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

Lilja, Hans LU and Lundwall, Åke LU (1992) In Proc Natl Acad Sci U S A 89(10). p.4559-63
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
4559 - 63
external identifiers
  • Scopus:0026507297
language
English
LU publication?
yes
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
2013-08-11 18:44:21
date last changed
2016-04-16 11:55:03
@misc{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},
  keyword      = {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        = {4559--63},
  series       = {Proc Natl Acad Sci U S A},
  title        = {Molecular cloning of epididymal and seminal vesicular transcripts encoding a semenogelin-related protein},
  volume       = {89},
  year         = {1992},
}