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PROSITE documentation PDOC00466 [for PROSITE entry PS00539]

Pyrokinins 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.

Technical section

PROSITE method (with tools and information) covered by this documentation:

PYROKININ, PS00539; Pyrokinins signature  (PATTERN)


1AuthorsNachman R.J., Roberts V.A., Dyson H.J., Holman G.M., Tainer J.A.
TitleActive conformation of an insect neuropeptide family.
SourceProc. Natl. Acad. Sci. U.S.A. 88:4518-4522(1991).
PubMed ID2034692

2AuthorsMatsumoto S., Fonagy A., Kurihara M., Uchiumi K., Nagamine T., Chijimatsu M., Mitsui T.
TitleIsolation and primary structure of a novel pheromonotropic neuropeptide structurally related to leucopyrokinin from the armyworm larvae, Pseudaletia separata.
SourceBiochem. Biophys. Res. Commun. 182:534-539(1992).
PubMed ID1734867

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