Molecular Biology and Evolution 17:114-126 (2000)
© 2000 Society for Molecular Biology and Evolution
Article |
A Phylogenetic Analysis of the Lipocalin Protein Family
*Department of Biology, University of Utah;
and
Departamento de Genética, Universidad de Sevilla, Seville, Spain
The lipocalins are a family of extracellular proteins that bind and transport small hydrophobic molecules. They are found in eubacteria and a great variety of eukaryotic cells, in which they play diverse physiological roles. We report here the detection of two new eukaryotic lipocalins and a phylogenetic analysis of 113 lipocalin family members performed with maximum-likelihood and parsimony methods on their amino acid sequences. Lipocalins segregate into 13 monophyletic clades, some of which are grouped in well-supported superclades. An examination of the G+C content of the bacterial lipocalin genes and the detection of four new conceptual lipocalins in other eubacterial species argue against a recent horizontal transfer as the origin of prokaryotic lipocalins. Therefore, we rooted our lipocalin tree using the clade containing the prokaryotic lipocalins. The topology of the rooted lipocalin tree is in general agreement with the currently accepted view of the organismal phylogeny of arthropods and chordates. The rooted tree allows us to assign polarity to character changes and suggests a plausible scenario for the evolution of important lipocalin properties. More recently evolved lipocalins tend to (1) show greater rates of amino acid substitutions, (2) have more flexible protein structures, (3) bind smaller hydrophobic ligands, and (4) increase the efficiency of their ligand-binding contacts. Finally, we found that the family of fatty-acid-binding proteins originated from the more derived lipocalins and therefore cannot be considered a sister group of the lipocalin family.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  E. Hofmann, P. Zerbe, and F. Schaller The Crystal Structure of Arabidopsis thaliana Allene Oxide Cyclase: Insights into the Oxylipin Cyclization Reaction PLANT CELL, November 1, 2006; 18(11): 3201 - 3217. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. T. F. Alako, D. Rainey, H. Nijveen, and J. A. M. Leunissen TreeDomViewer: a tool for the visualization of phylogeny and protein domain structure. Nucleic Acids Res., July 1, 2006; 34(Web Server issue): W104 - W109. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J.-B. Frenette Charron, F. Ouellet, M. Pelletier, J. Danyluk, C. Chauve, and F. Sarhan Identification, Expression, and Evolutionary Analyses of Plant Lipocalins Plant Physiology, December 1, 2005; 139(4): 2017 - 2028. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. K. O'Bryan, L. M. Foulds, J. F. Cannon, W. R. Winnall, J. A. Muir, K. Sebire, A. I. Smith, H.-H. Keah, M. T. W. Hearn, D. M. de Kretser, et al. Identification of a Novel Apolipoprotein, ApoN, in Ovarian Follicular Fluid Endocrinology, November 1, 2004; 145(11): 5231 - 5242. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Rzychon, R. Filipek, A. Sabat, K. Kosowska, A. Dubin, J. Potempa, and M. Bochtler Staphostatins resemble lipocalins, not cystatins in fold Protein Sci., October 1, 2003; 12(10): 2252 - 2256. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. A. Graham, D. Brewer, G. Lajoie, and P. L. Davies Characterization of a Subfamily of Beetle Odorant-binding Proteins Found in Hemolymph Mol. Cell. Proteomics, August 1, 2003; 2(8): 541 - 549. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Sanchez, M. D. Ganfornina, G. Gutierrez, and A. Marin Exon-Intron Structure and Evolution of the Lipocalin Gene Family Mol. Biol. Evol., May 1, 2003; 20(5): 775 - 783. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. H. Greene, E. D. Chrysina, L. I. Irons, A. C. Papageorgiou, K. R. Acharya, and K. Brew Role of conserved residues in structure and stability: Tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily Protein Sci., November 1, 2001; 10(11): 2301 - 2316. [Abstract] [Full Text] [PDF]
|
|