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Cathelicidin antimicrobial peptide (18 kDa cationic antimicrobial protein) (CAP-18) (hCAP-18) [Cleaved into: Antibacterial peptide FALL-39 (FALL-39 peptide antibiotic); Antibacterial peptide LL-37]

 CAMP_HUMAN              Reviewed;         170 AA.
P49913; Q71SN9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
30-AUG-2017, entry version 152.
RecName: Full=Cathelicidin antimicrobial peptide {ECO:0000312|HGNC:HGNC:1472};
AltName: Full=18 kDa cationic antimicrobial protein {ECO:0000303|PubMed:7615076};
Short=CAP-18 {ECO:0000303|PubMed:7615076};
Short=hCAP-18 {ECO:0000303|PubMed:7615076};
Contains:
RecName: Full=Antibacterial peptide FALL-39 {ECO:0000303|PubMed:7529412};
AltName: Full=FALL-39 peptide antibiotic {ECO:0000303|PubMed:7529412};
Contains:
RecName: Full=Antibacterial peptide LL-37 {ECO:0000303|PubMed:8681941};
Flags: Precursor;
Name=CAMP {ECO:0000312|HGNC:HGNC:1472};
Synonyms=CAP18 {ECO:0000303|PubMed:8946956},
FALL39 {ECO:0000303|PubMed:7529412}; ORFNames=HSD26;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SYNTHESIS OF 132-170.
TISSUE=Bone marrow;
PubMed=7529412; DOI=10.1073/pnas.92.1.195;
Agerberth B., Gunne H., Odeberg J., Kogner P., Boman H.G.,
Gudmundsson G.H.;
"FALL-39, a putative human peptide antibiotic, is cysteine-free and
expressed in bone marrow and testis.";
Proc. Natl. Acad. Sci. U.S.A. 92:195-199(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 42-68 AND 83-100.
TISSUE=Bone marrow;
PubMed=7615076; DOI=10.1016/0014-5793(95)00634-L;
Cowland J.B., Johnsen A.H., Borregaard N.;
"hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil
specific granules.";
FEBS Lett. 368:173-176(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Bone marrow;
PubMed=7890387;
Larrick J.W., Hirata M., Balint R.F., Lee J., Zhong J., Wright S.C.;
"Human CAP18: a novel antimicrobial lipopolysaccharide-binding
protein.";
Infect. Immun. 63:1291-1297(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8946956; DOI=10.1016/S0014-5793(96)01199-4;
Larrick J.W., Lee J., Ma S., Li X., Francke U., Wright S.C.,
Balint R.F.;
"Structural, functional analysis and localization of the human CAP18
gene.";
FEBS Lett. 398:74-80(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 134-143.
PubMed=8681941; DOI=10.1111/j.1432-1033.1996.0325z.x;
Gudmundsson G.H., Agerberth B., Odeberg J., Bergman T., Olsson B.,
Salcedo R.;
"The human gene FALL39 and processing of the cathelin precursor to the
antibacterial peptide LL-37 in granulocytes.";
Eur. J. Biochem. 238:325-332(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Epididymis;
Gao Y., Huang Y.F., Xia X.Y.;
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
Wu N., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.;
"A new spermatogenesis-related gene.";
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11238224; DOI=10.1128/CDLI.8.2.370-375.2001;
Bals R., Lang C., Weiner D.J., Vogelmeier C., Welsch U., Wilson J.M.;
"Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are
close homologues of human molecules.";
Clin. Diagn. Lab. Immunol. 8:370-375(2001).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
STRUCTURE BY NMR OF 146-170, AND FUNCTION.
PubMed=16637646; DOI=10.1021/ja0584875;
Li X., Li Y., Han H., Miller D.W., Wang G.;
"Solution structures of human LL-37 fragments and NMR-based
identification of a minimal membrane-targeting antimicrobial and
anticancer region.";
J. Am. Chem. Soc. 128:5776-5785(2006).
[12]
STRUCTURE BY NMR OF 134-170, AND FUNCTION.
PubMed=18818205; DOI=10.1074/jbc.M805533200;
Wang G.;
"Structures of human host defense cathelicidin LL-37 and its smallest
antimicrobial peptide KR-12 in lipid micelles.";
J. Biol. Chem. 283:32637-32643(2008).
-!- FUNCTION: Binds to bacterial lipopolysaccharides (LPS), has
antibacterial activity. {ECO:0000269|PubMed:16637646,
ECO:0000269|PubMed:18818205}.
-!- INTERACTION:
P08069:IGF1R; NbExp=3; IntAct=EBI-6378485, EBI-475981;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed in bone marrow and testis and
neutrophils.
-!- PTM: The N-terminus is blocked.
-!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
-!- CAUTION: PubMed:11238224 sequence was incorrectly assigned to
originate from M.mulatta. {ECO:0000305}.
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EMBL; Z38026; CAA86115.1; -; mRNA.
EMBL; X89658; CAA61805.1; -; mRNA.
EMBL; U19970; AAA74084.1; -; mRNA.
EMBL; U48795; AAC02634.1; -; Genomic_DNA.
EMBL; X96735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY162210; AAN78318.1; -; mRNA.
EMBL; AY251531; AAP20054.1; -; mRNA.
EMBL; AF288284; AAG40802.1; -; mRNA.
EMBL; CR457083; CAG33364.1; -; mRNA.
EMBL; CR541961; CAG46759.1; -; mRNA.
EMBL; BC055089; AAH55089.1; -; mRNA.
PIR; I38932; I38932.
PIR; S74248; S74248.
RefSeq; NP_004336.3; NM_004345.4.
