title: Mouse fatty acid transport protein 4 (FATP4): characterization of the gene and functional assessment as a very long chain acyl-CoA synthetase.
abstract: FATP4 (SLC27A4) is a member of the fatty acid transport protein (FATP) family, a group of evolutionarily conserved proteins that are involved in cellular uptake and metabolism of long and very long chain fatty acids. We cloned and characterized the murine FATP4 gene and its cDNA. From database analysis we identified the human FATP4 genomic sequence. The FATP4 gene was assigned to mouse chromosome 2 band B, syntenic to the region 9q34 encompassing the human gene. The open reading frame was determined to be 1929 bp in length, encoding a polypeptide of 643 amino acids. Within the coding region, the exon-intron structures of the murine FATP4 gene and its human counterpart are identical, revealing a high similarity to the FATP1 gene. The overall amino acid identity between the deduced murine and human FATP4 polypeptides is 92.2%, and between the murine FATP1 and FATP4 polypeptides is 60.3%. Northern analysis showed that FATP4 mRNA was expressed most abundantly in small intestine, brain, kidney, liver, skin and heart. 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.
authors.affiliation: Department of Internal Medicine IV, University of Heidelberg, Bergheimer Strasse 58, 69115, Heidelberg, Germany. thomas_herrmann@med.uni-heidelberg.de
authors.forename: T
authors.initials: T
authors.lastname: Herrmann
authors.forename: F
authors.initials: F
authors.lastname: Buchkremer
authors.forename: I
authors.initials: I
authors.lastname: Gosch
authors.forename: A M
authors.initials: AM
authors.lastname: Hall
authors.forename: D A
authors.initials: DA
authors.lastname: Bernlohr
authors.forename: W
authors.initials: W
authors.lastname: Stremmel
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics* / Q000378:metabolism; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D003066:Coenzyme A Ligases / Q000235:genetics / Q000378:metabolism; D004247:DNA / Q000737:chemistry / Q000235:genetics; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D005091:Exons; D050612:Fatty Acid Transport Proteins; D015870:Gene Expression; D005796:Genes / Q000235:genetics; D017404:In Situ Hybridization, Fluorescence; D007438:Introns; D008297:Male; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D026901:Membrane Transport Proteins; D051379:Mice; D008815:Mice, Inbred Strains; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D014018:Tissue Distribution; D000098859:Long-Chain-Fatty-Acid-CoA Ligase
chemical_list: D002352:Carrier Proteins; D018076:DNA, Complementary; D050612:Fatty Acid Transport Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D012333:RNA, Messenger; D012097:Repressor Proteins; C493571:SLC27A4 protein, human; D029701:Saccharomyces cerevisiae Proteins; C493569:Slc27a1 protein, mouse; C493572:Slc27a4 protein, mouse; D004247:DNA; D003066:Coenzyme A Ligases; C090799:FAA2 protein, S cerevisiae; D000098859:Long-Chain-Fatty-Acid-CoA Ligase