FGL1 (original) (raw)

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Protein-coding gene in the species Homo sapiens

FGL1
Identifiers
Aliases	FGL1, HFREP1, HP-041, LFIRE-1, LFIRE1, fibrinogen like 1, HPS
External IDs	OMIM: 605776; MGI: 102795; HomoloGene: 37927; GeneCards: FGL1; OMA:FGL1 - orthologs
Gene location (Human)Chr.Chromosome 8 (human)[1]Band8p22Start17,864,380 bp[1]End17,910,365 bp[1]
Gene location (Mouse)Chr.Chromosome 8 (mouse)[2]Band8|8 A4Start41,644,471 bp[2]End41,668,193 bp[2]
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed inright lobe of liverbody of pancreasspermislet of Langerhansbuccal mucosa celltesticlepancreatic epithelial cellendometriumplacentaleft testisTop expressed inleft lobe of liversexually immature organismmotor neuronprimary oocyteright kidneyproximal tubulesecondary oocyteprimitive streakPaneth cellsupraoptic nucleusMore reference expression dataBioGPSMore reference expression data
OrthologsSpeciesHuman MouseEntrez2267234199EnsemblENSG00000104760ENSMUSG00000031594UniProtQ08830Q71KU9RefSeq (mRNA)NM_201553NM_004467NM_147203NM_201552NM_145594RefSeq (protein)NP_004458NP_671736NP_963846NP_963847NP_663569Location (UCSC)Chr 8: 17.86 – 17.91 MbChr 8: 41.64 – 41.67 MbPubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Fibrinogen-like protein 1 (FGL-1) is a protein that is structurally related to fibrinogen. In humans, FGL-1 is encoded by the FGL1 gene.[5][6] It is classified as a hepatokine. Four splice variants exist for this gene.

Fibrinogen-like protein 1 is a member of the fibrinogen family of proteins, which also includes fibrinogen, fibrinogen-like protein 2, and clotting factors V, VIII, and XIII. FGL-1 is homologous to the carboxy terminus of the fibrinogen beta- and gamma- subunits which contains the four conserved cysteines of that are common to all members of the fibrinogen family. However, FGL-1 lacks the platelet-binding site, cross-linking region, and thrombin-sensitive site which allow the other members of the fibrinogen family to aid in fibrin clot formation.[6]

FGL-1 has also been observed to strongly bind to and activate LAG-3, a regulatory protein expressed on T cells. As LAG-3 has an important role in controlling activated T cells, manipulating FGL-1 binding to T cells has been proposed for both cancer immunotherapy and anti-inflammatory treatments.[7]

Clinical significance

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FGL-1 may play a role in the development of hepatocellular carcinomas.[6]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000104760 – Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031594 – 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. ^ Yamamoto T, Gotoh M, Sasaki H, Terada M, Kitajima M, Hirohashi S (Jul 1993). "Molecular cloning and initial characterization of a novel fibrinogen-related gene, HFREP-1". Biochem Biophys Res Commun. 193 (2): 681–7. doi:10.1006/bbrc.1993.1678. PMID 8390249.
6. ^ a b c "Entrez Gene: FGL1 fibrinogen-like 1".
7. ^ Wang J, Sanmamed MF, Datar I, Su TT, Ji L, Sun J, et al. (January 2019). "Fibrinogen-like Protein 1 Is a Major Immune Inhibitory Ligand of LAG-3". Cell. 176 (1–2): 334–347.e12. doi:10.1016/j.cell.2018.11.010. PMC 6365968. PMID 30580966.

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Hara H, Yoshimura H, Uchida S, et al. (2001). "Molecular cloning and functional expression analysis of a cDNA for human hepassocin, a liver-specific protein with hepatocyte mitogenic activity". Biochim. Biophys. Acta. 1520 (1): 45–53. doi:10.1016/s0167-4781(01)00249-4. PMID 11470158.
• 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.
• Yan J, Yu Y, Wang N, et al. (2004). "LFIRE-1/HFREP-1, a liver-specific gene, is frequently downregulated and has growth suppressor activity in hepatocellular carcinoma". Oncogene. 23 (10): 1939–49. doi:10.1038/sj.onc.1207306. PMID 14981537. S2CID 9243597.
• 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.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Rijken DC, Dirkx SP, Luider TM, Leebeek FW (2006). "Hepatocyte-derived fibrinogen-related protein-1 is associated with the fibrin matrix of a plasma clot". Biochem. Biophys. Res. Commun. 350 (1): 191–4. doi:10.1016/j.bbrc.2006.09.018. PMID 16996032.
• Liu Z, Ukomadu C (2008). "Fibrinogen-like protein 1, a hepatocyte derived protein is an acute phase reactant". Biochem. Biophys. Res. Commun. 365 (4): 729–34. doi:10.1016/j.bbrc.2007.11.069. PMC 2288651. PMID 18039467.