Molecular Cloning of Complementary DNA Encoding Mouse Seminal Vesicle-Secreted Protein SVS I and Demonstration of Homology with Copper Amine Oxidases

• Published in: Biology of reproduction Vol. 69; no. 6; pp. 1923 - 1930
• Main Authors: Ã ke Lundwall, Johan Malm, Adam Clauss, Camilla Valtonen-AndrÃ, A. Yvonne Olsson
• Format: Journal Article
• Language: English
• Published: Madison, WI Society for the Study of Reproduction 01.12.2003
• Subjects: Amine Oxidase (Copper-Containing) - genetics; Amine Oxidase (Copper-Containing) - metabolism; Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; Carrier Proteins - metabolism; Chromosome Mapping; Cloning, Molecular; Dihydroxyphenylalanine - analogs & derivatives; Dihydroxyphenylalanine - metabolism; DNA, Complementary; Exons; Fundamental and applied biological sciences. Psychology; Glycosylation; Humans; Introns; Male; Mammalian male genital system; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Molecular Weight; Morphology. Physiology; Rats; Seminal Vesicle Secretory Proteins - genetics; Seminal Vesicle Secretory Proteins - metabolism; Sequence Analysis; Sequence Homology, Amino Acid; Vertebrates: reproduction; Seminal vesicle; Rodentia; Homology; Male genital system; Protein; Vertebrata; Reproduction; Mammalia; Complementary DNA; Mouse; Animal; Molecular cloning; Copper; EC 1.4.3.4

The primary structure of mouse SVS I was determined by peptide sequencing and nucleotide sequencing of cloned cDNA. The precursor molecule consists of 820 amino acid residues, including a signal peptide of 24 residues, and the mature polypeptide chain of 91 kDa has one site for potential N-linked gl...