PROSITE documentation PDOC00466Pyrokinins signature
Pyrokinins are insect neuropeptides that mediate visceral muscle contractile activity (myotropic activity) [1]. The pyrokinins are peptides of 8 to 16 amino acids that share the amide-blocked C-terminal sequence Phe-Xaa-Pro-Arg-Leu-NH2, where Xaa is either Gly, Ser, Thr, or Val. This pentapeptide is sufficient to elicit a significant myotropic activity. The same C-terminal sequence is present in the following insect neuropeptides:
- Pheromone biosynthesis activating neuropeptide (PBAN). PBAN is a hormone that controls sex pheromone production in female moths as well as eliciting pyrokinin-like myotropic activity.
- Pheromonotropin [2], from Pseudaletia separata, which also controls sex pheromone production.
- Bombyx mori diapause hormone (DH).
If the sequence is processed, the peptide ends with a C-terminal amidated Leu while in a precursor sequence it is always followed by a Gly which subsequently provides the amide group.
Last update:December 1992 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Nachman R.J. Roberts V.A. Dyson H.J. Holman G.M. Tainer J.A. |
| Title | Active conformation of an insect neuropeptide family. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 88:4518-4522(1991). | |
| PubMed ID | 2034692 |
| 2 | Authors | Matsumoto S. Fonagy A. Kurihara M. Uchiumi K. Nagamine T. Chijimatsu M. Mitsui T. |
| Title | Isolation and primary structure of a novel pheromonotropic neuropeptide structurally related to leucopyrokinin from the armyworm larvae, Pseudaletia separata. | |
| Source | Biochem. Biophys. Res. Commun. 182:534-539(1992). | |
| PubMed ID | 1734867 |
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