P54150 (MSRA4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptide methionine sulfoxide reductase A4, chloroplastic
Short name=AtMSRA4
EC=1.8.4.11

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

Gene names

Name:	MSR4
Synonyms:	PMSR, PMSR4
Ordered Locus Names:	At4g25130
ORF Names:	F13M23.270

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. Prevents the methionine sulfoxidation of the heat shock protein HSP21 and its subsequent inactivation. MSRA family specifically reduces the MetSO S-enantiomer. Ref.6 Ref.7
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.
Subcellular location	Plastid › chloroplast stroma.
Tissue specificity	Expressed in rosette and cauline leaves, and at lower levels in stems and flowers (at protein level). Ref.6
Induction	By light in etiolated seedlings (at protein level). Ref.6
Sequence similarities	Belongs to the MsrA Met sulfoxide reductase family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.0. Ref.6

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular response to oxidative stress Inferred from expression pattern. Source: TAIR protein metabolic process Inferred from electronic annotation. Source: InterPro response to light stimulus Inferred from expression pattern Ref.6. Source: UniProtKB
Cellular component	chloroplast envelope Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay Ref.6. Source: UniProtKB
Molecular function	peptide-methionine-(S)-S-oxide reductase activity Inferred from direct assay Ref.6. Source: UniProtKB
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
	Transit peptide	1 – 68	68	Chloroplast Potential
	Chain	69 – 258	190	Peptide methionine sulfoxide reductase A4, chloroplastic		PRO_0000138632
Amino acid modifications
	Modified residue	130	1	Phosphoserine Ref.9
Experimental info
	Sequence conflict	131	1	Y → S in CAA65991. Ref.1
	Sequence conflict	195	1	E → D in AAK83645. Ref.4
	Sequence conflict	195	1	E → D in AAN46787. Ref.4
	Sequence conflict	212	1	R → K in AAM65092. Ref.5
	Sequence conflict	225	1	R → K in AAK83645. Ref.4
	Sequence conflict	225	1	R → K in AAN46787. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P54150 [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]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Differential regulation of plastidial and cytosolic isoforms of peptide methionine sulfoxide reductase in Arabidopsis." Sadanandom A., Poghosyan Z., Fairbairn D.J., Murphy D.J. Plant Physiol. 123:255-264(2000) [PubMed: 10806242] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION. Strain: cv. Columbia.
[7]	"A peptide methionine sulfoxide reductase highly expressed in photosynthetic tissue in Arabidopsis thaliana can protect the chaperone-like activity of a chloroplast-localized small heat shock protein." Gustavsson N., Kokke B.P., Haerndahl U., Silow M., Bechtold U., Poghosyan Z., Murphy D., Boelens W.C., Sundby C. Plant J. 29:545-553(2002) [PubMed: 11874568] [Abstract] Cited for: FUNCTION.
[8]	"Plant methionine sulfoxide reductase A and B multigenic families." Rouhier N., Vieira Dos Santos C., Tarrago L., Rey P. Photosyn. Res. 89:247-262(2006) [PubMed: 17031545] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[9]	"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. Strain: cv. Columbia. 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. CP002687 Genomic DNA. Translation: AEE85015.1. AY049303 mRNA. Translation: AAK83645.1. BT001033 mRNA. Translation: AAN46787.1. AY087550 mRNA. Translation: AAM65092.1.
IPI	IPI00543565.
PIR	T05534.
RefSeq	NP_194243.1. NM_118645.3.
UniGene	At.24140.
3D structure databases
HSSP	HSSP built from PDB template 1FF3 based on UniProtKB P27110.
ProteinModelPortal	P54150.
SMR	P54150. Positions 78-258.
ModBase	Search...
Protein-protein interaction databases
IntAct	P54150. 1 interaction.
STRING	P54150.
Proteomic databases
PRIDE	P54150.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G25130.1; AT4G25130.1; AT4G25130.
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.
GeneTree	EPGT00070000029005.
HOGENOM	HBG748152.
InParanoid	P54150.
OMA	QQKLLNR.
PhylomeDB	P54150.
ProtClustDB	CLSN2915968.
Enzyme and pathway databases
BRENDA	1.8.4.11. 399.
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.
KO	K07304.
Pfam	PF01625. PMSR. 1 hit. [Graphical view]
SUPFAM	SSF55068. MsrA. 1 hit.
TIGRFAMs	TIGR00401. MsrA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MSRA4_ARATH

Accession

Primary (citable) accession number: P54150
Secondary accession number(s): Q8LAX4, Q94A72, Q9SW13

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 11, 2001
Last modified:	January 25, 2012
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program