'''Ficolin-1''', and also commonly termed M-ficolin is a [[protein]] that in humans is encoded by the ''FCN1'' [[gene]].<ref name="pmid8573080">{{cite journal | vauthors = Lu J, Tay PN, Kon OL, Reid KB | title = Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9 | journal = Biochem J | volume = 313 | issue = 2| pages = 473–8 |date=Mar 1996 | pmid = 8573080 | pmc = 1216931 | doi = }}</ref><ref name="pmid8884275">{{cite journal | vauthors = Endo Y, Sato Y, Matsushita M, Fujita T | title = Cloning and characterization of the human lectin P35 gene and its related gene | journal = Genomics | volume = 36 | issue = 3 | pages = 515–21 |date=Feb 1997 | pmid = 8884275 | pmc = | doi = 10.1006/geno.1996.0497 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FCN1 ficolin (collagen/fibrinogen domain containing) 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2219| accessdate = }}</ref>
'''Ficolin-1''', and also commonly termed M-ficolin is a [[protein]] that in humans is encoded by the ''FCN1'' [[gene]].<ref name="pmid8573080">{{cite journal | vauthors = Lu J, Tay PN, Kon OL, Reid KB | title = Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9 | journal = Biochem J | volume = 313 | issue = 2| pages = 473–8 |date=Mar 1996 | pmid = 8573080 | pmc = 1216931 | doi = }}</ref><ref name="pmid8884275">{{cite journal | vauthors = Endo Y, Sato Y, Matsushita M, Fujita T | title = Cloning and characterization of the human lectin P35 gene and its related gene | journal = Genomics | volume = 36 | issue = 3 | pages = 515–21 |date=Feb 1997 | pmid = 8884275 | pmc = | doi = 10.1006/geno.1996.0497 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FCN1 ficolin (collagen/fibrinogen domain containing) 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2219| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->Proteins of the [[Ficolin|ficolin family]] consist of a leader [[peptide]], a short [[N-terminus|N-terminal segment]], followed by a [[Collagen|collagen-like]] domain, and a [[C-terminus|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 [[Tenascin|tenascins]], while the former is also found in complement protein [[Complement component 1q|C1q]] and [[Collectin|collectins]], which include [[Mannan-binding lectin|mannose-binding lectin]] and [[Pulmonary surfactant|lung surfactant proteins]]. Ficolins selectively recognize [[Acetylation|acetylated compounds]]. M-ficolin encoded by FCN1 is predominantly expressed in the [[Leukocytes|peripheral blood leukocytes]], and has been postulated to function as a [[Blood proteins|plasma protein]] with [[Elastin|elastin-binding]] activity. Several [[Single-nucleotide polymorphism|SNPs]] have been described in the ''FCN1'' gene with impact on [[Serology|serum concentrations]] of M-ficolin and the [[Ligand (biochemistry)|ligand binding]] ability
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez" /> Several SNPs have been described in the ''FCN1'' gene with impact on serum concentrations of M-ficolin and the ligand binding ability <ref>http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0050585</ref>
↑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. PMID8884275.
Ichijo H, Hellman U, Wernstedt C, et al. (1993). "Molecular cloning and characterization of ficolin, a multimeric protein with fibrinogen- and collagen-like domains". J. Biol. Chem. 268 (19): 14505–13. PMID7686157.
Matsushita M, Endo Y, Taira S, et al. (1996). "A novel human serum lectin with collagen- and fibrinogen-like domains that functions as an opsonin". J. Biol. Chem. 271 (5): 2448–54. doi:10.1074/jbc.271.5.2448. PMID8576206.
Harumiya S, Takeda K, Sugiura T, et al. (1997). "Characterization of ficolins as novel elastin-binding proteins and molecular cloning of human ficolin-1". J. Biochem. 120 (4): 745–51. doi:10.1093/oxfordjournals.jbchem.a021474. PMID8947836.
Le Y, Tan SM, Lee SH, et al. (1997). "Purification and binding properties of a human ficolin-like protein". J. Immunol. Methods. 204 (1): 43–9. doi:10.1016/S0022-1759(97)00029-X. PMID9202708.
Matsushita M, Endo Y, Fujita T (2000). "Cutting edge: complement-activating complex of ficolin and mannose-binding lectin-associated serine protease". J. Immunol. 164 (5): 2281–4. doi:10.4049/jimmunol.164.5.2281. PMID10679061.
Zeng L, Dai J, Ying K, et al. (2003). "Identification of a novel human angiopoietin-like gene expressed mainly in heart". J. Hum. Genet. 48 (3): 159–62. doi:10.1007/s100380300025. PMID12624729.
Gregory LA, Thielens NM, Matsushita M, et al. (2004). "The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin". J. Biol. Chem. 279 (28): 29391–7. doi:10.1074/jbc.M402687200. PMID15117939.
Frederiksen PD, Thiel S, Larsen CB, Jensenius JC (2006). "M-ficolin, an innate immune defence molecule, binds patterns of acetyl groups and activates complement". Scand. J. Immunol. 62 (5): 462–73. doi:10.1111/j.1365-3083.2005.01685.x. PMID16305643.
Tanio M, Kondo S, Sugio S, Kohno T (2007). "Trivalent recognition unit of innate immunity system: crystal structure of trimeric human M-ficolin fibrinogen-like domain". J. Biol. Chem. 282 (6): 3889–95. doi:10.1074/jbc.M608627200. PMID17148457.