The primary structure of BSP-30K, a major lipid-, gelatin-, and heparin-binding glycoprotein of bovine seminal plasma.
BSP-30K is a major acidic glycoprotein of bovine seminal plasma. It displays heparin-, gelatin-, and phospholipid-binding activities. BSP-30K binds to spermatozoa upon ejaculation and is thought to play a role in sperm capacitation. We have determined its amino acid sequence, disulfide bonds, and 0-glycosylation sites. BSP-30K consists of 158 amino acids arranged in a mosaic structure. BSP-30K has a unique 48-residue N-terminal extension which includes three 7-8- amino acid repeats and the six O-glycosylated threonine residues. The polypeptide stretch 49-71 is homologous to type 'A' domains found in heparin-binding proteins from other mammalian species. The C-terminal portion of BSP-30K is organized in a tandem of 40-44-residue domains each sharing the consensus pattern of the gelatin-binding fibronectin type II module. The mosaic structure of BSP-30K suggests that this glycoprotein might be a factor contributing to the different sperm-capacitating effects exerted by heparin in different mammalian species.
Calvete
J J
JJ
Institut für Reproduktionsmedizin, Tierärztliche Hochschule Hannover,Germany. jcalvete@repro.tiho-hannover.de
Mann
K
K
Sanz
L
L
Raida
M
M
Töpfer-Petersen
E
E
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D005353:Fibronectins / Q000737:chemistry / Q000378:metabolism; D005780:Gelatin / Q000378:metabolism*; D006031:Glycosylation; D006493:Heparin / Q000378:metabolism*; D050356:Lipid Metabolism; D008297:Male; D008969:Molecular Sequence Data; D029584:Prostatic Secretory Proteins; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D012661:Semen / Q000378:metabolism*; D029589:Seminal Plasma Proteins; D017386:Sequence Homology, Amino Acid
D005353:Fibronectins; D029584:Prostatic Secretory Proteins; D011506:Proteins; D029589:Seminal Plasma Proteins; C043076:beta-microseminoprotein; D005780:Gelatin; D006493:Heparin