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Biochem Biophys Res Commun. 2000 Aug 18;275(1):69-74.

Characterization of p40/GPR69A as a peripheral membrane protein related to the lantibiotic synthetase component C.

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Department of Biochemistry, Institute of Medical Biochemistry, University of Vienna, Vienna Biocenter, Dr. Bohr-Gasse 9/3, Vienna, A-1030, Austria.


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.

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