MSRA4_ARATH
ID MSRA4_ARATH Reviewed; 258 AA.
AC P54150; Q8LAX4; Q94A72; Q9SW13;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Peptide methionine sulfoxide reductase A4, chloroplastic;
DE Short=AtMSRA4;
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;
DE Flags: Precursor;
GN Name=MSR4; Synonyms=PMSR, PMSR4; OrderedLocusNames=At4g25130;
GN ORFNames=F13M23.270;
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].
RC STRAIN=cv. Columbia;
RA Piffanelli P., Batchedler C., Murphy D.J.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP 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 [7]
RP FUNCTION.
RX PubMed=11874568; DOI=10.1046/j.1365-313x.2002.029005545.x;
RA Gustavsson N., Kokke B.P., Haerndahl U., Silow M., Bechtold U.,
RA Poghosyan Z., Murphy D., Boelens W.C., Sundby C.;
RT "A peptide methionine sulfoxide reductase highly expressed in
RT photosynthetic tissue in Arabidopsis thaliana can protect the chaperone-
RT like activity of a chloroplast-localized small heat shock protein.";
RL Plant J. 29:545-553(2002).
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-54, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER PRO-53, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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. Prevents the methionine sulfoxidation of the heat
CC shock protein HSP21 and its subsequent inactivation. MSRA family
CC specifically reduces the MetSO S-enantiomer.
CC {ECO:0000269|PubMed:10806242, ECO:0000269|PubMed:11874568}.
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 -!- 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:10806242};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC -!- TISSUE SPECIFICITY: Expressed in rosette and cauline leaves, and at
CC lower levels in 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}.
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DR EMBL; X97326; CAA65991.1; -; Genomic_DNA.
DR EMBL; AL035523; CAB36755.1; -; Genomic_DNA.
DR EMBL; AL161562; CAB79422.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85015.1; -; Genomic_DNA.
DR EMBL; AY049303; AAK83645.1; -; mRNA.
DR EMBL; BT001033; AAN46787.1; -; mRNA.
DR EMBL; AY087550; AAM65092.1; -; mRNA.
DR PIR; T05534; T05534.
DR RefSeq; NP_194243.1; NM_118645.4.
DR AlphaFoldDB; P54150; -.
DR SMR; P54150; -.
DR IntAct; P54150; 1.
DR STRING; 3702.AT4G25130.1; -.
DR iPTMnet; P54150; -.
DR SwissPalm; P54150; -.
DR PaxDb; P54150; -.
DR PRIDE; P54150; -.
DR ProteomicsDB; 239011; -.
DR EnsemblPlants; AT4G25130.1; AT4G25130.1; AT4G25130.
DR GeneID; 828616; -.
DR Gramene; AT4G25130.1; AT4G25130.1; AT4G25130.
DR KEGG; ath:AT4G25130; -.
DR Araport; AT4G25130; -.
DR TAIR; locus:2117313; AT4G25130.
DR eggNOG; KOG1635; Eukaryota.
DR HOGENOM; CLU_031040_3_1_1; -.
DR InParanoid; P54150; -.
DR OMA; PAACKFD; -.
DR OrthoDB; 1383773at2759; -.
DR PhylomeDB; P54150; -.
DR BRENDA; 1.8.4.11; 399.
DR PRO; PR:P54150; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P54150; baseline and differential.
DR Genevisible; P54150; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; 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; IMP:TAIR.
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 Acetylation; Chloroplast; Oxidoreductase; Phosphoprotein; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 54..258
FT /note="Peptide methionine sulfoxide reductase A4,
FT chloroplastic"
FT /id="PRO_0000138632"
FT REGION 62..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LY15"
FT CONFLICT 131
FT /note="Y -> S (in Ref. 1; CAA65991)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="E -> D (in Ref. 4; AAK83645/AAN46787)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="R -> K (in Ref. 5; AAM65092)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="R -> K (in Ref. 4; AAK83645/AAN46787)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 258 AA; 28644 MW; DCB95E4B4CF88EA1 CRC64;
MQVLVVSPPL IAAASLSKPL NSLSKAALSF SRAKPICPFP QTSRRPISVY KSPMNNLFNR
LGFGSRPQAQ ADPSSAAIAQ GPDDDVPSSG QQFAQFGAGC FWGVELAYQR VPGVTKTEVG
YSHGIVHNPS YEDVCTGTTG HNEVVRVQYD PKECSFESLL DVFWNRHDPT TLNRQGGDVG
TQYRSGIYYY TDEQERIARE AVEKQQKILN KRIVTEILPA TKFYRAENYH QQYLAKGGRM
GLRQSAEKGC KDPIRCYG
