FCN1

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Ficolin-1, and also commonly termed M-ficolin is a protein that in humans is encoded by the FCN1 gene.[1][2][3]

Proteins of the ficolin family consist of a leader peptide, a short N-terminal segment, followed by a collagen-like domain, and a C-terminal fibrinogen-like domain. The name of ficolin was derived from the latter two domains. The collagen-like and the fibrinogen-like domains are also found in other proteins such as tenascins, while the former is also found in complement protein C1q and collectins, which include mannose-binding lectin and lung surfactant proteins. Ficolins selectively recognize acetylated compounds. M-ficolin encoded by FCN1 is predominantly expressed in the peripheral blood leukocytes, and has been postulated to function as a plasma protein with elastin-binding activity.[3] Several SNPs have been described in the FCN1 gene with impact on serum concentrations of M-ficolin and the ligand binding ability [4]

References

  1. Lu J, Tay PN, Kon OL, Reid KB (Mar 1996). "Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9". Biochem J. 313 (2): 473–8. PMC 1216931. PMID 8573080.
  2. Endo Y, Sato Y, Matsushita M, Fujita T (Feb 1997). "Cloning and characterization of the human lectin P35 gene and its related gene". Genomics. 36 (3): 515–21. doi:10.1006/geno.1996.0497. PMID 8884275.
  3. 3.0 3.1 "Entrez Gene: FCN1 ficolin (collagen/fibrinogen domain containing) 1".
  4. http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0050585

Further reading