Abstract
We have isolated and characterized the gene coding for the mouse Fc receptor that is termed FcγRIIa. The gene contains five exons and spans approximately 9 kilobases. Unlike most members of the immunoglobulin gene superfamily, this gene utilizes multiple exons to encode its leader peptide. The first exon encodes the hydrophobic region of the signal sequence; the second exon, which contains only 21 base pairs, encodes a segment of the signal peptidase recognition site; and the beginning of the third exon encodes the predicted site of peptidase cleavage. The third and fourth exons each code for immunoglobulin-like extracellular domains. The fifth exon encodes the hydrophobic transmembrane domain and the cytoplasmic tail. Partial characterization of the FcγRIIb gene indicates that it also contains multiple leader exons, including a 21-base-pair exon and two exons coding for homologous immunoglobulin-like extracellular domains. However, the FcγRIIb gene uses four exons to encode its intracytoplasmic region. Analysis using contour-clamped homogeneous electric field (CHEF) gels indicates that the FcγRIIa and FcγRIIb genes are linked within 160 kilobases on mouse chromosome 1.
Original language | English |
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Pages (from-to) | 2856-2860 |
Number of pages | 5 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 87 |
Issue number | 7 |
State | Published - Apr 1990 |
Keywords
- Exon-intron junctions
- Fc receptors
- Immunoglobulin gene superfamily
- Protein domains