Abstract
The 40 kDa erythrocyte membrane protein p40/GPR69A, previously assigned to the G-protein-coupled receptor superfamily, was now identified by peptide-antibodies and characterized as a loosely associated peripheral membrane protein. This result is in striking contrast to the proposed seven-transmembrane protein structure and function and therefore we wish to correct our previous proposal. p40 is located at the cytoplasmic side of the membrane and is neither associated with the cytoskeleton nor lipid rafts. Refined sequence analysis revealed that p40 is related to the LanC family of bacterial membrane-associated proteins which are involved in the biosynthesis of antimicrobial peptides. Therefore, we rename p40 to LanC-like protein 1 (LANCL1) and suggest that it may play a similar role as a peptide-modifying enzyme component in eukaryotic cells.
Copyright 2000 Academic Press.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Anti-Bacterial Agents / biosynthesis
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Bacteria / enzymology
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism
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Blotting, Western
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Conserved Sequence*
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Detergents / pharmacology
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Endopeptidase K / metabolism
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Erythrocyte Membrane / drug effects
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Erythrocyte Membrane / enzymology
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Erythrocyte Membrane / metabolism
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GTP-Binding Proteins*
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Gene Expression Profiling
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Humans
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Membrane Proteins / chemistry*
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Membrane Proteins / metabolism
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Molecular Sequence Data
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Molecular Weight
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism
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Phylogeny
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Protein Conformation
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Receptors, G-Protein-Coupled*
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
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Solubility / drug effects
Substances
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Anti-Bacterial Agents
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Bacterial Proteins
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Detergents
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LANCL1 protein, human
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Membrane Proteins
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Peptide Fragments
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Receptors, G-Protein-Coupled
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Recombinant Fusion Proteins
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Endopeptidase K
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GTP-Binding Proteins