| Primary Identifier | IPR007945 | Type | Family |
| Short Name | Secretogranin_V |
| description | Prohormone convertases (PCs) 1 and 2 are a family of eukaryotic subtilisins thought to mediate the proteolytic cleavage of many peptide precursors []. Protein 7B2 (secretogranin V) functions as a molecular chaperone for PC2, preventing its premature activation in the regulated secretory pathway []. 7B2 represents a potent inhibitor of PC2, and it is also required for the activation of PC2, which is synthesised as a zymogen. Protein 7B2 has an N-terminalactivation domain and a C-terminal (CT) inhibitory domain (MEROPS inhibitor family I21), separated by a furin cleavage site []. 7B2 is synthesised as a precursor protein that is cleaved into the N-terminal fragment and the C-terminal peptide [].7B2 has been linked to neurodegenerative diseases. It may act as an anti-aggregation chaperone []. However, in an APP model mouse 7B2 knockout has been shown to reduce rather than enhance plaque burden []. |
