ID   CAMP_MACMU              Reviewed;         170 AA.
AC   Q9GLV5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Cathelicidin antimicrobial peptide {ECO:0000250|UniProtKB:P49913};
DE   AltName: Full=18 kDa cationic antimicrobial protein {ECO:0000250|UniProtKB:P49913};
DE   AltName: Full=CAP-18 {ECO:0000250|UniProtKB:P49913};
DE   AltName: Full=rhCAP-18 {ECO:0000303|PubMed:11238224};
DE   Contains:
DE     RecName: Full=Antibacterial peptide FALL-39 {ECO:0000250|UniProtKB:P49913};
DE     AltName: Full=FALL-39 peptide antibiotic {ECO:0000250|UniProtKB:P49913};
DE   Contains:
DE     RecName: Full=Antibacterial peptide LL-37 {ECO:0000250|UniProtKB:P49913};
DE     AltName: Full=rhLL-37 {ECO:0000303|PubMed:11238224};
DE              Short=RL-37 {ECO:0000303|PubMed:11557457};
DE   Flags: Precursor;
GN   Name=CAMP; Synonyms=CAP18, FALL39;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=11557457; DOI=10.1128/aac.45.10.2695-2702.2001;
RA   Zhao C., Nguyen T., Boo L.M., Hong T., Espiritu C., Orlov D., Wang W.,
RA   Waring A., Lehrer R.I.;
RT   "RL-37, an alpha-helical antimicrobial peptide of the rhesus monkey.";
RL   Antimicrob. Agents Chemother. 45:2695-2702(2001).
RN   [2]
RP   TISSUE SPECIFICITY.
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).
CC   -!- FUNCTION: Binds to bacterial lipopolysaccharides (LPS) and has
CC       antibacterial activity. Acts via neutrophil N-formyl peptide receptors
CC       to enhance the release of CXCL2. {ECO:0000250|UniProtKB:P49913}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in epithelia of various organs. Most
CC       abundant peptide levels are found in organs lining outer or inner body
CC       surfaces, such as organs of the respiratory or gastrointestinal tract.
CC       {ECO:0000269|PubMed:11238224}.
CC   -!- PTM: Proteolytically cleaved by cathepsin CTSG.
CC       {ECO:0000250|UniProtKB:P49913}.
CC   -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR   EMBL; AF181954; AAG09440.1; -; mRNA.
DR   RefSeq; NP_001028681.1; NM_001033509.2.
DR   AlphaFoldDB; Q9GLV5; -.
DR   SMR; Q9GLV5; -.
DR   STRING; 9544.ENSMMUP00000013960; -.
DR   GeneID; 619186; -.
DR   KEGG; mcc:619186; -.
DR   CTD; 820; -.
DR   eggNOG; ENOG502SAES; Eukaryota.
DR   InParanoid; Q9GLV5; -.
DR   OrthoDB; 1534863at2759; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IBA:GO_Central.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0042119; P:neutrophil activation; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   PROPEP          31..131
FT                   /evidence="ECO:0000250|UniProtKB:P49913"
FT                   /id="PRO_0000251767"
FT   PEPTIDE         132..170
FT                   /note="Antibacterial peptide FALL-39"
FT                   /evidence="ECO:0000250|UniProtKB:P49913"
FT                   /id="PRO_0000251768"
FT   PEPTIDE         134..170
FT                   /note="Antibacterial peptide LL-37"
FT                   /evidence="ECO:0000250|UniProtKB:P49913"
FT                   /id="PRO_0000251769"
SQ   SEQUENCE   170 AA;  18861 MW;  355AB3BF510DBB83 CRC64;
     MKTQRNGPSL GRWSLVLLLL GLVMPLAIVA QVLSYQEAVL RAIDGINQRS SDANLYRLLD
     LDPRPTMDGD PDTPKPVSFT VKETVCPRTT QKSPEDCDFK EDGLVKRCVG TVILNQARDS
     FDISCDKDNR RSARLGNFFR KVKEKIGGGL KKVGQKIKDF LGNLVPRTAS