AMPDB_215 | Cathelicidin antimicrobial peptide
PEPTIDE SUMMARY
Cathelicidin antimicrobial peptide
1 General Description
AMPDB ID: AMPDB_215
Protein Names: 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; Antibacterial peptide KR-20; Antibacterial peptide LL-23; Antibacterial peptide LL-29; Antibacterial peptide KS-30; Antibacterial peptide RK-31; Antibacterial peptide FF-33]
Protein Family: Cathelicidin family
Gene Name: CAMP CAP18 FALL39 HSD26
Source Organism: Homo sapiens (Human)
Protein Length: 170 AA
Protein Existence: Evidence at protein level
2 Protein Sequence & Composition
2.1 Sequence
MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
FASTA format
2.2 Composition
Counts of Amino Acids
'A': 7, 'R': 15, 'N': 5, 'D': 16, 'C': 4, 'Q': 7, 'E': 6, 'G': 10, 'H': 1, 'I': 8, 'L': 20, 'K': 15, 'M': 4, 'F': 8, 'P': 9, 'S': 11, 'T': 10, 'W': 1, 'Y': 2, 'V': 11
Frequencies of Amino Acids
'A': 4.12%, 'R': 8.82%, 'N': 2.94%, 'D': 9.41%, 'C': 2.35%, 'Q': 4.12%, 'E': 3.53%, 'G': 5.88%, 'H': 0.59%, 'I': 4.71%, 'L': 11.76%, 'K': 8.82%, 'M': 2.35%, 'F': 4.71%, 'P': 5.29%, 'S': 6.47%, 'T': 5.88%, 'W': 0.59%, 'Y': 1.18%, 'V': 6.47%
Missing Amino Acid(s)
No Amino Acid(s) are missing in this protein
Most Occurring Amino Acid(s)
L
Less Occurring Amino Acid(s)
H, W
Hydrophobic Amino Acid(s) Count
78
Hydrophilic Amino Acid(s) Count
92
Basic Amino Acid(s) Count
22
Acidic Amino Acid(s) Count
31
Modified Amino Acid(s) Count
0
Modified Amino Acid(s) Frequencies
0
Computed by biopython (version 1.79) & proteinAnalysis (version 1)
3 Physicochemical Properties
Sl. No. Properties Values Reference
1. Molecular Mass 19301.4 Da Computed by ProtParam module (biopython 1.79)
2. Aliphatic Index 87.118 Computed by ProtParam module (biopython 1.79)
3. Instability Index (Half Life) 37.587 Computed by ProtParam module (biopython 1.79)
4. Hydrophobicity (GRAVY) -0.442 Computed by ProtParam module (biopython 1.79)
5. Hydrophobic Moment 0.966 Computed by ProtParam module (biopython 1.79)
6. Isoelectric Point 10.031 Computed by ProtParam module (biopython 1.79)
7. Charge (at pH 7) 7.853 Computed by ProtParam module (biopython 1.79)
8. Secondary Structure Fraction 0.294, 0.206, 0.218 [Helix, Turn, Sheet] Computed by ProtParam module (biopython 1.79)
9. Aromaticity 0.065 Computed by ProtParam module (biopython 1.79)
10. Molar Extinction Coefficient (cysteine|cystine) 8480, 8730 Computed by ProtParam module (biopython 1.79)
4 Activity Details
4.1 Target Organism(s)
B.megaterium, C.albicans, E.coli (Gram-negative), L.monocytogenes (Gram-positive), P.aeruginosa (Gram-negative), P.syringae (Gram-negative), S.aureus (Gram-positive), S.epidermidis (Gram-positive), S.pyogenes (Gram-positive), S.typhimurium
4.2 Antimicrobial Activity
Antibiotic, Antimicrobial, Anti-MRSA, Anti-biofilm, Anti-candida, Anti-gram-negative, Anti-gram-Positive
4.3 Enzymatic Activity
Not found
4.4 Inhibitory Effect
Not found
4.5 Other Biological Activity
Hemolytic, Signal peptide, Synergistic peptide, Non-ribosomal
Activity data manually curated from Literature and UniProt
5 Database Cross-references
5.1 Literature Database
5.1.1 PubMed
Citation 1: Agerberth B, Gunne H, Odeberg J, et al. 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;92(1):195-9. Published 1995 Jan 3. doi:10.1073/pnas.92.1.195
PMID: 7529412
Citation 2: Cowland JB, Johnsen AH, Borregaard N, et al. hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil specific granules. FEBS Lett. 1995;368(1):173-6. Published 1995 Jul 10. doi:10.1016/0014-5793(95)00634-l
PMID: 7615076
Citation 3: Larrick JW, Hirata M, Balint RF, et al. Human CAP18: a novel antimicrobial lipopolysaccharide-binding protein. Infect Immun. 1995;63(4):1291-7. Published 1995 Apr. doi:10.1128/iai.63.4.1291-1297.1995
PMID: 7890387
Citation 4: Larrick JW, Lee J, Ma S, et al. Structural, functional analysis and localization of the human CAP18 gene. FEBS Lett. 1996;398(1):74-80. Published 1996 Nov 25. doi:10.1016/s0014-5793(96)01199-4
PMID: 8946956
Citation 5: Gudmundsson GH, Agerberth B, Odeberg J, et al. The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur J Biochem. 1996;238(2):325-32. Published 1996 Jun 1. doi:10.1111/j.1432-1033.1996.0325z.x
PMID: 8681941
Citation 6: Bals R, Lang C, Weiner DJ, et al. Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules. Clin Diagn Lab Immunol. 2001;8(2):370-5. Published 2001 Mar. doi:10.1128/CDLI.8.2.370-375.2001
PMID: 11238224
Citation 7: Gerhard DS, Wagner L, Feingold EA, et al. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004;14(10B):2121-7. Published 2004 Oct. doi:10.1101/gr.2596504
