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Gene Review

FCN1  -  ficolin (collagen/fibrinogen domain...

Homo sapiens

Synonyms: Collagen/fibrinogen domain-containing protein 1, FCNM, Ficolin-1, Ficolin-A, Ficolin-alpha, ...
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Disease relevance of FCN1


High impact information on FCN1

  • Both FCN1 and FCN2 contained polymorphisms in the promoters and structural parts of the genes, but only polymorphisms in FCN2 resulted in amino acid exchanges [3].
  • For comparison, FCN1 and FCN3 were also investigated [3].
  • The ficolin 1, 2 and 3 (derived from the FCN1, 2 and 3 genes, respectively) are homologous soluble pattern recognition molecules of importance for innate immunity, comprising collagen-like and fibrinogen-like domains, binding to sugar groups on different types of microorganisms [3].
  • Trivalent Recognition Unit of Innate Immunity System: CRYSTAL STRUCTURE OF TRIMERIC HUMAN M-FICOLIN FIBRINOGEN-LIKE DOMAIN [4].
  • M-ficolin-MASP complexes activated complement on N-acetylglucosamine (GlcNAc)-coated microplates in a C4 deposition assay [1].

Biological context of FCN1


Anatomical context of FCN1


Associations of FCN1 with chemical compounds

  • M-ficolin bound to several neoglycoproteins bearing GlcNAc, N-acetylgalactosamine, and sialyl-N-acetyllactosamine, suggesting that M-ficolin can recognize the common carbohydrate residues found in microbes [1].
  • In the present study, the FBG domain of M-ficolin was expressed and shown to bind to N-acetyl-D-glucosamine [2].
  • Strain FCR-7/Kenya, isolated from a clinically chloroquine-resistant case, was more resistant to the drug in vitro than the two other strains (FCR-8/West Africa and FCN-1/Nigeria, both isolated from chloroquine-sensitive cases) [6].

Other interactions of FCN1

  • Upon binding to M-ficolin ligands, the associated MASP-2 zymogen is activated and cleaves C4, thus triggering the complement system [5].


  1. Human M-ficolin is a secretory protein that activates the lectin complement pathway. Liu, Y., Endo, Y., Iwaki, D., Nakata, M., Matsushita, M., Wada, I., Inoue, K., Munakata, M., Fujita, T. J. Immunol. (2005) [Pubmed]
  2. M-ficolin is expressed on monocytes and is a lectin binding to N-acetyl-D-glucosamine and mediates monocyte adhesion and phagocytosis of Escherichia coli. Teh, C., Le, Y., Lee, S.H., Lu, J. Immunology (2000) [Pubmed]
  3. Polymorphisms in the FCN2 gene determine serum variation and function of Ficolin-2. Hummelshoj, T., Munthe-Fog, L., Madsen, H.O., Fujita, T., Matsushita, M., Garred, P. Hum. Mol. Genet. (2005) [Pubmed]
  4. Trivalent Recognition Unit of Innate Immunity System: CRYSTAL STRUCTURE OF TRIMERIC HUMAN M-FICOLIN FIBRINOGEN-LIKE DOMAIN. Tanio, M., Kondo, S., Sugio, S., Kohno, T. J. Biol. Chem. (2007) [Pubmed]
  5. M-ficolin, an innate immune defence molecule, binds patterns of acetyl groups and activates complement. Frederiksen, P.D., Thiel, S., Larsen, C.B., Jensenius, J.C. Scand. J. Immunol. (2005) [Pubmed]
  6. Plasmodium falciparum in vitro: determination of chloroquine sensitivity of three new strains by a modified 48-hour test. Nguyen-Dinh, P., Trager, W. Am. J. Trop. Med. Hyg. (1980) [Pubmed]
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