PRSS2

PRSS2 belongs to the trypsin family of serine proteases and encodes anionic trypsinogen. It is part of a cluster of trypsinogen genes that are located within the T cell receptor beta locus. Enzymes of this family cleave peptide bonds that follow lysine or arginine residues. This protein is found at high levels in pancreatic juice and its upregulation is a characteristic feature of pancreatitis. This protein has also been found to activate pro-urokinase in ovarian tumors, suggesting a function in tumor invasion. In addition, this enzyme is able to cleave across the type II collagen triple helix in rheumatoid arthritis synovitis tissue, potentially participating in the degradation of type II collagen-rich cartilage matrix.

Serine Protease 2

In the ileum, may be involved in defensin processing, including DEFA5.

Antimicrobial humoral responseTAS:Reactome
Collagen catabolic processManual Assertion Based On ExperimentIDA:UniProtKB
DigestionIEA:UniProtKB-KW
Extracellular matrix disassemblyTAS:Reactome
Positive regulation of cell adhesionManual Assertion Based On ExperimentTAS:UniProtKB
Positive regulation of cell growthManual Assertion Based On ExperimentTAS:UniProtKB
ProteolysisManual Assertion Based On ExperimentIDA:UniProtKB

Secreted, extracellular space

Sulfated on tyrosine.
Sulfation at Tyr-154 increases selectivity towards basic versus apolar residues at the P2' position of inhibitors that bind in a substrate-like fashion. Although the increase in selectivity is relatively small, it may facilitate digestion of a broader range of dietary proteins.