J. Biol. Chem., Vol. 260, Issue 5, 2629-2632, 03, 1985
Human liver fatty acid binding protein cDNA and amino acid sequence. Functional and evolutionary implications
L Chan, CF Wei, WH Li, CY Yang, P Ratner, H Pownall, AM Gotto Jr and LC Smith
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.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?