Anti-Proprotein convertase PC4 antibody - Homo-B domain (ab39890)

Relevance

PC4 was the fifth of the human prohormone convertasae enzymes to be discovered. Like furin, PC1, PC2 and PACE4, PC4 is a serine proteinase that cleaves after pairs of basic amino acids, but with some differences in substrate specificity and distribution. The catalytic domain has homology to other PC enzymes, the prohormone convertase family initially discovered for their role in processing POMC, insulin and other pro-hormones, and later found to process a wider range of precursor proteins. Some have renamed the prohormone convertases as proprotein convertases, and another group has renamed the entire family with a uniform nomenclature of SPCs ( s ubtilisin-like p roprotein c onvertases). PC4 structure contains a propeptide domain, a catalytic domain and an RGD containing cystein-rich domain (homo-B). The PCs have an RxxR consensus cleavage requirement, and the propeptide is separated from the mature protein by just such a sequence. After cleavage of the propeptide domain, PC4 becomes a two-chain form, and the propeptide piece is released after a second internal cleavage.

Cellular localization

Membrane; single pass membrane protein

Alternative names

Database links