Semenogelin I

SEMG1
Identifiers
Aliases	SEMG1, CT103, SEMG, SGI, dJ172H20.2, Semenogelin I
External IDs	HomoloGene: 130511 GeneCards: SEMG1
Gene ontology Molecular function • protein binding • metal ion binding Cellular component • extracellular fluid • extracellular region • extracellular exosome • nucleus • protein complex Biological process • negative regulation of calcium ion import • cellular protein metabolic process • blood coagulation • insemination • antibacterial humoral response • positive regulation of serine-type endopeptidase activity • protein heterooligomerization • negative regulation of flagellated sperm motility Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6406	n/a
Ensembl	ENSG00000124233	n/a
UniProt	P04279	n/a
RefSeq (mRNA)	NM_198139 NM_003007	n/a
RefSeq (protein)	NP_002998.1	n/a
Location (UCSC)	Chr 20: 45.21 – 45.21 Mb	n/a
PubMed search	[1]	n/a
Wikidata

View/Edit Human

Semenogelin-1 is a protein that in humans is encoded by the SEMG1 gene.^[2][3][4]

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.^[4]

See also

• Semenogelin

References

1. "Human PubMed Reference:".
2. Lilja H; Abrahamsson PA; Lundwall A (Mar 1989). "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". J Biol Chem. 264 (3): 1894–900. PMID 2912989.
3. Jonsson M; Linse S; Frohm B; Lundwall A; Malm J (Apr 2005). "Semenogelins I and II bind zinc and regulate the activity of prostate-specific antigen". Biochem J. 387 (Pt 2): 447–53. doi:10.1042/BJ20041424. PMC 1134973. PMID 15563730.
4. "Entrez Gene: SEMG1 semenogelin I".

Further reading

• Robert M; Gagnon C (1999). "Semenogelin I: a coagulum forming, multifunctional seminal vesicle protein.". Cell. Mol. Life Sci. 55 (6-7): 944–60. doi:10.1007/s000180050346. PMID 10412373.
• Ulvsbäck M, Lazure C, Lilja H, et al. (1992). "Gene structure of semenogelin I and II. The predominant proteins in human semen are encoded by two homologous genes on chromosome 20.". J. Biol. Chem. 267 (25): 18080–4. PMID 1517240.
• Schneider K, Kausler W, Tripier D, et al. (1989). "[Isolation and structure determination of two peptides occurring in human seminal plasma]". Biol. Chem. Hoppe-Seyler. 370 (4): 353–6. PMID 2757795.
• Li CH; Hammonds RG; Ramasharma K; Chung D (1985). "Human seminal alpha inhibins: isolation, characterization, and structure.". Proc. Natl. Acad. Sci. U.S.A. 82 (12): 4041–4. doi:10.1073/pnas.82.12.4041. PMC 397930. PMID 3889920.
• Lilja H; Jeppsson JO (1985). "Amino acid sequence of the predominant basic protein in human seminal plasma.". FEBS Lett. 182 (1): 181–4. doi:10.1016/0014-5793(85)81179-0. PMID 3972122.
• Ramasharma K, Sairam MR, Seidah NG, et al. (1984). "Isolation, structure, and synthesis of a human seminal plasma peptide with inhibin-like activity.". Science. 223 (4641): 1199–202. doi:10.1126/science.6422553. PMID 6422553.
• Lilja H; Laurell CB; Jeppsson JO (1984). "Characterization of the predominant basic protein in human seminal plasma, one cleavage product of the major seminal vesicle protein.". Scand. J. Clin. Lab. Invest. 44 (5): 439–46. doi:10.3109/00365518409083835. PMID 6484484.
• Seidah NG; Ramasharma K; Sairam MR; Chrétien M (1984). "Partial amino acid sequence of a human seminal plasma peptide with inhibin-like activity.". FEBS Lett. 167 (1): 98–102. doi:10.1016/0014-5793(84)80840-6. PMID 6698208.
• Khan Z; Smyth DG (1993). "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.". Eur. J. Biochem. 212 (1): 35–40. doi:10.1111/j.1432-1033.1993.tb17629.x. PMID 8444163.
• Lundwall A (1996). "The structure of the semenogelin gene locus--nucleotide sequence of the intergenic and the flanking DNA.". Eur. J. Biochem. 235 (3): 466–70. doi:10.1111/j.1432-1033.1996.00466.x. PMID 8654389.
• Malm J, Hellman J, Magnusson H, et al. (1996). "Isolation and characterization of the major gel proteins in human semen, semenogelin I and semenogelin II.". Eur. J. Biochem. 238 (1): 48–53. doi:10.1111/j.1432-1033.1996.0048q.x. PMID 8665951.
• Bjartell A, Malm J, Moller C, et al. (1997). "Distribution and tissue expression of semenogelin I and II in man as demonstrated by in situ hybridization and immunocytochemistry.". J. Androl. 17 (1): 17–26. PMID 8833737.
• Robert M; Gibbs BF; Jacobson E; Gagnon C (1997). "Characterization of prostate-specific antigen proteolytic activity on its major physiological substrate, the sperm motility inhibitor precursor/semenogelin I.". Biochemistry. 36 (13): 3811–9. doi:10.1021/bi9626158. PMID 9092810.
• Peter A; Lilja H; Lundwall A; Malm J (1998). "Semenogelin I and semenogelin II, the major gel-forming proteins in human semen, are substrates for transglutaminase.". Eur. J. Biochem. 252 (2): 216–21. doi:10.1046/j.1432-1327.1998.2520216.x. PMID 9523691.
• Lövgren J; Airas K; Lilja H (1999). "Enzymatic action of human glandular kallikrein 2 (hK2). Substrate specificity and regulation by Zn2+ and extracellular protease inhibitors.". Eur. J. Biochem. 262 (3): 781–9. doi:10.1046/j.1432-1327.1999.00433.x. PMID 10411640.
• Malm J; Hellman J; Hogg P; Lilja H (2000). "Enzymatic action of prostate-specific antigen (PSA or hK3): substrate specificity and regulation by Zn(2+), a tight-binding inhibitor.". Prostate. 45 (2): 132–9. doi:10.1002/1097-0045(20001001)45:2<132::AID-PROS7>3.0.CO;2-3. PMID 11027412.
• Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
• Brillard-Bourdet M, Réhault S, Juliano L, et al. (2002). "Amidolytic activity of prostatic acid phosphatase on human semenogelins and semenogelin-derived synthetic substrates.". Eur. J. Biochem. 269 (1): 390–5. doi:10.1046/j.0014-2956.2001.02667.x. PMID 11784334.