Cathelicidin antimicrobial peptide

Details

Name
Cathelicidin antimicrobial peptide
Synonyms
  • 18 kDa cationic antimicrobial protein
  • CAP-18
  • CAP18
  • FALL39
  • hCAP-18
Gene Name
CAMP
Organism
Humans
Amino acid sequence
>lcl|BSEQ0013177|Cathelicidin antimicrobial peptide
MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLD
LDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGS
FDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
Number of residues
170
Molecular Weight
19301.175
Theoretical pI
Not Available
GO Classification
Processes
antibacterial humoral response / antifungal humoral response / chronic inflammatory response / defense response to bacterium / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / innate immune response / innate immune response in mucosa / killing by host of symbiont cells / negative regulation of growth of symbiont on or near host surface / phagosome maturation / positive regulation of interleukin-8 secretion / response to yeast
Components
cell wall / cytosol / extracellular exosome / extracellular space / intracellular / specific granule
General Function
Not Available
Specific Function
Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0013178|Cathelicidin antimicrobial peptide (CAMP)
ATGGGGACCATGAAGACCCAAAGGGATGGCCACTCCCTGGGGCGGTGGTCACTGGTGCTC
CTGCTGCTGGGCCTGGTGATGCCTCTGGCCATCATTGCCCAGGTCCTCAGCTACAAGGAA
GCTGTGCTTCGTGCTATAGATGGCATCAACCAGCGGTCCTCGGATGCTAACCTCTACCGC
CTCCTGGACCTGGACCCCAGGCCCACGATGGATGGGGACCCAGACACGCCAAAGCCTGTG
AGCTTCACAGTGAAGGAGACAGTGTGCCCCAGGACGACACAGCAGTCACCAGAGGATTGT
GACTTCAAGAAGGACGGGCTGGTGAAGCGGTGTATGGGGACAGTGACCCTCAACCAGGCC
AGGGGCTCCTTTGACATCAGTTGTGATAAGGATAACAAGAGATTTGCCCTGCTGGGTGAT
TTCTTCCGGAAATCTAAAGAGAAGATTGGCAAAGAGTTTAAAAGAATTGTCCAGAGAATC
AAGGATTTTTTGCGGAATCTTGTACCCAGGACAGAGTCCTAG
Chromosome Location
3
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP49913
UniProtKB Entry NameCAMP_HUMAN
HGNC IDHGNC:1472
General References
  1. Agerberth B, Gunne H, Odeberg J, Kogner P, Boman HG, Gudmundsson GH: FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis. Proc Natl Acad Sci U S A. 1995 Jan 3;92(1):195-9. [Article]
  2. Cowland JB, Johnsen AH, Borregaard N: hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil specific granules. FEBS Lett. 1995 Jul 10;368(1):173-6. [Article]
  3. Larrick JW, Hirata M, Balint RF, Lee J, Zhong J, Wright SC: Human CAP18: a novel antimicrobial lipopolysaccharide-binding protein. Infect Immun. 1995 Apr;63(4):1291-7. [Article]
  4. Larrick JW, Lee J, Ma S, Li X, Francke U, Wright SC, Balint RF: Structural, functional analysis and localization of the human CAP18 gene. FEBS Lett. 1996 Nov 25;398(1):74-80. [Article]
  5. Gudmundsson GH, 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. 1996 Jun 1;238(2):325-32. [Article]
  6. Bals R, Lang C, Weiner DJ, Vogelmeier C, Welsch U, Wilson JM: Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules. Clin Diagn Lab Immunol. 2001 Mar;8(2):370-5. [Article]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  8. Li X, Li Y, Han H, Miller DW, 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. 2006 May 3;128(17):5776-85. [Article]
  9. Wang G: Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles. J Biol Chem. 2008 Nov 21;283(47):32637-43. doi: 10.1074/jbc.M805533200. Epub 2008 Sep 25. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02345SelenocysteineexperimentalunknownDetails