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Reviewed, UniProtKB/Swiss-Prot P52552 (PRDX2_PIG)

Last modified November 25, 2008. Version 51. 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:
    Peroxiredoxin-2
    EC=1.11.1.15
Alternative name(s):
    Thioredoxin peroxidase 1
    Thioredoxin-dependent peroxide reductase 1
    Thiol-specific antioxidant protein
      Short name=TSA
Gene names
Name: PRDX2
Synonyms: TDPX1
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length127 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2).

Catalytic activity

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

Subunit structure

Homodimer; disulfide-linked, upon oxidation. Interacts with TIPIN By similarity.

Subcellular location

CytoplasmBy similarity.

Miscellaneous

The active site is the redox-active Cys-12 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-?-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.

Inactivated upon oxidative stress by overoxidation of Cys-12 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be irreversibly oxidized By similarity.

Sequence similarities

Belongs to the ahpC/TSA family.

Contains 1 thioredoxin domain.

Ontologies

Keywords

   Cellular componentCytoplasm
   DomainRedox-active center
   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 componentcytoplasm

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

Chain‹1 – ›127›127Peroxiredoxin-2
PRO_0000135082

Regions

Domain‹1 – 125›125Thioredoxin

Sites

Active site121Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Disulfide bond12Interchain (with C-?); in linked form By similarity

Experimental info

Non-terminal residue11
Non-terminal residue1271

Sequences

Sequence LengthMass (Da)Tools
P52552-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 1C05A9765EB69E84

FASTA12714,168
        10         20         30         40         50         60 
LFFYPLDFTF VCPTEIIAFS DRAEEFHQLG CEVLGVSVDX QXTHLAWINT PRKEGGLGPL 

        70         80         90        100        110        120 
KIPLLADVTR NLSLDYGVLK EDEGIAYRGL FIIDGKGVLR QITVNDLPVG RXVDEALRLV 


QGXQYTD 

« Hide

References

[1]"Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
Winteroe A.K., Fredholm M., Davies W.
Mamm. Genome 7:509-517(1996) [PubMed: 8672129] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Small intestine.

Cross-references

Sequence databases

F14561 mRNA. Translation: CAA23125.1.

3D structure databases

HSSPHSSP built from PDB template 1QMV based on UniProtKB P32119.
SMRP52552. Positions 1-127.
ModBaseSearch...

Phylogenomic databases

HOVERGENP52552.

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 namePRDX2_PIG
AccessionPrimary (citable) accession number: P52552
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 25, 2008
This is version 51 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