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Seminalplasmin: Recent Evolution of Another Member of the Neuropeptide Y Gene Family

Herbert Herzog, Yvonne Hort, Rainer Schneider and John Shine
Proceedings of the National Academy of Sciences of the United States of America
Vol. 92, No. 2 (Jan. 17, 1995), pp. 594-598
Stable URL: http://www.jstor.org/stable/2366672
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Seminalplasmin: Recent Evolution of Another Member of the Neuropeptide Y Gene Family
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Abstract

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.

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