{PDOC00729}
{PS00946; CATHELICIDINS_1}
{PS00947; CATHELICIDINS_2}
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* Cathelicidins signatures *
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The precursor  sequences  of  a  number  of antimicrobial peptides secreted by
neutrophils (polymorphonuclear  leukocytes) upon activation have been found to
be evolutionarily  related  and  are  collectively known as cathelicidins [1].
This family includes:

 - Pig cathelin, which may be the precursor of an antibacterial peptide.
 - Bovine  and  sheep  bactenecin 5 (Bac5) and 7 (Bac7), proline and arginine-
   rich antibiotics.
 - Bovine and sheep cyclic dodecapeptide, a potent antibiotic.
 - Bovine indolicidin, a tryptophan-rich potent antibiotic.
 - Rabbit  CAP18, a  protein  that  binds to the bacterial lipopolysaccharides
   (LPS) and which also has antibiotic activity.
 - Human FALL-39 (or LL-37), an antibacterial LPS-binding peptide.
 - Rabbit p15,  which  also  binds  to  LPS  and  modulates the  antibacterial
   activity of BPI.
 - Pig antibacterial peptide PR-39.
 - Bovine myeloid antibacterial peptides BMAP-27 and BMAP-28.
 - Pig myeloid antibacterial peptides PMAP-23, PMAP-36 and PMAP-37.
 - Pig protegrin-1 to -5.
 - Sheep myeloid antibacterial peptide SMAP-29 (SC-5).
 - Mouse CRAMP (CLP).

Structurally, these  proteins  consist  of three domains: a signal sequence, a
conserved region  of  about 100 residues that contains four cysteines involved
in two disulfide bonds, and a  highly divergent C-terminal section of variable
size. It  is  in  this  C-terminal section that the antibacterial peptides are
found; they are proteolytically processed from their precursor by enzymes such
as elastase.   This   structure   is   shown   in   the   following  schematic
representation:

   +---+-*******------*******-----------+--------------------+
   |Sig| Propeptide     C  C  C  C      | Antibacterial pep. |
   +---+----------------|--|--|--|------+--------------------+
                        |  |  |  |
                        +--+  +--+

'C': conserved cysteine involved in a disulfide bond.
'*': position of the patterns.

We derived   two   signature  patterns  for  these  proteins;  the  first  one
corresponds to  the  beginning  of  the  conserved  region and the second to a
central part that contains two of the conserved cysteines.

-Consensus pattern: Y-x-[ED]-x-V-x-[RQ]-A-[LIVMA]-[DQG]-x-[LIVMFY]-N-[EQ]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: F-x-[LIVM]-K-E-T-x-C-x(10)-C-x-F-[KR]-[KE]
                    [The 2 C's are involved in disulfide bonds]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Expert(s) to contact by email:
           Tossi A.; tossi@univ.trieste.it

-Last update: May 2004 / Text revised.

[ 1] Zanetti M., Gennaro R., Romeo D.
     "Cathelicidins: a novel protein family with a common proregion and a
     variable C-terminal antimicrobial domain."
     FEBS Lett. 374:1-5(1995).
     PubMed=7589491

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