MSRA1_ARATH
ID MSRA1_ARATH Reviewed; 202 AA.
AC Q9FKF7;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Peptide methionine sulfoxide reductase A1;
DE Short=AtMSRA1;
DE EC=1.8.4.11;
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=MSRA1; Synonyms=PMSR1; OrderedLocusNames=At5g61640; ORFNames=K11J9.18;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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].
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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. MSRA family specifically reduces the MetSO S-
CC enantiomer (By similarity). {ECO:0000250}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; AB012239; BAB09008.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97500.1; -; Genomic_DNA.
DR EMBL; BT005850; AAO64785.1; -; mRNA.
DR EMBL; AK227434; BAE99438.1; -; mRNA.
DR RefSeq; NP_568937.1; NM_125558.3.
DR AlphaFoldDB; Q9FKF7; -.
DR SMR; Q9FKF7; -.
DR BioGRID; 21530; 1.
DR STRING; 3702.AT5G61640.1; -.
DR PaxDb; Q9FKF7; -.
DR PRIDE; Q9FKF7; -.
DR ProteomicsDB; 238915; -.
DR EnsemblPlants; AT5G61640.1; AT5G61640.1; AT5G61640.
DR GeneID; 836286; -.
DR Gramene; AT5G61640.1; AT5G61640.1; AT5G61640.
DR KEGG; ath:AT5G61640; -.
DR Araport; AT5G61640; -.
DR TAIR; locus:2151646; AT5G61640.
DR eggNOG; KOG1635; Eukaryota.
DR HOGENOM; CLU_031040_3_0_1; -.
DR InParanoid; Q9FKF7; -.
DR OMA; KECNFET; -.
DR PhylomeDB; Q9FKF7; -.
DR PRO; PR:Q9FKF7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKF7; baseline and differential.
DR Genevisible; Q9FKF7; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..202
FT /note="Peptide methionine sulfoxide reductase A1"
FT /id="PRO_0000395511"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LY15"
SQ SEQUENCE 202 AA; 22898 MW; DECE495D96C6EF25 CRC64;
MNILNKLGIG SSRQTNMDPS PIAQVIDDEA PAPGNQFTQF GAGCFWSVEL AYQRVPGVTQ
TEVGYSQGIT HDPSYKDVCS GTTNHAEIVR VQYDPKECSY QSLLDLFWSK HDPTTLNRQG
NDVGTQYRSG IYFYNPEQEK LARESLERHQ QQVDRKVVTE ILPAKKFYRA EEHHQQYLSK
GGRFGLKQST EKGCNDPIRC YG
