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The protein encoded by SEMG1 is the predominant protein in semen.
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Data indicate that semenogelin I (Sg I) expression has potential value in predicting renal cell carcinoma (show MOK Proteins) (RCC (show XRCC1 Proteins)) progression and prognosis, suggesting the use of Sg I as a biomarker for RCC (show XRCC1 Proteins).
Peptides from the antimicrobial protein semenogelin I have antibacterial activity.
EPPIN and SEMG1 rapidly co-evolved in primates
SEMG1 was significantly changed in asthenozoosperm, which could be the candidate gene for the development of diagnostic marker and provided the opportunity to further illustrate the biological mechanisms of asthenozoospermia.
Three regions of SEM1 (show SHFM1 Proteins)(86-107) comprise the amyloid fibril core that enhances HIV-1 infection.
Interaction analysis identifies semenogelin I fragments as new binding partners of PIP (show PIP Proteins) in human seminal plasma
EPPIN's semenogelin I binding site: a contraceptive drug target.
Nuclear semenogelin I expression could be a reliable prognosticator in men who undergo radical prostatectomy.
The proteomes of the type-1 diabetic, type-2 diabetic, and non-diabetic obese patients presented elevated amounts of the same set of one molecular form of semenogelin-1, one form of clusterin (show CLU Proteins), and two forms of lactotransferrin (show LTF Proteins).
Peptides released by physiological cleavage of Semg1 and Semg2 (show SEMG2 Proteins) form amyloids that enhance HIV infection.
SVS2 keeps sterols on the sperm plasma membrane and plays a key role in unlocking sperm capacitation in vivo.
Seminal vesicle protein SVS2 is required for sperm survival in the uterus.
the fertility of ejaculated sperm is associated with SVS2 distribution in the female reproductive tract, SVS2 functions as a decapacitation factor for mouse sperm.
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.
, semenogelin 1
, semenogelin I isoform a preproprotein
, cancer/testis antigen 103
, semen coagulating protein
, SVS II
, seminal vesicle protein, secretion 1
, seminal vesicle protein, secretion 2
, seminal vesicle secretory protein 2
, seminal vesicle secretory protein II