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)[1]
End	50,236,385 bp[1]
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)[2]
End	126,430,163 bp[2]
RNA expression pattern
	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
	; ;
	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
	11001
	26458
	ENSG00000140284
	ENSMUSG00000027359
	O14975
	O35488
	NM_003645; NM_001159629
	NM_011978
	NP_001153101; NP_003636
	NP_036108
	Wikidata
View/Edit Human	View/Edit Mouse

Very long-chain acyl-CoA synthetase is an enzyme that in humans is encoded by the SLC27A2 gene.[5][6]

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.[6]

References

GRCh38: Ensembl release 89: ENSG00000140284 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000027359 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Wakui K, Aoyama T, Uchiyama A, Hashimoto T, Fukushima Y (Oct 1998). "Assignment of human fatty-acid-coenzyme A ligase, very long-chain 1 gene (FACVL1) to human chromosome band 15q21.2 by fluorescence in situ hybridization". Cytogenet Cell Genet. 81 (3–4): 292–3. doi:10.1159/000015051. PMID 9730624. S2CID 46774274.
"Entrez Gene: SLC27A2 solute carrier family 27 (fatty acid transporter), member 2".

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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000140284 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000027359 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9730624-5] Wakui K, Aoyama T, Uchiyama A, Hashimoto T, Fukushima Y (Oct 1998). "Assignment of human fatty-acid-coenzyme A ligase, very long-chain 1 gene (FACVL1) to human chromosome band 15q21.2 by fluorescence in situ hybridization". Cytogenet Cell Genet. 81 (3–4): 292–3. doi:10.1159/000015051. PMID 9730624. S2CID 46774274.

[entrez-6] "Entrez Gene: SLC27A2 solute carrier family 27 (fatty acid transporter), member 2".

Peroxisomal and lysosomal proteins
Enzymes	Mevalonate kinase Catalase Acetyl-CoA C-acyltransferase Glyceronephosphate O-acyltransferase Alkylglycerone phosphate synthase Phytanoyl-CoA dioxygenase HSD17B4 AMACR
Transporters	SLC27A2
Structure/Peroxin	PEX1 PXMP3 PEX3 PEX5 PEX6 PEX7 PEX10 PEX11A PEX11B PEX11G PEX12 PEX13 PEX14 PEX16 PEX19 PEX26
LAMP	CD68 LAMP1 LAMP2 LAMP3
see also intermediates, disorders

Very long-chain acyl-CoA synthetase

See also

References

Further reading