Abstract
Human liver fatty acid binding protein (L-FABP) cDNA clones were identified in a liver cDNA library. The two longest clones were completely sequenced. The nucleotide sequence predicts a protein of 127 amino acid residues. Identity of the clones was confirmed by limited amino acid sequence analysis of purified human L-FABP peptides and Edman degradation of radiolabeled in vitro translated FABP. Statistical analysis of the amino acid and mRNA sequences of human L-FABP, rat L-FABP, rat intestinal (I-) FABP, and mouse 422 protein indicates that the human and rat L-FABPs are highly homologous and that L-FABP and I-FABP diverged a long time ago (approximately 650-690 million years ago), although they are more closely related to each other than either of them is to 422 protein. Secondary structure predictions from the primary sequence of human and rat L-FABP reveal a region (residues 12-30) that might be the putative fatty acid binding domain of the two L-FABPs. Knowledge of the primary amino acid sequence of L-FABP and possible functional domains will be pivotal in further defining and understanding the mechanism of ligand binding and transfer by this protein.
Highlights
Human liverfatty acid binding protein (L-Fatty acid binding protein (FABP)) cDNA clones were identified in a liver cDNA library
Statistical analysisof the amino acid and mRNA sequences ofhumanLFABP, rat L-FABP, rat intestinal (I-) FABP, and mouse 422 protein indicates that the human andrat LFABPs are highlyhomologousand that L-FABP and IFABP diverged a long time ago (-650-690 million years ago), they are more closely related to each other than either of them is to 422 protein
We report the primary structure of human liver FABP deduced from its cloned cDNA sequence, partial sequenceanalysis of purified FABP, and of FABP synthesized in vitro
Summary
Human liverfatty acid binding protein (L-FABP) cDNA clones were identified in a liver cDNA library. Statistical analysisof the amino acid and mRNA sequences ofhumanLFABP, rat L-FABP, rat intestinal (I-) FABP, and mouse 422 protein indicates that the human andrat LFABPs are highlyhomologousand that L-FABP and IFABP diverged a long time ago (-650-690 million years ago), they are more closely related to each other than either of them is to 422 protein. Secondary structure predictions from the primary sequence of human and rat L-FABP reveal a region (residues 12-30) that might be the putative fatty acid binding domain of the two L-FABPs. Knowledge of the primary amino acid sequence of L-FABP and possible functional domains will be pivotal in further defining and understanding the mechanism of ligand binding and transfer by this protein. We estimate the divergence time between each pair of the FABP-related proteins andpropose an evolutionary tree for these proteins
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