{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P49913","secondaryAccessions":["Q71SN9"],"uniProtkbId":"CAMP_HUMAN","entryAudit":{"firstPublicDate":"1996-10-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-10-01","entryVersion":198,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:1472"}],"value":"Cathelicidin antimicrobial peptide"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7615076"}],"value":"18 kDa cationic antimicrobial protein"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7615076"}],"value":"CAP-18"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7615076"}],"value":"hCAP-18"}]}],"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7529412"}],"value":"Antibacterial peptide FALL-39"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7529412"}],"value":"FALL-39 peptide antibiotic"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8681941"}],"value":"Antibacterial peptide LL-37"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14978112"}],"value":"Antibacterial peptide KR-20"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14978112"}],"value":"Antibacterial peptide LL-23"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14978112"}],"value":"Antibacterial peptide LL-29"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14978112"}],"value":"Antibacterial peptide KS-30"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14978112"}],"value":"Antibacterial peptide RK-31"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14978112"}],"value":"Antibacterial peptide FF-33"}}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:1472"}],"value":"CAMP"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8946956"}],"value":"CAP18"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7529412"}],"value":"FALL39"}],"orfNames":[{"value":"HSD26"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16637646"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18818205"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22879591"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9736536"}],"value":"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)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10417311"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15778390"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16637646"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18818205"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22879591"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29133814"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32753597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33060695"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34708076"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8681941"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9736536"}],"value":"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)"}],"commentType":"FUNCTION","molecule":"Antibacterial peptide LL-37"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7529412"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8681941"}],"value":"Exhibits antimicrobial activity against E.coli and B.megaterium (in vitro)"}],"commentType":"FUNCTION","molecule":"Antibacterial peptide FALL-39"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"value":"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)"}],"commentType":"FUNCTION","molecule":"Antibacterial peptide KR-20"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"value":"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)"}],"commentType":"FUNCTION","molecule":"Antibacterial peptide LL-23"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"value":"Moderately antibacterial"}],"commentType":"FUNCTION","molecule":"Antibacterial peptide LL-29"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"value":"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)"}],"commentType":"FUNCTION","molecule":"Antibacterial peptide KS-30"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"value":"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)"}],"commentType":"FUNCTION","molecule":"Antibacterial peptide RK-31"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"value":"Inhibits the growth of E.coli and B.megaterium and exhibits hemolytic activity against human red blood cells"}],"commentType":"FUNCTION","molecule":"Antibacterial peptide FF-33"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10417311"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29133814"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32753597"}],"value":"Monomer, homodimer or homotrimer (in vitro) (PubMed:10417311). Oligomerizes as tetra- or hexamer in solution (in vitro) (PubMed:10417311, PubMed:29133814, PubMed:32753597)"}],"commentType":"SUBUNIT","molecule":"Antibacterial peptide LL-37"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"chainId":"PRO_0000004724","intActId":"EBI-6378485"},"interactantTwo":{"uniProtKBAccession":"P08069","geneName":"IGF1R","intActId":"EBI-475981"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7529412"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9736536"}],"value":"Stored as pro-peptide in granules and phagolysosomes of neutrophils (PubMed:7529412, PubMed:9736536). Secreted in sweat onto skin (PubMed:14978112)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7529412"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9736536"}],"value":"Vesicle","id":"SL-0498"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7529412"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7615076"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7890387"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8681941"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8946956"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9736536"}],"value":"Expressed in neutrophilic granulocytes (at protein level) (PubMed:7529412, PubMed:7615076, PubMed:7890387, PubMed:8681941, PubMed:8946956, PubMed:9736536). Expressed in bone marrow (PubMed:7890387)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8681941"}],"value":"Expressed in granulocytes (at protein level) (PubMed:8681941). Expressed by the eccrine apparatus and secreted into sweat on skin (at protein level) (PubMed:14978112)"}],"commentType":"TISSUE SPECIFICITY","molecule":"Antibacterial peptide LL-37"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7529412"}],"value":"Expressed in bone marrow and testis"}],"commentType":"TISSUE SPECIFICITY","molecule":"Antibacterial