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Literature summary for 3.4.21.75 extracted from
- Furin functions as a nonproteolytic chaperone for matrix metalloproteinase-28: MMP-28 propeptide sequence requirement (2011), Biochem. Res. Int., 2011, 630319.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in COS-1 cell | Mus musculus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasm | colocalization with matrix metalloproteinase MMP-28 | Mus musculus | 5737 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | furin serves as an intermolecular chaperone for matrix metalloprotease MMP-28 secretion by interacting with the propeptide domain of MMP-28. cleavage of MMP-28 at the furin consensus sequence does not occur and proteolytic inactive furin is equally effective in enhancing MMP-28 secretion | Mus musculus |
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Release 2023.1 (January 2023)
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