Search by BoMiProt ID - Bomi148


Primary Information

BoMiProt ID Bomi148
Protein Name Vitamin D-binding protein
Organism Bos taurus
Uniprot IdQ3MHN5
Milk FractionWhey
Ref Sequence Id NP_001030457.1
Amino Acid Lenth 474
Molecular Weight 53342
Fasta Sequence https://www.uniprot.org/uniprot/Q3MHN5.fasta
Gene Name GC
Gene Id 530076
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondry Information

Presence in other biological fluids/tissue/cells Serum,
Protein Function Role in the transport of vitamin D metabolites; maintains total levels of vitamin D and regulates the amounts of free (unbound) vitamin D available for specific tissues and cell types to utilize; binds actin and fatty acids preventing their polymerization; immune functions such as in B-cells, DBP seems to participate in the linkage of surface immunoglobulins
Biochemical Properties Associated and copurified with actin; existence of three major polymorphic forms -GC1F, GC1S and GC2; most DBP circulates without any vitamin D ligands attached; DBP binds actin with an affinity of 1 109 M^(–1) and fatty acids with reported affinity of 6–7 105 M(^–1)
Significance in milk Colostrum could be a rich source of vitamin D associated with DBP and could play an important role in the intake of vitamin D sterols in the newborn.
PTMs Glycosylated; GC1 forms have glycosylations at positions 418 and 420, whereas GC2 has glycosylation only at 418; trisaccharides as most frequent in GC1 with lesser amounts of disaccharides as found in humans
Bibliography 1. Ena, J., Pérez, M. D., Aranda, P., Sánchez, L., and Calvo, M. (1992) Presence and changes in the concentration of vitamin D-binding protein throughout early lactation in human and bovine colostrum and milk. J. Nutr. Biochem. 3, 498–502.
2. HIRSCHFELD, J. (1959) Immune-electrophoretic demonstration of qualitative differences in human sera and their relation to the haptoglobins. Acta Pathol. Microbiol. Scand. 47, 160–168.
3. Svasti, J., Kurosky, A., Bennett, A., and Bowman, B. H. (1979) Molecular basis for the three major forms of human serum vitamin D binding protein (group-specific component). Biochemistry 18, 1611–1617.
4. Cooke, N. E. and David, E. V. (1985) Serum vitamin D-binding protein is a third member of the albumin and alpha fetoprotein gene family. J. Clin. Invest. 76, 2420–2424.
5. Svasti, J. and Bowman, B. H. (1978) Human group-specific component. Changes in electrophoretic mobility resulting from vitamin D binding and from neuraminidase digestion. J. Biol. Chem. 253, 4188–4194.
6. Ravnsborg, T., Olsen, D. T., Thysen, A. H., Christiansen, M., Houen, G., and Højrup, P. (2010) The glycosylation and characterization of the candidate Gc macrophage activating factor. Biochim. Biophys. Acta 1804, 909–917.
7. Mc Leod, J. F., Kowalski, M. A., and Haddad, J. G. (1989) Interactions among serum vitamin D binding protein, monomeric actin, profilin, and profilactin. J. Biol. Chem. 264, 1260–1267.
8. Calvo, M. and Ena, J. M. (1989) Relations between vitamin D and fatty acid binding properties of vitamin D-binding protein. Biochem. Biophys. Res. Commun. 163, 14–17.