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- *******************************
- * Tachykinin family signature *
- *******************************
-
- Tachykinins [1,2,3] are a group of biologically active peptides which excite
- neurons, evoke behavioral responses, are potent vasodilatators and contract
- (directly or indirectly) many smooth muscles. Peptides known to belong to the
- tachykinin family are listed below:
-
- - Substance P from mammals, birds and fish.
- - Neurokinin A (substance K or neuromedin L) from mammals, birds and fish.
- - Neurokinin B (neuromedin K) from mammals and frogs.
- - Kassinin from frogs.
- - Hylambatin from frogs.
- - Phyllomedusin from a frog.
- - Physalaemin from a frog.
- - Uperolein from frogs.
- - Ranatachykinins A to D from frogs [4].
- - Scyliorhinins from dogfish.
- - Carassin from goldfish [5].
- - Eledoisin from octopus.
-
- Tachykinins, like most other active peptides, are synthesized as larger
- protein precursors that are enzymatically converted to their mature forms.
- Tachykinins are from ten to twelve residues long. We use, as a signature
- pattern, the last five residues of the C-terminal, which are conserved and are
- essential to the biological activity.
-
- -Consensus pattern: F-[IVFY]-G-[LM]-M-[G>]
- [See the note]
- -Sequences known to belong to this class detected by the pattern: ALL, except
- for ranatachykinin D from Rana catesbeiana which has Ala-Pro instead of Gly-
- Leu/Met.
- -Other sequence(s) detected in SWISS-PROT: 5.
-
- -Note: if the sequence is processed, the peptide ends with a C-terminal
- amidated Met while in a precursor sequence it is always followed by a Gly
- which subsequently provides the amide group.
- -Note: locust myotropic peptides locustatachykinin I and II [6] are distantly
- related to the tachykinin family but their C-terminal sequence is different
- (Val-Arg instead of Leu/Met-Met). Thus, they are not detected by the above
- pattern.
-
- -Last update: December 1992 / Text revised.
-
- [ 1] Maggio J.E.
- Annu. Rev. Neurosci. 11:13-28(1988).
- [ 2] Helke C.J., Krause J.E., Mantyh P.W., Couture R., Bannon M.J.
- FASEB J. 4:1606-1615(1990).
- [ 3] Avanov A.Y.
- Mol. Biol. (Mosk) 26:5-24(1992).
- [ 4] Kozawa H., Hino J., Minamino N., Kangawa K., Matsuo H.
- Biochem. Biophys. Res. Commun. 177:588-595(1991).
- [ 5] Conlon J.M., O'Harte F., Peter R.E., Kah O.
- J. Neurochem. 56:1432-1436(1991).
- [ 6] Schoofs L., Holman G.M., Hayes T.K., Nachman R.J., de Loof A.
- FEBS Lett. 261:397-401(1990).
-