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

J. T. Moore, J. Hagstrom, Daniel J Mc Cormick, S. Harvey, B. Madden, E. Holicky, D. R. Stanford, Eric D Wieben

Research output: Contribution to journalArticle

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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 γ-glutamyl-ε-lysine crosslinks, it is likely that the 24-amino acid repeating unit is the unit of function of SVP-1.

Original languageEnglish (US)
Pages (from-to)6712-6724
Number of pages13
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number19
StatePublished - 1987

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Seminal Vesicles
Guinea Pigs
Amino Acids
Protein Precursors
Lysine
Proteins
Nucleotides
Glutamine
Amino Acid Sequence
Complementary DNA
Clone Cells
Messenger RNA

ASJC Scopus subject areas

  • General
  • Genetics

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The major clotting protein from guinea pig seminal vesicle contains eight repeats of a 24-amino acid domain. / Moore, J. T.; Hagstrom, J.; Mc Cormick, Daniel J; Harvey, S.; Madden, B.; Holicky, E.; Stanford, D. R.; Wieben, Eric D.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 84, No. 19, 1987, p. 6712-6724.

Research output: Contribution to journalArticle

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AU - Moore, J. T.

AU - Hagstrom, J.

AU - Mc Cormick, Daniel J

AU - Harvey, S.

AU - Madden, B.

AU - Holicky, E.

AU - Stanford, D. R.

AU - Wieben, Eric D

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N2 - 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 γ-glutamyl-ε-lysine crosslinks, it is likely that the 24-amino acid repeating unit is the unit of function of SVP-1.

AB - 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 γ-glutamyl-ε-lysine crosslinks, it is likely that the 24-amino acid repeating unit is the unit of function of SVP-1.

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