ID   CAMP_CHLAE              Reviewed;         170 AA.
AC   Q1KLY6;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Cathelicidin antimicrobial peptide {ECO:0000250|UniProtKB:P49913};
DE   Contains:
DE     RecName: Full=Antibacterial peptide FALL-39 {ECO:0000250|UniProtKB:P49913};
DE     AltName: Full=FALL-39 peptide antibiotic {ECO:0000250|UniProtKB:P49913};
DE   Contains:
DE     RecName: Full=Antibacterial peptide LL-37 {ECO:0000250|UniProtKB:P49913};
DE   Flags: Precursor;
GN   Name=CAMP {ECO:0000250|UniProtKB:P49913};
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16720578; DOI=10.1074/jbc.m511108200;
RA   Zelezetsky I., Pontillo A., Puzzi L., Antcheva N., Segat L., Pacor S.,
RA   Crovella S., Tossi A.;
RT   "Evolution of the primate cathelicidin. Correlation between structural
RT   variations and antimicrobial activity.";
RL   J. Biol. Chem. 281:19861-19871(2006).
CC   -!- FUNCTION: Binds to bacterial lipopolysaccharides (LPS) and has
CC       antibacterial activity. Acts via neutrophil N-formyl peptide receptors
CC       to enhance the release of CXCL2. {ECO:0000250|UniProtKB:P49913}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Proteolytically cleaved by cathepsin CTSG.
CC       {ECO:0000250|UniProtKB:P49913}.
CC   -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR   EMBL; DQ471356; ABE96620.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1KLY6; -.
DR   SMR; Q1KLY6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0042119; P:neutrophil activation; ISS:UniProtKB.
DR   InterPro; IPR001894; Cathelicidin-like.
DR   InterPro; IPR018216; Cathelicidin_CS.
DR   InterPro; IPR022746; Cathlecidin_C.
DR   InterPro; IPR046350; Cystatin_sf.
DR   PANTHER; PTHR10206; PTHR10206; 1.
DR   Pfam; PF12153; CAP18_C; 1.
DR   SUPFAM; SSF54403; SSF54403; 1.
DR   PROSITE; PS00947; CATHELICIDINS_2; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Secreted;
KW   Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   PROPEP          31..131
FT                   /evidence="ECO:0000250|UniProtKB:P49913"
FT                   /id="PRO_0000251749"
FT   PEPTIDE         132..170
FT                   /note="Antibacterial peptide FALL-39"
FT                   /evidence="ECO:0000250|UniProtKB:P49913"
FT                   /id="PRO_0000251750"
FT   PEPTIDE         134..170
FT                   /note="Antibacterial peptide LL-37"
FT                   /evidence="ECO:0000250|UniProtKB:P49913"
FT                   /id="PRO_0000251751"
SQ   SEQUENCE   170 AA;  18951 MW;  1675C3D77704EAE9 CRC64;
     MKTQRDGPSL GRWSLVLLLL GLVMPLAIVA QVLSYQEAVL RAIEGINQRS SDANLYRLLD
     LDPRPTMDGD PDTPKPVSFT VKETVCPRTT QKSPEDCDFK EDGLVKRCVG TVTLNQARDS
     FDISCDKDNR RFARLGKFFR KVKKKIGGGL KKIGQKIKDF LGNLVPRTAS