Q9GLW9 (PRDX5_PAPHA) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 63.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Peroxiredoxin-5, mitochondrial EC=1.11.1.15 Alternative name(s): Peroxiredoxin V Short name=Prx-V Thioredoxin reductase | ||
| Gene names |
| ||
| Organism | Papio hamadryas (Hamadryas baboon) | ||
| Taxonomic identifier | 9557 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Papio |
Protein attributes
| Sequence length | 215 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 | Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling By similarity. |
| Catalytic activity | 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Mitochondrion By similarity. Cytoplasm By similarity. Peroxisome By similarity. |
| Sequence similarities | Belongs to the peroxiredoxin 2 family. Contains 1 thioredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Mitochondrion Peroxisome |
| Coding sequence diversity | Alternative initiation |
| Domain | Redox-active center Transit peptide |
| Molecular function | Antioxidant Oxidoreductase Peroxidase |
| PTM | Acetylation Disulfide bond |
| Gene Ontology (GO) | |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisomeInferred 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... | |
Alternative products
| This entry describes 2 isoforms produced by alternative initiation. [Align] [Select] | ||||||
| Isoform Mitochondrial (identifier: Q9GLW9-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform Cytoplasmic+peroxisomal (identifier: Q9GLW9-2) The sequence of this isoform differs from the canonical sequence as follows: 1-53: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 53 | 53 | Mitochondrion Potential | ||||||||
| Chain | 54 – 215 | 162 | Peroxiredoxin-5, mitochondrial | PRO_0000023797 | |||||||
Regions | |||||||||||
| Domain | 57 – 215 | 159 | Thioredoxin | ||||||||
| Motif | 213 – 215 | 3 | Microbody targeting signal By similarity | ||||||||
Sites | |||||||||||
| Active site | 101 | 1 | Cysteine sulfenic acid (-SOH) intermediate Potential | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 84 | 1 | N6-acetyllysine By similarity | ||||||||
| Disulfide bond | 101 ↔ 205 | Redox-active By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 1 – 53 | 53 | Missing in isoform Cytoplasmic+peroxisomal. | VSP_018831 | |||||||
Sequences
| ||||||||||||||||||||||||
References
| [1] | "Cloning and characterization of baboon AOEB166/PRDX5." Knoops B., Cherif H. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF110734 mRNA. Translation: AAG13451.2. |
3D structure databases | |
| ProteinModelPortal | Q9GLW9. |
| SMR | Q9GLW9. Positions 55-215. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG053675. |
Family and domain databases | |
| InterPro | IPR013740. Redoxin. IPR012336. Thioredoxin-like_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| Pfam | PF08534. Redoxin. 1 hit. [Graphical view] |
| SUPFAM | SSF52833. Thiordxn-like_fd. 1 hit. |
| PROSITE | PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PRDX5_PAPHA | ||||||||
| Accession | Primary (citable) accession number: Q9GLW9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with