This target displays homology in the following species: Cow: 100%; Dog: 100%; Guinea Pig: 100%; Horse: 100%; Human: 100%; Mouse: 100%; Rabbit: 100%; Rat: 100%; Zebrafish: 100%
The subtilisin-like prohormone convertase (PC) family is a group of cellular enzymes that cleave most prohormones and neuropeptide precursors. Numerous other cellular proteins, some viral proteins, and bacterial toxins that are transported by the constitutive secretory pathway are also targeted for maturation by PCs. PC family members share structural similarities, which include a heterogeneous approximately 10 kDa amino-terminal proregion, a highly conserved approximately 55 kDa subtilisin-like catalytic domain, and carboxyl-terminal domain that is heterogeneous in length and sequence. These enzymes become catalytically active following proregion cleavage within the appropriate cellular compartment. The subcellular localization of PC family members varies. Immunolocalization studies show that PC1 is found in the perinuclear region as well as the trans-Golgi network, whereas PC2 can be found in the trans-Golgi network as well as diffusely distributed in the peripheral cytoplasm.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: EC 18.104.22.168; KEX2-like endoprotease 2; NEC 2; Neuroendocrine convertase 2; PC2; Prohormone convertase 2; Proprotein convertase 2
Gene Aliases: NEC 2; NEC-2; NEC2; PC2; PCSK2; SPC2
UniProt ID: (Human) P16519
Entrez Gene ID: (Human) 5126
Molecular Function: serine protease