Molecular Cloning, Characterization, and Tissue-Specific Expression of Human LANCL2, a Novel Member of the LanC-Like Protein Family

Abstract

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 pep-tide-modifying complex.