PROSITE documentation PDOC00282
Seminal vesicle protein I repeats signature


Seminal vesicle protein I (SVP-1) [1] is one of the four major secretory proteins secreted by guinea-pig seminal vesicle epithelium. It is a clotting protein that serves as the substrate in the formation of the copulatory plug. Covalent clotting of this protein is catalyzed by a transglutaminase and involves the formation of γ-glutamyl-epsilon-lysine crosslinks. SVP-1 sequence contains eight repeats of a twenty four amino acid residue domain. There are seven invariant residues in these repeats, three of them (two lysines and one glutamine) probably participate in the cross-links. The pattern we have developed comprises positions 1 to 19 of the domain and includes the three cross-linking residues.

This pattern is also present twice [2] in the N-terminal region of the precursor of human skin elafin, an inhibitor of elastase as well as in the precursor of pig sodium/potassium atpase inhibitor SPAI-2.

Last update:

November 1997 / Text revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

SVP_I, PS00313; Seminal vesicle protein I repeats signature  (PATTERN)


1AuthorsMoore J.T. Hagstrom J. McCormick D.J. Harvey S. Madden B. Holicky E. Stanford D.R. Wieben E.D.
TitleThe major clotting protein from guinea pig seminal vesicle contains eight repeats of a 24-amino acid domain.
SourceProc. Natl. Acad. Sci. U.S.A. 84:6712-6714(1987).
PubMed ID3477802

2AuthorsBairoch A.
SourceUnpublished observations (1993).

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