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. 1987 Oct;84(19):6712–6714. doi: 10.1073/pnas.84.19.6712

The major clotting protein from guinea pig seminal vesicle contains eight repeats of a 24-amino acid domain.

J T Moore 1, J Hagstrom 1, D J McCormick 1, S Harvey 1, B Madden 1, E Holicky 1, D R Stanford 1, E D Wieben 1
PMCID: PMC299153  PMID: 3477802

Abstract

The complete amino acid sequence of the major clotting protein from the guinea pig seminal vesicle (SVP-1) has been determined by nucleotide sequencing of cDNA clones corresponding to the 3' terminus of an mRNA that codes for a protein precursor to SVP-1. The first 40 amino acids of the derived protein sequence are identical to those determined by N-terminal sequencing of SVP-1 isolated from the lumen of the seminal vesicle. This finding confirms that SVP-1 is cleaved from the C terminus of a larger precursor protein. The portion of the nucleotide sequence that codes for SVP-1 contains eight highly homologous but imperfect repeats of a 72-nucleotide domain. This repeated structure is also evident at the amino acid level. The consensus 24-amino acid repeat unit contains two lysine and three glutamine residues. Since the clotting of SVP-1 is known to involve the formation of gamma-glutamyl-epsilon-lysine crosslinks, it is likely that the 24-amino acid repeating unit is the unit of function of SVP-1.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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