We isolated and characterized the cDNA coding for rat LANCL1, a new member of the eukaryotic LanC-like protein family which is related to the bacterial lanthionine synthetase components C (LanC). LanC is involved in the synthesis of antimicrobial peptides. Rat LANCL1 showed 91.5% and 96% identity when compared with the previously characterized human and mouse orthologs, respectively. Northern blot analysis revealed the presence of two major transcripts, at 1.5 kb and 5 kb, probably arising from the usage of two different polyadenylation signals. The 1.5 kb mRNA is massively expressed in testis, whereas the 5 kb transcript is most abundant in brain. The high level of expression of rat LANCL1 in these tissues was confirmed by Western blotting. In situ hybridization analyses of various rat tissues revealed a strong signal in the germinal cells of the seminiferous tubules in testis, in the neurons of the cerebellum, in liver hepatocytes, and in cardiac myocytes. The clear relationship between LANCL1 and bacterial LanC proteins suggests similar functions as peptide-modifying enzymes synthesizing antimicrobial peptides. In particular, the high expression of LANCL1 in testis and brain, organs separated by blood-tissue barriers, may hint at a role in the immune surveillance of these organs.