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	• long-chain fatty acid-CoA ligase activity • ATP binding • protein kinase binding • protein domain specific binding
Cellular component	• mitochondrial outer membrane • peroxisomal membrane • endoplasmic reticulum • endoplasmic reticulum membrane • Golgi apparatus • lipid particle • membrane • integral component of membrane • perinuclear region of cytoplasm
Biological process	• long-chain fatty acid metabolic process • fatty acid biosynthetic process • brain development • response to nutrient • response to organic cyclic compound • very-low-density lipoprotein particle assembly • positive regulation of Golgi to plasma membrane protein transport • long-chain fatty acid import • positive regulation of secretion • positive regulation of phosphatidylcholine biosynthetic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
223.73 – 223.81 Mb

Chr 1:
78.66 – 78.71 Mb

PubMed search

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

Function

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

↑ 1.0 1.1 "Entrez Gene: ACSL3 acyl-CoA synthetase long-chain family member 3".

Brueton LA, van Herwerden L, Chotai KA, Winter RM (Oct 1992). "The mapping of a gene for craniosynostosis: evidence for linkage of the Saethre-Chotzen syndrome to distal chromosome 7p". Journal of Medical Genetics 29 (10): 681–685. doi:10.1136/jmg.29.10.681. PMC 1016122. PMID 1433226.
Bakken AM, Farstad M, Holmsen H (Feb 1991). "Identity between palmitoyl-CoA synthetase and arachidonoyl-CoA synthetase in human platelet?". The Biochemical Journal. 274 ( Pt 1) (1): 145–52. PMC 1149932. PMID 1848073.
Bronfman M, Inestrosa NC, Nervi FO, Leighton F (Dec 1984). "Acyl-CoA synthetase and the peroxisomal enzymes of beta-oxidation in human liver. Quantitative analysis of their subcellular localization". The Biochemical Journal 224 (3): 709–20. PMC 1144505. PMID 6240978.
Rose CS, King AA, Summers D, Palmer R, Yang S, Wilkie AO et al. (Aug 1994). "Localization of the genetic locus for Saethre-Chotzen syndrome to a 6 cM region of chromosome 7 using four cases with apparently balanced translocations at 7p21.2". Human Molecular Genetics 3 (8): 1405–1408. doi:10.1093/hmg/3.8.1405. PMID 7987323.
Fujino T, Kang MJ, Suzuki H, Iijima H, Yamamoto T (Jul 1996). "Molecular characterization and expression of rat acyl-CoA synthetase 3". The Journal of Biological Chemistry 271 (28): 16748–16752. doi:10.1074/jbc.271.28.16748. PMID 8663269.
Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Minekura H, Fujino T, Kang MJ, Fujita T, Endo Y, Yamamoto TT (May 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, Suzuki H, Sato H, Fujino T et al. (Oct 2001). "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, Derge JG, Klausner RD, Collins FS et al. (Dec 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Mashek DG, Bornfeldt KE, Coleman RA, Berger J, Bernlohr DA, Black P et al. (Oct 2004). "Revised nomenclature for the mammalian long-chain acyl-CoA synthetase gene family". Journal of Lipid Research 45 (10): 1958–1961. doi:10.1194/jlr.E400002-JLR200. PMID 15292367.
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J et al. (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America 101 (33): 12130–12135. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935. Vancouver style error (help)
Qiao S, Tuohimaa P (Nov 2004). "Vitamin D3 inhibits fatty acid synthase expression by stimulating the expression of long-chain fatty-acid-CoA ligase 3 in prostate cancer cells". FEBS Letters 577 (3): 451–454. doi:10.1016/j.febslet.2004.10.044. PMID 15556626.
Rohozinski J, Lamb DJ, Bishop CE (Apr 2006). "UTP14c is a recently acquired retrogene associated with spermatogenesis and fertility in man". Biology of Reproduction 74 (4): 644–651. doi:10.1095/biolreprod.105.046698. PMID 16354793.
Tu LC, Yan X, Hood L, Lin B (Apr 2007). "Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells". Molecular & Cellular Proteomics 6 (4): 575–588. doi:10.1074/mcp.M600249-MCP200. PMID 17220478.
Zhou Y, Abidi P, Kim A, Chen W, Huang TT, Kraemer FB et al. (Oct 2007). "Transcriptional activation of hepatic ACSL3 and ACSL5 by oncostatin m reduces hypertriglyceridemia through enhanced beta-oxidation". Arteriosclerosis, Thrombosis, and Vascular Biology 27 (10): 2198–2205. doi:10.1161/ATVBAHA.107.148429. PMID 17761945.

ACSL3

Function

References

Further reading