Search by BoMiProt ID - Bomi25


Primary Information

BoMiProt ID Bomi25
Protein Name Complement factor H
Organism Bos taurus
Uniprot IdQ28085
Milk FractionWhey
Ref Sequence Id NP_001029108.1
Amino Acid Lenth 1236
Molecular Weight 140374
Fasta Sequence https://www.uniprot.org/uniprot/Q28085.fasta
Gene Name CFH
Gene Id 280816
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Presence in other biological fluids/tissue/cells retinal pigment epithelial cells,endothelial cells, epithelial cells, platelets, mesenchymal stem cells, liver
Protein Function Serum glycoprotein; accelerates the decay of the alternative pathway C3 convertase; cofactor for factor I-mediated cleavage and inactivation of C3b; recognize specific markers on host cells and control complement on self surfaces; detects and binds to initial C3b deposits in combination with specific markers on host cells;
Biochemical Properties actual conformation of factor H may be affected by the ionic strength and pH of its local microenvironment;
Significance in milk immune protection against environmental pathogens
PTMs Glycosylation; as found in humans, eight N-glycans; forty disulfide bonds; absence of hybrid and oligomannose structures; presence of complex, diantennary disialylated, non-fucosylated glycans; Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified; Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative; absence of hybrid and oligomannose structures
Additional Comments In the absence of factor H, spontaneous activation of the alternative pathway of complement occurs in plasma, which leads to consumption of complement components C3 and factor B
Bibliography 1. Fenaille, F., Le Mignon, M., Groseil, C., Ramon, C., Riandé, S., Siret, L., & Bihoreau, N. (2007). Site-specific N-glycan characterization of human complement factor H. Glycobiology, 17(9), 932–944. https://doi.org/10.1093/glycob/cwm060.
2. Okemefuna, A. I., Li, K., Nan, R., Ormsby, R. J., Sadlon, T., Gordon, D. L., & Perkins, S. J. (2009). Multimeric Interactions between Complement Factor H and Its C3d Ligand Provide New Insight on Complement Regulation. Journal of Molecular Biology, 391(1), 119–135. https://doi.org/10.1016/j.jmb.2009.06.013.
3. Harrison, R. A., & Lachmann, P. J. (1980). The physiological breakdown of the third component of human complement. Molecular Immunology, 17(1), 9–20. https://doi.org/10.1016/0161-5890(80)90119-4.
4. Licht, C., Pluthero, F. G., Li, L., Christensen, H., Habbig, S., Hoppe, B., … Kahr, W. H. A. (2009). Platelet-associated complement factor H in healthy persons and patients with atypical HUS. Blood, 114(20), 4538–4545. https://doi.org/10.1182/blood-2009-03-205096.
5. Chen, M., Forrester, J. V, & Xu, H. (2007). Synthesis of complement factor H by retinal pigment epithelial cells is down-regulated by oxidized photoreceptor outer segments. Experimental Eye Research, 84(4), 635–645. https://doi.org/10.1016/j.exer.2006.11.015.
6. Brooimans, R. A., van der Ark, A. A., Buurman, W. A., van Es, L. A., & Daha, M. R. (1990). Differential regulation of complement factor H and C3 production in human umbilical vein endothelial cells by IFN-gamma and IL-1. Journal of Immunology (Baltimore, Md. : 1950), 144(10), 3835–3840. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/2139673.
7. Adinolfi, M., Dobson, N. C., & Bradwell, A. R. (1981). Synthesis of two components of human complement, beta 1H and C3bINA, during fetal life. Acta Paediatrica Scandinavica, 70(5), 705–710. https://doi.org/10.1111/j.1651-2227.1981.tb05772.