Abstract
By aligning nucleotide and amino acid sequences of lipoprotein lipase in eight species (man, pig, cow, sheep, mouse, rat, guinea-pig and chicken), we found that the main domains (catalytic, N-glycosylation and putative heparin binding sites) are well conserved. The longest identical amino acid chain was encoded by a sequence between the end of exon 2 and the beginning of exon 3, emphasizing the importance of this region which encodes the beta 5-loop of the active site, among other domains. Exon 10 is entirely untranslated in the seven mammals studied here and contains species-characteristic deletions, insertions or elements rich in A or A + T. In chicken, the beginning of exon 10 is translated. These eight previously unreported alignments could be a useful tool for further studies on LPL function.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Apolipoprotein C-II
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Apolipoproteins B / metabolism
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Apolipoproteins C / metabolism
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Base Sequence
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Binding Sites
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Biological Evolution
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Cattle
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Chickens
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Conserved Sequence
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DNA, Complementary / chemistry
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DNA, Complementary / genetics
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Exons
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Glycosylation
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Guinea Pigs
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Heparin / metabolism
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Humans
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Lipid Metabolism
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Lipoprotein Lipase / chemistry*
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Lipoprotein Lipase / genetics*
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Lipoprotein Lipase / metabolism
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Lipoproteins / metabolism
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Mice
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Molecular Sequence Data
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Protein Binding
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Rats
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Receptors, LDL / physiology
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Sequence Alignment
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Sequence Homology, Amino Acid
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Sequence Homology, Nucleic Acid
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Sheep
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Swine
Substances
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Apolipoprotein C-II
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Apolipoproteins B
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Apolipoproteins C
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DNA, Complementary
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Lipoproteins
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Receptors, LDL
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Heparin
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Lipoprotein Lipase