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{{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>
<!-- 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.
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | vauthors=Lu J, Le Y |title=Ficolins and the fibrinogen-like domain |journal=Immunobiology |volume=199 |issue= 2 |pages= 190–9 |year= 1999 |pmid= 9777405 |doi=  10.1016/s0171-2985(98)80026-0}}
*{{cite journal  | vauthors=Ichijo H, Hellman U, Wernstedt C |title=Molecular cloning and characterization of ficolin, a multimeric protein with fibrinogen- and collagen-like domains |journal=J. Biol. Chem. |volume=268 |issue= 19 |pages= 14505–13 |year= 1993 |pmid= 7686157 |doi=  |display-authors=etal}}
*{{cite journal  | vauthors=Matsushita M, Endo Y, Taira S |title=A novel human serum lectin with collagen- and fibrinogen-like domains that functions as an opsonin |journal=J. Biol. Chem. |volume=271 |issue= 5 |pages= 2448–54 |year= 1996 |pmid= 8576206 |doi=10.1074/jbc.271.5.2448  |display-authors=etal}}
*{{cite journal  | vauthors=Harumiya S, Takeda K, Sugiura T |title=Characterization of ficolins as novel elastin-binding proteins and molecular cloning of human ficolin-1 |journal=J. Biochem. |volume=120 |issue= 4 |pages= 745–51 |year= 1997 |pmid= 8947836 |doi=  10.1093/oxfordjournals.jbchem.a021474|display-authors=etal}}
*{{cite journal  | vauthors=Le Y, Tan SM, Lee SH |title=Purification and binding properties of a human ficolin-like protein |journal=J. Immunol. Methods |volume=204 |issue= 1 |pages= 43–9 |year= 1997 |pmid= 9202708 |doi=10.1016/S0022-1759(97)00029-X  |display-authors=etal}}
*{{cite journal  | vauthors=Matsushita M, Endo Y, Fujita T |title=Cutting edge: complement-activating complex of ficolin and mannose-binding lectin-associated serine protease |journal=J. Immunol. |volume=164 |issue= 5 |pages= 2281–4 |year= 2000 |pmid= 10679061 |doi=  10.4049/jimmunol.164.5.2281}}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
*{{cite journal  | vauthors=Zeng L, Dai J, Ying K |title=Identification of a novel human angiopoietin-like gene expressed mainly in heart |journal=J. Hum. Genet. |volume=48 |issue= 3 |pages= 159–62 |year= 2003 |pmid= 12624729 |doi= 10.1007/s100380300025 |display-authors=etal}}
*{{cite journal  | vauthors=Gregory LA, Thielens NM, Matsushita M |title=The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin |journal=J. Biol. Chem. |volume=279 |issue= 28 |pages= 29391–7 |year= 2004 |pmid= 15117939 |doi= 10.1074/jbc.M402687200 |display-authors=etal}}
*{{cite journal  | vauthors=Zhang Z, Henzel WJ |title=Signal peptide prediction based on analysis of experimentally verified cleavage sites |journal=Protein Sci. |volume=13 |issue= 10 |pages= 2819–24 |year= 2005 |pmid= 15340161 |doi= 10.1110/ps.04682504  | pmc=2286551 }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
*{{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 }}
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}}
{{PDB Gallery|geneid=2219}}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Category:Ficolins]]
{{GNF_Protein_box
| image = PBB_Protein_FCN1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2d39.
