Search by BoMiProt ID - Bomi133

Primary Information

BoMiProt ID Bomi133
Protein Name Complement factor B
Organism Bos taurus
Uniprot IdP81187
Milk FractionWhey
Ref Sequence Id NP_001035616.1
Amino Acid Lenth 761
Molecular Weight 85366
Fasta Sequence
Gene Name CFB
Gene Id 514076
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Protein Function key glycoprotein in the alternative pathway of complement activation; role in assembly of the C3 convertase complex by association with a C3b molecule; unusual type of serine proteinase
Biochemical Properties Bb fragment contains 11 cysteine residues; three commonly conserved disulphide bonds are present and are represented by disulphide bridges linking Cys-252 to Cys-286, Cys-396 to Cys-423 and Cys-436 to Cys-466; homology with thrombin; sequence containing the catalytic residues is considerably longer than that of other serine proteinases;
Significance in milk immune protection against environmental pathogens
PTMs Glycosylated; glucose is covalently attached; sialylated complex biantennary sugars
Significance of PTMs N-linked oligosaccharide may be involved in the regulation of FB binding to C3b
Bibliography 1. Christie, D. L., & Gagnon, J. (1983). Amino acid sequence of the Bb fragment from complement factor B. Sequence of the major cyanogen bromide-cleavage peptide (CB-II) and completion of the sequence of the Bb fragment. Biochemical Journal, 209(1), 61–70.
2. Niemann, M. A., Bhown, A. S., & Miller, E. J. (1991). The principal site of glycation of human complement Factor B. Biochemical Journal, 274(2), 473–480.
3. Rainard, P. (2002). Complement factor B and the alternative pathway of complement activation in bovine milk. The Journal of Dairy Research, 69(1), 1–12.
4. Davrinche, C., Abbal, M., & Clerc, A. (1990). Molecular characterization of human complement factor B subtypes. Immunogenetics, 32(5), 309–312.