Human liver fatty acid binding protein. Isolation of a full length cDNA and comparative sequence analyses of orthologous and paralogous proteins.

M S Boguski,J M Taylor,J I Gordon,D A Sweetser,N A Elshourbagy,J B Lowe

doi:10.1016/s0021-9258(19)83637-2

Abstract

We have determined the primary structure of human liver fatty acid binding protein from an analysis of a full length cDNA. This 127-residue 14,178-Da protein exhibits a high degree of sequence conservation when compared to its orthologous homologue, rat liver fatty acid binding protein. It appears likely that this polypeptide arose from two intragenic duplication events. Using a variety of computational techniques, we were unable to find any evidence of amphipathic alpha helical domains in this protein nor any sequence similarities to apolipoproteins and serum albumins. A family of paralogous proteins was defined, whose members share a remarkable degree of sequence homology with share a remarkable degree of sequence homology with human liver fatty acid binding protein. These include rat intestinal fatty acid binding protein, the cellular the P2 protein of myelin. It appears that the small cytosolic fatty acid binding proteins have evolved structural features necessary for lipid-protein interaction which are different from those present in some familiar and better studied extracellular sequences.

Highlights

We have determined the primary structure of humupatnake and utilization
The highest concentrations of the liver fatty acid binding protein from ananalysis of a protein and its mRNA are found in those tissues
Using a variety of computational techniques,we were unable to find any evidence of amphipathic a helical domains in this protein nor any sequence similarities to apolipoproteins and serum albumins

Summary

Human Liver Fatty Acid Binding Protein

ISOLATION OF A FULL LENGTH cDNA AND COMPARATIVESEQUENCE ANALYSES OF ORTHOLOGOUS AND PARALOGOUS PROTEINS (Received for publication, October 19, 1984). Compared toits orthologous homologue, raltiver fatty An understanding of the structural basis of FABP-fatty acid binding protein. A family of paralogousproteins was definedw, hosemembers share a remarkable degree of sequence homolwogityh human liver fatty acid binding protein. These include specific rolein intracellular lipid transport andcompartmentalization as well as give more general insights into mechanismsby which lipidasnd proteins associatewith one another. It appears that 1 mol of rat liver FABP binds, on average, 1 mol of long chain (CL6-Cmu) nsaturated and saturated fatty acids in a noncovalent fashion [2]. The concentration of rat liver FABP directly correlates with the rate of hepatic fatty acid

RESULTS AND DISCUSSION

1Supported by Medical Scientist Training Program Grant GM

AluI I