Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mitochondrial peptide methionine sulfoxide reductase

Gene

MSRA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin.
L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

BRENDAi1.8.4.11. 908.
ReactomeiR-BTA-5676934. Protein repair.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial peptide methionine sulfoxide reductase (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 namesi
Name:MSRA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 8

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2007622.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2020MitochondrionBy similarityAdd
BLAST
Chaini21 – 233213Mitochondrial peptide methionine sulfoxide reductasePRO_0000138625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041N6-acetyllysine; alternateBy similarity
Modified residuei104 – 1041N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP54149.
PRIDEiP54149.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000028825.

Chemistry

BindingDBiP54149.

Structurei

Secondary structure

1
233
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni31 – 333Combined sources
Turni49 – 513Combined sources
Beta strandi56 – 583Combined sources
Beta strandi64 – 729Combined sources
Helixi73 – 819Combined sources
Beta strandi86 – 9712Combined sources
Helixi103 – 1075Combined sources
Beta strandi114 – 1218Combined sources
Turni123 – 1253Combined sources
Helixi128 – 13710Combined sources
Beta strandi144 – 1474Combined sources
Beta strandi150 – 1523Combined sources
Helixi153 – 1553Combined sources
Beta strandi157 – 1593Combined sources
Helixi164 – 18320Combined sources
Helixi204 – 2063Combined sources
Helixi209 – 2124Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FVAX-ray1.70A/B13-229[»]
1FVGX-ray1.60A21-219[»]
ProteinModelPortaliP54149.
SMRiP54149. Positions 28-228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54149.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1635. Eukaryota.
COG0225. LUCA.
GeneTreeiENSGT00390000003823.
HOVERGENiHBG006401.
InParanoidiP54149.
KOiK07304.
OMAiMVLRSEI.
OrthoDBiEOG76X610.
TreeFamiTF353884.

Family and domain databases

Gene3Di3.30.1060.10. 1 hit.
HAMAPiMF_01401. MsrA.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002569. Met_Sox_Rdtase_MsrA.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 1 hit.
PfamiPF01625. PMSR. 1 hit.
[Graphical view]
SUPFAMiSSF55068. SSF55068. 1 hit.
TIGRFAMsiTIGR00401. msrA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P54149-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSATRRALQ LFHSLFPIPR MGDSAAKIVS PQEALPGRKE PLVVAAKHHV
60 70 80 90 100
NGNRTVEPFP EGTQMAVFGM GCFWGAERKF WTLKGVYSTQ VGFAGGYTPN
110 120 130 140 150
PTYKEVCSGK TGHAEVVRVV FQPEHISFEE LLKVFWENHD PTQGMRQGND
160 170 180 190 200
HGSQYRSAIY PTSAEHVGAA LKSKEDYQKV LSEHGFGLIT TDIREGQTFY
210 220 230
YAEDYHQQYL SKDPDGYCGL GGTGVSCPLG IKK
Length:233
Mass (Da):25,818
Last modified:May 30, 2006 - v2
Checksum:iDA09151E42FB6C08
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41A → V in AAC48539 (PubMed:8700890).Curated
Sequence conflicti125 – 1251H → R in AAX09061 (PubMed:16305752).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37150 mRNA. Translation: AAC48539.1.
BT021044 mRNA. Translation: AAX09061.1.
BC102980 mRNA. Translation: AAI02981.1.
RefSeqiNP_776539.1. NM_174114.2.
UniGeneiBt.4655.

Genome annotation databases

EnsembliENSBTAT00000028825; ENSBTAP00000028825; ENSBTAG00000021632.
GeneIDi281312.
KEGGibta:281312.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37150 mRNA. Translation: AAC48539.1.
BT021044 mRNA. Translation: AAX09061.1.
BC102980 mRNA. Translation: AAI02981.1.
RefSeqiNP_776539.1. NM_174114.2.
UniGeneiBt.4655.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FVAX-ray1.70A/B13-229[»]
1FVGX-ray1.60A21-219[»]
ProteinModelPortaliP54149.
SMRiP54149. Positions 28-228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000028825.

Chemistry

BindingDBiP54149.
ChEMBLiCHEMBL2007622.

Proteomic databases

PaxDbiP54149.
PRIDEiP54149.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000028825; ENSBTAP00000028825; ENSBTAG00000021632.
GeneIDi281312.
KEGGibta:281312.

Organism-specific databases

CTDi4482.

Phylogenomic databases

eggNOGiKOG1635. Eukaryota.
COG0225. LUCA.
GeneTreeiENSGT00390000003823.
HOVERGENiHBG006401.
InParanoidiP54149.
KOiK07304.
OMAiMVLRSEI.
OrthoDBiEOG76X610.
TreeFamiTF353884.

Enzyme and pathway databases

BRENDAi1.8.4.11. 908.
ReactomeiR-BTA-5676934. Protein repair.

Miscellaneous databases

EvolutionaryTraceiP54149.

Family and domain databases

Gene3Di3.30.1060.10. 1 hit.
HAMAPiMF_01401. MsrA.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002569. Met_Sox_Rdtase_MsrA.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 1 hit.
PfamiPF01625. PMSR. 1 hit.
[Graphical view]
SUPFAMiSSF55068. SSF55068. 1 hit.
TIGRFAMsiTIGR00401. msrA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Adrenal medulla.
  2. 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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Entry informationi

Entry nameiMSRA_BOVIN
AccessioniPrimary (citable) accession number: P54149
Secondary accession number(s): Q3ZC16, Q5E976
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2006
Last modified: June 8, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.