Inhibits platelet aggregation and vasoconstriction through binding to distinct eicosanoids involved in inflammation (acts as a scavenger), and has a role in inhibiting host innate immunity by impairing platelet-assisted formation of neutrophil extracellular traps (NETs). Inhibits platelet aggregation by collagen, and low doses of thromboxane A2 mimetic (TXA2 mimetic), and arachidonic acid (AA) without affecting aggregation induced by ADP, convulxin (GP6 agonist), and PMA. Binds to TXA2, TXB2, prostaglandine H2 mimetic (PGH2 mimetic), PGJ2, and PGF2alpha. Binding is not observed to leukotrienes, AA, and biogenic amines (PGE1, 5(S)-HETE, 12(S)-HETE, 20-HETE, norepinephrine, epinephrine, serotonine, LTC4 and ADP). Induces relaxation of aorta rat previously contracted with TXA2 mimetic. Moreover, it also impairs platelet-assisted formation of neutrophil extracellular traps (NETs). NETs are web-like structures of DNA and proteins that play an important role in killing of pathogens. In addition, NETs are implicated in thrombus formation. In vivo, this protein exhibits antithrombotic activity in two distinct mice models that are highly dependent on platelets. It is noteworthy that it inhibits thrombosis without promoting excessive bleeding. Expressed in salivary glands. Belongs to the calycin superfamily. Triabin family. Morita et al. (2006) suggested that this protein inhibits collagen-induce platelet aggregation by binding to platelet glycoprotein VI, but a surface plasmon resonance experiment failed to demonstrate an interaction between these two proteins.