The domain within your query sequence starts at position 1 and ends at position 76; the E-value for the LEAP-2 domain shown below is 4.2e-45.
MLQLKLFAVLLTCLLLLGQVNSSPVPEVSSAKRSRRMTPFWRGVSLRPIGASCRDDSECI TRLCRKRRCSLSVAQE
LEAP-2 |
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PFAM accession number: | PF07359 |
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Interpro abstract (IPR009955): | 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 disulphide 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 [ (PUBMED:12493837) ]. The exact function of this family is unclear. |
GO process: | defense response to bacterium (GO:0042742) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry LEAP-2