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 18.104.22.168; Secreted; Secreted, signal peptide
Cellular Component: extracellular space; protein complex; extracellular region; nucleus
Molecular Function: protein binding; serine-type peptidase activity; serine-type endopeptidase activity; endopeptidase activity; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Biological Process: antibacterial peptide production; negative regulation of angiogenesis; cellular protein metabolic process; small GTPase mediated signal transduction; proteolysis
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.