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The Journal of Immunology, Vol 155, Issue 3 1203-1209, Copyright © 1995 by American Association of Immunologists
ARTICLES |
TP de Wit, HC Morton, PJ Capel and JG van de Winkel
Department of Immunology, University Hospital of Utrecht, The Netherlands.
A better understanding of IgA's role in immunity requires insight in IgAR complexity. We have now isolated, characterized, and sequenced the gene encoding the prototypic human myeloid IgA FcR (CD89). The gene consists of five exons and spans approximately 12 kilobase pairs. The leader peptide is encoded by two exons, the second of which is 36 bp long and specifies the predicted peptidase cleavage site. A similar, but shorter (21 bp) mini-exon has been found in the FcR for IgG (Fc gamma R) genes, and the FcR for IgE (Fc epsilon RI alpha) gene (human and rodent). The third and fourth exons code for two homologous Ig-like domains. The final exon encodes a short extracellular region, a hydrophobic transmembrane region, and a short cytoplasmic tail. The sequence of the 5'-flanking region was determined, and one major and several minor transcription initiation sites were mapped by primer extension studies. A putative TATA box was located at an appropriate location relative to the start site. Southern blot analyses of genomic DNA confirm the restriction map generated from cloned DNA. These data define the Fc alpha R gene as a distantly related member of the IgR gene family.
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