Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q5REY3 (PRDX3_PONAB)

Last modified November 25, 2008. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
    Thioredoxin-dependent peroxide reductase, mitochondrial
    EC=1.11.1.15
Alternative name(s):
    Peroxiredoxin-3
Gene names
Name: PRDX3
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system By similarity.

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.

Subunit structure

Homodimer; disulfide-linked, upon oxidation By similarity. Binds MAP3K13 By similarity.

Subcellular location

MitochondrionBy similarity.

Miscellaneous

The active site is the redox-active Cys-108 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-229-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin By similarity.

Irreversibly inactivated by overoxidation of Cys-108 (to Cys-SO(3)H) upon oxidative stress By similarity.

Sequence similarities

Belongs to the ahpC/TSA family.

Contains 1 thioredoxin domain.

Ontologies

Keywords

   Cellular componentMitochondrion
   DomainRedox-active center
Transit peptide
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase

Gene Ontology (GO)

   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionperoxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6262Mitochondrion By similarity
Chain63 – 256194Thioredoxin-dependent peroxide reductase, mitochondrial By similarity
PRO_0000256858

Regions

Domain63 – 221159Thioredoxin

Sites

Active site1081Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Disulfide bond108Interchain (with C-229); in linked form By similarity
Disulfide bond229Interchain (with C-108); in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5REY3-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: BF425B99C7794406

FASTA25627,700
        10         20         30         40         50         60 
MAAAVGRLLR ASVARGVSAI PWGISATAAL RPAACGRTSL TNLLCSGSSQ AKLFSTSSSY 

        70         80         90        100        110        120 
HAPAVTQHAP YFKGTAVVNG EFKDLSLDDF KGKYLVLFFY PLDFTFVCPT EIVAFSDKAN 

       130        140        150        160        170        180 
EFHDVNCEVV AVSVDSHFSH LAWINTPRKN GGLGHMNIAL LSDLTKQISR DYGVLLEGSG 

       190        200        210        220        230        240 
LALRGLFIID PNGVIKHLSV NDLPVGRSVE ETLRLVKAFQ YVETHGEVCP ANWTPDSPTI 

       250 
KPNPAASKEY FQKVNQ 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.

Cross-references

Sequence databases

CR857380 mRNA. Translation: CAH89674.1.
RefSeqNP_001127184.1.

3D structure databases

SMRQ5REY3. Positions 63-223.
ModBaseSearch...

Protein family/group databases

PeroxiBase4500. Ppy2CysPrx03.

Genome annotation databases

GeneID100174238.

Phylogenomic databases

HOVERGENQ5REY3.

Family and domain databases

InterProIPR000866. AhpC-TSA.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF00578. AhpC-TSA. 1 hit.
[Graphical view]
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRDX3_PONAB
AccessionPrimary (citable) accession number: Q5REY3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: December 21, 2004
Last modified: November 25, 2008
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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