Molecular cloning, characterization, and tissue-specific expression of human LANCL2, a novel member of the LanC-like protein family.
We identified and characterized the cDNA coding for human LANCL2, a new member of the eukaryotic LanC-like protein family which is related to the bacterial lanthionine synthetase components C (LanC). The composite nucleotide sequence revealed a coding region of 1353 bp, a 5'-UTR of 186 bp and a 3'-UTR of 2421 bp. The deduced sequence of 450 amino acids showed 57.9% identity (74.7% similarity) when compared with the human LANCL1 homologue. In contrast to LANCL1, a unique ATP/GTP-binding site motif A was found in LANCL2. Northern blot analysis revealed the presence of two major transcripts in the brain, 4.7 kb and 4.1 kb in size, and a major 1.8 kb transcript in testis. Accordingly, expression array analysis showed prominent signals in these tissues. Because of the structural similarity to LanC, we postulate that LANCL2 may play a role as a component of a peptide-modifying complex.
Mayer
H
H
Institute of Medical Biochemistry, University of Vienna, Vienna Biocenter, Dr. Bohr-Gasse 9/3, A-1030 Vienna, Austria.
Pongratz
M
M
Prohaska
R
R
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D019204:GTP-Binding Proteins / Q000235:genetics*; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D005810:Multigene Family / Q000235:genetics*; D009928:Organ Specificity; D043562:Receptors, G-Protein-Coupled; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA
C485881:LANCL1 protein, human; D008565:Membrane Proteins; D043562:Receptors, G-Protein-Coupled; D019204:GTP-Binding Proteins