Very long-chain acyl-CoA synthetase

SLC27A2
Identifiers
Aliases	SLC27A2, ACSVL1, FACVL1, FATP2, HsT17226, VLACS, VLCS, hFACVL1, solute carrier family 27 member 2
External IDs	OMIM: 603247 MGI: 1347099 HomoloGene: 37830 GeneCards: SLC27A2
EC number	6.2.1.3
Gene location (Human) Chr. Chromosome 15 (human) Band 15q21.2 Start 50,182,196 bp End 50,236,385 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 F1 Start 126,394,327 bp End 126,430,163 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bronchial epithelial cell liver right lobe of liver kidney tubule corpus epididymis caput epididymis glomerulus metanephric glomerulus kidney rectum Top expressed in proximal tubule kidney left lobe of liver saccule olfactory epithelium parotid gland Paneth cell gallbladder lacrimal gland duodenum More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding fatty acid transmembrane transporter activity ligase activity catalytic activity enzyme binding signaling receptor binding very long-chain fatty acid-CoA ligase activity ATP binding phytanate-CoA ligase activity pristanate-CoA ligase activity decanoate-CoA ligase activity long-chain fatty acid-CoA ligase activity long-chain fatty acid transporter activity Cellular component integral component of membrane endoplasmic reticulum lumen endoplasmic reticulum membrane membrane peroxisomal membrane peroxisome integral component of endoplasmic reticulum membrane endoplasmic reticulum mitochondrion integral component of peroxisomal membrane extracellular exosome plasma membrane specific granule membrane cytosol Biological process lipid metabolism very long-chain fatty acid metabolic process fatty acid transport fatty acid metabolic process long-chain fatty acid import into cell fatty acid alpha-oxidation very long-chain fatty acid catabolic process fatty acid beta-oxidation metabolism long-chain fatty acid metabolic process bile acid biosynthetic process methyl-branched fatty acid metabolic process neutrophil degranulation protein targeting to peroxisome Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11001 26458 Ensembl ENSG00000140284 ENSMUSG00000027359 UniProt O14975 O35488 RefSeq (mRNA) NM_003645 NM_001159629 NM_011978 RefSeq (protein) NP_001153101 NP_003636 NP_036108 Location (UCSC) Chr 15: 50.18 – 50.24 Mb Chr 2: 126.39 – 126.43 Mb PubMed search
Wikidata
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Very long-chain acyl-CoA synthetase is an enzyme that in humans is encoded by the SLC27A2 gene.

The protein encoded by this gene is an isozyme of 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 activates long-chain, branched-chain and very long chain fatty acids containing 22 or more carbons to their CoA derivatives. It is expressed primarily in liver and kidney and is present in both endoplasmic reticulum and peroxisomes but not in mitochondria. Its decreased peroxisomal enzyme activity is in part responsible for the biochemical pathology in X-linked adrenoleukodystrophy.

See also

• Solute carrier family

Further reading

• Perez VM, Gabell J, Behrens M, Wase N, DiRusso CD, Black PN (2020). "Deletion of fatty acid transport protein 2 (FATP2) in the mouse liver changes the metabolic landscape by increasing the expression of PPAR-regulated genes". J. Biol. Chem. 295 (17): 5737–5750. doi:10.1074/jbc.RA120.012730. PMC 7186177. PMID 32188695.
• 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.
• Uchiyama A, Aoyama T, Kamijo K, et al. (1997). "Molecular cloning of cDNA encoding rat very long-chain acyl-CoA synthetase". J. Biol. Chem. 271 (48): 30360–5. doi:10.1074/jbc.271.48.30360. PMID 8939997.
• 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.
• Hirsch D, Stahl A, Lodish HF (1998). "A family of fatty acid transporters conserved from mycobacterium to man". Proc. Natl. Acad. Sci. U.S.A. 95 (15): 8625–9. Bibcode:1998PNAS...95.8625H. doi:10.1073/pnas.95.15.8625. PMC 21126. PMID 9671728.
• Steinberg SJ, Wang SJ, Kim DG, et al. (1999). "Human very-long-chain acyl-CoA synthetase: cloning, topography, and relevance to branched-chain fatty acid metabolism". Biochem. Biophys. Res. Commun. 257 (2): 615–21. doi:10.1006/bbrc.1999.0510. PMID 10198260.
• Watkins PA, Pevsner J, Steinberg SJ (2000). "Human very long-chain acyl-CoA synthetase and two human homologs: initial characterization and relationship to fatty acid transport protein". Prostaglandins Leukot. Essent. Fatty Acids. 60 (5–6): 323–8. doi:10.1016/S0952-3278(99)80007-6. PMID 10471116.
• Steinberg SJ, Wang SJ, McGuinness MC, Watkins PA (1999). "Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA cloning and characterization of a second enzymatically active protein". Mol. Genet. Metab. 68 (1): 32–42. doi:10.1006/mgme.1999.2883. PMID 10479480.
• Mihalik SJ, Steinberg SJ, Pei Z, et al. (2002). "Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling". J. Biol. Chem. 277 (27): 24771–9. doi:10.1074/jbc.M203295200. PMID 11980911.
• 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.
• 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.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.