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Gene Review

BSP1  -  binder of sperm 1

Bos taurus

Synonyms: PDC-109, PDC109, SVSP109
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High impact information on PDC-109

  • Gross differences between the two domains occur in exterior loops and potential functional sites in these regions of the type II structures as found in fibronectin, Factor XII and seminal fluid protein PDC-109 are proposed [1].
  • These results suggest that PDC-109/b may recognize specific leucine and/or isoleucine-containing sequences within collagen [2].
  • The results indicate that the interaction of SP-1/2 with (lipid) membranes is similar to that of PDC-109 which can be explained by homologous amino acid sequences of both proteins [3].
  • Like PDC-109, SP-1/2 has a specificity for phospholipids with the phosphocholine headgroup [3].
  • Furthermore, different to PDC-109, SP-1/2 was not able to extract lipids from human red blood cells [3].

Biological context of PDC-109

  • The results of distance geometry and restrained molecular dynamics calculations indicate that the global fold of the PDC-109 b domain, a type II module related to those found in fibronectin, is somewhat different from that predicted by modeling the structure on the basis of homology between type II and kringle units [4].
  • The complete 109-residue amino acid sequence of PDC-109 has been established by automated Edman degradation of the intact peptide as well as its proteolytic digestion and cyanogen bromide cleavage fragments [5].
  • The SVSP109 gene may provide an excellent example for functional properties of exons: exon 1 encodes the entire signal peptide and exon 4 the complete fibronectin type II-domain, responsible for protein-protein interactions [6].
  • In the present study the kinetics and mechanism of the interaction of PDC-109 with phospholipid membranes were investigated by the surface plasmon resonance technique [7].
  • The effect of PDC-109 on sperm motility was analyzed using the CASA-method [8].

Anatomical context of PDC-109


Associations of PDC-109 with chemical compounds


Physical interactions of PDC-109


Other interactions of PDC-109

  • In the bull, these proteins consist predominantly of the bovine seminal plasma family of proteins (BSPs): PDC-109 (BSP-A1/-A2), BSP-A3, and BSP-30-kDa [12].
  • RNAase dimer, PDC-109 and metalloproteinase inhibitor (TIMP-2) were identified [14].
  • The protein components of this fraction were identified on the basis of relative molecular mass determination and N-terminal amino acid sequencing: RNAase dimer, PDC-109 and a protein homologous to BSP-30K (relative molecular mass 14,500) [15].

Analytical, diagnostic and therapeutic context of PDC-109


  1. Deriving the generic structure of the fibronectin type II domain from the prothrombin Kringle 1 crystal structure. Holland, S.K., Harlos, K., Blake, C.C. EMBO J. (1987) [Pubmed]
  2. Refined solution structure and ligand-binding properties of PDC-109 domain b. A collagen-binding type II domain. Constantine, K.L., Madrid, M., Bányai, L., Trexler, M., Patthy, L., Llinás, M. J. Mol. Biol. (1992) [Pubmed]
  3. Interaction of fibronectin type II proteins with membranes: the stallion seminal plasma protein SP-1/2. Greube, A., Müller, K., Töpfer-Petersen, E., Herrmann, A., Müller, P. Biochemistry (2004) [Pubmed]
  4. Sequence-specific 1H NMR assignments and structural characterization of bovine seminal fluid protein PDC-109 domain b. Constantine, K.L., Ramesh, V., Bányai, L., Trexler, M., Patthy, L., Llinás, M. Biochemistry (1991) [Pubmed]
  5. Primary structure of PDC-109, a major protein constituent of bovine seminal plasma. Esch, F.S., Ling, N.C., Böhlen, P., Ying, S.Y., Guillemin, R. Biochem. Biophys. Res. Commun. (1983) [Pubmed]
  6. Characterization of the gene for the bovine seminal vesicle secretory protein SVSP109. Bräuer, C., Scheit, K.H. Biochim. Biophys. Acta (1991) [Pubmed]
  7. Mechanism of membrane binding by the bovine seminal plasma protein, PDC-109: a surface plasmon resonance study. Thomas, C.J., Anbazhagan, V., Ramakrishnan, M., Sultan, N., Surolia, I., Swamy, M.J. Biophys. J. (2003) [Pubmed]
  8. Interaction of PDC-109, the major secretory protein from bull seminal vesicles, with bovine sperm membrane Ca2+-ATPase. Sánchez-Luengo, S., Aumüller, G., Albrecht, M., Sen, P.C., Röhm, K., Wilhelm, B. J. Androl. (2004) [Pubmed]
  9. The structure of the O-linked carbohydrate chain of bovine seminal plasma protein PDC-109 revised by H-NMR spectroscopy A correction. Gerwig, G.L., Calvete, J.J., Töpfer-Petersen, E., Vliegenthart, J.F. FEBS Lett. (1996) [Pubmed]
  10. PDC-109 (BSP-A1/A2) promotes bull sperm binding to oviductal epithelium in vitro and may be involved in forming the oviductal sperm reservoir. Gwathmey, T.M., Ignotz, G.G., Suarez, S.S. Biol. Reprod. (2003) [Pubmed]
  11. Localization and structural characterization of an oligosaccharide O-linked to bovine PDC-109. Quantitation of the glycoprotein in seminal plasma and on the surface of ejaculated and capacitated spermatozoa. Calvete, J.J., Raida, M., Sanz, L., Wempe, F., Scheit, K.H., Romero, A., Töpfer-Petersen, E. FEBS Lett. (1994) [Pubmed]
  12. Bovine Seminal Plasma Proteins PDC-109, BSP-A3, and BSP-30-kDa Share Functional Roles in Storing Sperm in the Oviduct. Gwathmey, T.M., Ignotz, G.G., Mueller, J.L., Manjunath, P., Suarez, S.S. Biol. Reprod. (2006) [Pubmed]
  13. Complete amino acid sequence of BSP-A3 from bovine seminal plasma. Homology to PDC-109 and to the collagen-binding domain of fibronectin. Seidah, N.G., Manjunath, P., Rochemont, J., Sairam, M.R., Chrétien, M. Biochem. J. (1987) [Pubmed]
  14. D-fructose-binding proteins in bull seminal plasma: isolation and characterization. Liberda, J., Kraus, M., Ryslavá, H., Vlasáková, M., Jonáková, V., Tichá, M. Folia Biol. (Praha) (2001) [Pubmed]
  15. Affinity chromatography of bull seminal proteins on mannan-Sepharose. Liberda, J., Ryslavá, H., Jelínková, P., Jonáková, V., Tichá, M. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. (2002) [Pubmed]
  16. Characterisation of the conformational and quaternary structure-dependent heparin-binding region of bovine seminal plasma protein PDC-109. Calvete, J.J., Campanero-Rhodes, M.A., Raida, M., Sanz, L. FEBS Lett. (1999) [Pubmed]
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