MSRA3_ARATH
ID MSRA3_ARATH Reviewed; 202 AA.
AC Q9LY14; Q8GX95; Q8LBR1; Q9S813;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Peptide methionine sulfoxide reductase A3;
DE Short=AtMSRA3;
DE EC=1.8.4.11 {ECO:0000269|PubMed:10806242};
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE Short=Peptide Met(O) reductase;
DE AltName: Full=Protein-methionine-S-oxide reductase;
GN Name=MSRA3; Synonyms=MSR, PMSR3; OrderedLocusNames=At5g07470;
GN ORFNames=T2I1.180;
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10806242; DOI=10.1104/pp.123.1.255;
RA Sadanandom A., Poghosyan Z., Fairbairn D.J., Murphy D.J.;
RT "Differential regulation of plastidial and cytosolic isoforms of peptide
RT methionine sulfoxide reductase in Arabidopsis.";
RL Plant Physiol. 123:255-264(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-202.
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 [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).
CC -!- FUNCTION: Catalyzes the reduction of methionine sulfoxide (MetSO) to
CC methionine in proteins. Plays a protective role against oxidative
CC stress by restoring activity to proteins that have been inactivated by
CC methionine oxidation. May prevent cellular oxidative damage due to
CC light exposure. MSRA family specifically reduces the MetSO S-
CC enantiomer. {ECO:0000269|PubMed:10806242}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC ChEBI:CHEBI:50058; EC=1.8.4.11;
CC Evidence={ECO:0000269|PubMed:10806242};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14219;
CC Evidence={ECO:0000305|PubMed:10806242};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, 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:58772; EC=1.8.4.11;
CC Evidence={ECO:0000269|PubMed:10806242};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19995;
CC Evidence={ECO:0000305|PubMed:10806242};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:10806242};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC -!- TISSUE SPECIFICITY: Expressed in rosette and cauline leaves, and at
CC lower levels in roots, stems and flowers (at protein level).
CC {ECO:0000269|PubMed:10806242}.
CC -!- INDUCTION: By light in etiolated seedlings (at protein level).
CC {ECO:0000269|PubMed:10806242}.
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC42967.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ133753; CAB43186.1; -; mRNA.
DR EMBL; AJ133754; CAB43187.1; -; Genomic_DNA.
DR EMBL; AL163912; CAB87936.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91162.1; -; Genomic_DNA.
DR EMBL; AY044316; AAK73257.1; -; mRNA.
DR EMBL; AY087046; AAM64607.1; -; mRNA.
DR EMBL; AK118353; BAC42967.1; ALT_INIT; mRNA.
DR PIR; T49886; T49886.
DR PIR; T52657; T52657.
DR RefSeq; NP_196364.1; NM_120829.3.
DR AlphaFoldDB; Q9LY14; -.
DR SMR; Q9LY14; -.
DR STRING; 3702.AT5G07470.1; -.
DR MetOSite; Q9LY14; -.
DR PaxDb; Q9LY14; -.
DR PRIDE; Q9LY14; -.
DR ProteomicsDB; 239010; -.
DR EnsemblPlants; AT5G07470.1; AT5G07470.1; AT5G07470.
DR GeneID; 830638; -.
DR Gramene; AT5G07470.1; AT5G07470.1; AT5G07470.
DR KEGG; ath:AT5G07470; -.
DR Araport; AT5G07470; -.
DR TAIR; locus:2183419; AT5G07470.
DR eggNOG; KOG1635; Eukaryota.
DR HOGENOM; CLU_031040_3_0_1; -.
DR InParanoid; Q9LY14; -.
DR OMA; NDCSYES; -.
DR OrthoDB; 1383773at2759; -.
DR PhylomeDB; Q9LY14; -.
DR PRO; PR:Q9LY14; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LY14; baseline and differential.
DR Genevisible; Q9LY14; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IDA:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR Gene3D; 3.30.1060.10; -; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR Pfam; PF01625; PMSR; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..202
FT /note="Peptide methionine sulfoxide reductase A3"
FT /id="PRO_0000395513"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LY15"
FT CONFLICT 71
FT /note="D -> H (in Ref. 5; AAM64607)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="G -> V (in Ref. 1; CAB43186/CAB43187)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="Q -> H (in Ref. 1; CAB43186/CAB43187)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="R -> RHQ (in Ref. 1; CAB43186/CAB43187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22545 MW; 9AC13CB8A9336C84 CRC64;
MNILNRLGLG SSGQTNMDPS PIAQGNDDDT PAPGNQFAQF GAGCFWGVEL AFQRVPGVTQ
TEAGYTQGTV DNPSYGDVCS GTTGHSEVVR VQYDLNDCTY ESLLDLFWSR HDPTTLNRQG
NDVGTQYRSG IYFYTPEQEK LARESLERHQ QQMERKIMTE ILPAKKFYRA EEHHQQYLSK
GGRFGQGQST AKGCNDPIRC YG
