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   09-DEC-2015, entry version 137.
DE   RecName: Full=Cathelicidin antimicrobial peptide;
DE   AltName: Full=18 kDa cationic antimicrobial protein;
DE            Short=CAP-18;
DE            Short=hCAP-18;
DE   Contains:
DE     RecName: Full=Antibacterial protein FALL-39;
DE     AltName: Full=FALL-39 peptide antibiotic;
DE   Contains:
DE     RecName: Full=Antibacterial protein LL-37;
DE   Flags: Precursor;
GN   Name=CAMP; Synonyms=CAP18, FALL39; ORFNames=HSD26;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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;
RA   Larrick J.W., Hirata M., Balint R.F., Lee J., Zhong J., Wright S.C.;
RT   "Human CAP18: a novel antimicrobial lipopolysaccharide-binding
RT   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.,
RA   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].
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
RT   close 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.,
RA   Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA   Korn B., Zuo D., Hu Y., 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
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
RT   identification of a minimal membrane-targeting antimicrobial and
RT   anticancer region.";
RL   J. Am. Chem. Soc. 128:5776-5785(2006).
RN   [12]
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), has
CC       antibacterial activity. {ECO:0000269|PubMed:16637646,
CC       ECO:0000269|PubMed:18818205}.
CC   -!- INTERACTION:
CC       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   -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
CC   -!- CAUTION: PubMed:11238224 sequence was incorrectly assigned to
CC       originate from M.mulatta. {ECO:0000305}.
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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   PIR; I38932; I38932.
DR   PIR; S74248; S74248.
DR   RefSeq; NP_004336.3; NM_004345.4.
DR   UniGene; Hs.51120; -.
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; 4EYC; X-ray; 1.90 A; A/B=31-133.
DR   PDBsum; 2FBS; -.
DR   PDBsum; 2FBU; -.
DR   PDBsum; 2FCG; -.
DR   PDBsum; 2K6O; -.
DR   PDBsum; 2LMF; -.
DR   PDBsum; 4EYC; -.
DR   DisProt; DP00004; -.
DR   ProteinModelPortal; P49913; -.
DR   SMR; P49913; 31-130, 134-170.
DR   BioGrid; 107270; 2.
DR   IntAct; P49913; 2.
DR   STRING; 9606.ENSP00000458149; -.
DR   TCDB; 1.C.33.1.10; the cathelicidin (cathelicidin) family.
DR   BioMuta; CAMP; -.
DR   DMDM; 1706745; -.
DR   PaxDb; P49913; -.
DR   PRIDE; P49913; -.
DR   DNASU; 820; -.
DR   Ensembl; ENST00000576243; ENSP00000458149; ENSG00000164047.
DR   GeneID; 820; -.
DR   KEGG; hsa:820; -.
DR   CTD; 820; -.
DR   GeneCards; CAMP; -.
DR   HGNC; HGNC:1472; CAMP.
DR   HPA; CAB015949; -.
DR   HPA; CAB016522; -.
DR   HPA; HPA029874; -.
DR   MIM; 600474; gene.
DR   neXtProt; NX_P49913; -.
DR   PharmGKB; PA26054; -.
DR   eggNOG; ENOG410J18R; Eukaryota.
DR   eggNOG; ENOG41119S0; LUCA.
DR   HOGENOM; HOG000093184; -.
DR   HOVERGEN; HBG006116; -.
DR   InParanoid; P49913; -.
DR   KO; K13916; -.
DR   PhylomeDB; P49913; -.
DR   TreeFam; TF338457; -.
DR   Reactome; R-HSA-1222556; ROS production in response to bacteria.
DR   EvolutionaryTrace; P49913; -.
DR   GeneWiki; Cathelicidin; -.
DR   GenomeRNAi; 820; -.
DR   NextBio; 3356; -.
DR   PMAP-CutDB; P49913; -.
DR   PRO; PR:P49913; -.
DR   Proteomes; UP000005640; Unplaced.
DR   Bgee; P49913; -.
DR   CleanEx; HS_CAMP; -.
DR   GO; GO:0005618; C:cell wall; TAS:Reactome.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005622; C:intracellular; IDA:UniProtKB.
DR   GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR   GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR   GO; GO:0019732; P:antifungal humoral response; IDA:UniProtKB.
DR   GO; GO:0002544; P:chronic inflammatory response; IMP:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; TAS:ProtInc.
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:MGI.
DR   GO; GO:0044140; P:negative regulation of growth of symbiont on or near host surface; IDA:MGI.
DR   GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR   GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IMP:UniProtKB.
DR   GO; GO:0001878; P:response to yeast; IDA:UniProtKB.
DR   InterPro; IPR001894; Cathelicidin.
DR   InterPro; IPR018216; Cathelicidin_CS.
DR   InterPro; IPR022746; Cathlecidin_C.
DR   Pfam; PF12153; CAP18_C; 1.
DR   Pfam; PF00666; Cathelicidins; 1.
DR   ProDom; PD001838; Cathelicidin; 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; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL        1     30       {ECO:0000255}.
FT   PROPEP       31    131
FT                                /FTId=PRO_0000004722.
FT   CHAIN       132    170       Antibacterial protein FALL-39.
FT                                /FTId=PRO_0000004723.
FT   CHAIN       134    170       Antibacterial protein LL-37.
FT                                /FTId=PRO_0000004724.
FT   DISULFID     86     97       {ECO:0000250}.
FT   DISULFID    108    125       {ECO:0000250}.
FT   CONFLICT      6      6       D -> N (in Ref. 1, 6, 7 and 9; CAG46759).
FT                                {ECO:0000305}.
FT   HELIX        35     49       {ECO:0000244|PDB:4EYC}.
FT   STRAND       53     61       {ECO:0000244|PDB:4EYC}.
FT   STRAND       75     87       {ECO:0000244|PDB:4EYC}.
FT   HELIX        94     96       {ECO:0000244|PDB:4EYC}.
FT   STRAND      105    112       {ECO:0000244|PDB:4EYC}.
FT   STRAND      122    126       {ECO:0000244|PDB:4EYC}.
FT   HELIX       136    140       {ECO:0000244|PDB:2FBU}.
FT   HELIX       151    161       {ECO:0000244|PDB:2FBS}.
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
//