Molecular cloning of complementary DNA encoding mouse seminal vesicle-secreted protein SVSI and demonstration of homology with copper amine oxidases
Lundwall, Åke LU ; Malm, Johan LU ; Clauss, Adam LU ; Valtonen-André, Camilla LU and Ceder, Yvonne LU
(2003)
In Biology of Reproduction
69(6).
p.1923-1930
- 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... (More)
- 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 1, 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/294676
- author
- Lundwall, Åke
LU
; Malm, Johan
LU
; Clauss, Adam
LU
; Valtonen-André, Camilla
LU
and Ceder, Yvonne
LU
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- male reproductive tract, seminal vesicles, sperm motility and transport
- in
- Biology of Reproduction
- volume
- 69
- issue
- 6
- pages
- 1923 - 1930
- publisher
- Oxford University Press
- external identifiers
-
- wos:000186772300021
- pmid:12930721
- scopus:0344306689
- ISSN
- 1529-7268
- DOI
- 10.1095/biolreprod.103.019984
- language
- English
- LU publication?
- yes
- id
- dbad109c-faa7-46c9-8967-c2bcc61e392a (old id 294676)
- date added to LUP
- 2016-04-01 11:53:02
- date last changed
- 2022-05-19 02:20:00
@article{dbad109c-faa7-46c9-8967-c2bcc61e392a,
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 1, 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 = {{Lundwall, Åke and Malm, Johan and Clauss, Adam and Valtonen-André, Camilla and Ceder, Yvonne}},
issn = {{1529-7268}},
keywords = {{male reproductive tract; seminal vesicles; sperm motility and transport}},
language = {{eng}},
number = {{6}},
pages = {{1923--1930}},
publisher = {{Oxford University Press}},
series = {{Biology of Reproduction}},
title = {{Molecular cloning of complementary DNA encoding mouse seminal vesicle-secreted protein SVSI and demonstration of homology with copper amine oxidases}},
url = {{http://dx.doi.org/10.1095/biolreprod.103.019984}},
doi = {{10.1095/biolreprod.103.019984}},
volume = {{69}},
year = {{2003}},
}