{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,16]],"date-time":"2026-07-16T19:42:47Z","timestamp":1784230967605,"version":"3.55.0"},"reference-count":54,"publisher":"National Academy of Sciences","issue":"17","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2002,8,20]]},"abstract":"<jats:p>\n                    G-protein coupled receptors (GPCRs) are ancient, ubiquitous sensors vital to environmental and physiological signaling throughout organismal life. With the publication of the\n                    <jats:italic>Drosophila<\/jats:italic>\n                    genome, numerous \u201corphan\u201d GPCRs have become available for functional analysis. Here we characterize two groups of GPCRs predicted as receptors for peptides with a C-terminal amino acid sequence motif consisting of \u2212PRXamide (PRXa). Assuming ligand-receptor coevolution, two alternative hypotheses were constructed and tested. The insect PRXa peptides are evolutionarily related to the vertebrate peptide neuromedin U (NMU), or are related to arginine vasopressin (AVP), both of which have PRXa motifs. Seven\n                    <jats:italic>Drosophila<\/jats:italic>\n                    GPCRs related to receptors for NMU and AVP were cloned and expressed in\n                    <jats:italic>Xenopus<\/jats:italic>\n                    oocytes for functional analysis. Four\n                    <jats:italic>Drosophila<\/jats:italic>\n                    GPCRs in the NMU group (CG11475, CG8795, CG9918, CG8784) are activated by insect PRXa pyrokinins, (\u2212FXPRXamide), Cap2b-like peptides (\u2212FPRXamide), or ecdysis triggering hormones (\u2212PRXamide). Three\n                    <jats:italic>Drosophila<\/jats:italic>\n                    GPCRs in the vasopressin receptor group respond to crustacean cardioactive peptide (CCAP), corazonin, or adipokinetic hormone (AKH), none of which are PRXa peptides. These findings support a theory of coevolution for NMU and\n                    <jats:italic>Drosophila<\/jats:italic>\n                    PRXa peptides and their respective receptors.\n                  <\/jats:p>","DOI":"10.1073\/pnas.162276199","type":"journal-article","created":{"date-parts":[[2002,9,30]],"date-time":"2002-09-30T12:42:53Z","timestamp":1033389773000},"page":"11423-11428","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":350,"title":["Identification of G protein-coupled receptors for\n                    <i>Drosophila<\/i>\n                    PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution"],"prefix":"10.1073","volume":"99","author":[{"given":"Yoonseong","family":"Park","sequence":"first","affiliation":[{"name":"Departments of Entomology and Cell Biology and Neuroscience, 5429 Boyce Hall, University of California, Riverside, CA 92521"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Young-Joon","family":"Kim","sequence":"additional","affiliation":[{"name":"Departments of Entomology and Cell Biology and Neuroscience, 5429 Boyce Hall, University of California, Riverside, CA 92521"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael E.","family":"Adams","sequence":"additional","affiliation":[{"name":"Departments of Entomology and Cell Biology and Neuroscience, 5429 Boyce Hall, University of California, Riverside, CA 92521"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2002,8,12]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0196-9781(00)00376-4"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1101\/gr.169901"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.241231298"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.150.2.F83"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1152\/physrev.1997.77.4.963"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.244.4906.796"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-1910(90)90060-S"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(95)00929-4"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/300643a0"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1006\/bbrc.1996.5915"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(99)01622-1"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1242\/dev.129.2.493"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.271.5245.88"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0896-6273(00)80805-3"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M001546200"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1038\/35017610"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)41863-1"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(87)91621-4"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1006\/bbrc.1998.9230"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.052556499"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1101\/gr.10.4.516"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.287.5461.2185"},{"key":"e_1_3_3_23_2","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(92)07018-J"},{"key":"e_1_3_3_24_2","unstructured":"Meng X. 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