We report the cloning and characterization of two alternately spliced forms of ovine testicular follitropin receptor mRNA. A smaller receptor cDNA (151 A1) of 727 bp codes for a possible soluble receptor protein of 134 amino acids arising from exons 1-4 of the full length receptor. The 1.1 Kb cDNA clone (HK 18) extending up to the 8th exon codes for a mature protein of 259 amino acids with a single membrane spanning domain predicted by hydropathy analysis. As these structures account for 34% and 61% respectively of the extracellular domain of the full length receptor, we suggest that their putative protein products are likely to possess moderate or high affinity binding sites of physiological significance.