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{{Underlinked|date=May 2016}}
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{{Infobox_gene}}
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'''Ficolin-2''', which was initially identified as L-ficolin, is a [[protein]] that in humans is encoded by the ''FCN2'' [[gene]].<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: FCN2 ficolin (collagen/fibrinogen domain containing lectin) 2 (hucolin)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2220| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_FCN2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2j0g.
| PDB = {{PDB2|2j0g}}, {{PDB2|2j0h}}, {{PDB2|2j0y}}, {{PDB2|2j1g}}, {{PDB2|2j2p}}, {{PDB2|2j3f}}, {{PDB2|2j3g}}, {{PDB2|2j3o}}, {{PDB2|2j3u}}, {{PDB2|2j61}}
| Name = Ficolin (collagen/fibrinogen domain containing lectin) 2 (hucolin)
| HGNCid = 3624
| Symbol = FCN2
| AltSymbols =; EBP-37; FCNL; P35; ficolin-2
| OMIM = 601624
| ECnumber =
| Homologene = 3031
| MGIid =
  | GeneAtlas_image1 = PBB_GE_FCN2_207804_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003823 |text = antigen binding}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{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}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2220
    | Hs_Ensembl = ENSG00000160339
    | Hs_RefseqProtein = NP_004099
    | Hs_RefseqmRNA = NM_004108
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 136912479
    | Hs_GenLoc_end = 136919187
    | Hs_Uniprot = Q15485
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Ficolin (collagen/fibrinogen domain containing lectin) 2 (hucolin)''', also known as '''FCN2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FCN2 ficolin (collagen/fibrinogen domain containing lectin) 2 (hucolin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2220| accessdate = }}</ref>


