Nonselective, voltage-independent cation channel that mediates Ca(2+) and to a lesser extent Na(+) influx, leading to increased cytoplasmic Ca(2+) levels (PubMed:25620041, PubMed:27333281, PubMed:28775320, PubMed:29745897). Functions as ligand-gated ion channel (PubMed:25620041, PubMed:27333281, PubMed:28775320, PubMed:29745897). Binding of ADP-ribose causes a conformation change; the channel is primed but still requires Ca(2+) binding to trigger channel opening (PubMed:25620041, PubMed:27333281, PubMed:28775320, PubMed:29745897). May have ADP-ribose pyrophosphatase activity which reduces ADP-ribose levels induced by oxidative stress, thus preventing the channel activation by reactive oxygen species (PubMed:25620041, PubMed:27333281). Activated by phosphatidylinositol 4,5-bisphosphate (PIP2) (PubMed:29745897). Although PIP2 is essential for the channel activation, its contribution to the level of channel activity is minimal (PubMed:29745897). Also activated by diphosphate ribose-2'-phosphate (PubMed:27333281). Upon binding to ADPR, channel activation requires only a short initial cytosolic Ca(2+) increase, then the activation is sustained by the uptake of extracellular Ca(2+) (PubMed:29745897, PubMed:25620041). Activated by 2-aminoethyl diphenylborinate (2-APB) in a Ca(2+)-dependent manner (PubMed:28775320). 2-APB prevents the inactivation of the channel (PubMed:28775320). Homotetramer. The Nudix hydrolase domain is dispensable for ADP-ribose-dependent channel activation. May be involved in the regulation of ADP-ribose intracellular levels. Essential to prevent response to oxidative stress. Belongs to the transient receptor (TC 1.A.4) family. LTrpC subfamily. TRPM2 sub-subfamily. Unlike in human TRPM2, residues in the Nudix box (AEFGE) that are important for ADP-ribose pyrophosphatase activity are conserved suggesting that N.vectensis TRPM2 may have ADP-ribose pyrophosphatase activity.