FADS1

FADS1
Identifiers
Aliases	FADS1, D5D, FADS6, FADSD5, LLCDL1, TU12, fatty acid desaturase 1
External IDs	MGI: 1923517 HomoloGene: 22753 GeneCards: FADS1
Genetically Related Diseases
disease of metabolism[1]
Gene ontology Molecular function • C-5 sterol desaturase activity • oxidoreductase activity • omega-6 fatty acid desaturase activity Cellular component • integral component of membrane • endoplasmic reticulum membrane • membrane • intracellular membrane-bounded organelle • mitochondrion • endoplasmic reticulum Biological process • linoleic acid metabolic process • regulation of transcription, DNA-templated • lipid metabolic process • cellular response to starvation • cell-cell signaling • alpha-linolenic acid metabolic process • fatty acid metabolic process • icosanoid biosynthetic process • fatty acid biosynthetic process • phospholipid biosynthetic process • unsaturated fatty acid biosynthetic process • regulation of cell differentiation • oxidation-reduction process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3992	76267
Ensembl	ENSG00000149485	ENSMUSG00000010663
UniProt	O60427	Q920L1
RefSeq (mRNA)	NM_013402	NM_146094
RefSeq (protein)	NP_037534.3	NP_666206.1
Location (UCSC)	Chr 11: 61.8 – 61.83 Mb	Chr 19: 10.18 – 10.2 Mb
PubMed search	[2]	[3]
Wikidata

View/Edit Human

View/Edit Mouse

Fatty acid desaturase 1 is an enzyme that in humans is encoded by the FADS1 gene.^[4]

Function

The protein encoded by this gene is a member of the fatty acid desaturase (FADS) gene family. Desaturase enzymes regulate unsaturation of fatty acids through the introduction of double bonds between defined carbons of the fatty acyl chain. FADS family members are considered fusion products composed of an N-terminal cytochrome b5-like domain and a C-terminal multiple membrane-spanning desaturase portion, both of which are characterized by conserved histidine motifs. This gene is clustered with family members FADS1 and FADS2 at 11q12-q13.1; this cluster is thought to have arisen evolutionarily from gene duplication based on its similar exon/intron organization.^[4]

Clinical significance

Single nucleotide polymorphisms (SNPs) of FADS1 and FADS2 may affect long-chain polyunsaturated fatty acids (LC-PUFA) metabolism and have a potential role in the development of atopic diseases.^[5]

References

1. "Diseases that are genetically associated with FADS1 view/edit references on wikidata".
2. "Human PubMed Reference:".
3. "Mouse PubMed Reference:".
4. "Entrez Gene: FADS1 fatty acid desaturase 1".
5. Lattka, E.; Illig, T.; Heinrich, J.; Koletzko, B. (2009). "FADS Gene Cluster Polymorphisms: Important Modulators of Fatty Acid Levels and Their Impact on Atopic Diseases". Journal of Nutrigenetics and Nutrigenomics. 2 (3): 119–128. doi:10.1159/000235559. PMID 19776639.

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.
• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• 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.
• Stöhr H, Marquardt A, Rivera A, et al. (1998). "A Gene Map of the Best's Vitelliform Macular Dystrophy Region in Chromosome 11q12–q13.1". Genome Res. 8 (1): 48–56. doi:10.1101/gr.8.1.48. PMC 310689. PMID 9445487.
• Cho HP, Nakamura M, Clarke SD (2000). "Cloning, expression, and fatty acid regulation of the human delta-5 desaturase". J. Biol. Chem. 274 (52): 37335–9. doi:10.1074/jbc.274.52.37335. PMID 10601301.
• Leonard AE, Kelder B, Bobik EG, et al. (2000). "cDNA cloning and characterization of human Delta5-desaturase involved in the biosynthesis of arachidonic acid". Biochem. J. 347 Pt 3 (3): 719–24. doi:10.1042/0264-6021:3470719. PMC 1221008. PMID 10769175.
• Marquardt A, Stöhr H, White K, Weber BH (2000). "cDNA cloning, genomic structure, and chromosomal localization of three members of the human fatty acid desaturase family". Genomics. 66 (2): 175–83. doi:10.1006/geno.2000.6196. PMID 10860662.
• Brizio C, Galluccio M, Wait R, et al. (2006). "Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase". Biochem. Biophys. Res. Commun. 344 (3): 1008–16. doi:10.1016/j.bbrc.2006.04.003. PMID 16643857.
• Schaeffer L, Gohlke H, Müller M, et al. (2006). "Common genetic variants of the FADS1 FADS2 gene cluster and their reconstructed haplotypes are associated with the fatty acid composition in phospholipids". Hum. Mol. Genet. 15 (11): 1745–56. doi:10.1093/hmg/ddl117. PMID 16670158.
• Ma J, Dempsey AA, Stamatiou D, et al. (2007). "Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects". Atherosclerosis. 191 (1): 63–72. doi:10.1016/j.atherosclerosis.2006.05.032. PMID 16806233.
• Dreesen TD, Adamson AW, Tekle M, et al. (2006). "A newly discovered member of the fatty acid desaturase gene family: a non-coding, antisense RNA gene to delta5-desaturase". Prostaglandins Leukot. Essent. Fatty Acids. 75 (2): 97–106. doi:10.1016/j.plefa.2006.05.001. PMID 16846730.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Risé P, Ghezzi S, Carissimi R, et al. (2007). "Delta5 desaturase mRNA levels are increased by simvastatin via SREBP-1 at early stages, not via PPARalpha, in THP-1 cells". Eur. J. Pharmacol. 571 (2–3): 97–105. doi:10.1016/j.ejphar.2007.06.021. PMID 17655842.