DR Gramene; AT1G53670.2; AT1G53670.2; AT1G53670. [Q9C8M2-2]
DR KEGG; ath:AT1G53670; -.
DR Araport; AT1G53670; -.
DR TAIR; locus:2024817; AT1G53670.
DR eggNOG; KOG0856; Eukaryota.
DR HOGENOM; CLU_031040_8_0_1; -.
DR InParanoid; Q9C8M2; -.
DR OMA; CAMGSAP; -.
DR OrthoDB; 1549489at2759; -.
DR PhylomeDB; Q9C8M2; -.
DR SABIO-RK; Q9C8M2; -.
DR PRO; PR:Q9C8M2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8M2; baseline and differential.
DR Genevisible; Q9C8M2; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; 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 Alternative splicing; Chloroplast; Electron transport; Metal-binding;
KW Oxidoreductase; Plastid; Redox-active center; Reference proteome;
KW 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 B1,
FT chloroplastic"
FT /id="PRO_0000395519"
FT DOMAIN 75..197
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT REGION 48..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT VAR_SEQ 124..130
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_039509"
FT MUTAGEN 116
FT /note="C->S: Decreases activity 2-fold."
FT /evidence="ECO:0000269|PubMed:19457862"
FT MUTAGEN 132
FT /note="T->C: Decreases activity 6-fold."
FT /evidence="ECO:0000269|PubMed:19457862"
FT MUTAGEN 132
FT /note="T->S: Decreases activity 14-fold."
FT /evidence="ECO:0000269|PubMed:19457862"
FT MUTAGEN 186
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19457862,
FT ECO:0000269|PubMed:20236937"
SQ SEQUENCE 202 AA; 22607 MW; DBF2554E14511B6C CRC64;
MASSTRLTII QSSFVSARTR LNYVSKTNHS GFACRSLSKP RNLSLSVYSM GSSSSSPKPD
NVQEAEKNEF ASLSENEWKK RLTPEQYYIT RQKGTERAFT GEYWNSKTPG VYNCVCCDTP
LFDSSTKFDS GTGWPSYYQP IGNNVKTKLD LSIIFMPRQE VVCAVCNAHL GHVFDDGPRP
TGKRYCLNSA ALKLNALEKT RD
