CAMP_HUMAN
ID CAMP_HUMAN Reviewed; 170 AA.
AC P49913; Q71SN9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Cathelicidin antimicrobial peptide {ECO:0000312|HGNC:HGNC:1472};
DE AltName: Full=18 kDa cationic antimicrobial protein {ECO:0000303|PubMed:7615076};
DE Short=CAP-18 {ECO:0000303|PubMed:7615076};
DE Short=hCAP-18 {ECO:0000303|PubMed:7615076};
DE Contains:
DE RecName: Full=Antibacterial peptide FALL-39 {ECO:0000303|PubMed:7529412};
DE AltName: Full=FALL-39 peptide antibiotic {ECO:0000303|PubMed:7529412};
DE Contains:
DE RecName: Full=Antibacterial peptide LL-37 {ECO:0000303|PubMed:8681941};
DE Flags: Precursor;
GN Name=CAMP {ECO:0000312|HGNC:HGNC:1472};
GN Synonyms=CAP18 {ECO:0000303|PubMed:8946956},
GN FALL39 {ECO:0000303|PubMed:7529412}; ORFNames=HSD26;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SYNTHESIS OF 132-170.
RC TISSUE=Bone marrow;
RX PubMed=7529412; DOI=10.1073/pnas.92.1.195;
RA Agerberth B., Gunne H., Odeberg J., Kogner P., Boman H.G.,
RA Gudmundsson G.H.;
RT "FALL-39, a putative human peptide antibiotic, is cysteine-free and
RT expressed in bone marrow and testis.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:195-199(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 42-68 AND 83-100.
RC TISSUE=Bone marrow;
RX PubMed=7615076; DOI=10.1016/0014-5793(95)00634-l;
RA Cowland J.B., Johnsen A.H., Borregaard N.;
RT "hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil
RT specific granules.";
RL FEBS Lett. 368:173-176(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7890387; DOI=10.1128/iai.63.4.1291-1297.1995;
RA Larrick J.W., Hirata M., Balint R.F., Lee J., Zhong J., Wright S.C.;
RT "Human CAP18: a novel antimicrobial lipopolysaccharide-binding protein.";
RL Infect. Immun. 63:1291-1297(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8946956; DOI=10.1016/s0014-5793(96)01199-4;
RA Larrick J.W., Lee J., Ma S., Li X., Francke U., Wright S.C., Balint R.F.;
RT "Structural, functional analysis and localization of the human CAP18
RT gene.";
RL FEBS Lett. 398:74-80(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 134-143.
RX PubMed=8681941; DOI=10.1111/j.1432-1033.1996.0325z.x;
RA Gudmundsson G.H., Agerberth B., Odeberg J., Bergman T., Olsson B.,
RA Salcedo R.;
RT "The human gene FALL39 and processing of the cathelin precursor to the
RT antibacterial peptide LL-37 in granulocytes.";
RL Eur. J. Biochem. 238:325-332(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epididymis;
RA Gao Y., Huang Y.F., Xia X.Y.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RA Wu N., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.;
RT "A new spermatogenesis-related gene.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11238224; DOI=10.1128/cdli.8.2.370-375.2001;
RA Bals R., Lang C., Weiner D.J., Vogelmeier C., Welsch U., Wilson J.M.;
RT "Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close
RT homologues of human molecules.";
RL Clin. Diagn. Lab. Immunol. 8:370-375(2001).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=22879591; DOI=10.1074/jbc.m112.394452;
RA Woloszynek J.C., Hu Y., Pham C.T.;
RT "Cathepsin G-regulated release of formyl peptide receptor agonists modulate
RT neutrophil effector functions.";
RL J. Biol. Chem. 287:34101-34109(2012).
RN [12]
RP STRUCTURE BY NMR OF 146-170, AND FUNCTION.
RX PubMed=16637646; DOI=10.1021/ja0584875;
RA Li X., Li Y., Han H., Miller D.W., Wang G.;
RT "Solution structures of human LL-37 fragments and NMR-based identification
RT of a minimal membrane-targeting antimicrobial and anticancer region.";
RL J. Am. Chem. Soc. 128:5776-5785(2006).
RN [13]
RP STRUCTURE BY NMR OF 134-170, AND FUNCTION.
RX PubMed=18818205; DOI=10.1074/jbc.m805533200;
RA Wang G.;
RT "Structures of human host defense cathelicidin LL-37 and its smallest
RT antimicrobial peptide KR-12 in lipid micelles.";
RL J. Biol. Chem. 283:32637-32643(2008).
