We have found a single class of progesterone binding sites at the amphibian oocyte plasma membrane, whereas two progesterone receptor forms, similar to those in chick and human, are present in the cytosol. In this study both plasma membranes and 105,000 x g cytosol from Rana pipiens oocytes were photoaffinity labeled with the synthetic progestin [3H]R5020. SDS-polyacrylamide gel electrophoresis of the photolabeled proteins in the oocyte cytosol indicate that the two forms have molecular weights essentially identical to that found for human breast tissue and chick oviduct, i.e., 80 and 110 kDa, and that the forms were present in approximately equimolar ratios. In contrast, the plasma membrane form is present as a single 110 kDa species and accounts for at least 50% of the total 110 kDa species. The presence of large amounts of the 110 kDa protein in both membrane and cytosol suggests that the plasma membrane receptor may not be unique, and that the 110 kDa form may function both in membrane and cytosol and/or that part of the cytosolic 110 kDa form represents progesterone receptor in the process of being transported to or from the plasma membrane.