FCN1

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; OMA:FCN1 - orthologs
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 27,966,390 bp[2] End 27,974,897 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte granulocyte trabecular bone bone marrow blood bone marrow cells buccal mucosa cell appendix spleen periodontal fiber Top expressed in granulocyte morula bone marrow body of femur lumbar subsegment of spinal cord cochlea vestibular membrane of cochlear duct spleen triceps brachii muscle submandibular gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function sialic acid binding protein binding G protein-coupled receptor binding metal ion binding carbohydrate binding pattern recognition receptor activity serine-type endopeptidase activity carbohydrate derivative binding Cellular component extracellular region plasma 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 response 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: 27.97 – 27.97 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. doi:10.1016/S0021-9258(19)85267-5. 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. Bibcode:2002PNAS...9916899M. 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.