[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Adrenal medulla; DOI=10.1073/pnas.93.5.2095; PubMed=8700890 [NCBI, ExPASy, EBI, Israel, Japan] Moskovitz J., Weissbach H., Brot N.; "Cloning the expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins."; Proc. Natl. Acad. Sci. U.S.A. 93:2095-2099(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan] Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; "Characterization of 954 bovine full-CDS cDNA sequences."; BMC Genomics 6:166-166(2005).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Hypothalamus; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[4]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). DOI=10.1021/bi0020269; PubMed=11063566 [NCBI, ExPASy, EBI, Israel, Japan] Lowther W.T., Brot N., Weissbach H., Matthews B.W.; "Structure and mechanism of peptide methionine sulfoxide reductase, an 'anti-oxidation' enzyme."; Biochemistry 39:13307-13312(2000).

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

U37150; AAC48539.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT021044; AAX09061.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC102980; AAI02981.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_776539.1; -.

UniGene

Bt.4655

3D structure databases

PDB

1FVA; X-ray; 1.70 A; A/B=13-229.	[ExPASy / RCSB / EBI]
1FVG; X-ray; 1.60 A; A=21-219.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1FVA; -.
1FVG; -.

ModBase

P54149.

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]

TIGRFAMs

TIGR00401; msrA; 1.

BLOCKS

P54149.

Genome annotation databases

GeneID

281312; -.

KEGG

bta:281312; -.

Phylogenomic databases

HOVERGEN

P54149; -.

Other

ProtoNet

P54149.

UniRef

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

Keywords

3D-structure; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 233`	`233`	`Peptide methionine sulfoxide reductase.`	`PRO_0000138625`
`CONFLICT`	`4 4`		`A -> V (in Ref. 1; AAC48539).`
`CONFLICT`	`125 125`		`H -> R (in Ref. 2; AAX09061).`
`TURN`	`31 33`	`3`
`TURN`	`49 51`	`3`
`STRAND`	`54 58`	`5`
`STRAND`	`64 72`	`9`
`HELIX`	`73 81`	`9`
`STRAND`	`86 100`	`15`
`HELIX`	`103 107`	`5`
`STRAND`	`114 121`	`8`
`TURN`	`123 125`	`3`
`HELIX`	`128 137`	`10`
`STRAND`	`143 147`	`5`
`STRAND`	`150 152`	`3`
`HELIX`	`153 155`	`3`
`STRAND`	`157 159`	`3`
`HELIX`	`164 183`	`20`
`HELIX`	`204 206`	`3`
`TURN`	`207 211`	`5`

Sequence information

Length: 233 AA [This is the length of the unprocessed precursor]

Molecular weight: 25818 Da [This is the MW of the unprocessed precursor]

CRC64: DA09151E42FB6C08 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSATRRALQ LFHSLFPIPR MGDSAAKIVS PQEALPGRKE PLVVAAKHHV NGNRTVEPFP 

        70         80         90        100        110        120 
EGTQMAVFGM GCFWGAERKF WTLKGVYSTQ VGFAGGYTPN PTYKEVCSGK TGHAEVVRVV 

       130        140        150        160        170        180 
FQPEHISFEE LLKVFWENHD PTQGMRQGND HGSQYRSAIY PTSAEHVGAA LKSKEDYQKV 

       190        200        210        220        230 
LSEHGFGLIT TDIREGQTFY YAEDYHQQYL SKDPDGYCGL GGTGVSCPLG IKK

P54149 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