LEAP-2

Description
This family consists of several mammalian liver-expressed antimicrobial peptide 2 (LEAP-2) sequences. LEAP-2 is a cationic cysteine-rich 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 [PMID: 12493837].
Pfam
Interpro
Sequences retrieved from pattern (1)
CAMPLEAP M-T-P-F-W-R-G-V-S-L-R-P-[IV]-G-A-S-C-R-D-[DN]-S-E-C-I-T-x-L-C-R-K-x(0,1)-R-x(0,1)-C-x-L-[RS]-[TV]-A-[QS]-E  
  UniProt Name
  Q969E1 LEAP-2
  Q95M25 Liver-expressed antimicrobial peptide 2
  Q91V13 Liver-expressed antimicrobial peptide 2
  Q6QLQ6 Liver expressed antimicrobial peptide 2
  B0KWP9 Liver-expressed antimicrobial peptide 2
Sequences retrieved from HMM ( 1 )
CAMPLEAH  
  GI UniProt Name
  20138667 Q969E1 LEAP-2
  20138666 Q95M25 Liver-expressed antimicrobial peptide 2
  20138665 Q95JC3 Liver-expressed antimicrobial peptide 2
  20138646 Q91X13 Liver-expressed antimicrobial peptide 2
  20138644 Q91V13 Liver-expressed antimicrobial peptide 2
 

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