MSRA4_ORYSJ
ID MSRA4_ORYSJ Reviewed; 263 AA.
AC Q336R9; A0A0P0XX97; Q336S0;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Peptide methionine sulfoxide reductase A4, chloroplastic {ECO:0000305};
DE Short=OsMSRA4 {ECO:0000303|PubMed:17031545};
DE EC=1.8.4.11 {ECO:0000269|PubMed:19415325};
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000305};
DE Short=Peptide Met(O) reductase {ECO:0000305};
DE AltName: Full=Protein-methionine-S-oxide reductase {ECO:0000305};
DE Flags: Precursor;
GN Name=MSRA4 {ECO:0000303|PubMed:17031545};
GN OrderedLocusNames=Os10g0563600 {ECO:0000312|EMBL:BAT12084.1},
GN LOC_Os10g41400 {ECO:0000312|EMBL:ABB47990.2};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=19415325; DOI=10.1007/s00425-009-0934-2;
RA Guo X., Wu Y., Wang Y., Chen Y., Chu C.;
RT "OsMSRA4.1 and OsMSRB1.1, two rice plastidial methionine sulfoxide
RT reductases, are involved in abiotic stress responses.";
RL Planta 230:227-238(2009).
CC -!- FUNCTION: Catalyzes the reduction of methionine sulfoxide (MetSO) to
CC methionine in proteins. Involved in abiotic and salt stress responses.
CC Plays a protective role against oxidative stress by restoring activity
CC to proteins that have been inactivated by methionine oxidation. MSRA
CC family specifically reduces the MetSO S-enantiomer.
CC {ECO:0000269|PubMed:19415325}.
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:19415325};
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:19415325};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19415325}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q336R9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q336R9-2; Sequence=VSP_039507, VSP_039508;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers.
CC {ECO:0000269|PubMed:19415325}.
CC -!- INDUCTION: By salt, mannitol, cold, high temperatures and methyl
CC viologen. {ECO:0000269|PubMed:19415325}.
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; DP000086; ABB47990.2; -; Genomic_DNA.
DR EMBL; DP000086; ABB47991.2; -; Genomic_DNA.
DR EMBL; AP008216; BAF27240.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT12084.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT12085.1; -; Genomic_DNA.
DR EMBL; AK067167; BAG90297.1; -; mRNA.
DR EMBL; AK109715; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015614143.1; XM_015758657.1. [Q336R9-1]
DR AlphaFoldDB; Q336R9; -.
DR SMR; Q336R9; -.
DR STRING; 4530.OS10T0563600-01; -.
DR iPTMnet; Q336R9; -.
DR PaxDb; Q336R9; -.
DR PRIDE; Q336R9; -.
DR EnsemblPlants; Os10t0563600-01; Os10t0563600-01; Os10g0563600. [Q336R9-1]
DR EnsemblPlants; Os10t0563600-02; Os10t0563600-02; Os10g0563600. [Q336R9-2]
DR GeneID; 4349402; -.
DR Gramene; Os10t0563600-01; Os10t0563600-01; Os10g0563600. [Q336R9-1]
DR Gramene; Os10t0563600-02; Os10t0563600-02; Os10g0563600. [Q336R9-2]
DR KEGG; osa:4349402; -.
DR eggNOG; KOG1635; Eukaryota.
DR HOGENOM; CLU_031040_3_0_1; -.
DR InParanoid; Q336R9; -.
DR OMA; PAACKFD; -.
DR OrthoDB; 1383773at2759; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR Genevisible; Q336R9; OS.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP: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 Alternative splicing; Chloroplast; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..75
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 76..263
FT /note="Peptide methionine sulfoxide reductase A4,
FT chloroplastic"
FT /id="PRO_0000395517"
FT VAR_SEQ 181..211
FT /note="GNDVGTQYRSGIYYYTPEQEKAARESLEKQQ -> VSQPQINSIHKPNRMIS
FT FTVPCSMLNFGFFD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_039507"
FT VAR_SEQ 212..263
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_039508"
FT CONFLICT 44
FT /note="P -> S (in Ref. 5; AK109715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 28639 MW; 7A2AEB0862DF5A47 CRC64;
MPPLLASTSS TSPLLLASRL RGGGGCGCGG APLLHRTRRG FLAPSTTTTQ TTRTSFAAMS
WLGKLGLGGL GGSPRASAAS AALAQGPDED RPAAGNEFAQ FGAGCFWGVE LAFQRVPGVT
RTEVGYSQGN LHDPTYEDVC TGATYHNEVV RVHYDVSACK FDDLLDVFWA RHDPTTPNRQ
GNDVGTQYRS GIYYYTPEQE KAARESLEKQ QKLLNRTIVT EILPAKRFYR AEEYHQQYLA
KGGRFGFRQS AEKGCNDPIR CYG
