Characterization of p40/GPR69A as a Peripheral Membrane Protein Related to the Lantibiotic Synthetase Component C

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-transmembra...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2000-08, Vol.275 (1), p.69-74
Main Authors: Bauer, Hemma, Mayer, Herbert, Marchler-Bauer, Aron, Salzer, Ulrich, Prohaska, Rainer
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Anti-Bacterial Agents - biosynthesis
Bacteria - enzymology
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Blotting, Western
Conserved Sequence
Detergents - pharmacology
Endopeptidase K - metabolism
erythrocyte
Erythrocyte Membrane - drug effects
Erythrocyte Membrane - enzymology
Erythrocyte Membrane - metabolism
G-protein-coupled receptor
Gene Expression Profiling
GPR69A
GTP-Binding Proteins
Humans
lanthionine synthetase
lantibiotic
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Molecular Sequence Data
Molecular Weight
peptide antibody
Peptide Fragments - chemistry
Peptide Fragments - metabolism
peripheral membrane protein
Phylogeny
Protein Conformation
proteolysis
Receptors, G-Protein-Coupled
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - metabolism
red blood cell
Sequence Alignment
Sequence Homology, Amino Acid
Solubility - drug effects
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2000.3260