| PDB = {{PDB2|2d39}}
| Name = Ficolin (collagen/fibrinogen domain containing) 1
| HGNCid = 3623
| Symbol = FCN1
| AltSymbols =; FCNM
| OMIM = 601252
| ECnumber = 
| Homologene = 1518
| MGIid = 1341158
| GeneAtlas_image1 = PBB_GE_FCN1_205237_at_tn.png
| Function = {{GNF_GO|id=GO:0003823 |text = antigen binding}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008228 |text = opsonization}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2219
    | Hs_Ensembl = ENSG00000085265
    | Hs_RefseqProtein = NP_001994
    | Hs_RefseqmRNA = NM_002003
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 136940837
    | Hs_GenLoc_end = 136949630
    | Hs_Uniprot = O00602
    | Mm_EntrezGene = 14134
    | Mm_Ensembl = ENSMUSG00000026835
    | Mm_RefseqmRNA = NM_010190
    | Mm_RefseqProtein = NP_034320
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 27898389
    | Mm_GenLoc_end = 27906866
    | Mm_Uniprot = Q3U9R5
  }}
}}
'''Ficolin (collagen/fibrinogen domain containing) 1''', also known as '''FCN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FCN1 ficolin (collagen/fibrinogen domain containing) 1| url = http://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. -->
{{PBB_Summary
| section_title =
| summary_text = The ficolin family of proteins are characterized by the presence of a leader peptide, a short N-terminal segment, followed by a collagen-like region, and a C-terminal fibrinogen-like domain. The collagen-like and the fibrinogen-like domains are also found separately in other proteins such as complement protein C1q, C-type lectins known as collectins, and tenascins.  However, all these proteins recognize different targets, and are functionally distinct.  Ficolin 1 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">{{cite web | title = Entrez Gene: FCN1 ficolin (collagen/fibrinogen domain containing) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2219| accessdate = }}</ref>
}}
==References==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Lu J, Le Y |title=Ficolins and the fibrinogen-like domain. |journal=Immunobiology |volume=199 |issue= 2 |pages= 190-9 |year= 1999 |pmid= 9777405 |doi=  }}
*{{cite journal  | author=Ichijo H, Hellman U, Wernstedt C, ''et al.'' |title=Molecular cloning and characterization of ficolin, a multimeric protein with fibrinogen- and collagen-like domains. |journal=J. Biol. Chem. |volume=268 |issue= 19 |pages= 14505-13 |year= 1993 |pmid= 7686157 |doi=  }}
*{{cite journal  | author=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 ( Pt 2) |issue=  |pages= 473-8 |year= 1996 |pmid= 8573080 |doi=  }}
*{{cite journal  | author=Matsushita M, Endo Y, Taira S, ''et al.'' |title=A novel human serum lectin with collagen- and fibrinogen-like domains that functions as an opsonin. |journal=J. Biol. Chem. |volume=271 |issue= 5 |pages= 2448-54 |year= 1996 |pmid= 8576206 |doi=  }}
*{{cite journal  | author=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 |year= 1997 |pmid= 8884275 |doi= 10.1006/geno.1996.0497 }}
*{{cite journal  | author=Harumiya S, Takeda K, Sugiura T, ''et al.'' |title=Characterization of ficolins as novel elastin-binding proteins and molecular cloning of human ficolin-1. |journal=J. Biochem. |volume=120 |issue= 4 |pages= 745-51 |year= 1997 |pmid= 8947836 |doi=  }}
*{{cite journal  | author=Le Y, Tan SM, Lee SH, ''et al.'' |title=Purification and binding properties of a human ficolin-like protein. |journal=J. Immunol. Methods |volume=204 |issue= 1 |pages= 43-9 |year= 1997 |pmid= 9202708 |doi=  }}
*{{cite journal  | author=Matsushita M, Endo Y, Fujita T |title=Cutting edge: complement-activating complex of ficolin and mannose-binding lectin-associated serine protease. |journal=J. Immunol. |volume=164 |issue= 5 |pages= 2281-4 |year= 2000 |pmid= 10679061 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Zeng L, Dai J, Ying K, ''et al.'' |title=Identification of a novel human angiopoietin-like gene expressed mainly in heart. |journal=J. Hum. Genet. |volume=48 |issue= 3 |pages= 159-62 |year= 2003 |pmid= 12624729 |doi= 10.1007/s100380300025 }}
*{{cite journal  | author=Gregory LA, Thielens NM, Matsushita M, ''et al.'' |title=The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin. |journal=J. Biol. Chem. |volume=279 |issue= 28 |pages= 29391-7 |year= 2004 |pmid= 15117939 |doi= 10.1074/jbc.M402687200 }}
*{{cite journal  | author=Zhang Z, Henzel WJ |title=Signal peptide prediction based on analysis of experimentally verified cleavage sites. |journal=Protein Sci. |volume=13 |issue= 10 |pages= 2819-24 |year= 2005 |pmid= 15340161 |doi= 10.1110/ps.04682504 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=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  | author=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 }}
}}
{{refend}}


{{protein-stub}}
{{gene-9-stub}}
{{WikiDoc Sources}}

Latest revision as of 12:15, 14 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
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.