{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Xu JP"],"funding":["NINDS NIH HHS"],"pagination":["1132066"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10067623"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14"],"pubmed_abstract":["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 (IP1"],"journal":["Frontiers in pharmacology"],"pubmed_title":["Characterization of an <i>Aplysia</i> vasotocin signaling system and actions of posttranslational modifications and individual residues of the ligand on receptor activity."],"pmcid":["PMC10067623"],"funding_grant_id":["R01 NS066587","R01 NS118606","RF1 NS118606"],"pubmed_authors":["Zhang G","Jiang HM","Chen P","Jing J","Xu JP","Mei YS","Wang HY","Ding XY","Li YD","Guo SQ","Liu WJ","Zhou HB","Fu P"],"additional_accession":[]},"is_claimable":false,"name":"Characterization of an <i>Aplysia</i> vasotocin signaling system and actions of posttranslational modifications and individual residues of the ligand on receptor activity.","description":"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 (IP1","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023","modification":"2026-05-10T03:11:59.463Z","creation":"2024-11-06T04:39:07.258Z"},"accession":"S-EPMC10067623","cross_references":{"pubmed":["37021048"],"doi":["10.3389/fphar.2023.1132066"]}}