Reviewed,
UniProtKB/Swiss-Prot P52552 (PRDX2_PIG)
Last modified
November 25, 2008.
Version 51.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Sus scrofa (Pig) | ||||
| Taxonomic identifier | 9823 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 127 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 component | Cytoplasm |
| Domain | Redox-active center |
| Molecular function | Antioxidant Oxidoreductase Peroxidase |
Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | peroxiredoxin activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – ›127 | ›127 | Peroxiredoxin-2 | PRO_0000135082 | |||||
Regions | |||||||||
| Domain | ‹1 – 125 | ›125 | Thioredoxin | ||||||
Sites | |||||||||
| Active site | 12 | 1 | Cysteine sulfenic acid (-SOH) intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Disulfide bond | 12 | Interchain (with C-?); in linked form By similarity | |||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 127 | 1 | |||||||
Sequences
| ||||||||||||||||||
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 | |
| HSSP | HSSP built from PDB template 1QMV based on UniProtKB P32119. |
| SMR | P52552. Positions 1-127. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P52552. |
Family and domain databases | |
| InterPro | IPR000866. AhpC-TSA. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| Pfam | PF00578. AhpC-TSA. 1 hit. [Graphical view] |
| PROSITE | PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PRDX2_PIG | ||||||||
| Accession | Primary (citable) accession number: P52552 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


