v5.1.0.3
Glycine data from LIS
Type | Family |
Description | The LanC-like protein superfamily encompasses a highly divergent group of peptide-modifying enzymes, including the eukaryotic and bacterial lanthionine synthetase C-like proteins (LanC) [ , , ]; subtilin biosynthesis protein SpaC from Bacillus subtilis [, ]; epidermin biosynthesis protein EpiC from Staphylococcus epidermidis []; nisin biosynthesis protein NisC from Lactococcus lactis [, , ]; GCR2 from Arabidopsis thaliana (Mouse-ear cress) []; and many others. The 3D structure of the lantibiotic cyclase from L. lactis has been determined by X-ray crystallography to 2.5A resolution [ ]. The globular structure is characterised by an all-α fold, in which an outer ring of helices envelops an inner toroid composed of 7 shorter, hydrophobic helices. This 7-fold hydrophobic periodicity has led several authors to claim various members of the family, including eukaryotic LanC-1 and GCR2, to be novel G protein-coupled receptors [, ]; some of these claims have since been corrected [, , ]. The eukaryotic lanthionine synthetase C-like proteins 1-3, are relatives of the bacterial lanthionine synthetase components C (LanC) [ , , ]. They are ubiquitous in nature, being variously expressed in brain, spinal cord, pituitary gland, kidney, heart, skeletal muscle, pancreas, ovary and testis. LanC-like protein 1 is a glutathione-binding protein []. LanC-like protein 2 is a bystander gene co-amplified and overexpressed with epidermal growth factor receptor (EGFR) in 20% of glioblastomas; its exogenous expression in a sarcoma cell line decreases the expression of ABCB1 (P-glycoprotein 1) and increases cellular sensitivity to the anticancer drug adriamycin []. |
Short Name | LanC-like_prot_euk |