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'''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
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| 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>
}}


==References==
==References==

Revision as of 17:21, 18 April 2018

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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. Several SNPs have been described in the FCN1 gene with impact on serum concentrations of M-ficolin and the ligand binding ability

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. "Entrez Gene: FCN1 ficolin (collagen/fibrinogen domain containing) 1".

Further reading