CC -!- FUNCTION: Binds to bacterial lipopolysaccharides (LPS) and has
CC antibacterial activity (PubMed:16637646, PubMed:18818205). Acts via
CC neutrophil N-formyl peptide receptors to enhance the release of CXCL2
CC (PubMed:22879591). {ECO:0000269|PubMed:16637646,
CC ECO:0000269|PubMed:18818205, ECO:0000269|PubMed:22879591}.
CC -!- INTERACTION:
CC PRO_0000004724; P08069: IGF1R; NbExp=3; IntAct=EBI-6378485, EBI-475981;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow and testis and
CC neutrophils.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Proteolytically cleaved by cathepsin CTSG.
CC {ECO:0000269|PubMed:22879591}.
CC -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
CC -!- CAUTION: PubMed:11238224 sequence was incorrectly assigned to originate
CC from M.mulatta. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z38026; CAA86115.1; -; mRNA.
DR EMBL; X89658; CAA61805.1; -; mRNA.
DR EMBL; U19970; AAA74084.1; -; mRNA.
DR EMBL; U48795; AAC02634.1; -; Genomic_DNA.
DR EMBL; X96735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY162210; AAN78318.1; -; mRNA.
DR EMBL; AY251531; AAP20054.1; -; mRNA.
DR EMBL; AF288284; AAG40802.1; -; mRNA.
DR EMBL; CR457083; CAG33364.1; -; mRNA.
DR EMBL; CR541961; CAG46759.1; -; mRNA.
DR EMBL; BC055089; AAH55089.1; -; mRNA.
DR CCDS; CCDS2762.2; -.
DR PIR; I38932; I38932.
DR PIR; S74248; S74248.
DR RefSeq; NP_004336.3; NM_004345.4.
DR PDB; 2FBS; NMR; -; N=150-162.
DR PDB; 2FBU; NMR; -; H=134-145.
DR PDB; 2FCG; NMR; -; F=146-170.
DR PDB; 2K6O; NMR; -; A=134-170.
DR PDB; 2LMF; NMR; -; A=134-156.
DR PDB; 2NA3; NMR; -; A=151-162.
DR PDB; 4EYC; X-ray; 1.90 A; A/B=31-133.
DR PDB; 5NMN; X-ray; 0.95 A; A=134-170.
DR PDB; 5NNK; X-ray; 1.80 A; A=134-170.
DR PDB; 5NNM; X-ray; 1.90 A; A/B=134-170.
DR PDB; 5NNT; X-ray; 2.21 A; A/B=134-170.
DR PDB; 5XNG; NMR; -; A=149-165.
DR PDB; 5XRX; NMR; -; A=149-165.
DR PDB; 6BIV; X-ray; 2.90 A; C=83-95.
DR PDB; 6BIX; X-ray; 2.20 A; C=83-95.
DR PDB; 6S6M; X-ray; 1.35 A; A/B=150-162.
DR PDB; 6S6N; X-ray; 1.10 A; A/B=150-162.
DR PDB; 7NPQ; X-ray; 1.50 A; A/B=150-162.
DR PDB; 7PDC; X-ray; 1.83 A; A/B=134-170.
DR PDBsum; 2FBS; -.
DR PDBsum; 2FBU; -.
DR PDBsum; 2FCG; -.
DR PDBsum; 2K6O; -.
DR PDBsum; 2LMF; -.
DR PDBsum; 2NA3; -.
DR PDBsum; 4EYC; -.
DR PDBsum; 5NMN; -.
DR PDBsum; 5NNK; -.
DR PDBsum; 5NNM; -.
DR PDBsum; 5NNT; -.
DR PDBsum; 5XNG; -.
DR PDBsum; 5XRX; -.
DR PDBsum; 6BIV; -.
DR PDBsum; 6BIX; -.
DR PDBsum; 6S6M; -.
DR PDBsum; 6S6N; -.
DR PDBsum; 7NPQ; -.
DR PDBsum; 7PDC; -.
DR AlphaFoldDB; P49913; -.
DR BMRB; P49913; -.
DR SMR; P49913; -.
DR BioGRID; 107270; 17.
DR IntAct; P49913; 2.
DR STRING; 9606.ENSP00000296435; -.
DR DrugBank; DB02345; Selenocysteine.
DR TCDB; 1.C.33.1.10; the cathelicidin (cathelicidin) family.
DR GlyGen; P49913; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; P49913; -.
DR PhosphoSitePlus; P49913; -.
DR BioMuta; CAMP; -.
DR DMDM; 1706745; -.
DR jPOST; P49913; -.
