FCN2

FCN2
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 2J0G, 2J0H, 2J0Y, 2J1G, 2J2P, 2J3F, 2J3G, 2J3O, 2J3U, 2J61, 4NYT, 4R9J, 4R9T
Identifiers
Aliases	FCN2, EBP-37, FCNL, P35, ficolin-2, ficolin 2
External IDs	OMIM: 601624; HomoloGene: 3031; GeneCards: FCN2; OMA:FCN2 - orthologs
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver spleen pituitary gland subcutaneous adipose tissue prostate right lobe of thyroid gland kidney anterior pituitary minor salivary glands left lobe of thyroid gland n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function antigen binding protein binding mannan binding metal ion binding calcium-dependent protein binding carbohydrate binding proteoglycan binding serine-type endopeptidase activity Cellular component extracellular region collagen blood microparticle extracellular exosome Biological process immune system process complement activation, lectin pathway complement activation recognition of apoptotic cell opsonization defense response to Gram-positive bacterium innate immune response proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2220 n/a Ensembl n/a n/a UniProt Q15485 n/a RefSeq (mRNA) NM_004108 NM_015837 NM_015838 NM_015839 n/a RefSeq (protein) NP_004099 NP_056652 n/a Location (UCSC) n/a n/a PubMed search n/a
Wikidata
View/Edit Human

Ficolin-2, which was initially identified as L-ficolin, is a protein that in humans is encoded by the FCN2 gene.

The product of this gene belongs to the ficolin family of proteins. This family is 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. This gene is predominantly expressed in the liver, and has been shown to have carbohydrate binding and opsonic activities. Alternatively spliced transcript variants encoding different isoforms have been identified.

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.
• Edgar PF (1996). "Hucolin, a new corticosteroid-binding protein from human plasma with structural similarities to ficolins, transforming growth factor-beta 1-binding proteins". FEBS Lett. 375 (1–2): 159–61. doi:10.1016/0014-5793(95)01205-S. PMID 7498469. S2CID 35484726.
• 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.
• 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.
• Kilpatrick DC, Fujita T, Matsushita M (1999). "P35, an opsonic lectin of the ficolin family, in human blood from neonates, normal adults, and recurrent miscarriage patients". Immunol. Lett. 67 (2): 109–12. doi:10.1016/S0165-2478(98)00147-3. PMID 10232391.
• Taira S, Kodama N, Matsushita M, Fujita T (2001). "Opsonic function and concentration of human serum ficolin/P35". Fukushima Journal of Medical Science. 46 (1–2): 13–23. doi:10.5387/fms.46.13. PMID 11446374.
• Cseh S, Vera L, Matsushita M, et al. (2003). "Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2". J. Immunol. 169 (10): 5735–43. doi:10.4049/jimmunol.169.10.5735. PMID 12421953.
• 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.
• Ohashi T, Erickson HP (2004). "The disulfide bonding pattern in ficolin multimers". J. Biol. Chem. 279 (8): 6534–9. doi:10.1074/jbc.M310555200. PMID 14660572.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Lynch NJ, Roscher S, Hartung T, et al. (2004). "L-ficolin specifically binds to lipoteichoic acid, a cell wall constituent of Gram-positive bacteria, and activates the lectin pathway of complement". J. Immunol. 172 (2): 1198–202. doi:10.4049/jimmunol.172.2.1198. PMID 14707097.
• Krarup A, Thiel S, Hansen A, et al. (2005). "L-ficolin is a pattern recognition molecule specific for acetyl groups". J. Biol. Chem. 279 (46): 47513–9. doi:10.1074/jbc.M407161200. PMID 15331601.
• Herpers BL, Immink MM, de Jong BA, et al. (2006). "Coding and non-coding polymorphisms in the lectin pathway activator L-ficolin gene in 188 Dutch blood bank donors". Mol. Immunol. 43 (7): 851–5. doi:10.1016/j.molimm.2005.06.035. PMID 16076493.
• Tanio M, Kondo S, Sugio S, Kohno T (2006). "Overexpression, purification and preliminary crystallographic analysis of human M-ficolin fibrinogen-like domain". Acta Crystallographica Section F. 62 (Pt 7): 652–5. doi:10.1107/S1744309106019786. PMC 2242945. PMID 16820685.
• Chen X, Katoh Y, Nakamura K, et al. (2006). "Single nucleotide polymorphisms of Ficolin 2 gene in Behçet's disease". J. Dermatol. Sci. 43 (3): 201–5. doi:10.1016/j.jdermsci.2006.05.010. PMID 16839748.
• Garlatti V, Belloy N, Martin L, et al. (2007). "Structural insights into the innate immune recognition specificities of L- and H-ficolins". EMBO J. 26 (2): 623–33. doi:10.1038/sj.emboj.7601500. PMC 1783469. PMID 17215869.
• Chapman SJ, Vannberg FO, Khor CC, et al. (2007). "Functional polymorphisms in the FCN2 gene are not associated with invasive pneumococcal disease". Mol. Immunol. 44 (12): 3267–70. doi:10.1016/j.molimm.2006.04.013. PMID 17382393.
• Munthe-Fog L, Hummelshøj T, Hansen BE, et al. (2007). "The impact of FCN2 polymorphisms and haplotypes on the Ficolin-2 serum levels". Scand. J. Immunol. 65 (4): 383–92. doi:10.1111/j.1365-3083.2007.01915.x. PMID 17386030. S2CID 33698114.