Reviewed, UniProtKB/Swiss-Prot P54150 (MSRA_ARATH)

Names and origin

Protein names

Recommended name:
    Peptide methionine sulfoxide reductase
    EC=1.8.4.11
Alternative name(s):
    Protein-methionine-S-oxide reductase
    Peptide-methionine (S)-S-oxide reductase
      Short name=Peptide Met(O) reductase

Gene names

Name:	PMSR
Ordered Locus Names:	At4g25130
ORF Names:	F13M23.270

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic activity	Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin. L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
Sequence similarities	Belongs to the msrA Met sulfoxide reductase family.

Ontologies

Keywords
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast stroma Inferred from direct assay. Source: TAIR
Molecular function	peptide-methionine-(S)-S-oxide reductase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRX3	Q42403	1	EBI-449349,EBI-449157

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 258	258	Peptide methionine sulfoxide reductase		PRO_0000138632
Amino acid modifications
	Modified residue	130	1	Phosphoserine Ref.3
Experimental info
	Sequence conflict	131	1	Y → S in CAA65991. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54150-1 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: DCB95E4B4CF88EA1	FASTA	258	28,644
	10 20 30 40 50 60 MQVLVVSPPL IAAASLSKPL NSLSKAALSF SRAKPICPFP QTSRRPISVY KSPMNNLFNR 70 80 90 100 110 120 LGFGSRPQAQ ADPSSAAIAQ GPDDDVPSSG QQFAQFGAGC FWGVELAYQR VPGVTKTEVG 130 140 150 160 170 180 YSHGIVHNPS YEDVCTGTTG HNEVVRVQYD PKECSFESLL DVFWNRHDPT TLNRQGGDVG 190 200 210 220 230 240 TQYRSGIYYY TDEQERIARE AVEKQQKILN KRIVTEILPA TKFYRAENYH QQYLAKGGRM 250 GLRQSAEKGC KDPIRCYG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Piffanelli P., Batchedler C., Murphy D.J. Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, MASS SPECTROMETRY. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X97326 Genomic DNA. Translation: CAA65991.1. AL035523 Genomic DNA. Translation: CAB36755.1. AL161562 Genomic DNA. Translation: CAB79422.1.
IPI	IPI00543565.
PIR	T05534.
RefSeq	NP_194243.1.
UniGene	At.24140 Rra.22928
3D structure databases
SMR	P54150. Positions 78-258.
ModBase	Search...
Protein-protein interaction databases
IntAct	P54150. 1 interaction.
STRING	P54150.
Proteomic databases
PRIDE	P54150.
Genome annotation databases
GeneID	828616.
GenomeReviews	Gene locus AT4G25130 in contig CT486007_GR.
KEGG	ath:AT4G25130.
NMPDR	fig|3702.1.peg.20418.
Organism-specific databases
TAIR	At4g25130.
Phylogenomic databases
eggNOG	KOG1635.
HOGENOM	HBG748152.
InParanoid	P54150.
OMA	QQKLLNR.
PhylomeDB	P54150.
Enzyme and pathway databases
BRENDA	1.8.4.11. 302.
Gene expression databases
ArrayExpress	P54150.
Genevestigator	P54150.
GermOnline	AT4G25130. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002569. Peptide_Met_Sox_Rdtase_MsrA. [Graphical view]
Gene3D	G3DSA:3.30.1060.10. MsrA. 1 hit.
Pfam	PF01625. PMSR. 1 hit. [Graphical view]
TIGRFAMs	TIGR00401. msrA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MSRA_ARATH

Accession

Primary (citable) accession number: P54150
Secondary accession number(s): Q9SW13

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 11, 2001
Last modified:	February 9, 2010
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)