The human Fc receptor with low affinity for IgG (FcRIII, CD16) is encoded by two nearly identical genes, FcRIII-A and FcRIII-B, resulting in tissue-specific expression of alternative membrane-anchored isoforms. The transmembrane CD16 receptor forms a heteromeric structure with the FcRI () and/or CD3 () subunits on the surface of activated monocytes/macrophages, NK cells, and a subset of T cells. The expression of the glycosylphosphatidylinositol-anchored CD16 isoform encoded by the FcRIII-B gene is restricted to polymorphonuclear leukocytes and can be induced by MeSO differentiation of HL60 cells. We have isolated and sequenced genomic clones of the human FcRIII-A and FcRIII-B genes, located their transcription initiation sites, identified a different organization of their 5` regions, and demonstrated four distinct classes of FcRIII-A transcripts (a1-a4) compared with a single class of FcRIII-Bb1 transcripts. Both CD16 promoters (positions -198 to -10) lack the classical ``TATA'' positioning consensus sequence but confer transcriptional activity when coupled to the human lysozyme enhancer. Both promoters also display different tissue-specific transcriptional activities reflecting the expected gene expression of FcRIII-A and FcRIII-B in NK cells versus polymorphonuclear leukocytes. Within the -198/-10 fragments, the sequences of the two CD16 genes have been identified to differ in 10 positions. It is suggested that these nucleotide differences might contribute to cell type-specific transcription of FcRIII genes.

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