Exon structure of a XXXX -binding protein gene reflects its evolutionary relationship to the asialoglycoprotein receptor and nonfibrillar collagens.

@entity2228 @entity535 @entity1735 @entity71004 @entity2733 @entity3913 @entity35 @entity1473
Cloned cDNAs encoding @entity3913 -binding proteins isolated from @entity35 liver have been used to isolate one of the genes encoding this group of proteins. This gene, which encodes the minor form of binding protein (designated @entity71004 ), has been characterized by sequence analysis. The protein-coding portion of the mRNA for the @entity71004 is encoded by four exons separated by three introns. The @entity2733 -terminal, collagen-like portion of the protein is encoded by the first two exons. These exons resemble the exons found in the genes for nonfibrillar collagens in that the intron which divides them is inserted between the first two bases of a @entity2228 codon and the exons do not have the 54- or 108-base pair lengths characteristic of fibrillar collagen genes. The @entity1735 -binding portion of @entity71004 is encoded by the remaining two exons. This portion of the protein is homologous to the @entity1735 -recognition domain of the hepatic asialoglycoprotein receptor, which is encoded by four exons. It appears that the three @entity1473 -terminal exons of the asialoglycoprotein receptor gene have been fused into a single exon in the @entity71004 gene. The organization of the @entity71004 gene is very similar to the arrangement of the gene encoding the highly homologous pulmonary surfactant apoprotein, although one of the intron positions is shifted by a single @entity535 . The 3' end of a @entity3913 -binding protein pseudogene has also been characterized.
