Q8K3U7 (PRDX2_CRIGR) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 52.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Peroxiredoxin-2 EC=1.11.1.15 | ||
| Gene names |
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| Organism | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) | ||
| Taxonomic identifier | 10029 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus |
Protein attributes
| Sequence length | 198 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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 H2O2 By similarity. |
| Catalytic activity | 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. |
| Subunit structure | Homodimer; disulfide-linked, upon oxidation. Interacts with TIPIN By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Miscellaneous | The active site is the redox-active Cys-51 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-172-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-51 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H 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 |
| PTM | Acetylation Disulfide bond |
| Gene Ontology (GO) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW peroxiredoxin activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 198 | 197 | Peroxiredoxin-2 | PRO_0000256855 | |||||
Regions | |||||||||
| Domain | 6 – 164 | 159 | Thioredoxin | ||||||
Sites | |||||||||
| Active site | 51 | 1 | Cysteine sulfenic acid (-SOH) intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Disulfide bond | 51 | Interchain (with C-172); in linked form By similarity | |||||||
| Disulfide bond | 172 | Interchain (with C-51); in linked form By similarity | |||||||
Sequences
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References
| [1] | "2D Gel analysis of the proteomic adaptation of a mammalian cell line to oxidative stress reveals changes in the expression of metabolically relevant enzymes." Keightley J.A., Shang L., Kinter M. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF532110 mRNA. Translation: AAM95673.1. |
| RefSeq | NP_001233709.1. NM_001246780.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1QMV based on UniProtKB P32119. |
| ProteinModelPortal | Q8K3U7. |
| SMR | Q8K3U7. Positions 3-198. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100689349. |
Phylogenomic databases | |
| HOVERGEN | HBG000286. |
Family and domain databases | |
| InterPro | IPR000866. AhpC/TSA. IPR024706. Peroxiredoxin_AhpC-typ. IPR019479. Peroxiredoxin_C. IPR012336. Thioredoxin-like_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| Pfam | PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view] |
| PIRSF | PIRSF000239. AHPC. 1 hit. |
| SUPFAM | SSF52833. Thiordxn-like_fd. 1 hit. |
| PROSITE | PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PRDX2_CRIGR | ||||||||
| Accession | Primary (citable) accession number: Q8K3U7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with