Extensive structural differences between genes for the alpha 1 and alpha 2 chains of type IV collagen despite conservation of coding sequences.

Analysis of the structure of the 3'-end of the human alpha 2(IV) gene demonstrated that the alpha 1(IV) and alpha 2(IV) genes have diverged extensively in spite of the apparent homology of the respective gene products. The NC-1 domain and the 3'-untranslated region are encoded by three exons in the alpha 2(IV) gene but five exons in the alpha 1(IV) gene. The two introns present in the NC-1 domain coding part of the alpha 2(IV) gene had the same location as two of the introns of the alpha 1(IV) gene. The junction exon in the alpha 2(IV) gene contains 53 bp coding for Gly-X-Y sequences whereas there are 71 bp in the alpha 1(IV) gene. Three other Gly-X-Y coding exons studied from the human alpha 2(IV) gene have sizes that differ from corresponding exons in the alpha 1(IV) gene and only one intron location matches here between the two genes. None of the exons studied has 54 bp or multiples thereof.