Cloning of a cDNA encoding rat intestinal fatty acid binding protein.

Abstract
Intestinal fatty acid binding protein [IFABP] mRNA is one of the most abundant mRNA species in the rat small intestinal epithelium. RNA transfer blot analyses disclosed that the mRNA encoding IFABP is .apprxeq. 900 nucleotides long and not represented in liver RNA. A total of 564 nucleotides of this mRNA, including 12 nucleotides of the 5'' nontranslated region, the coding portion and 155 nucleotides of the 3'' nontranslated domain were identified. The primary translation product encoded by this mRNA contains 132 amino acids and has a MW of 15,062. The derived protein sequence was verified by automated sequential Edman degradation of the intact polypeptide isolated from a wheat germ cell-free system. The in vitro product is NH2-terminally acetylated, a finding that is consistent with its ultimate cytoplasmic destination. Comparison of the amino acid sequence of this protein with liver fatty acid binding protein, a polypeptide specified by the most abundant small intestinal epithelial mRNA, revealed significant homology and similarity in the predicted secondary structures of their NH2-terminal domains.