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Molecular cloning of epididymal and seminal vesicular transcripts encoding a semenogelin-related protein

Lilja, Hans LU orcid and Lundwall, Åke LU (1992) In Proc Natl Acad Sci U S A 89(10). p.63-4559
Abstract
Freshly ejaculated human semen has the appearance of a loose gel in which the predominant structural protein components are the seminal vesicle-secreted semenogelins (Sg). The primary structure of the 439-residue SgI has previously been obtained by cDNA cloning. This cDNA cross-hybridizes to a larger transcript coding for a second secretory protein, SgII. Here we report the almost complete structure of a precursor of SgII established by lambda gt11 clones isolated from epididymal and seminal vesicular cDNA libraries. The deduced amino acid sequence of the 559-residue mature protein has a molecular weight of 62,931 but an increase in weight may be provided by asparagine-linked oligosaccharide attachment at residue 249. SgII, which has 78%... (More)
Freshly ejaculated human semen has the appearance of a loose gel in which the predominant structural protein components are the seminal vesicle-secreted semenogelins (Sg). The primary structure of the 439-residue SgI has previously been obtained by cDNA cloning. This cDNA cross-hybridizes to a larger transcript coding for a second secretory protein, SgII. Here we report the almost complete structure of a precursor of SgII established by lambda gt11 clones isolated from epididymal and seminal vesicular cDNA libraries. The deduced amino acid sequence of the 559-residue mature protein has a molecular weight of 62,931 but an increase in weight may be provided by asparagine-linked oligosaccharide attachment at residue 249. SgII, which has 78% overall identity with SgI, contains eight 60-residue regions that display conspicuous internal sequence similarity, whereas SgI only contains six of these regions. The SgII structure is translated from an open reading frame in a polyadenylylated 2.4-kilobase transcript. The message is abundant in the seminal vesicles but rare in the epididymis. (Less)
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keywords
Research Support, Protein Precursors/*genetics, Oligodeoxyribonucleotides, Molecular Weight, Molecular Sequence Data, Male, Humans, Gonadal Steroid Hormones/*genetics, Gene Library, Epididymis/*physiology, DNA/genetics/isolation & purification, Comparative Study, Molecular/methods, Cloning, Northern, Blotting, Amino Acid Sequence, Base Sequence, Non-U.S. Gov't, Restriction Mapping, Semen/*physiology, *Seminal Plasma Proteins, *Seminal Vesicle Secretory Proteins, Seminal Vesicles/*physiology, Sequence Homology, Nucleic Acid, *Transcription, Genetic
in
Proc Natl Acad Sci U S A
volume
89
issue
10
pages
63 - 4559
external identifiers
  • scopus:0026507297
language
English
LU publication?
yes
additional info
10
id
748c6d8f-e6cb-412c-adb1-75c3be57976d (old id 3965209)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1584792
date added to LUP
2016-04-04 13:58:04
date last changed
2021-05-23 03:33:28
@article{748c6d8f-e6cb-412c-adb1-75c3be57976d,
  abstract     = {{Freshly ejaculated human semen has the appearance of a loose gel in which the predominant structural protein components are the seminal vesicle-secreted semenogelins (Sg). The primary structure of the 439-residue SgI has previously been obtained by cDNA cloning. This cDNA cross-hybridizes to a larger transcript coding for a second secretory protein, SgII. Here we report the almost complete structure of a precursor of SgII established by lambda gt11 clones isolated from epididymal and seminal vesicular cDNA libraries. The deduced amino acid sequence of the 559-residue mature protein has a molecular weight of 62,931 but an increase in weight may be provided by asparagine-linked oligosaccharide attachment at residue 249. SgII, which has 78% overall identity with SgI, contains eight 60-residue regions that display conspicuous internal sequence similarity, whereas SgI only contains six of these regions. The SgII structure is translated from an open reading frame in a polyadenylylated 2.4-kilobase transcript. The message is abundant in the seminal vesicles but rare in the epididymis.}},
  author       = {{Lilja, Hans and Lundwall, Åke}},
  keywords     = {{Research Support; Protein Precursors/*genetics; Oligodeoxyribonucleotides; Molecular Weight; Molecular Sequence Data; Male; Humans; Gonadal Steroid Hormones/*genetics; Gene Library; Epididymis/*physiology; DNA/genetics/isolation & purification; Comparative Study; Molecular/methods; Cloning; Northern; Blotting; Amino Acid Sequence; Base Sequence; Non-U.S. Gov't; Restriction Mapping; Semen/*physiology; *Seminal Plasma Proteins; *Seminal Vesicle Secretory Proteins; Seminal Vesicles/*physiology; Sequence Homology; Nucleic Acid; *Transcription; Genetic}},
  language     = {{eng}},
  number       = {{10}},
  pages        = {{63--4559}},
  series       = {{Proc Natl Acad Sci U S A}},
  title        = {{Molecular cloning of epididymal and seminal vesicular transcripts encoding a semenogelin-related protein}},
  url          = {{http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1584792}},
  volume       = {{89}},
  year         = {{1992}},
}