ACSL3

Acyl-CoA synthetase long-chain family member 3

Identifiers

ACSL3; ACS3; FACL3; PRO2194

External IDs

OMIM: 602371 MGI: 1921455 HomoloGene: 3278 GeneCards: ACSL3 Gene

6.2.1.3

Gene Ontology
Molecular function	• nucleotide binding • fatty-acyl-CoA synthase activity • long-chain fatty acid-CoA ligase activity • protein binding • 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 biosynthetic process • brain development • response to nutrient • response to organic cyclic compound • triglyceride biosynthetic process • long-chain fatty-acyl-CoA biosynthetic process • cellular lipid metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
223.73 – 223.81 Mb

Chr 1:
78.65 – 78.7 Mb

PubMed search

[1]

[2]

Long-chain-fatty-acid—CoA ligase 3 is an enzyme that in humans is encoded by the ACSL3 gene.^[1]

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. This isozyme is highly expressed in brain, and preferentially utilizes myristate, arachidonate, and eicosapentaenoate as substrates. The amino acid sequence of this isozyme is 92% identical to that of rat homolog. Two transcript variants encoding the same protein have been found for this gene.^[1]

References

^ ^a ^b "Entrez Gene: ACSL3 acyl-CoA synthetase long-chain family member 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2181.

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Fujino T, Kang MJ, Suzuki H et al. (1996). "Molecular characterization and expression of rat acyl-CoA synthetase 3". J. Biol. Chem. 271 (28): 16748–16752. doi:10.1074/jbc.271.28.16748. PMID 8663269.
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.
Minekura H, Fujino T, Kang MJ et al. (1997). "Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene (ACS3) to chromosome band 2q34-q35". Genomics 42 (1): 180–181. doi:10.1006/geno.1997.4710. PMID 9177793.
Minekura H, Kang MJ, Inagaki Y et al. (2002). "Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene". Gene 278 (1–2): 185–192. doi:10.1016/S0378-1119(01)00714-4. PMID 11707336.
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): 16899–16903. 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): 40–45. 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): 1958–1961. doi:10.1194/jlr.E400002-JLR200. PMID 15292367.
Beausoleil SA, Jedrychowski M, Schwartz D et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–12135. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=514446.
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): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Qiao S, Tuohimaa P (2005). "Vitamin D3 inhibits fatty acid synthase expression by stimulating the expression of long-chain fatty-acid-CoA ligase 3 in prostate cancer cells". FEBS Lett. 577 (3): 451–454. doi:10.1016/j.febslet.2004.10.044. PMID 15556626.
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Zhou Y, Abidi P, Kim A et al. (2007). "Transcriptional activation of hepatic ACSL3 and ACSL5 by oncostatin m reduces hypertriglyceridemia through enhanced beta-oxidation". Arterioscler. Thromb. Vasc. Biol. 27 (10): 2198–2205. doi:10.1161/ATVBAHA.107.148429. PMID 17761945.

ACSL3

References

Further reading