The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

SLC27A2  -  solute carrier family 27 (fatty acid...

Homo sapiens

Synonyms: ACSVL1, FACVL1, FATP-2, FATP2, Fatty acid transport protein 2, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of SLC27A2


High impact information on SLC27A2

  • Furthermore, hVLCS was topographically oriented facing the peroxisomal matrix in both control and X-ALD fibroblasts, contradicting the alternative hypothesis that ALDP is required to translocate VLCS into peroxisomes [2].
  • However, overexpression of both hVLCS and ALDP in X-ALD fibroblasts synergistically increased very-long-chain fatty acid beta-oxidation, indicating that these proteins interact functionally [2].
  • We reported previously that homolog 2 of very long-chain acyl-CoA synthetase (VLCS) can activate cholate (Steinberg, S. J., Mihalik, S. J., Kim, D. G., Cuebas, D. A., and Watkins, P. A. (2000) J. Biol. Chem. 275, 15605-15608) [3].
  • The most recently identified family is the very long-chain acyl-CoA synthetases (VLCS) [4].
  • Furthermore, activation of PPARgamma and RXR enhanced the expression of the fat droplet-associated protein adipophilin along with fatty acid transport protein (FATP)4, whereas expression of FATP2 was decreased by activation of RXR [5].

Biological context of SLC27A2


Anatomical context of SLC27A2


Associations of SLC27A2 with chemical compounds

  • While one motif is also present in long-chain acyl-CoA synthetases, the other serves to distinguish the VLCS/FATP family from the long-chain synthetase family [9].
  • Very-long-chain acyl-CoA synthetases (VLCS) activate very-long-chain fatty acids (VLCFA) containing 22 or more carbons to their CoA derivatives [7].
  • An additional finding was that acitretin (15-30 microM) activated significantly human liver microsomal long-chain fatty acid-CoA ligase (E.C., LCL), resulting in enhanced formation of palmitoyl-CoA [10].

Other interactions of SLC27A2


  1. Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA cloning and characterization of a second enzymatically active protein. Steinberg, S.J., Wang, S.J., McGuinness, M.C., Watkins, P.A. Mol. Genet. Metab. (1999) [Pubmed]
  2. Role of very-long-chain acyl-coenzyme A synthetase in X-linked adrenoleukodystrophy. Steinberg, S.J., Kemp, S., Braiterman, L.T., Watkins, P.A. Ann. Neurol. (1999) [Pubmed]
  3. Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling. Mihalik, S.J., Steinberg, S.J., Pei, Z., Park, J., Kim, d.o. .G., Heinzer, A.K., Dacremont, G., Wanders, R.J., Cuebas, D.A., Smith, K.D., Watkins, P.A. J. Biol. Chem. (2002) [Pubmed]
  4. Very long-chain acyl-CoA synthetases. Human "bubblegum" represents a new family of proteins capable of activating very long-chain fatty acids. Steinberg, S.J., Morgenthaler, J., Heinzer, A.K., Smith, K.D., Watkins, P.A. J. Biol. Chem. (2000) [Pubmed]
  5. Peroxisome proliferator-activated receptor-gamma and retinoid X receptor signaling regulate fatty acid uptake by primary human placental trophoblasts. Schaiff, W.T., Bildirici, I., Cheong, M., Chern, P.L., Nelson, D.M., Sadovsky, Y. J. Clin. Endocrinol. Metab. (2005) [Pubmed]
  6. 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. Wakui, K., Aoyama, T., Uchiyama, A., Hashimoto, T., Fukushima, Y. Cytogenet. Cell Genet. (1998) [Pubmed]
  7. Human very-long-chain acyl-CoA synthetase: cloning, topography, and relevance to branched-chain fatty acid metabolism. Steinberg, S.J., Wang, S.J., Kim, D.G., Mihalik, S.J., Watkins, P.A. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  8. Disruption of a yeast very-long-chain acyl-CoA synthetase gene simulates the cellular phenotype of X-linked adrenoleukodystrophy. Watkins, P.A., Lu, J.F., Braiterman, L.T., Steinberg, S.J., Smith, K.D. Cell Biochem. Biophys. (2000) [Pubmed]
  9. Human very long-chain acyl-CoA synthetase and two human homologs: initial characterization and relationship to fatty acid transport protein. Watkins, P.A., Pevsner, J., Steinberg, S.J. Prostaglandins Leukot. Essent. Fatty Acids (1999) [Pubmed]
  10. In vitro metabolism of acitretin by human liver microsomes: evidence of an acitretinoyl-coenzyme A thioester conjugate in the transesterification to etretinate. Knights, K.M., Gasser, R., Klemisch, W. Biochem. Pharmacol. (2000) [Pubmed]
  11. Molecular organization of peroxisomal enzymes: protein-protein interactions in the membrane and in the matrix. Makkar, R.S., Contreras, M.A., Paintlia, A.S., Smith, B.T., Haq, E., Singh, I. Arch. Biochem. Biophys. (2006) [Pubmed]
WikiGenes - Universities