Semenogelin I

Semenogelin I

Semenogelin I, also known as SEMG1, is a human gene.cite web | title = Entrez Gene: SEMG1 semenogelin I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6406| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene is the predominant protein in semen. The encoded secreted protein is involved in the formation of a gel matrix that encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes this protein into smaller peptides, with each possibly having a separate function. The proteolysis process breaks down the gel matrix and allows the spermatozoa to move more freely. Two transcript variants encoding different isoforms have been found for this gene.cite web | title = Entrez Gene: SEMG1 semenogelin I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6406| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Robert M, Gagnon C |title=Semenogelin I: a coagulum forming, multifunctional seminal vesicle protein. |journal=Cell. Mol. Life Sci. |volume=55 |issue= 6-7 |pages= 944–60 |year= 1999 |pmid= 10412373 |doi=
*cite journal | author=Ulvsbäck M, Lazure C, Lilja H, "et al." |title=Gene structure of semenogelin I and II. The predominant proteins in human semen are encoded by two homologous genes on chromosome 20. |journal=J. Biol. Chem. |volume=267 |issue= 25 |pages= 18080–4 |year= 1992 |pmid= 1517240 |doi=
*cite journal | author=Schneider K, Kausler W, Tripier D, "et al." |title= [Isolation and structure determination of two peptides occurring in human seminal plasma] |journal=Biol. Chem. Hoppe-Seyler |volume=370 |issue= 4 |pages= 353–6 |year= 1989 |pmid= 2757795 |doi=
*cite journal | author=Lilja H, Abrahamsson PA, Lundwall A |title=Semenogelin, the predominant protein in human semen. Primary structure and identification of closely related proteins in the male accessory sex glands and on the spermatozoa. |journal=J. Biol. Chem. |volume=264 |issue= 3 |pages= 1894–900 |year= 1989 |pmid= 2912989 |doi=
*cite journal | author=Li CH, Hammonds RG, Ramasharma K, Chung D |title=Human seminal alpha inhibins: isolation, characterization, and structure. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 12 |pages= 4041–4 |year= 1985 |pmid= 3889920 |doi=
*cite journal | author=Lilja H, Jeppsson JO |title=Amino acid sequence of the predominant basic protein in human seminal plasma. |journal=FEBS Lett. |volume=182 |issue= 1 |pages= 181–4 |year= 1985 |pmid= 3972122 |doi=
*cite journal | author=Ramasharma K, Sairam MR, Seidah NG, "et al." |title=Isolation, structure, and synthesis of a human seminal plasma peptide with inhibin-like activity. |journal=Science |volume=223 |issue= 4641 |pages= 1199–202 |year= 1984 |pmid= 6422553 |doi=
*cite journal | author=Lilja H, Laurell CB, Jeppsson JO |title=Characterization of the predominant basic protein in human seminal plasma, one cleavage product of the major seminal vesicle protein. |journal=Scand. J. Clin. Lab. Invest. |volume=44 |issue= 5 |pages= 439–46 |year= 1984 |pmid= 6484484 |doi=
*cite journal | author=Seidah NG, Ramasharma K, Sairam MR, Chrétien M |title=Partial amino acid sequence of a human seminal plasma peptide with inhibin-like activity. |journal=FEBS Lett. |volume=167 |issue= 1 |pages= 98–102 |year= 1984 |pmid= 6698208 |doi=
*cite journal | author=Khan Z, Smyth DG |title=Isolation and identification of N-terminally extended forms of 5-oxoprolylglutamylprolinamide (Glp-Glu-Pro-NH2), a thyrotropin-releasing-hormone (TRH)-like peptide present in human semen. |journal=Eur. J. Biochem. |volume=212 |issue= 1 |pages= 35–40 |year= 1993 |pmid= 8444163 |doi=
*cite journal | author=Lundwall A |title=The structure of the semenogelin gene locus--nucleotide sequence of the intergenic and the flanking DNA. |journal=Eur. J. Biochem. |volume=235 |issue= 3 |pages= 466–70 |year= 1996 |pmid= 8654389 |doi=
*cite journal | author=Malm J, Hellman J, Magnusson H, "et al." |title=Isolation and characterization of the major gel proteins in human semen, semenogelin I and semenogelin II. |journal=Eur. J. Biochem. |volume=238 |issue= 1 |pages= 48–53 |year= 1996 |pmid= 8665951 |doi=
*cite journal | author=Bjartell A, Malm J, Moller C, "et al." |title=Distribution and tissue expression of semenogelin I and II in man as demonstrated by in situ hybridization and immunocytochemistry. |journal=J. Androl. |volume=17 |issue= 1 |pages= 17–26 |year= 1997 |pmid= 8833737 |doi=
*cite journal | author=Robert M, Gibbs BF, Jacobson E, Gagnon C |title=Characterization of prostate-specific antigen proteolytic activity on its major physiological substrate, the sperm motility inhibitor precursor/semenogelin I. |journal=Biochemistry |volume=36 |issue= 13 |pages= 3811–9 |year= 1997 |pmid= 9092810 |doi= 10.1021/bi9626158
*cite journal | author=Peter A, Lilja H, Lundwall A, Malm J |title=Semenogelin I and semenogelin II, the major gel-forming proteins in human semen, are substrates for transglutaminase. |journal=Eur. J. Biochem. |volume=252 |issue= 2 |pages= 216–21 |year= 1998 |pmid= 9523691 |doi=
*cite journal | author=Lövgren J, Airas K, Lilja H |title=Enzymatic action of human glandular kallikrein 2 (hK2). Substrate specificity and regulation by Zn2+ and extracellular protease inhibitors. |journal=Eur. J. Biochem. |volume=262 |issue= 3 |pages= 781–9 |year= 1999 |pmid= 10411640 |doi=
*cite journal | author=Malm J, Hellman J, Hogg P, Lilja H |title=Enzymatic action of prostate-specific antigen (PSA or hK3): substrate specificity and regulation by Zn(2+), a tight-binding inhibitor. |journal=Prostate |volume=45 |issue= 2 |pages= 132–9 |year= 2000 |pmid= 11027412 |doi=
*cite journal | author=Deloukas P, Matthews LH, Ashurst J, "et al." |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a
*cite journal | author=Brillard-Bourdet M, Réhault S, Juliano L, "et al." |title=Amidolytic activity of prostatic acid phosphatase on human semenogelins and semenogelin-derived synthetic substrates. |journal=Eur. J. Biochem. |volume=269 |issue= 1 |pages= 390–5 |year= 2002 |pmid= 11784334 |doi=

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