Reviewed,
UniProtKB/Swiss-Prot Q5ZJF4 (PRDX6_CHICK)
Last modified
June 16, 2009.
Version 41.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Peroxiredoxin-6 EC=1.11.1.15 | ||||
| Gene names |
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| Organism | Gallus gallus (Chicken) | ||||
| Taxonomic identifier | 9031 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus |
Protein attributes
| Sequence length | 224 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. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury By similarity. |
| Catalytic activity | 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. Lysosome By similarity. Cytoplasmic vesicle By similarity. |
| Miscellaneous | The active site is the redox-active Cys-46 oxidized to Cys-SOH. Cys-SOH may rapidly react with a 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. Irreversibly inactivated by overoxidation of Cys-46 (to Cys-SO3H) upon oxidative stress By similarity. |
| Sequence similarities | Belongs to the ahpC/TSA family. Rehydrin subfamily. Contains 1 thioredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Cellular component | Cytoplasm Cytoplasmic vesicle Lysosome |
| Domain | Redox-active center |
| Molecular function | Antioxidant Hydrolase Oxidoreductase Peroxidase |
| PTM | Disulfide bond Phosphoprotein |
| Technical term | Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro lipid catabolic processInferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasmic vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell lysosomeInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | hydrolase 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 – 224 | 223 | Peroxiredoxin-6 | PRO_0000256863 | |||||
Regions | |||||||||
| Domain | 4 – 168 | 165 | Thioredoxin | ||||||
Sites | |||||||||
| Active site | 31 | 1 | For phospholipase activity By similarity | ||||||
| Active site | 46 | 1 | Cysteine sulfenic acid (-SOH) intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 88 | 1 | Phosphotyrosine By similarity | ||||||
| Disulfide bond | 46 | Interchain; in linked form By similarity | |||||||
Sequences
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References
| [1] | "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis." Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M. Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005) [PubMed: 15642098] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: CB. Tissue: Bursa of Fabricius. |
Cross-references
Sequence databases | |
|---|---|
| AJ720480 mRNA. Translation: CAG32139.1. | |
| IPI | IPI00577013. |
| RefSeq | NP_001034418.1. |
| UniGene | Gga.34325 |
3D structure databases | |
| SMR | Q5ZJF4. Positions 3-222, 4-223. |
| ModBase | Search... |
Protein family/group databases | |
| PeroxiBase | 4421. Gga1CysPrx. |
Genome annotation databases | |
| Ensembl | ENSGALG00000003053. Gallus gallus. [Contig view] |
| GeneID | 429062. |
| KEGG | gga:429062. |
Phylogenomic databases | |
| HOVERGEN | Q5ZJF4. |
Enzyme and pathway databases | |
| BRENDA | 1.11.1.15. 4. |
Family and domain databases | |
| InterPro | IPR000866. Alkyl_hydroperoxide_Rdtase. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. IPR012335. Thioredoxin_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] |
| PROSITE | PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PRDX6_CHICK | ||||||||
| Accession | Primary (citable) accession number: Q5ZJF4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

Clusters with


