[1]	NUCLEOTIDE SEQUENCE. STRAIN=cv. Jet neuf; DOI=10.1007/BF00020171; PubMed=8111035 [NCBI, ExPASy, EBI, Israel, Japan] Keddie J.S., Tsiantis M., Piffanelli P., Cella R., Hatzopoulos P., Murphy D.J.; "A seed-specific Brassica napus oleosin promoter interacts with a G-box-specific protein and may be bi-directional."; Plant Mol. Biol. 24:327-340(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-4; ALA-14; SER-24; ALA-75 AND SER-129. TISSUE=Leaf; PubMed=8771781 [NCBI, ExPASy, EBI, Israel, Japan] Sadanandom A.C., Piffanelli P., Knott T., Robinson C., Sharpe A., Lydiate D., Murphy D.J., Fairbairn D.J.; "Identification of a peptide methionine sulphoxide reductase gene in an oleosin promoter from Brassica napus."; Plant J. 10:235-242(1996).

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.
CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H₂O = L-methionine (S)-S-oxide + thioredoxin.
SIMILARITY: Belongs to the msrA Met sulfoxide reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X94225; CAA63919.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z48619; CAA88538.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X91486; CAA62760.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S55365; S55365.
T47215; T47215.

3D structure databases

HSSP

P27110; 1FF3. [HSSP ENTRY / PDB]

SMR

P54151; 77-257.

ModBase

P54151.

Ontologies

GO:0008113;	Molecular function: peptide-methionine-(S)-S-oxide reductase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002569; MsrA.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.1060.10; MsrA; 1.

Pfam

PF01625; PMSR; 1.
Pfam graphical view of domain structure.

ProDom

PD003489; PMSR; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGR00401; msrA; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Oxidoreductase; Polymorphism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 257`	`257`	`Peptide methionine sulfoxide reductase.`	`PRO_0000138633`
`VARIANT`	`4 4`	`1`	`I -> L.`
`VARIANT`	`14 14`	`1`	`V -> A.`
`VARIANT`	`24 24`	`1`	`A -> S.`
`VARIANT`	`75 75`	`1`	`S -> A.`
`VARIANT`	`129 129`	`1`	`T -> S.`

Sequence information

Length: 257 AA [This is the length of the unprocessed precursor]

Molecular weight: 28466 Da [This is the MW of the unprocessed precursor]

CRC64: 41F4440E41772788 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSIVASPPV ISAVSLSKPL QSLAKAALSL SKRAKPTSPF PKTARSISVY KSPMNNLFTR 

        70         80         90        100        110        120 
LGFGSRPQPD PAASSAIAQG PDDDVPSPGQ QFAQFGAGCF WGAELAYQRV PGVTKTEVGY 

       130        140        150        160        170        180 
SHGFVDNPTY EDVCSETTGH NEIVRVQYDP KEVSFESLLD VFWKRHDPTT LNRQGNDVGT 

       190        200        210        220        230        240 
RYRSGIYFYT DEQEKLAREA MEKQQKILNR KIVTEILPAT KFYRAENYHQ QYLAKGGRMG 

       250 
LSQSAEKGCN DPIRCYG

P54151 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools