Reviewed,
UniProtKB/Swiss-Prot P52033 (GPXC_DIRIM)
Last modified
November 25, 2008.
Version 45.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Glutathione peroxidase EC=1.11.1.9 Alternative name(s): Di29 |
| Organism | Dirofilaria immitis (Canine heartworm) |
| Taxonomic identifier | 6287 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Nematoda › Chromadorea › Spirurida › Filarioidea › Onchocercidae › Dirofilaria |
Protein attributes
| Sequence length | 221 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)
| Catalytic activity | 2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Secreted › extracellular spaceBy similarity. |
| Sequence similarities | Belongs to the glutathione peroxidase family. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Oxidoreductase Peroxidase |
| PTM | Glycoprotein |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stressInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | glutathione peroxidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Potential | ||||||
| Chain | 20 – 221 | 202 | Glutathione peroxidase | PRO_0000013094 | |||||
Sites | |||||||||
| Active site | 72 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 28 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 87 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 90 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | Venkatakrishnaiah L., James E. Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Dirofilaria immitis: molecular cloning and expression of a cDNA encoding a selenium-independent secreted glutathione peroxidase." Tripp C.A., Frank R.S., Selkirk M.E., Tang L., Mika-Grieve M., Frank G.R., Grieve R.B. Exp. Parasitol. 88:43-50(1998) [PubMed: 9501847] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| U04693 mRNA. Translation: AAA16224.1. U87457 mRNA. Translation: AAB58573.1. U87458 Genomic DNA. Translation: AAB58574.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GP1 based on UniProtKB P00435. |
| ModBase | Search... |
Protein family/group databases | |
| PeroxiBase | 3752. DiGPx01. |
Family and domain databases | |
| InterPro | IPR000889. Glut_peroxidase. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| PANTHER | PTHR11592. Glut_peroxidase. 1 hit. |
| Pfam | PF00255. GSHPx. 1 hit. [Graphical view] |
| PIRSF | PIRSF000303. Glutathion_perox. 1 hit. |
| PRINTS | PR01011. GLUTPROXDASE. |
| PROSITE | PS00460. GLUTATHIONE_PEROXID_1. 1 hit. PS00763. GLUTATHIONE_PEROXID_2. 1 hit. PS51355. GLUTATHIONE_PEROXID_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GPXC_DIRIM | ||||||||
| Accession | Primary (citable) accession number: P52033 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

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