CAMP
entrez
820
canonical
uniprot
P49913
canonical
ensembl
ENSG00000164047
resolver
ensp
ENSP00000296435
resolver
ensp
ENSP00000498425
resolver
enst
ENST00000296435
resolver
enst
ENST00000652295
resolver
genesymbol
CAMP
resolver
genesymbol_syn
CAP18
resolver
genesymbol_syn
FALL39
resolver
hgnc
HGNC:1472
resolver
uniprot
A0A384NPR0
resolver
uniprot
J3KNB4
resolver
uniprot
Q71SN9
resolver
uniprot_entry
A0A384NPR0_HUMAN
resolver
uniprot_entry
CAMP_HUMAN
resolver
uniprot_entry
J3KNB4_HUMAN
resolver
uniprot_sec
Q71SN9
resolver
amino_acid_sequence
MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
uniprot
proteins
function
FUNCTION: Antimicrobial protein that is an integral component of the innate immune system (PubMed:14978112, PubMed:16637646, PubMed:18818205, PubMed:22879591, PubMed:9736536). Binds to bacterial lipopolysaccharides (LPS) (PubMed:16637646, PubMed:18818205). Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (PubMed:22879591). Postsecretory processing generates multiple cathelicidin antimicrobial peptides with various lengths which act as a topical antimicrobial defense in sweat on skin (PubMed:14978112). The unprocessed precursor form, cathelicidin antimicrobial peptide, inhibits the growth of Gram-negative E.coli and E.aerogenes with efficiencies comparable to that of the mature peptide LL-37 (in vitro) (PubMed:9736536). {ECO:0000269|PubMed:14978112, ECO:0000269|PubMed:16637646, ECO:0000269|PubMed:18818205, ECO:0000269|PubMed:22879591, ECO:0000269|PubMed:9736536}.; FUNCTION: [Antibacterial peptide LL-37]: Antimicrobial peptide that is an integral component of the innate immune system (PubMed:10417311, PubMed:15778390, PubMed:16637646, PubMed:18818205, PubMed:22879591, PubMed:32753597, PubMed:33060695, PubMed:34708076, PubMed:8681941, PubMed:9736536). Binds to bacterial lipopolysaccharides (LPS) (PubMed:10417311, PubMed:16637646, PubMed:18818205, PubMed:33060695, PubMed:9736536). Causes membrane permeabilization by forming transmembrane pores (in vitro) (PubMed:22879591, PubMed:32753597, PubMed:33060695). Causes lysis of E.coli (PubMed:10417311). Exhibits antimicrobial activity against Gram-negative bacteria such as P.aeruginosa, S.typhimurium, E.aerogenes, E.coli and P.syringae, Gram-positive bacteria such as L.monocytogenes, S.epidermidis, S.pyogenes and S.aureus, as well as vancomycin-resistant enterococci (in vitro) (PubMed:10417311, PubMed:32753597, PubMed:8681941, PubMed:9736536). Exhibits antimicrobial activity against methicillin-resistant S.aureus, P.mirabilis, and C.albicans in low-salt media, but not in media containing 100 mM NaCl (in vitro) (PubMed:9736536). Forms chiral supramolecular assemblies with quinolone signal (PQS) molecules of P.aeruginosa, which may lead to interference of bacterial quorum signaling and perturbance of bacterial biofilm formation (PubMed:34708076). May form supramolecular fiber-like assemblies on bacterial membranes (PubMed:29133814). Induces cytokine and chemokine production as well as TNF/TNFA and CSF2/GMCSF production in normal human keratinocytes (PubMed:15778390). Exhibits hemolytic activity against red blood cells (PubMed:10417311). {ECO:0000269|PubMed:10417311, ECO:0000269|PubMed:15778390, ECO:0000269|PubMed:16637646, ECO:0000269|PubMed:18818205, ECO:0000269|PubMed:22879591, ECO:0000269|PubMed:29133814, ECO:0000269|PubMed:32753597, ECO:0000269|PubMed:33060695, ECO:0000269|PubMed:34708076, ECO:0000269|PubMed:8681941, ECO:0000269|PubMed:9736536}.; FUNCTION: [Antibacterial peptide FALL-39]: Exhibits antimicrobial activity against E.coli and B.megaterium (in vitro). {ECO:0000269|PubMed:7529412, ECO:0000269|PubMed:8681941}.; FUNCTION: [Antibacterial peptide KR-20]: Acts synergistically with peptides KS-30 and KR-31, killing bacteria such as S.aureus, E.coli and C.albicans at lower concentrations when present together, and maintains activity at increased salt condition (PubMed:14978112). Does not have the ability to stimulate CXCL8/IL8 release from keratinocytes (PubMed:14978112). {ECO:0000269|PubMed:14978112}.; FUNCTION: [Antibacterial peptide LL-23]: Poorly active (MIC > 150 uM) against E.coli strain K12 (PubMed:14978112). Is able to induce the pro-inflammatory cytokine TNF/TNFA or the chemokine CCL2/MCP1 (PubMed:14978112). {ECO:0000269|PubMed:14978112}.; FUNCTION: [Antibacterial peptide LL-29]: Moderately antibacterial. {ECO:0000269|PubMed:14978112}.; FUNCTION: [Antibacterial peptide KS-30]: Moderately antibacterial (PubMed:14978112). Acts synergistically with peptides KR-20 and KR-31, killing bacteria such as S.aureus, E.coli and C.albicans at lower concentrations when present together, and maintain activity at increased salt condition (PubMed:14978112). Does not have the ability to stimulate CXCL8/IL8 release from keratinocytes (PubMed:14978112). {ECO:0000269|PubMed:14978112}.; FUNCTION: [Antibacterial peptide RK-31]: Acts synergistically with peptides KS-30 and KR-31, killing bacteria such as S.aureus, E.coli and C.albicans at lower concentrations when present together, and maintain activity at increased salt condition (PubMed:14978112). Does not have the ability to stimulate CXCL8/IL8 release from keratinocytes (PubMed:14978112). {ECO:0000269|PubMed:14978112}.; FUNCTION: [Antibacterial peptide FF-33]: Inhibits the growth of E.coli and B.megaterium and exhibits hemolytic activity against human red blood cells. {ECO:0000269|PubMed:14978112}.
uniprot
proteins
mass_dalton
19301
uniprot
proteins
mutagenesis
MUTAGEN 142; /note="S->A: Slightly increased MIC against E.coli K12 (MIC=15 compared to MIC=5)."; /evidence="ECO:0000269|PubMed:22185690"; MUTAGEN 142; /note="S->V: Slightly increased MIC against E.coli K12 (MIC=25 compared to MIC=5)."; /evidence="ECO:0000269|PubMed:22185690"; MUTAGEN 149; /note="E->A: Disrupts oligomerization. Loss of antimicrobial activity."; /evidence="ECO:0000269|PubMed:33060695"; MUTAGEN 150; /note="F->A: Loss of antimicrobial activity against M.luteus."; /evidence="ECO:0000269|PubMed:32753597"; MUTAGEN 150; /note="F->S: Loss of antimicrobial activity against M.luteus."; /evidence="ECO:0000269|PubMed:32753597"; MUTAGEN 151; /note="K->A: Loss of antimicrobial activity against M.luteus."; /evidence="ECO:0000269|PubMed:32753597"; MUTAGEN 151; /note="K->H: Reduced antimicrobial activity against M.luteus."; /evidence="ECO:0000269|PubMed:32753597"; MUTAGEN 151; /note="K->Q: Loss of antimicrobial activity against M.luteus."; /evidence="ECO:0000269|PubMed:32753597"; MUTAGEN 151; /note="K->R: No impact on antimicrobial activity against M.luteus."; /evidence="ECO:0000269|PubMed:32753597"; MUTAGEN 155; /note="Q->A: No impact on antimicrobial activity against M.luteus."; /evidence="ECO:0000269|PubMed:32753597"; MUTAGEN 