|PROSITE documentation PDOC00282 [for PROSITE entry PS00313]|
Seminal vesicle protein I (SVP-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  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.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Moore J.T. Hagstrom J. McCormick D.J. Harvey S. Madden B. Holicky E. Stanford D.R. Wieben E.D.|
|Title||The major clotting protein from guinea pig seminal vesicle contains eight repeats of a 24-amino acid domain.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 84:6712-6714(1987).|
|Source||Unpublished observations (1993).|