{PDOC00282}
{PS00313; SVP_I}
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* Seminal vesicle protein I repeats signature *
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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  gamma-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.

-Consensus pattern: [IVM]-x-G-Q-D-x-V-K-x(5)-[KN]-G-x(3)-[STLV]
                    [Q and K are involved in covalent cross-links]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 1997 / Text revised.

[ 1] Moore J.T., Hagstrom J., McCormick D.J., Harvey S., Madden B.,
     Holicky E., Stanford D.R., Wieben E.D.
     "The major clotting protein from guinea pig seminal vesicle contains
     eight repeats of a 24-amino acid domain."
     Proc. Natl. Acad. Sci. U.S.A. 84:6712-6714(1987).
     PubMed=3477802
[ 2] Bairoch A.
     Unpublished observations (1993).

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