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) (PubMed:22159626, PubMed:26110417). 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 (PubMed:16759235, PubMed:22159626, PubMed:26110417). Binds to TXA2, TXB2, prostaglandine H2 mimetic (PGH2 mimetic), PGJ2, and PGF2alpha (PubMed:22159626). 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) (PubMed:22159626). Induces relaxation of aorta rat previously contracted with TXA2 mimetic (PubMed:22159626). Moreover, it also impairs platelet-assisted formation of neutrophil extracellular traps (NETs) (PubMed:26110417). NETs are web-like structures of DNA and proteins that play an important role in killing of pathogens (PubMed:26110417). In addition, NETs are implicated in thrombus formation (PubMed:26110417). In vivo, this protein exhibits antithrombotic activity in two distinct mice models that are highly dependent on platelets (PubMed:26110417). It is noteworthy that it inhibits thrombosis without promoting excessive bleeding (PubMed:26110417). 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.