{PDOC00466}
{PS00539; PYROKININ}
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* Pyrokinins signature *
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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).

-Consensus pattern: F-[GSTV]-P-R-L-[G>]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: 3.

-Note: 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.

[ 1] Nachman R.J., Roberts V.A., Dyson H.J., Holman G.M., Tainer J.A.
     "Active conformation of an insect neuropeptide family."
     Proc. Natl. Acad. Sci. U.S.A. 88:4518-4522(1991).
     PubMed=2034692
[ 2] Matsumoto S., Fonagy A., Kurihara M., Uchiumi K., Nagamine T.,
     Chijimatsu M., Mitsui T.
     "Isolation and primary structure of a novel pheromonotropic
     neuropeptide structurally related to leucopyrokinin from the armyworm
     larvae, Pseudaletia separata."
     Biochem. Biophys. Res. Commun. 182:534-539(1992).
     PubMed=1734867

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