Lipocalins (Molecular Biology Intelligence Unit by Bo Åkerström

By Bo Åkerström

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Salier J-P. Chromosomal location, exon/intron organization and evolution of lipocalin genes. Biochim Biophys Acta 2000; 1482(1-2):25-34. 2. Sanchez D, Ganfornina MD, Gutierrez G et al. Exon-intron structure and evolution of the lipocalin gene family. Mol Biol Evol 2003; 20(5):775-783. 3. Mans BJ, Louw AI, Neitz AWH. The major tick salivary gland proteins and toxins from the soft tick, Ornithodoros savignyi, are part of the tick lipocalin family: Implications for the origins of tick toxicoses. Mol Biol Evol 2003; 20(7):1158-1167.

Gutierrez G, Ganfornina MD, Sanchez D. Evolution of the lipocalin family as inferred from a protein sequence phylogeny. Biochim Biophys Acta 2000; 1482(1-2):35-45. 13. Thompson JD, Gibson TJ, Plewniak F et al. The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tool. Nucleic Acids Res 1997; 24:4876-4882. 14. Ronquist F, Huelsenbeck JP. MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 2003; 19(12):1572-1574. 15.

Alignments here are much less dependable than for higher levels of sequence identities. Certain pairs of lipocalins show less than 12% identity. This is generally apparent between the prokaryotic lipocalins and the odorant-binding lipocalins of chordates, while more specific examples include retinol-binding protein and the major urinary protein, aphrodisin and α-crustacyanin, the bilin-binding protein and lipocalin allergen Bos d 2. This value is deep within the “midnight zone”, where sequence alignments lose almost all reliability and certainty.

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