TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.C.33.1.1









preProtegrin 2
Eukaryota
Metazoa
preProtegrin 2 of Sus scrofa
*1.C.33.1.2









PreIndolicidin (pre-Cathelicidin-4). May function by a carrier mechanism to selectively transport anions (Rokitskaya et al., 2011).  The pig (ovine) homologue (SMAP29) is the source from which ovispirin, novispirin and novicidin, which may form torroidal pores, are derived (Sawai et al. 2002).

Eukaryota
Metazoa
PreIndolicidin of Bos taurus
*1.C.33.1.3









preBactinecin
Eukaryota
Metazoa
preBactinecin of Ovis aries
*1.C.33.1.4









preCathelin
Eukaryota
Metazoa
Cathelin of Sus scrofa
*1.C.33.1.5









preMyeloid cathelicidin 1
Eukaryota
Metazoa
preMyeloid cathelicidin 1 of Equus caballus
*1.C.33.1.6









Lipopolysaccharide (LPS) binding protein precursor
Eukaryota
Metazoa
LPS binding protein precursor of Oryctolagus cuniculus
*1.C.33.1.7









Myeloid secondary granule protein
Eukaryota
Metazoa
Myeloid secondary granule protein of Mus musculus
*1.C.33.1.8









Cathelicidin-B1; reported to be processed, and the mature C-terminal active peptide is localized to the basolateral surface of M cells where it protects against bacterial infection (Goitsuka et al., 2007).
Eukaryota
Metazoa
 Cathelicidin-B1 of Gallus gallus (Q5F378)
*1.C.33.1.9









Pro-protegrin-1 (PG-1) (149aas;1 N-terminal TMS) produced by porcine leukocytes. It forms an anion-selective β-sheet toroidal channel of 8 β-hairpins in a consecutive NCCN packing organization, yielding both parallel and antiparallel β-sheets (Jang et al., 2008; Capone et al., 2010). The 3-d structure is known. 97% identical to protegrin-2 (1.C.33.1.1).  A model of the protein in Gram-negative bacterial membranes has been proposed (Bolintineanu et al. 2012).  Protegrin peptides form octameric pores, and about 100 pores are sufficient to kill E. coli (Bolintineanu et al. 2010). The membrane-bound structure, lipid interactions, and dynamics of the arginine-rich beta-hairpin antimicrobial peptide PG-1 as studied by solid-state NMR are described by Tang and Hong 2009.  Protegrin stabilizes partial lipid-forming pores (Prieto et al. 2014).  A model of the protegrin-1 pore has been presented, suggesting that permeability of water through a single PG-1 pore is sufficient to cause fast cell death by osmotic lysis (Langham et al. 2008). Possibly, toroidal pore formation is driven by guanidinium-phosphate complexation, where the cationic Arg residues drag the anionic phosphate groups along as they insert into the hydrophobic part of the membrane (Tang et al. 2007).

Eukaryota
Metazoa
Protegrin-1 of Sus scrofa (P32194)
*1.C.33.1.10









The LL-37 peptide (selectively permeabilizes the membranes of apoptotic human leukocytes, leaving viable cells unaffected (Björstad et al., 2009). It forms transmembrane pores (Lee et al., 2011).  It is derived by proteolysis from the cathelin (FALL-39) precursor in granulocytes (Gudmundsson et al. 1996; Li et al. 2016).

Eukaryota
Metazoa
LL-37 peptide precursor of Homo sapiens (P49913)
*1.C.33.1.11









Antimicrobial and antitumor cathelicidin 6 or BMAP27 of 158 aas and 1 or 2 TMSs. The structure and dynamics have been examined (Sahoo and Fujiwara 2016).

Eukaryota
Metazoa
Cathelicidin 6 of Bos taurus (Bovine)