FCN1

Ficolin-1, and also commonly termed M-ficolin is a protein that in humans is encoded by the FCN1 gene.[5][6][7]

FCN1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2D39, 2JHH, 2JHI, 2JHK, 2JHL, 2JHM, 2WNP
Identifiers
Aliases	FCN1, FCNM, ficolin 1
External IDs	OMIM: 601252 MGI: 1341158 HomoloGene: 1518 GeneCards: FCN1
Gene location (Human) Chr. Chromosome 9 (human)[1] Band 9q34.3 Start 134,903,232 bp[1] End 134,917,912 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 A3 Start 28,076,378 bp[2] End 28,084,885 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • sialic acid binding • GO:0001948 protein binding • G-protein coupled receptor binding • metal ion binding • carbohydrate binding • GO:0008329 pattern recognition receptor activity • serine-type endopeptidase activity • carbohydrate derivative binding Cellular component • extracellular region • cell membrane • collagen • extrinsic component of external side of plasma membrane • membrane • secretory granule lumen • ficolin-1-rich granule lumen • collagen-containing extracellular matrix Biological process • complement activation, lectin pathway • complement activation • G-protein coupled receptor signaling pathway • recognition of apoptotic cell • protein localization to cell surface • cell surface pattern recognition receptor signaling pathway • immune system process • proteolysis • innate immune system • neutrophil degranulation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2219	14134
Ensembl	ENSG00000085265	ENSMUSG00000026835
UniProt	O00602	O70497
RefSeq (mRNA)	NM_002003	NM_010190
RefSeq (protein)	NP_001994	NP_034320
Location (UCSC)	Chr 9: 134.9 – 134.92 Mb	Chr 2: 28.08 – 28.08 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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. GRCh38: Ensembl release 89: ENSG00000085265 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026835 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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. doi:10.1042/bj3130473. PMC 1216931. PMID 8573080.
6. 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.
7. "Entrez Gene: FCN1 ficolin (collagen/fibrinogen domain containing) 1".

Further reading

• Lu J, Le Y (1999). "Ficolins and the fibrinogen-like domain". Immunobiology. 199 (2): 190–9. doi:10.1016/s0171-2985(98)80026-0. PMID 9777405.
• 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. PMID 7686157.
• 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. PMID 8576206.
• 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. PMID 8947836.
• 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. PMID 9202708.
• 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. PMID 10679061.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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. PMID 12624729.
• 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. PMID 15117939.
• Zhang Z, Henzel WJ (2005). "Signal peptide prediction based on analysis of experimentally verified cleavage sites". Protein Sci. 13 (10): 2819–24. doi:10.1110/ps.04682504. PMC 2286551. PMID 15340161.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• 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. PMID 16305643. S2CID 35639359.
• 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. PMID 17148457.

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.