peptide FALL-39"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23406372"}],"value":"The cathelin-like domain (CLD), which is the propeptide part, does not seem to exhibit auto-inhibitory function, as it does not inhibit the antibacterial activity of antibacterial peptide LL-37"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9736536"}],"value":"Undergoes conformational change in the presence of lipid A, transitioning from a random coil to an alpha-helical structure"}],"commentType":"DOMAIN","molecule":"Antibacterial peptide LL-37"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32753597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35061360"}],"value":"Residues 17-29 of LL-37 represent the active core of the antimicrobial peptide (PubMed:32753597, PubMed:35061360). Forms ribbon-like fibrils and exhibits antibacterial activity against Gram-positive M.luteus (MIC=22-25 uM) and S.hominis (MIC=39 uM) (PubMed:32753597, PubMed:35061360). Also exhibits antibacterial activity against Gram-negative E.coli (MIC=47 uM) and P.fluorescens (MIC=136 uM) (PubMed:35061360)"}],"commentType":"DOMAIN","molecule":"Antibacterial peptide LL-37"},{"texts":[{"value":"The N-terminus is blocked"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11389039"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22879591"}],"value":"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)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10417311"}],"value":"Resistant to proteolytic degradation in solution, and when bound to both zwitterionic (mimicking mammalian membranes) and negatively charged membranes (mimicking bacterial membranes)"}],"commentType":"PTM","molecule":"Antibacterial peptide LL-37"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"value":"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)"}],"commentType":"PTM"},{"commentType":"MASS SPECTROMETRY","molecule":"Antibacterial peptide LL-37","method":"Electrospray","molWeight":4492.9,"molWeightError":0.0,"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23406372"}]},{"commentType":"MASS SPECTROMETRY","method":"Electrospray","molWeight":16424.5,"molWeightError":0.0,"note":"Precursor form pro-cathelicidin.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23406372"}]},{"commentType":"MASS SPECTROMETRY","method":"Electrospray","molWeight":11949.2,"molWeightError":0.0,"note":"Propeptide Cathelin-like domain (CLD).","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23406372"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9736536"}],"value":"The potent activity of antibacterial peptide LL-37 against P.aeruginosa, including mucoid and antibiotic-resistant strains, suggests that the peptide or related molecules might have utility as topical bronchopulmonary microbicides in cystic fibrosis"}],"commentType":"PHARMACEUTICAL"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9736536"}],"value":"The propeptide shows high sequence homology to cathelin, a protein of 96 residues isolated from porcine neutrophils, and is therefore also named cathelin-like domain (CLD) (PubMed:9736536). Cathelin was initially classified into the cystatin family of cysteine protease inhibitors based on its inhibitory activity against cathepsin L (PubMed:9736536). Human CLD itself lacks antimicrobial function and does not inhibit the cysteine protease, cathepsin L (PubMed:9736536)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the cathelicidin family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"PubMed:11238224 sequence was incorrectly assigned to originate from M.mulatta"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Propeptide","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"Cathelin-like domain (CLD)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7615076"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9736536"}],"featureId":"PRO_0000004722"},{"type":"Peptide","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"Antibacterial peptide FALL-39","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7529412"}],"featureId":"PRO_0000004723"},{"type":"Peptide","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"Antibacterial peptide LL-37","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8681941"}],"featureId":"PRO_0000004724"},{"type":"Peptide","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"Antibacterial peptide LL-29","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"featureId":"PRO_0000456769"},{"type":"Peptide","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"Antibacterial peptide LL-23","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"featureId":"PRO_0000456768"},{"type":"Peptide","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"Antibacterial peptide FF-33","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"featureId":"PRO_0000456772"},{"type":"Peptide","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"Antibacterial peptide RK-31","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"featureId":"PRO_0000456771"},{"type":"Peptide","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"Antibacterial peptide KS-30","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"featureId":"PRO_0000456770"},{"type":"Peptide","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"Antibacterial peptide KR-20","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14978112"}],"featureId":"PRO_0000456767"},{"type":"Region","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"Active core","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32753597"}]},{"type":"Disulfide bond","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23406372"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4EYC"}]},{"type":"Disulfide bond","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23406372"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4EYC"}]},{"type":"Mutagenesis","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"Slightly increased MIC against E.coli K12 (MIC=15 compared to MIC=5).","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22185690"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"Slightly increased MIC against E.coli K12 (MIC=25 compared to MIC=5).","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22185690"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["V"]}},{"type":"Mutagenesis","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"Disrupts oligomerization. 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