Tachykinins are members of a family of peptides which act as neurohormones in mammals. These peptide hormones have been implicated in a number of mammalian motor and sensory functions, particularly related to central and peripheral neuron activity and the contraction of smooth muscle.' There is evidence for three classes of tachykinin receptors in mammals with variations in amino acid (aa) sequence occumng between species.? The classification of receptors is based on interactions with specific natural tachykinins and synthetic agonists which selectively act on only one of the three receptor classes. Tachykinin-like peptides have been purified from invertebrate^,^ and several cDNAs from Drosophila have been cloned which code for proteins with structural and biochemical properties similar to mammalian tachykinin receptor^.^.^ The stable fly, Stomoxys calcitrans, is a major hematophagous pest of livestock causing an estimated $400 million annual loss to the United States livestock industry.6 Current control methodologies include good animal husbandry and insecticide spraying. Ongoing studies seek alternative ways of controlling infestations as concerns increase over the use of insecticides. As part of these studies, we sought to clone the receptor for tachykinin peptides in the stable fly to study the molecular interaction between the receptor and the peptide.A stable fly cDNA library was synthesized in a hgt22 cloning vector using polyA+ RNA from whole adult flies and screened with a Drosophila rnelanogaster DTKR tachykinin receptor DNA probe.4 One 4118 bp clone, designated STKR, was purified and sequenced and found to have an open reading frame which encoded a 678 aa protein with significant homology to the D . melanogaster DTKR open reading frame. The DTKR cDNA is reported to encode a 519 aa receptorlike protein with homology to vertebrae tachykinin receptors and whose mRNA is expressed in the adult insect's central nervous system and specific subsets of neurons in the developing e m b r y~.~ In expression studies, DTKR is activated by vertebrate substance P-like peptides. Homology between the STKR open reading frame and reported tachykinin receptors is highest in the seven putative membrane spanning regions of this receptor family. Comparison of the DTKR and STKR open reading frame sequence spanning transmembrane regions I-VII shows 227 of 283 aligned aa are identical (80%), whereas 266 of 283 (94%) are either identical or conservative substitutions as determined by the pam250S scoring matrix analysis of MacVector Sequence Analysis Software (International Biotechnologies Inc., 310