ACSL1

Acyl-CoA synthetase long-chain family member 1
Identifiers
Symbols	ACSL1; ACS1; FACL1; FACL2; LACS; LACS1; LACS2
External IDs	OMIM: 152425 MGI: 102797 HomoloGene: 37561 GeneCards: ACSL1 Gene
EC number	6.2.1.3
Gene Ontology Molecular function • nucleotide binding • long-chain fatty acid-CoA ligase activity • ATP binding • ligase activity Cellular component • mitochondrion • mitochondrial outer membrane • peroxisome • peroxisomal membrane • endoplasmic reticulum • endoplasmic reticulum membrane • microsome • membrane • integral to membrane Biological process • fatty acid metabolic process • digestion • triglyceride biosynthetic process • long-chain fatty-acyl-CoA biosynthetic process • cellular lipid metabolic process • regulation of fatty acid oxidation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2180	14081
Ensembl	ENSG00000151726	ENSMUSG00000018796
UniProt	P33121	Q6GTG6
RefSeq (mRNA)	NM_001995	NM_007981.3
RefSeq (protein)	NP_001986	NP_032007.2
Location (UCSC)	Chr 4: 185.68 – 185.75 Mb	Chr 8: 47.56 – 47.62 Mb
PubMed search	[1]	[2]

Long-chain-fatty-acid—CoA ligase 1 is an enzyme that in humans is encoded by the ACSL1 gene.

The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation.

In melanocytic cells ACSL1 gene expression may be regulated by MITF.

Further reading

• Amigo L, McElroy MC, Morales MN, Bronfman M (1992). "Subcellular distribution and characteristics of ciprofibroyl-CoA synthetase in rat liver. Its possible identity with long-chain acyl-CoA synthetase.". Biochem. J. 284 (1): 283–7. PMC 1132728. PMID 1599407. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1132728. 
• Abe T, Fujino T, Fukuyama R, et al. (1992). "Human long-chain acyl-CoA synthetase: structure and chromosomal location.". J. Biochem. 111 (1): 123–8. PMID 1607358. 
• Lageweg W, Wanders RJ, Tager JM (1991). "Long-chain-acyl-CoA synthetase and very-long-chain-acyl-CoA synthetase activities in peroxisomes and microsomes from rat liver. An enzymological study.". Eur. J. Biochem. 196 (2): 519–23. doi:10.1111/j.1432-1033.1991.tb15844.x. PMID 2007410. 
• Singh I, Bhushan A, Relan NK, Hashimoto T (1989). "Acyl-CoA ligases from rat brain microsomes: an immunochemical study.". Biochim. Biophys. Acta 963 (3): 509–14. PMID 2973813. 
• Bierbach H (1981). "Studies on long chain fatty acid:CoA ligase from human small intestine.". Gut 21 (8): 689–94. doi:10.1136/gut.21.8.689. PMC 1419104. PMID 7429333. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1419104. 
• Cantú ES, Sprinkle TJ, Ghosh B, Singh I (1996). "The human palmitoyl-CoA ligase (FACL2) gene maps to the chromosome 4q34-q35 region by fluorescence in situ hybridization (FISH) and somatic cell hybrid panels.". Genomics 28 (3): 600–2. doi:10.1006/geno.1995.1199. PMID 7490105. 
• Wu P, Bremer J (1994). "Activation of alkylthioacrylic acids in subcellular fractions of rat tissues: a new spectrophotometric method for assay of acyl-CoA synthetase.". Biochim. Biophys. Acta 1215 (1-2): 87–92. doi:10.1016/0005-2760(94)90095-7. PMID 7948012. 
• Singh I, Lazo O, Kremser K (1993). "Purification of peroxisomes and subcellular distribution of enzyme activities for activation and oxidation of very-long-chain fatty acids in rat brain.". Biochim. Biophys. Acta 1170 (1): 44–52. doi:10.1016/0005-2760(93)90174-8. PMID 8399326. 
• Ghosh B, Barbosa E, Singh I (1996). "Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression.". Mol. Cell. Biochem. 151 (1): 77–81. doi:10.1007/BF01076899. PMID 8584017. 
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548. 
• Malhotra KT, Malhotra K, Lubin BH, Kuypers FA (2000). "Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors.". Biochem. J. 344 (1): 135–43. PMC 1220623. PMID 10548543. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1220623. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Mashek DG, Bornfeldt KE, Coleman RA, et al. (2005). "Revised nomenclature for the mammalian long-chain acyl-CoA synthetase gene family.". J. Lipid Res. 45 (10): 1958–61. doi:10.1194/jlr.E400002-JLR200. PMID 15292367. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Soupene E, Kuypers FA (2006). "Multiple erythroid isoforms of human long-chain acyl-CoA synthetases are produced by switch of the fatty acid gate domains.". BMC Mol. Biol. 7: 21. doi:10.1186/1471-2199-7-21. PMC 1543647. PMID 16834775. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1543647.