The major clotting protein from guinea pig seminal vesicle contains eight repeats of a 24-amino acid domain.
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.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis; D008297:Male; D008969:Molecular Sequence Data; D011506:Proteins / Q000235:genetics*; D012091:Repetitive Sequences, Nucleic Acid; D029607:Seminal Vesicle Secretory Proteins; D012669:Seminal Vesicles / Q000378:metabolism*; D013552:Swine
D011506:Proteins; D029607:Seminal Vesicle Secretory Proteins; D004247:DNA