LEAP-2

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].

The below sequences were used to create LEAP-2 sequence signatures:

> LEAP-2H_6, LEAP-2P_6 | CAMPSQ739 | Q969E1 | 20138667
MTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLSVAQE
> LEAP-2H_6, LEAP-2P_6 | CAMPSQ792 | |
MTPFWRGVSLRPVGASCRDNSECITMLCRKNRCFLRTASE
> LEAP-2H_6, LEAP-2P_6 | CAMPSQ10076 | |
MTPLWRIMNSKPFGAYCQNNYECSTGLCRAGHCSTSHRAPSETVNY
> LEAP-2H_6, LEAP-2P_6 | CAMPSQ10889 | |
MLSDIFNSRAIVVCIGVLMLSYQVCSSPILKADSSIVVDSPASLSLQALKRFARMTPLWR
NIGTKPHGAYCQHHHECSTKICREGHCSLNQNFKS
> LEAP-2H_6, LEAP-2P_6 | CAMPSQ10890 | |
MRTVICRVFAISLILFLICDIQVQAAALPRGDGVQLVNRVKRSMMWRWITQRPIGASCRD
HSECGTNYCKDDYCSIRVFSS
> LEAP-2H_6, LEAP-2P_6 | CAMPSQ11099 | |
MTPLWRVMGNKPFGAYCQDHVECSTGICKGGHCIYSQPIKS

The below sequences were retrieved using LEAP-2 sequence signatures:

> LEAP-2H_6, LEAP-2P_6 | CAMPSQ739 | Q969E1 | 20138667
MTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLSVAQE
> LEAP-2H_6, LEAP-2P_6 | CAMPSQ1720 | Q95M25 | 20138666
MTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLSVAQE
> LEAP-2H_6, LEAP-2P_6 | CAMPSQ1721 | Q95JC3 | 20138665
MTPFWRAVSLRPIGASCRDDSECITRLCRKRRCSLSVAQE
> LEAP-2H_6, LEAP-2P_6 | CAMPSQ1722 | Q91X13 | 20138646
MTPFWRGVSLRPIGASCRDDSECITRLCKKRRCSLSVAQE
> LEAP-2H_6, LEAP-2P_6 | CAMPSQ1723 | Q91V13 | 20138644
MTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLSVAQE
> LEAP-2H_6, LEAP-2P_6 | CAMPSQ1724 | Q95JB4 | 20138457
MTPFWRAVSLRPIGASCRDDSECLTRLCRKRRCSLSVAQE
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