Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum. Forms heterodimer with SERPINA5. Inhibited by SERPINA5. Activity is strongly inhibited by Zn2+, 100 times more abundant in semen than in serum. This inhibition is relieved by exposure to semenogelins, which are avid zinc binders. Belongs to the peptidase S1 family. Kallikrein subfamily. Note: This description may include information from UniProtKB.
Protein type: Protease; EC 188.8.131.52; Secreted; Secreted, signal peptide
Cellular Component: extracellular region; extracellular space; nucleus; protein complex
Molecular Function: endopeptidase activity; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; protein binding; serine-type endopeptidase activity; serine-type peptidase activity
Biological Process: antibacterial peptide production; cellular protein metabolic process; negative regulation of angiogenesis; proteolysis; small GTPase mediated signal transduction
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.