Molecular cloning of epididymal and seminal vesicular transcripts encoding a semenogelin-related protein
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3965209
- author
- Lilja, Hans LU and Lundwall, Åke LU
- organization
- publishing date
- 1992
- type
- Contribution to journal
- publication status
- published
- subject
- 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}}, }