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Gene Review

Slc27a4  -  solute carrier family 27 (fatty acid...

Mus musculus

Synonyms: Acsvl4, BB144259, FATP-4, FATP4, Fatp4, ...
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Disease relevance of Slc27a4

  • FATP4 is the primary intestinal FATP and is thought to play a major role in dietary fatty acid uptake; it therefore is viewed as a target to prevent or reverse obesity [1].

High impact information on Slc27a4

  • Further, overexpression of FATP4 in 293 cells facilitates uptake of long chain FAs with the same specificity as enterocytes, while reduction of FATP4 expression in primary enterocytes by antisense oligonucleotides inhibits FA uptake by 50% [2].
  • Here, we show that FATP4, a member of a large family of FA transport proteins (FATPs), is expressed at high levels on the apical side of mature enterocytes in the small intestine [2].
  • Positional cloning of the wrfr mutation revealed a retrotransposon insertion into a coding exon of Slc27a4, the gene encoding fatty acid transport protein (FATP)4 [1].
  • FATP4 exhibited substrate specificity for C16:0 and C24:0 fatty acids with a V(max)/K(m) (C16:0)/V(max)/K(m) (C24:0) of 1 [3].
  • However, expression of FATP4 in human adipose tissue was increased in obesity (independent of genetic factors) [4].

Biological context of Slc27a4

  • Transfection of FATP4 cDNA into COS1 cells resulted in a 2-fold increase in palmitoyl-CoA synthetase (C16:0) and a 5-fold increase in lignoceroyl-CoA synthetase (C24:0) activity from membrane extracts, indicating that the FATP4 gene encodes an acyl-CoA synthetase with substrate specificity biased towards very long chain fatty acids [5].
  • The FATP4 gene was assigned to mouse chromosome 2 band B, syntenic to the region 9q34 encompassing the human gene [5].
  • So far, both FATP1 and FATP4 have been associated with parameters related to insulin resistance [4].
  • This localization is consistent with a role for FATP4 in fat absorption in early embryogenesis and suggests a novel requirement for FATP4 function during development [6].
  • Deletion of both FATP4 alleles resulted in embryonic lethality as crosses between heterozygous FATP4 parents resulted in no homozygous offspring; furthermore, no homozygous embryos were detected as early as day 9.5 of gestation [6].

Anatomical context of Slc27a4

  • Northern analysis showed that FATP4 mRNA was expressed most abundantly in small intestine, brain, kidney, liver, skin and heart [5].
  • Deletion of one allele of FATP4 resulted in 48% reduction of FATP4 protein levels and a 40% reduction of fatty acid uptake by isolated enterocytes [6].
  • FATP4 has been hypothesized to be bifunctional, exhibiting both fatty acid transport and acyl-CoA synthetase activities that work in concert to mediate fatty acid influx across biological membranes [3].
  • We previously demonstrated, using in vitro antisense experiments, that FATP4 is required for fatty acid uptake into intestinal epithelial cells [6].
  • Fatty acid transport protein 4 (FATP4) is an integral membrane protein expressed in the plasma and internal membranes of the small intestine and adipocyte as well as in the brain, kidney, liver, skin, and heart [3].

Associations of Slc27a4 with chemical compounds


Analytical, diagnostic and therapeutic context of Slc27a4

  • To determine whether FATP4 is an acyl-CoA synthetase, the murine protein was engineered to contain a C-terminal FLAG epitope tag, expressed in COS1 cells via adenovirus-mediated infection and purified to near homogeneity using alpha-FLAG affinity chromatography [3].


  1. Cloning of wrinkle-free, a previously uncharacterized mouse mutation, reveals crucial roles for fatty acid transport protein 4 in skin and hair development. Moulson, C.L., Martin, D.R., Lugus, J.J., Schaffer, J.E., Lind, A.C., Miner, J.H. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  2. Identification of the major intestinal fatty acid transport protein. Stahl, A., Hirsch, D.J., Gimeno, R.E., Punreddy, S., Ge, P., Watson, N., Patel, S., Kotler, M., Raimondi, A., Tartaglia, L.A., Lodish, H.F. Mol. Cell (1999) [Pubmed]
  3. Enzymatic properties of purified murine fatty acid transport protein 4 and analysis of acyl-CoA synthetase activities in tissues from FATP4 null mice. Hall, A.M., Wiczer, B.M., Herrmann, T., Stremmel, W., Bernlohr, D.A. J. Biol. Chem. (2005) [Pubmed]
  4. Fatty acid transport proteins and insulin resistance. Fisher, R.M., Gertow, K. Curr. Opin. Lipidol. (2005) [Pubmed]
  5. Mouse fatty acid transport protein 4 (FATP4): characterization of the gene and functional assessment as a very long chain acyl-CoA synthetase. Herrmann, T., Buchkremer, F., Gosch, I., Hall, A.M., Bernlohr, D.A., Stremmel, W. Gene (2001) [Pubmed]
  6. Targeted deletion of fatty acid transport protein-4 results in early embryonic lethality. Gimeno, R.E., Hirsch, D.J., Punreddy, S., Sun, Y., Ortegon, A.M., Wu, H., Daniels, T., Stricker-Krongrad, A., Lodish, H.F., Stahl, A. J. Biol. Chem. (2003) [Pubmed]
  7. Peroxisome proliferator-activated receptor-alpha,gamma-agonist improves insulin sensitivity and prevents loss of left ventricular function in obese dyslipidemic mice. Verreth, W., Ganame, J., Mertens, A., Bernar, H., Herregods, M.C., Holvoet, P. Arterioscler. Thromb. Vasc. Biol. (2006) [Pubmed]
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