156; /note="R->A: Impacts oligomerization. Loss of antimicrobial activity."; /evidence="ECO:0000269|PubMed:33060695"; MUTAGEN 157; /note="I->A: Loss of antimicrobial activity against M.luteus."; /evidence="ECO:0000269|PubMed:32753597"; MUTAGEN 157; /note="I->D: Loss of antimicrobial activity against M.luteus."; /evidence="ECO:0000269|PubMed:32753597"; MUTAGEN 157; /note="I->K: Loss of antimicrobial activity against M.luteus."; /evidence="ECO:0000269|PubMed:32753597"; MUTAGEN 157; /note="I->Q: Loss of antimicrobial activity against M.luteus."; /evidence="ECO:0000269|PubMed:32753597"; MUTAGEN 157; /note="I->S: Loss of antimicrobial activity against M.luteus."; /evidence="ECO:0000269|PubMed:32753597"; MUTAGEN 160; /note="F->A: Loss of antimicrobial activity against M.luteus."; /evidence="ECO:0000269|PubMed:32753597
uniprot
proteins
post_translational_modification
PTM: The N-terminus is blocked.; PTM: Proteolytically cleaved by proteinase PRTN3 into antibacterial peptide LL-37 (PubMed:11389039). Proteolytically cleaved by cathepsin CTSG and neutrophil elastase ELANE (PubMed:11389039, PubMed:22879591). {ECO:0000269|PubMed:11389039, ECO:0000269|PubMed:22879591}.; PTM: [Antibacterial peptide LL-37]: Resistant to proteolytic degradation in solution, and when bound to both zwitterionic (mimicking mammalian membranes) and negatively charged membranes (mimicking bacterial membranes). {ECO:0000269|PubMed:10417311}.; PTM: After secretion onto the skin surface, the CAMP gene product is processed by a serine protease-dependent mechanism into multiple novel antimicrobial peptides distinct from and shorter than cathelicidin LL-37, such as peptides KR-20 (residues 151-170), LL-23 (residues 134-156), LL-29 (residues 134-162), KS-30 (residues 141-170), RK-31 (residues 140-170) and FF-33 (residues 138-170) (PubMed:14978112). The peptides act synergistically, killing bacteria at lower concentrations when present together, and maintain activity at increased salt condition (PubMed:14978112). {ECO:0000269|PubMed:14978112}.
uniprot
proteins
protein_family
Cathelicidin family
uniprot
proteins
pubmed
10417311
uniprot
proteins
pubmed
11238224
uniprot
proteins
pubmed
11389039
uniprot
proteins
pubmed
14978112
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15778390
uniprot
proteins
pubmed
16637646
uniprot
proteins
pubmed
18818205
uniprot
proteins
pubmed
21463582
uniprot
proteins
pubmed
22185690
uniprot
proteins
pubmed
22879591
uniprot
proteins
pubmed
23406372
uniprot
proteins
pubmed
29087182
uniprot
proteins
pubmed
29133814
uniprot
proteins
pubmed
29317506
uniprot
proteins
pubmed
32753597
uniprot
proteins
pubmed
33060695
uniprot
proteins
pubmed
34708076
uniprot
proteins
pubmed
35061360
uniprot
proteins
pubmed
7529412
uniprot
proteins
pubmed
7615076
uniprot
proteins
pubmed
7890387
uniprot
proteins
pubmed
8681941
uniprot
proteins
pubmed
8946956
uniprot
proteins
pubmed
9736536
uniprot
proteins
sequence_length
170
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14978112}. Vesicle {ECO:0000269|PubMed:7529412, ECO:0000269|PubMed:9736536}. Note=Stored as pro-peptide in granules and phagolysosomes of neutrophils (PubMed:7529412, PubMed:9736536). Secreted in sweat onto skin (PubMed:14978112). {ECO:0000269|PubMed:14978112, ECO:0000269|PubMed:7529412, ECO:0000269|PubMed:9736536}.
uniprot
proteins