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

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...

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Published inBiology of reproduction Vol. 69; no. 6; pp. 1923 - 1930
Main Authors Åke Lundwall, Johan Malm, Adam Clauss, Camilla Valtonen-AndrÃ, A. Yvonne Olsson
Format Journal Article
LanguageEnglish
Published Madison, WI Society for the Study of Reproduction 01.12.2003
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Abstract 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 glycosylation. The SVS I is homologous with amiloride-binding protein 1 (ABP1), a diamine oxidase. However, it probably lacks enzymatic activity, because the cDNA codes for His instead of Tyr at the position of the active-site topaquinon. The SVS I monomer probably binds one molecule of copper, because the His residues coordinated by Cu(II) are conserved. The SVS I gene consists of five exons and is situated on mouse chromosome 6,B2.3. It is located in a region of 100 kilobases (kb) containing several genes with homology to SVS I, including the gene of ABP1 and two other proteins with homology to diamine oxidase. The locus is conserved on rat chromosome 4q24, but the homologous region on human chromosome 7q34-q36 solely contains ABP1. The other genes with homology to diamine oxidase were probably present in a progenitor of primates and rodents but were lost in the evolutionary lineage leading to humans—presumably during recombination between chromosomes. The estimated molecular mass of rat SVS I is 102 kDa (excluding glycosylation). The species difference in size of SVS I is caused by tandem repeats of 18 amino acid residues in the central part of the molecule: The mouse has seven repeats, and the rat has 12 repeats.
AbstractList 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 glycosylation. The SVS I is homologous with amiloride-binding protein 1 (ABP1), a diamine oxidase. However, it probably lacks enzymatic activity, because the cDNA codes for His instead of Tyr at the position of the active-site topaquinon. The SVS I monomer probably binds one molecule of copper, because the His residues coordinated by Cu(II) are conserved. The SVS I gene consists of five exons and is situated on mouse chromosome 6,B2.3. It is located in a region of 100 kilobases (kb) containing several genes with homology to SVS I, including the gene of ABP1 and two other proteins with homology to diamine oxidase. The locus is conserved on rat chromosome 4q24, but the homologous region on human chromosome 7q34-q36 solely contains ABP1. The other genes with homology to diamine oxidase were probably present in a progenitor of primates and rodents but were lost in the evolutionary lineage leading to humans—presumably during recombination between chromosomes. The estimated molecular mass of rat SVS I is 102 kDa (excluding glycosylation). The species difference in size of SVS I is caused by tandem repeats of 18 amino acid residues in the central part of the molecule: The mouse has seven repeats, and the rat has 12 repeats.
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 glycosylation. The SVS I is homologous with amiloride-binding protein 1 (ABP1), a diamine oxidase. However, it probably lacks enzymatic activity, because the cDNA codes for His instead of Tyr at the position of the active-site topaquinon. The SVS I monomer probably binds one molecule of copper, because the His residues coordinated by Cu(II) are conserved. The SVS I gene consists of five exons and is situated on mouse chromosome 6,B2.3. It is located in a region of 100 kilobases (kb) containing several genes with homology to SVS I, including the gene of ABP1 and two other proteins with homology to diamine oxidase. The locus is conserved on rat chromosome 4q24, but the homologous region on human chromosome 7q34-q36 solely contains ABP1. The other genes with homology to diamine oxidase were probably present in a progenitor of primates and rodents but were lost in the evolutionary lineage leading to humans-presumably during recombination between chromosomes. The estimated molecular mass of rat SVS I is 102 kDa (excluding glycosylation). The species difference in size of SVS I is caused by tandem repeats of 18 amino acid residues in the central part of the molecule: The mouse has seven repeats, and the rat has 12 repeats.
Author Camilla Valtonen-AndrÃ
Åke Lundwall
Adam Clauss
A. Yvonne Olsson
Johan Malm
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Issue 6
Keywords Seminal vesicle
Rodentia
Homology
Male genital system
Protein
Vertebrata
Reproduction
Mammalia
Complementary DNA
Mouse
Animal
Molecular cloning
Copper
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Snippet The primary structure of mouse SVS I was determined by peptide sequencing and nucleotide sequencing of cloned cDNA. The precursor molecule consists of 820...
The primary structure of mouse SVS I was determined by peptide sequencing and nucleotide sequencing of cloned cDNA. The precursor molecule consists of 820...
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SubjectTerms 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
Title Molecular Cloning of Complementary DNA Encoding Mouse Seminal Vesicle-Secreted Protein SVS I and Demonstration of Homology with Copper Amine Oxidases
URI http://www.biolreprod.org/content/69/6/1923.abstract
https://www.ncbi.nlm.nih.gov/pubmed/12930721
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