Herzog H, Hort Y, Schneider R, Shine J
Garvan Institute of Medical Research, St. Vincent's Hospital, Darlinghurst, New South Wales, Sydney, Australia.
Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):594-8. doi: 10.1073/pnas.92.2.594.
Seminalplasmin, the major basic protein of bull semen, an important regulator of calcium transport in bovine sperm and a positive modulator of the zona pellucida-induced acrosome reaction, is shown to be a recently created member of the neuropeptide Y gene family. Sequence analysis of the bovine peptide YY-pancreatic polypeptide gene cluster reveals an unexpected and extensive homology between seminalplasmin and the neuropeptide Y gene family, at the level of both gene structure and primary amino acid and nucleotide sequences. The extremely high degree of homology to the peptide YY gene, in both coding and especially noncoding regions, suggests that the seminalplasmin gene has arisen by a very recent gene duplication of the bovine peptide YY gene. Despite the more than 95% nucleotide sequence identity, a few specific mutations in the seminalplasmin gene have resulted in both the loss of the amino- and carboxyl-terminal cleavage sites characteristic of all other members of the neuropeptide Y family and the acquisition of a function apparently unrelated to the neurotransmitter/endocrine role of peptide YY.
精浆蛋白是公牛精液中的主要碱性蛋白,是牛精子中钙转运的重要调节因子,也是透明带诱导的顶体反应的正调节剂,它被证明是神经肽Y基因家族的一个新成员。对牛肽YY - 胰多肽基因簇的序列分析显示,精浆蛋白与神经肽Y基因家族在基因结构、一级氨基酸和核苷酸序列水平上存在意想不到的广泛同源性。在编码区尤其是非编码区与肽YY基因的极高同源性表明,精浆蛋白基因是通过牛肽YY基因最近的一次基因复制产生的。尽管核苷酸序列同一性超过95%,但精浆蛋白基因中的一些特定突变导致了神经肽Y家族所有其他成员特有的氨基和羧基末端切割位点的丧失,并获得了一种显然与肽YY的神经递质/内分泌作用无关的功能。