A complementary DNA (cDNA) clone encoding rat Fc gamma receptor II (Fc gamma RII) was isolated from rat neutrophils and characterized. The cDNA encodes a type I transmembrane protein with 285 amino acids having an extracellular domain consisting of two immunoglobulin-like domains (179 amino acids), a transmembrane domain (26 amino acids), and a cytoplasmic domain (47 amino acids). The nucleotide sequences are identical to that of recently cloned Fc gamma RII from rat mast cells. This protein was expressed on FcR-negative Chinese hamster ovary (CHO) cells. The characterization of cDNA-transfected CHO cells clearly indicated that the protein encoded by the cDNA clone binds guinea-pig IgG1 and IgG2 complexes and unexpectedly binds monomeric rat IgG1, but not IgG2. Furthermore, the affinity for immune complexes was significantly augmented by protease treatment of transfectants. In addition, endocytosis of immune complex was noted in transfectants.