DR MassIVE; P49913; -.
DR PaxDb; P49913; -.
DR PeptideAtlas; P49913; -.
DR PRIDE; P49913; -.
DR ProteomicsDB; 56178; -.
DR ABCD; P49913; 13 sequenced antibodies.
DR Antibodypedia; 13077; 428 antibodies from 35 providers.
DR DNASU; 820; -.
DR Ensembl; ENST00000652295.2; ENSP00000498425.1; ENSG00000164047.6.
DR GeneID; 820; -.
DR KEGG; hsa:820; -.
DR MANE-Select; ENST00000652295.2; ENSP00000498425.1; NM_004345.5; NP_004336.4.
DR CTD; 820; -.
DR DisGeNET; 820; -.
DR GeneCards; CAMP; -.
DR HGNC; HGNC:1472; CAMP.
DR HPA; ENSG00000164047; Tissue enriched (bone).
DR MIM; 600474; gene.
DR neXtProt; NX_P49913; -.
DR OpenTargets; ENSG00000164047; -.
DR PharmGKB; PA26054; -.
DR VEuPathDB; HostDB:ENSG00000164047; -.
DR eggNOG; ENOG502SAES; Eukaryota.
DR GeneTree; ENSGT00390000000410; -.
DR InParanoid; P49913; -.
DR OrthoDB; 1534863at2759; -.
DR PhylomeDB; P49913; -.
DR TreeFam; TF338457; -.
DR BioCyc; MetaCyc:ENSG00000164047-MON; -.
DR PathwayCommons; P49913; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6803157; Antimicrobial peptides.
DR SignaLink; P49913; -.
DR SIGNOR; P49913; -.
DR BioGRID-ORCS; 820; 12 hits in 1070 CRISPR screens.
DR EvolutionaryTrace; P49913; -.
DR GeneWiki; Cathelicidin; -.
DR GenomeRNAi; 820; -.
DR Pharos; P49913; Tbio.
DR PRO; PR:P49913; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P49913; protein.
DR Bgee; ENSG00000164047; Expressed in trabecular bone tissue and 116 other tissues.
DR ExpressionAtlas; P49913; baseline and differential.
DR GO; GO:0042995; C:cell projection; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0001530; F:lipopolysaccharide binding; IBA:GO_Central.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0019732; P:antifungal humoral response; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071224; P:cellular response to peptidoglycan; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0002544; P:chronic inflammatory response; IMP:UniProtKB.
DR GO; GO:0051838; P:cytolysis by host of symbiont cells; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; IDA:UniProtKB.
DR GO; GO:0051873; P:killing by host of symbiont cells; IDA:CACAO.
DR GO; GO:0035821; P:modulation of process of another organism; IDA:UniProtKB.
DR GO; GO:0042119; P:neutrophil activation; IDA:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0001878; P:response to yeast; IDA:UniProtKB.
DR DisProt; DP00004; -.
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; PS00946; CATHELICIDINS_1; 1.
DR PROSITE; PS00947; CATHELICIDINS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..131
FT /evidence="ECO:0000269|PubMed:7615076"
FT /id="PRO_0000004722"
FT PEPTIDE 132..170
FT /note="Antibacterial peptide FALL-39"
FT /evidence="ECO:0000269|PubMed:7529412"
FT /id="PRO_0000004723"
FT PEPTIDE 134..170
FT /note="Antibacterial peptide LL-37"
FT /evidence="ECO:0000269|PubMed:8681941"
FT /id="PRO_0000004724"
FT DISULFID 86..97
FT /evidence="ECO:0000250"
FT DISULFID 108..125
FT /evidence="ECO:0000250"
FT CONFLICT 6
FT /note="D -> N (in Ref. 1, 6, 7 and 9; CAG46759)"
FT /evidence="ECO:0000305"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:4EYC"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:4EYC"
FT STRAND 75..87
FT /evidence="ECO:0007829|PDB:4EYC"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:4EYC"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:4EYC"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:4EYC"
FT HELIX 135..163
FT /evidence="ECO:0007829|PDB:5NMN"
SQ SEQUENCE 170 AA; 19301 MW; 055B07DCA95A7D16 CRC64;
MKTQRDGHSL GRWSLVLLLL GLVMPLAIIA QVLSYKEAVL RAIDGINQRS SDANLYRLLD
LDPRPTMDGD PDTPKPVSFT VKETVCPRTT QQSPEDCDFK KDGLVKRCMG TVTLNQARGS
FDISCDKDNK RFALLGDFFR KSKEKIGKEF KRIVQRIKDF LRNLVPRTES
