Reviewed,
UniProtKB/Swiss-Prot Q9BGI2 (PRDX4_BOVIN)
Last modified
June 16, 2009.
Version 49.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Peroxiredoxin-4 EC=1.11.1.15 Alternative name(s): Prx-IV | ||
| Gene names |
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| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 274 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation By similarity. |
| Catalytic activity | 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. |
| Subunit structure | Homodimer or heterodimer with PRDX1; disulfide-linked, upon oxidation By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Miscellaneous | The active site is the redox-active Cys-127 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-248-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-127 (to Cys-SO3H) upon oxidative stress 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 | Disulfide bond |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reductionInferred 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 – 274 | 274 | Peroxiredoxin-4 | PRO_0000135097 | |||||
Regions | |||||||||
| Domain | 82 – 240 | 159 | Thioredoxin | ||||||
Sites | |||||||||
| Active site | 127 | 1 | Cysteine sulfenic acid (-SOH) intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Disulfide bond | 127 | Interchain (with C-248); in linked form By similarity | |||||||
| Disulfide bond | 248 | Interchain (with C-127); in linked form By similarity | |||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning of 4 new bovine peroxiredoxins, and screening of the complete peroxiredoxin family in different bovine tissues." Leyens G., Donnay I., Knoops B. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| AF305563 mRNA. Translation: AAG53660.1. BC109824 mRNA. Translation: AAI09825.1. | |
| IPI | IPI00691994. |
| RefSeq | NP_776858.1. |
| UniGene | Bt.5203 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1QQ2 based on UniProtKB Q63716. |
| ModBase | Search... |
Protein family/group databases | |
| PeroxiBase | 4531. Bt2CysPrx04. |
Genome annotation databases | |
| Ensembl | ENSBTAG00000006165. Bos taurus. [Contig view] |
| GeneID | 281999. |
| KEGG | bta:281999. |
Phylogenomic databases | |
| HOVERGEN | Q9BGI2. |
| OMA | Q9BGI2. AINTEVV. |
Enzyme and pathway databases | |
| BRENDA | 1.11.1.15. 251. |
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 | PRDX4_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q9BGI2 Secondary accession number(s): Q32L06 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