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{{PBB_Summary
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| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: FCN2 ficolin (collagen/fibrinogen domain containing lectin) 2 (hucolin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2220| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| 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  | 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  | author=Edgar PF |title=Hucolin, a new corticosteroid-binding protein from human plasma with structural similarities to ficolins, transforming growth factor-beta 1-binding proteins. |journal=FEBS Lett. |volume=375 |issue= 1-2 |pages= 159-61 |year= 1996 |pmid= 7498469 |doi=  }}
*{{cite journal  | author=Edgar PF |title=Hucolin, a new corticosteroid-binding protein from human plasma with structural similarities to ficolins, transforming growth factor-beta 1-binding proteins |journal=FEBS Lett. |volume=375 |issue= 1–2 |pages= 159–61 |year= 1996 |pmid= 7498469 |doi=10.1016/0014-5793(95)01205-S }}
*{{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  | 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  | 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  | 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  | 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  | vauthors=Kilpatrick DC, Fujita T, Matsushita M |title=P35, an opsonic lectin of the ficolin family, in human blood from neonates, normal adults, and recurrent miscarriage patients |journal=Immunol. Lett. |volume=67 |issue= 2 |pages= 109–12 |year= 1999 |pmid= 10232391 |doi=10.1016/S0165-2478(98)00147-3 }}
*{{cite journal  | author=Kilpatrick DC, Fujita T, Matsushita M |title=P35, an opsonic lectin of the ficolin family, in human blood from neonates, normal adults, and recurrent miscarriage patients. |journal=Immunol. Lett. |volume=67 |issue= 2 |pages= 109-12 |year= 1999 |pmid= 10232391 |doi=  }}
*{{cite journal  | vauthors=Taira S, Kodama N, Matsushita M, Fujita T |title=Opsonic function and concentration of human serum ficolin/P35 |journal=Fukushima journal of medical science |volume=46 |issue= 1–2 |pages= 13–23 |year= 2001 |pmid= 11446374 |doi=  10.5387/fms.46.13}}
*{{cite journal  | author=Taira S, Kodama N, Matsushita M, Fujita T |title=Opsonic function and concentration of human serum ficolin/P35. |journal=Fukushima journal of medical science |volume=46 |issue= 1-2 |pages= 13-23 |year= 2001 |pmid= 11446374 |doi=  }}
*{{cite journal  | vauthors=Cseh S, Vera L, Matsushita M |title=Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2 |journal=J. Immunol. |volume=169 |issue= 10 |pages= 5735–43 |year= 2003 |pmid= 12421953 |doi=  10.4049/jimmunol.169.10.5735|display-authors=etal}}
*{{cite journal  | author=Cseh S, Vera L, Matsushita M, ''et al.'' |title=Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2. |journal=J. Immunol. |volume=169 |issue= 10 |pages= 5735-43 |year= 2003 |pmid= 12421953 |doi=  }}
*{{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  | 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  | vauthors=Ohashi T, Erickson HP |title=The disulfide bonding pattern in ficolin multimers |journal=J. Biol. Chem. |volume=279 |issue= 8 |pages= 6534–9 |year= 2004 |pmid= 14660572 |doi= 10.1074/jbc.M310555200 }}
*{{cite journal  | author=Ohashi T, Erickson HP |title=The disulfide bonding pattern in ficolin multimers. |journal=J. Biol. Chem. |volume=279 |issue= 8 |pages= 6534-9 |year= 2004 |pmid= 14660572 |doi= 10.1074/jbc.M310555200 }}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | vauthors=Lynch NJ, Roscher S, Hartung T |title=L-ficolin specifically binds to lipoteichoic acid, a cell wall constituent of Gram-positive bacteria, and activates the lectin pathway of complement |journal=J. Immunol. |volume=172 |issue= 2 |pages= 1198–202 |year= 2004 |pmid= 14707097 |doi= 10.4049/jimmunol.172.2.1198|display-authors=etal}}
*{{cite journal  | author=Lynch NJ, Roscher S, Hartung T, ''et al.'' |title=L-ficolin specifically binds to lipoteichoic acid, a cell wall constituent of Gram-positive bacteria, and activates the lectin pathway of complement. |journal=J. Immunol. |volume=172 |issue= 2 |pages= 1198-202 |year= 2004 |pmid= 14707097 |doi= }}
*{{cite journal  | vauthors=Krarup A, Thiel S, Hansen A |title=L-ficolin is a pattern recognition molecule specific for acetyl groups |journal=J. Biol. Chem. |volume=279 |issue= 46 |pages= 47513–9 |year= 2005 |pmid= 15331601 |doi= 10.1074/jbc.M407161200 |display-authors=etal}}
