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'''Ficolin-1''', and also commonly termed M-ficolin is a [[protein]] that in humans is encoded by the ''FCN1'' [[gene]].<ref name="pmid8573080">{{cite journal | vauthors = Lu J, Tay PN, Kon OL, Reid KB | title = Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9 | journal = Biochem J | volume = 313 | issue = 2| pages = 473–8 |date=Mar 1996 | pmid = 8573080 | pmc = 1216931 | doi = }}</ref><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: FCN1 ficolin (collagen/fibrinogen domain containing) 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2219| accessdate = }}</ref> | '''Ficolin-1''', and also commonly termed M-ficolin is a [[protein]] that in humans is encoded by the ''FCN1'' [[gene]].<ref name="pmid8573080">{{cite journal | vauthors = Lu J, Tay PN, Kon OL, Reid KB | title = Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9 | journal = Biochem J | volume = 313 | issue = 2| pages = 473–8 |date=Mar 1996 | pmid = 8573080 | pmc = 1216931 | doi = }}</ref><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: FCN1 ficolin (collagen/fibrinogen domain containing) 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2219| accessdate = }}</ref> | ||
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->Proteins of the [[Ficolin|ficolin family]] consist of a leader [[peptide]], a short [[N-terminus|N-terminal segment]], followed by a [[Collagen|collagen-like]] domain, and a [[C-terminus|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 [[Tenascin|tenascins]], while the former is also found in complement protein [[Complement component 1q|C1q]] and [[Collectin|collectins]], which include [[Mannan-binding lectin|mannose-binding lectin]] and [[Pulmonary surfactant|lung surfactant proteins]]. Ficolins selectively recognize [[Acetylation|acetylated compounds]]. M-ficolin encoded by FCN1 is predominantly expressed in the [[Leukocytes|peripheral blood leukocytes]], and has been postulated to function as a [[Blood proteins|plasma protein]] with [[Elastin|elastin-binding]] activity. Several [[Single-nucleotide polymorphism|SNPs]] have been described in the ''FCN1'' gene with impact on [[Serology|serum concentrations]] of M-ficolin and the [[Ligand (biochemistry)|ligand binding]] ability | <!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->Proteins of the [[Ficolin|ficolin family]] consist of a leader [[peptide]], a short [[N-terminus|N-terminal segment]], followed by a [[Collagen|collagen-like]] domain, and a [[C-terminus|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 [[Tenascin|tenascins]], while the former is also found in complement protein [[Complement component 1q|C1q]] and [[Collectin|collectins]], which include [[Mannan-binding lectin|mannose-binding lectin]] and [[Pulmonary surfactant|lung surfactant proteins]]. Ficolins selectively recognize [[Acetylation|acetylated compounds]]. M-ficolin encoded by FCN1 is predominantly expressed in the [[Leukocytes|peripheral blood leukocytes]], and has been postulated to function as a [[Blood proteins|plasma protein]] with [[Elastin|elastin-binding]] activity. Several [[Single-nucleotide polymorphism|SNPs]] have been described in the ''FCN1'' gene with impact on [[Serology|serum concentrations]] of M-ficolin and the [[Ligand (biochemistry)|ligand binding]] ability. M-ficolin levels reflect disease activity and predict remission in early rheumatoid arthritis. | ||
==References== | ==References== | ||
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*{{cite journal | vauthors=Frederiksen PD, Thiel S, Larsen CB, Jensenius JC |title=M-ficolin, an innate immune defence molecule, binds patterns of acetyl groups and activates complement |journal=Scand. J. Immunol. |volume=62 |issue= 5 |pages= 462–73 |year= 2006 |pmid= 16305643 |doi= 10.1111/j.1365-3083.2005.01685.x }} | *{{cite journal | vauthors=Frederiksen PD, Thiel S, Larsen CB, Jensenius JC |title=M-ficolin, an innate immune defence molecule, binds patterns of acetyl groups and activates complement |journal=Scand. J. Immunol. |volume=62 |issue= 5 |pages= 462–73 |year= 2006 |pmid= 16305643 |doi= 10.1111/j.1365-3083.2005.01685.x }} | ||
*{{cite journal | vauthors=Tanio M, Kondo S, Sugio S, Kohno T |title=Trivalent recognition unit of innate immunity system: crystal structure of trimeric human M-ficolin fibrinogen-like domain |journal=J. Biol. Chem. |volume=282 |issue= 6 |pages= 3889–95 |year= 2007 |pmid= 17148457 |doi= 10.1074/jbc.M608627200 }} | *{{cite journal | vauthors=Tanio M, Kondo S, Sugio S, Kohno T |title=Trivalent recognition unit of innate immunity system: crystal structure of trimeric human M-ficolin fibrinogen-like domain |journal=J. Biol. Chem. |volume=282 |issue= 6 |pages= 3889–95 |year= 2007 |pmid= 17148457 |doi= 10.1074/jbc.M608627200 }} | ||
}} | 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.}} | |||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=2219}} | {{PDB Gallery|geneid=2219}} | ||
Latest revision as of 12:15, 14 January 2019
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Ficolin-1, and also commonly termed M-ficolin is a protein that in humans is encoded by the FCN1 gene.[1][2][3]
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
- ↑ 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. PMC 1216931. PMID 8573080.
- ↑ 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.
- ↑ "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.
- 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.
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