FGL1

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] Band 8p22 Start 17,864,380 bp [1] End 17,910,365 bp [1]
Gene location (Mouse) Chr. Chromosome 8 (mouse) [2] Band 8|8 A4 Start 41,644,471 bp [2] End 41,668,193 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver body of pancreas sperm islet of Langerhans buccal mucosa cell testicle pancreatic epithelial cell endometrium placenta left testis Top expressed in left lobe of liver sexually immature organism motor neuron primary oocyte right kidney proximal tubule secondary oocyte primitive streak Paneth cell supraoptic nucleus More reference expression data BioGPS More reference expression data
Orthologs Species Human Mouse Entrez 2267 234199 Ensembl ENSG00000104760 ENSMUSG00000031594 UniProt Q08830 Q71KU9 RefSeq (mRNA) NM_201553 NM_004467 NM_147203 NM_201552 NM_145594 RefSeq (protein) NP_004458 NP_671736 NP_963846 NP_963847 NP_663569 Location (UCSC) Chr 8: 17.86 – 17.91 Mb Chr 8: 41.64 – 41.67 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/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.

Function

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

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

References

1. GRCh38: Ensembl release 89: ENSG00000104760 – Ensembl, May 2017
2. 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. "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.

Further reading

• 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.