Abstract
The DC antigen is one of the class II major histocompatibility antigens involved in the regulation of the immune response. This molecule is a heterodimer composed of an .alpha. and a .beta. chain. Southern blot analysis of several homozygous cell lines shows that there are 2 DC.beta. genes. The DC-3.beta. gene, corresponding to a polymorphic restriction fragment, was cloned and sequenced and found to exist in 5 exons spanning 8 kilobase pairs of DNA. These exons correspond to the functional domains of the DC.beta. protein. Comparisons of the .beta.1 domains of known DC.beta. chains shows that the polymorphism is clustered in 4 regions. A similar comparison of the mouse A.beta. sequences shows only 2 prominent diversity regions. The DC.beta. chain sequences are 8 amino acids shorter than the A.beta. chain sequences due to the elimination of a small exon by an aberrant splice acceptor.