FCN2

Protein-coding gene in the species Homo sapiens
FCN2
Available structures
PDBHuman UniProt search: PDBe RCSB
List of PDB id codes

2J0G, 2J0H, 2J0Y, 2J1G, 2J2P, 2J3F, 2J3G, 2J3O, 2J3U, 2J61, 4NYT, 4R9J, 4R9T

Identifiers
AliasesFCN2, EBP-37, FCNL, P35, ficolin-2, ficolin 2
External IDsOMIM: 601624; HomoloGene: 3031; GeneCards: FCN2; OMA:FCN2 - orthologs
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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/an/a
PubMed search[1]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.[2][3]

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.[3]

References

  1. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  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. ^ a b "Entrez Gene: FCN2 ficolin (collagen/fibrinogen domain containing lectin) 2 (hucolin)".

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.
  • v
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  • 2j0g: L-FICOLIN COMPLEXED TO N-ACETYL-MANNOSAMINE
    2j0g: L-FICOLIN COMPLEXED TO N-ACETYL-MANNOSAMINE
  • 2j0h: L-FICOLIN COMPLEXED TO ACETYL-CHOLINE
    2j0h: L-FICOLIN COMPLEXED TO ACETYL-CHOLINE
  • 2j0y: L-FICOLIN COMPLEXED TO B-1,3-D-GLUCAN
    2j0y: L-FICOLIN COMPLEXED TO B-1,3-D-GLUCAN
  • 2j1g: L-FICOLIN COMPLEXED TO N-ACETYL-CYSTEIN
    2j1g: L-FICOLIN COMPLEXED TO N-ACETYL-CYSTEIN
  • 2j2p: L-FICOLIN COMPLEXED TO N-ACETYL-CYSTEIN (150MM)
    2j2p: L-FICOLIN COMPLEXED TO N-ACETYL-CYSTEIN (150MM)
  • 2j3f: L-FICOLIN COMPLEXED TO N-ACETYL-D-GALACTOSAMINE
    2j3f: L-FICOLIN COMPLEXED TO N-ACETYL-D-GALACTOSAMINE
  • 2j3g: L-FICOLIN
    2j3g: L-FICOLIN
  • 2j3o: L-FICOLIN COMPLEXED TO N-ACETYL-D-GLUCOSAMIN
    2j3o: L-FICOLIN COMPLEXED TO N-ACETYL-D-GLUCOSAMIN
  • 2j3u: L-FICOLIN COMPLEXED TO GALACTOSE
    2j3u: L-FICOLIN COMPLEXED TO GALACTOSE
  • 2j61: L-FICOLIN COMPLEXED TO N-ACETYLGLUCOSAMINE (FORME C)
    2j61: L-FICOLIN COMPLEXED TO N-ACETYLGLUCOSAMINE (FORME C)