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Liver-expressed antimicrobial peptide 2 precursor (LEAP-2). This family consists of several mammalian liver-expressed antimicrobial peptide 2 (LEAP-2) sequences. LEAP-2 is a cysteine-rich, and cationic protein. LEAP-2 contains a core structure with two disulfide bonds formed by cysteine residues in relative 1-3 and 2-4 positions. LEAP-2 is synthesised as a 77-residue precursor, which is predominantly expressed in the liver and highly conserved among mammals. The largest native LEAP-2 form of 40 amino acid residues is generated from the precursor at a putative cleavage site for a furin-like endoprotease. In contrast to smaller LEAP-2 variants, this peptide exhibits dose-dependent antimicrobial activity against selected microbial model organisms. The exact function of this family is unclear.
No pairwise interactions found for the domain LEAP-2
Tips:  If you've navigated here from a protein, hovering over a position on the weblogo will display the corresponding protein position for that domain position. The histograms below the weblogo indicate mutations found on the domain. Red is for disease (OMIM) and blue is for SNPs. Functional Features are displayed as orange boxes under the histograms. You can choose which features are displayed in the box below. Range on the Protein: Protein ID Protein Position Domain Position:  No Conserved Features/Sites Found for LEAP-2
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