A full-length cDNA clone encoding for the chick CNTFR alpha (alpha component of the ciliary neurotrophic factor receptor) was isolated by screening an embryonic day 13 chick brain cDNA library with a rat CNTFR alpha probe. The isolated cDNA clone contained a approximately 2-kb insert with an open reading frame of 362 amino acids. The identification of this clone as chick CNTFR alpha was based on the homology in amino acid sequence (approximately 70%) with the rat and human CNTFR alpha. Hydropathy analysis revealed that the chick CNTFR alpha contains a hydrophobic region at the amino terminus that is typical of secretory signal peptides, as well as a hydrophobic region at the carboxyl terminus that is characteristic of glycosylphosphatidylinositol-linked proteins. The expression of chick CNTFR alpha was developmentally regulated and was widely distributed in neural tissues, such as brain and spinal cord. In the periphery, chick CNTFR alpha transcript was expressed at high levels in the skeletal muscle and was only barely detectable in the liver. Unexpectedly, the expression of chick CNTFR alpha mRNA in skeletal muscle was decreased by approximately 10-fold at 1.5 days after denervation. This is in sharp contrast to the result previously obtained with CNTFR alpha in denervated rat muscle.