Pannexins are a family of large, oligomeric ion channels involved in a number of broad physiological processes. As ATP release channels, pannexins have important implications for purinergic signaling pathways, especially in context of neurological signaling where ATP acts as a neurotransmitter, or in context of vascular signaling, where ATP regulates vasoconstriction. Pannexin-1 is the best characterized member of the pannexin family largely because it presents readily observable currents when expressed heterologously and studied using patch clamp electrophysiology. Curiously, pannexin-1 channels can be activated using strong depolarizing voltage potentials (greater than +20 mV), suggesting the presence of a voltage sensing motif not found in other members of the pannexin family. To localize a potential voltage sensor in pannexin-1, we borrowed domains from pannexin-3 - a member of the pannexin family not activated by a voltage stimulus - and generated chimeric channels. Interestingly, we find that the extracellular and intracellular domains of pannexin-1 are dispensable for voltage sensing, suggesting an intrinsic voltage sensor within the transmembrane domains of pannexin-1.