Hayano T, Sogawa K, Ichihara Y, Fujii-Kuriyama Y, Takahashi K
Department of Biochemistry, Japanese Foundation for Cancer Research, Tokyo.
J Biol Chem. 1988 Jan 25;263(3):1382-5.
The entire human pepsinogen C gene has been isolated from a cosmid genomic library. The nucleotide sequences of all the exons and the 5'- and 3'-flanking regions of the gene are presented. The organization of the gene is fundamentally compatible with those of other aspartic proteinases, allowing us to conclude that the genes of these aspartic proteinases including pepsinogen C are derived from a common ancestral gene. The predicted 388-residue amino acid sequence of human pepsinogen C consists of a signal sequence of 16-amino acid residues, an activation peptide of 43 residues, and the mature pepsin of 329 residues containing the two active-site aspartic acids. In the light of present notions about eukaryotic gene expression, possible regulatory roles of the oligonucleotide DNA sequences in the promoter region of the gene are discussed.
完整的人胃蛋白酶原C基因已从黏粒基因组文库中分离出来。文中给出了该基因所有外显子以及5′和3′侧翼区域的核苷酸序列。该基因的结构与其他天冬氨酸蛋白酶的结构基本一致，这使我们能够得出结论，包括胃蛋白酶原C在内的这些天冬氨酸蛋白酶的基因都源自一个共同的祖先基因。预测的人胃蛋白酶原C的388个氨基酸残基的序列由一个16个氨基酸残基的信号序列、一个43个残基的激活肽以及包含两个活性位点天冬氨酸的329个残基的成熟胃蛋白酶组成。根据目前关于真核基因表达的观点，讨论了该基因启动子区域寡核苷酸DNA序列可能的调控作用。
