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Reviewed, UniProtKB/Swiss-Prot Q9GLW9 (PRDX5_PAPHA)

Last modified June 16, 2009. Version 53. 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 · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxiredoxin-5, mitochondrial
    EC=1.11.1.15
Alternative name(s):
    Prx-V
    Thioredoxin reductase
Gene names
Name: PRDX5
OrganismPapio hamadryas (Hamadryas baboon)
Taxonomic identifier9557 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaePapio

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling By similarity.

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion By similarity. Cytoplasm By similarity. Peroxisome By similarity.

Sequence similarities

Belongs to the peroxiredoxin 2 family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
Peroxisome
   Coding sequence diversityAlternative initiation
   DomainRedox-active center
Transit peptide
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMDisulfide bond
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-SubCell

peroxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionperoxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Mitochondrial (identifier: Q9GLW9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Cytoplasmic+peroxisomal (identifier: Q9GLW9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5353Mitochondrion Potential
Chain54 – 215162Peroxiredoxin-5, mitochondrial
PRO_0000023797

Regions

Domain57 – 215159Thioredoxin
Motif213 – 2153Microbody targeting signal By similarity

Sites

Active site1011Cysteine sulfenic acid (-SOH) intermediate Potential

Amino acid modifications

Disulfide bond101 ↔ 205Redox-active By similarity

Natural variations

Alternative sequence1 – 5353Missing in isoform Cytoplasmic+peroxisomal.
VSP_018831

Sequences

Sequence LengthMass (Da)Tools
Isoform Mitochondrial [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 65183A24535C1617

FASTA21522,166
        10         20         30         40         50         60 
MGLAGVCVLR RSAGYILGGA AGQSVAATAA ARRRSEGGWA SGGVRSFSRA AAAMAPIKVG 

        70         80         90        100        110        120 
DAIPAVEVFE GEPGNKVNLA ELFKGKKGVL FGVPGAFTPG CSKTHLPGFV EQAEALKAKG 

       130        140        150        160        170        180 
VQVLACLSVN DAFVTGEWGR AHKVEGKVRL LADPTGAFGK ETDLLLDDSL VSIFGNRRLK 

       190        200        210 
RFSMVVQDGI VKALNVEPDG TGLTCSLAPS IISQL 

« Hide

Isoform Cytoplasmic+peroxisomal.

Checksum: 2A2D04A33025D9A8
Show »

FASTA16217,046

References

[1]"Cloning and characterization of baboon AOEB166/PRDX5."
Knoops B., Cherif H.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

AF110734 mRNA. Translation: AAG13451.2.

3D structure databases

HSSPHSSP built from PDB template 1HD2 based on UniProtKB P30044.
SMRQ9GLW9. Positions 55-215.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ9GLW9.

Enzyme and pathway databases

BRENDA1.11.1.15. 39388.

Family and domain databases

InterProIPR013740. Redoxin.
IPR017936. Thioredoxin-like.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF08534. Redoxin. 1 hit.
[Graphical view]
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRDX5_PAPHA
AccessionPrimary (citable) accession number: Q9GLW9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: March 1, 2001
Last modified: June 16, 2009
This is version 53 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 · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents