The structure of rat and mouse growth hormone-releasing factor (GRF) peptide and precursor shows considerable divergence from that of the human counterpart and also within rodents themselves. To study such structural divergence in another rodent, we cloned a cDNA encoding the GRF precursor from golden hamster. The hamster GRF (haGRF) cDNA clone had an open-reading frame that predicts a haGRF precursor protein with 107 amino acids. The haGRF precursor bore greater overall homology (82%) to the human than the same rodent homologue (58-64%) and contained two processing sites identical to the human sequence that would generate mature haGRF peptide. Furthermore, the haGRF peptide, like human but unlike rat or mouse GRF, consisted of 44 amino acids and also had greater homology to the human (89%) than the rodent sequence (64-75%), conserving a Tyr residue at the N-terminus and an amidated Leu residue at the C-terminus. Thus, both haGRF precursor and peptide are structurally more related to those of human than of other rodents, suggesting that rodent GRF precursor diverged from the human sequence at differential rates within the species.