*{{cite journal  | author=Krarup A, Thiel S, Hansen A, ''et al.'' |title=L-ficolin is a pattern recognition molecule specific for acetyl groups. |journal=J. Biol. Chem. |volume=279 |issue= 46 |pages= 47513-9 |year= 2005 |pmid= 15331601 |doi= 10.1074/jbc.M407161200 }}
*{{cite journal  | vauthors=Herpers BL, Immink MM, de Jong BA |title=Coding and non-coding polymorphisms in the lectin pathway activator L-ficolin gene in 188 Dutch blood bank donors |journal=Mol. Immunol. |volume=43 |issue= 7 |pages= 851–5 |year= 2006 |pmid= 16076493 |doi= 10.1016/j.molimm.2005.06.035 |display-authors=etal}}
*{{cite journal  | author=Herpers BL, Immink MM, de Jong BA, ''et al.'' |title=Coding and non-coding polymorphisms in the lectin pathway activator L-ficolin gene in 188 Dutch blood bank donors. |journal=Mol. Immunol. |volume=43 |issue= 7 |pages= 851-5 |year= 2006 |pmid= 16076493 |doi= 10.1016/j.molimm.2005.06.035 }}
*{{cite journal  | vauthors=Tanio M, Kondo S, Sugio S, Kohno T |title=Overexpression, purification and preliminary crystallographic analysis of human M-ficolin fibrinogen-like domain |journal=Acta Crystallographica Section F |volume=62 |issue= Pt 7 |pages= 652–5 |year= 2006 |pmid= 16820685 |doi= 10.1107/S1744309106019786  | pmc=2242945 }}
*{{cite journal  | author=Tanio M, Kondo S, Sugio S, Kohno T |title=Overexpression, purification and preliminary crystallographic analysis of human M-ficolin fibrinogen-like domain. |journal=Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |volume=62 |issue= Pt 7 |pages= 652-5 |year= 2006 |pmid= 16820685 |doi= 10.1107/S1744309106019786 }}
*{{cite journal  | vauthors=Chen X, Katoh Y, Nakamura K |title=Single nucleotide polymorphisms of Ficolin 2 gene in Behçet's disease |journal=J. Dermatol. Sci. |volume=43 |issue= 3 |pages= 201–5 |year= 2006 |pmid= 16839748 |doi= 10.1016/j.jdermsci.2006.05.010 |display-authors=etal}}
*{{cite journal  | author=Chen X, Katoh Y, Nakamura K, ''et al.'' |title=Single nucleotide polymorphisms of Ficolin 2 gene in Behçet's disease. |journal=J. Dermatol. Sci. |volume=43 |issue= 3 |pages= 201-5 |year= 2006 |pmid= 16839748 |doi= 10.1016/j.jdermsci.2006.05.010 }}
*{{cite journal  | vauthors=Garlatti V, Belloy N, Martin L |title=Structural insights into the innate immune recognition specificities of L- and H-ficolins |journal=EMBO J. |volume=26 |issue= 2 |pages= 623–33 |year= 2007 |pmid= 17215869 |doi= 10.1038/sj.emboj.7601500  | pmc=1783469 |display-authors=etal}}
*{{cite journal  | author=Garlatti V, Belloy N, Martin L, ''et al.'' |title=Structural insights into the innate immune recognition specificities of L- and H-ficolins. |journal=EMBO J. |volume=26 |issue= 2 |pages= 623-33 |year= 2007 |pmid= 17215869 |doi= 10.1038/sj.emboj.7601500 }}
*{{cite journal  | vauthors=Chapman SJ, Vannberg FO, Khor CC |title=Functional polymorphisms in the FCN2 gene are not associated with invasive pneumococcal disease |journal=Mol. Immunol. |volume=44 |issue= 12 |pages= 3267–70 |year= 2007 |pmid= 17382393 |doi= 10.1016/j.molimm.2006.04.013 |display-authors=etal}}
*{{cite journal  | author=Chapman SJ, Vannberg FO, Khor CC, ''et al.'' |title=Functional polymorphisms in the FCN2 gene are not associated with invasive pneumococcal disease. |journal=Mol. Immunol. |volume=44 |issue= 12 |pages= 3267-70 |year= 2007 |pmid= 17382393 |doi= 10.1016/j.molimm.2006.04.013 }}
*{{cite journal  | vauthors=Munthe-Fog L, Hummelshøj T, Hansen BE |title=The impact of FCN2 polymorphisms and haplotypes on the Ficolin-2 serum levels |journal=Scand. J. Immunol. |volume=65 |issue= 4 |pages= 383–92 |year= 2007 |pmid= 17386030 |doi= 10.1111/j.1365-3083.2007.01915.x |display-authors=etal}}
*{{cite journal  | author=Munthe-Fog L, Hummelshøj T, Hansen BE, ''et al.'' |title=The impact of FCN2 polymorphisms and haplotypes on the Ficolin-2 serum levels. |journal=Scand. J. Immunol. |volume=65 |issue= 4 |pages= 383-92 |year= 2007 |pmid= 17386030 |doi= 10.1111/j.1365-3083.2007.01915.x }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=2220}}
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[[Category:Ficolins]]


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Latest revision as of 07:36, 10 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/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.[1][2]

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.[2]

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: FCN2 ficolin (collagen/fibrinogen domain containing lectin) 2 (hucolin)".

Further reading


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