UniGene; Hs.51120; -.
PDB; 2FBS; NMR; -; N=150-162.
PDB; 2FBU; NMR; -; H=134-145.
PDB; 2FCG; NMR; -; F=146-170.
PDB; 2K6O; NMR; -; A=134-170.
PDB; 2LMF; NMR; -; A=134-156.
PDB; 2NA3; NMR; -; A=151-162.
PDB; 4EYC; X-ray; 1.90 A; A/B=31-133.
PDBsum; 2FBS; -.
PDBsum; 2FBU; -.
PDBsum; 2FCG; -.
PDBsum; 2K6O; -.
PDBsum; 2LMF; -.
PDBsum; 2NA3; -.
PDBsum; 4EYC; -.
DisProt; DP00004; -.
ProteinModelPortal; P49913; -.
SMR; P49913; -.
BioGrid; 107270; 2.
IntAct; P49913; 2.
STRING; 9606.ENSP00000458149; -.
DrugBank; DB02345; Selenocysteine.
TCDB; 1.C.33.1.10; the cathelicidin (cathelicidin) family.
iPTMnet; P49913; -.
PhosphoSitePlus; P49913; -.
BioMuta; CAMP; -.
DMDM; 1706745; -.
PaxDb; P49913; -.
PeptideAtlas; P49913; -.
PRIDE; P49913; -.
DNASU; 820; -.
Ensembl; ENST00000576243; ENSP00000458149; ENSG00000164047.
GeneID; 820; -.
KEGG; hsa:820; -.
CTD; 820; -.
DisGeNET; 820; -.
GeneCards; CAMP; -.
HGNC; HGNC:1472; CAMP.
HPA; HPA029874; -.
MIM; 600474; gene.
neXtProt; NX_P49913; -.
PharmGKB; PA26054; -.
eggNOG; ENOG410J18R; Eukaryota.
eggNOG; ENOG41119S0; LUCA.
HOGENOM; HOG000093184; -.
HOVERGEN; HBG006116; -.
InParanoid; P49913; -.
KO; K13916; -.
PhylomeDB; P49913; -.
TreeFam; TF338457; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6803157; Antimicrobial peptides.
SIGNOR; P49913; -.
EvolutionaryTrace; P49913; -.
GeneWiki; Cathelicidin; -.
GenomeRNAi; 820; -.
PMAP-CutDB; P49913; -.
PRO; PR:P49913; -.
Proteomes; UP000005640; Unplaced.
CleanEx; HS_CAMP; -.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0042581; C:specific granule; IDA:UniProtKB.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
GO; GO:0019732; P:antifungal humoral response; IDA:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0002544; P:chronic inflammatory response; IMP:UniProtKB.
GO; GO:0051838; P:cytolysis by host of symbiont cells; IDA:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0002227; P:innate immune response in mucosa; IDA:UniProtKB.
GO; GO:0051873; P:killing by host of symbiont cells; IDA:MGI.
GO; GO:0035821; P:modification of morphology or physiology of other organism; IDA:UniProtKB.
GO; GO:0044140; P:negative regulation of growth of symbiont on or near host surface; IDA:MGI.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IMP:UniProtKB.
GO; GO:0001878; P:response to yeast; IDA:UniProtKB.
InterPro; IPR001894; Cathelicidin.
InterPro; IPR018216; Cathelicidin_CS.
InterPro; IPR022746; Cathlecidin_C.
PANTHER; PTHR10206; PTHR10206; 1.
Pfam; PF12153; CAP18_C; 1.
PROSITE; PS00946; CATHELICIDINS_1; 1.
PROSITE; PS00947; CATHELICIDINS_2; 1.
1: Evidence at protein level;
3D-structure; Antibiotic; Antimicrobial;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Reference proteome;
Secreted; Signal.
SIGNAL 1 30 {ECO:0000255}.
PROPEP 31 131 {ECO:0000269|PubMed:7615076}.
/FTId=PRO_0000004722.
PEPTIDE 132 170 Antibacterial peptide FALL-39.
{ECO:0000269|PubMed:7529412}.
/FTId=PRO_0000004723.
PEPTIDE 134 170 Antibacterial peptide LL-37.
{ECO:0000269|PubMed:8681941}.
/FTId=PRO_0000004724.
DISULFID 86 97 {ECO:0000250}.
DISULFID 108 125 {ECO:0000250}.
CONFLICT 6 6 D -> N (in Ref. 1, 6, 7 and 9; CAG46759).
{ECO:0000305}.
HELIX 35 49 {ECO:0000244|PDB:4EYC}.
STRAND 53 61 {ECO:0000244|PDB:4EYC}.
STRAND 75 87 {ECO:0000244|PDB:4EYC}.
HELIX 94 96 {ECO:0000244|PDB:4EYC}.
STRAND 105 112 {ECO:0000244|PDB:4EYC}.
STRAND 122 126 {ECO:0000244|PDB:4EYC}.
HELIX 136 140 {ECO:0000244|PDB:2FBU}.
HELIX 151 161 {ECO:0000244|PDB:2FBS}.
SEQUENCE 170 AA; 19301 MW; 055B07DCA95A7D16 CRC64;
MKTQRDGHSL GRWSLVLLLL GLVMPLAIIA QVLSYKEAVL RAIDGINQRS SDANLYRLLD
LDPRPTMDGD PDTPKPVSFT VKETVCPRTT QQSPEDCDFK KDGLVKRCMG TVTLNQARGS
FDISCDKDNK RFALLGDFFR KSKEKIGKEF KRIVQRIKDF LRNLVPRTES


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