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{{Underlinked|date=May 2016}}
{{Infobox_gene}}
{{Infobox_gene}}
'''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. M-ficolin levels reflect disease activity and predict remission in early rheumatoid arthritis.
{{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>
}}


==References==
==References==
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*{{cite journal  | vauthors=Frederiksen PD, Thiel S, Larsen CB, Jensenius JC |title=M-ficolin, an innate immune defence molecule, binds patterns of acetyl groups and activates complement |journal=Scand. J. Immunol. |volume=62 |issue= 5 |pages= 462–73 |year= 2006 |pmid= 16305643 |doi= 10.1111/j.1365-3083.2005.01685.x }}
*{{cite journal  | vauthors=Frederiksen PD, Thiel S, Larsen CB, Jensenius JC |title=M-ficolin, an innate immune defence molecule, binds patterns of acetyl groups and activates complement |journal=Scand. J. Immunol. |volume=62 |issue= 5 |pages= 462–73 |year= 2006 |pmid= 16305643 |doi= 10.1111/j.1365-3083.2005.01685.x }}
*{{cite journal  | vauthors=Tanio M, Kondo S, Sugio S, Kohno T |title=Trivalent recognition unit of innate immunity system: crystal structure of trimeric human M-ficolin fibrinogen-like domain |journal=J. Biol. Chem. |volume=282 |issue= 6 |pages= 3889–95 |year= 2007 |pmid= 17148457 |doi= 10.1074/jbc.M608627200 }}
*{{cite journal  | vauthors=Tanio M, Kondo S, Sugio S, Kohno T |title=Trivalent recognition unit of innate immunity system: crystal structure of trimeric human M-ficolin fibrinogen-like domain |journal=J. Biol. Chem. |volume=282 |issue= 6 |pages= 3889–95 |year= 2007 |pmid= 17148457 |doi= 10.1074/jbc.M608627200 }}
}}
Arthritis Rheum. 2013 Dec;65(12):3045-50. doi: 10.1002/art.38179.
M-ficolin levels reflect disease activity and predict remission in early rheumatoid arthritis.
Ammitzbøll CG1, Thiel S, Jensenius JC, Ellingsen T, Hørslev-Petersen K, Hetland ML, Junker P, Krogh NS, Østergaard M, Stengaard-Pedersen K.}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=2219}}
{{PDB Gallery|geneid=2219}}

Latest revision as of 12:15, 14 January 2019

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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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Wikidata
View/Edit Human

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. M-ficolin levels reflect disease activity and predict remission in early rheumatoid arthritis.

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

Arthritis Rheum. 2013 Dec;65(12):3045-50. doi: 10.1002/art.38179. M-ficolin levels reflect disease activity and predict remission in early rheumatoid arthritis. Ammitzbøll CG1, Thiel S, Jensenius JC, Ellingsen T, Hørslev-Petersen K, Hetland ML, Junker P, Krogh NS, Østergaard M, Stengaard-Pedersen K.


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