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Reviewed, UniProtKB/Swiss-Prot P54149 (MSRA_BOVIN)

Last modified November 25, 2008. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: MSRA
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 + H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin.

L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S-oxide + thioredoxin.

Sequence similarities

Belongs to the msrA Met sulfoxide reductase family.

Ontologies

Keywords

   Molecular functionOxidoreductase
   Technical term3D-structure

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

protein metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionpeptide-methionine-(S)-S-oxide reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 233233Peptide methionine sulfoxide reductase
PRO_0000138625

Experimental info

Sequence conflict41A → V in AAC48539. Ref.1
Sequence conflict1251H → R in AAX09061. Ref.2

Secondary structure

................................ 233
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54149-1 [UniParc].

Last modified May 30, 2006. Version 2.
Checksum: DA09151E42FB6C08

FASTA23325,818
        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 

« Hide

References

« Hide 'large scale' references
[1]"Cloning the expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins."
Moskovitz J., Weissbach H., Brot N.
Proc. Natl. Acad. Sci. U.S.A. 93:2095-2099(1996) [PubMed: 8700890] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adrenal medulla.
[2]"Characterization of 954 bovine full-CDS cDNA sequences."
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.
BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Hypothalamus.
[4]"Structure and mechanism of peptide methionine sulfoxide reductase, an 'anti-oxidation' enzyme."
Lowther W.T., Brot N., Weissbach H., Matthews B.W.
Biochemistry 39:13307-13312(2000) [PubMed: 11063566] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Cross-references

Sequence databases

U37150 mRNA. Translation: AAC48539.1.
BT021044 mRNA. Translation: AAX09061.1.
BC102980 mRNA. Translation: AAI02981.1.
RefSeqNP_776539.1.
UniGeneBt.4655

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FVAX-ray1.70A/B13-229[»]
1FVGX-ray1.60A21-219[»]
ModBaseSearch...

Genome annotation databases

GeneID281312.
KEGGbta:281312.

Phylogenomic databases

HOVERGENP54149.

Family and domain databases

InterProIPR002569. MsrA.
[Graphical view]
Gene3DG3DSA:3.30.1060.10. MsrA. 1 hit.
PfamPF01625. PMSR. 1 hit.
[Graphical view]
ProDomPD003489. PMSR. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00401. msrA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMSRA_BOVIN
AccessionPrimary (citable) accession number: P54149
Secondary accession number(s): Q3ZC16, Q5E976
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2006
Last modified: November 25, 2008
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents