biostudies-literatureXu JPNINDS NIH HHS1132066https://www.ebi.ac.uk/biostudies/studies/S-EPMC10067623biostudies-literatureUnknown14The vasopressin/oxytocin signaling system is present in both protostomes and deuterostomes and plays various physiological roles. Although there were reports for both vasopressin-like peptides and receptors in mollusc <i>Lymnaea</i> and Octopus, no precursor or receptors have been described in mollusc <i>Aplysia</i>. Here, through bioinformatics, molecular and cellular biology, we identified both the precursor and two receptors for <i>Aplysia</i> vasopressin-like peptide, which we named <i>Aplysia</i> vasotocin (apVT). The precursor provides evidence for the exact sequence of apVT, which is identical to conopressin G from cone snail venom, and contains 9 amino acids, with two cysteines at position 1 and 6, similar to nearly all vasopressin-like peptides. Through inositol monophosphate (IP1Frontiers in pharmacologyCharacterization of an <i>Aplysia</i> vasotocin signaling system and actions of posttranslational modifications and individual residues of the ligand on receptor activity.PMC10067623R01 NS066587R01 NS118606RF1 NS118606Zhang GJiang HMChen PJing JXu JPMei YSWang HYDing XYLi YDGuo SQLiu WJZhou HBFu PfalseCharacterization of an <i>Aplysia</i> vasotocin signaling system and actions of posttranslational modifications and individual residues of the ligand on receptor activity.The vasopressin/oxytocin signaling system is present in both protostomes and deuterostomes and plays various physiological roles. Although there were reports for both vasopressin-like peptides and receptors in mollusc <i>Lymnaea</i> and Octopus, no precursor or receptors have been described in mollusc <i>Aplysia</i>. Here, through bioinformatics, molecular and cellular biology, we identified both the precursor and two receptors for <i>Aplysia</i> vasopressin-like peptide, which we named <i>Aplysia</i> vasotocin (apVT). The precursor provides evidence for the exact sequence of apVT, which is identical to conopressin G from cone snail venom, and contains 9 amino acids, with two cysteines at position 1 and 6, similar to nearly all vasopressin-like peptides. Through inositol monophosphate (IP12023-01-01T00:00:00Z20232026-05-10T03:11:59.463Z2024-11-06T04:39:07.258ZS-EPMC100676233702104810.3389/fphar.2023.1132066