Molecular cloning, characterization, and tissue-specific expression of human LANCL2, a novel member of the LanC-like protein family

DNA Seq. 2001;12(3):161-6. doi: 10.3109/10425170109080770.

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 peptide-modifying complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • GTP-Binding Proteins / genetics*
  • Humans
  • Membrane Proteins / genetics*
  • Molecular Sequence Data
  • Multigene Family / genetics*
  • Organ Specificity
  • Receptors, G-Protein-Coupled*
  • Sequence Alignment
  • Sequence Analysis, DNA

Substances

  • LANCL1 protein, human
  • Membrane Proteins
  • Receptors, G-Protein-Coupled
  • GTP-Binding Proteins

Associated data

  • GENBANK/AJ278245