PMID: 15489334
Citation 8: Turner J, Cho Y, Dinh NN, et al. Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob Agents Chemother. 1998;42(9):2206-14. Published 1998 Sep. doi:10.1128/AAC.42.9.2206
PMID: 9736536
Citation 9: Oren Z, Lerman JC, Gudmundsson GH, et al. Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity. Biochem J. 1999;341 ( Pt 3)(Pt 3):501-13. Published 1999 Aug 1. doi:
PMID: 10417311
Citation 10: Sørensen OE, Follin P, Johnsen AH, et al. Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood. 2001;97(12):3951-9. Published 2001 Jun 15. doi:10.1182/blood.v97.12.3951
PMID: 11389039
Citation 11: Murakami M, Lopez-Garcia B, Braff M, et al. Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense. J Immunol. 2004;172(5):3070-7. Published 2004 Mar 1. doi:10.4049/jimmunol.172.5.3070
PMID: 14978112
Citation 12: Braff MH, Hawkins MA, Di Nardo A, et al. Structure-function relationships among human cathelicidin peptides: dissociation of antimicrobial properties from host immunostimulatory activities. J Immunol. 2005;174(7):4271-8. Published 2005 Apr 1. doi:10.4049/jimmunol.174.7.4271
PMID: 15778390
Citation 13: Lee CC, Sun Y, Qian S, et al. Transmembrane pores formed by human antimicrobial peptide LL-37. Biophys J. 2011;100(7):1688-96. Published 2011 Apr 6. doi:10.1016/j.bpj.2011.02.018
PMID: 21463582
Citation 14: Woloszynek JC, Hu Y, Pham CT, et al. Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions. J Biol Chem. 2012;287(41):34101-9. Published 2012 Oct 5. doi:10.1074/jbc.M112.394452
PMID: 22879591
Citation 15: Zsila F, Ricci M, Szigyártó IC, et al. Quorum Sensing Pseudomonas Quinolone Signal Forms Chiral Supramolecular Assemblies With the Host Defense Peptide LL-37. Front Mol Biosci. 2021;8:742023. Published 2021. doi:10.3389/fmolb.2021.742023
PMID: 34708076
Citation 16: Li X, Li Y, Han H, et al. 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;128(17):5776-85. Published 2006 May 3. doi:10.1021/ja0584875
PMID: 16637646
Citation 17: Wang G, Wang G. Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles. J Biol Chem. 2008;283(47):32637-43. Published 2008 Nov 21. doi:10.1074/jbc.M805533200
PMID: 18818205
Citation 18: Wang G, Elliott M, Cogen AL, et al. Structure, dynamics, and antimicrobial and immune modulatory activities of human LL-23 and its single-residue variants mutated on the basis of homologous primate cathelicidins. Biochemistry. 2012;51(2):653-64. Published 2012 Jan 17. doi:10.1021/bi2016266
PMID: 22185690
Citation 19: Pazgier M, Ericksen B, Ling M, et al. Structural and functional analysis of the pro-domain of human cathelicidin, LL-37. Biochemistry. 2013;52(9):1547-58. Published 2013 Mar 5. doi:10.1021/bi301008r
PMID: 23406372
Citation 20: Singh S, Datta A, Borro BC, et al. Conformational Aspects of High Content Packing of Antimicrobial Peptides in Polymer Microgels. ACS Appl Mater Interfaces. 2017;9(46):40094-40106. Published 2017 Nov 22. doi:10.1021/acsami.7b13714
PMID: 29087182
Citation 21: Sancho-Vaello E, François P, Bonetti EJ, et al. Structural remodeling and oligomerization of human cathelicidin on membranes suggest fibril-like structures as active species. Sci Rep. 2017;7(1):15371. Published 2017 Nov 13. doi:10.1038/s41598-017-14206-1
PMID: 29133814
Citation 22: Ting YT, Petersen J, Ramarathinam SH, et al. The interplay between citrullination and HLA-DRB1 polymorphism in shaping peptide binding hierarchies in rheumatoid arthritis. J Biol Chem. 2018;293(9):3236-3251. Published 2018 Mar 2. doi:10.1074/jbc.RA117.001013
PMID: 29317506
Citation 23: Engelberg Y, Landau M, Landau M. The Human LL-37(17-29) antimicrobial peptide reveals a functional supramolecular structure. Nat Commun. 2020;11(1):3894. Published 2020 Aug 4. doi:10.1038/s41467-020-17736-x
PMID: 32753597
Citation 24: Sancho-Vaello E, Gil-Carton D, François P, et al. The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics. Sci Rep. 2020;10(1):17356. Published 2020 Oct 15. doi:10.1038/s41598-020-74401-5
PMID: 33060695
Citation 25: Engelberg Y, Ragonis-Bachar P, Landau M, et al. Rare by Natural Selection: Disulfide-Bonded Supramolecular Antimicrobial Peptides. Biomacromolecules. 2022;23(3):926-936. Published 2022 Mar 14. doi:10.1021/acs.biomac.1c01353
PMID: 35061360
5.2 Protein Sequence Databases
UniProt: P49913
5.3 3D Structure Databases
Sl. no. PDB ID Method Resolution Access Links 3D View
AlphaFoldDB: P49913
5.4 Nucleotide Sequence Databases
Sl. no. Accession(s) Access Link(s)
1. Z38026 GenBank || EMBL
2. X89658 GenBank || EMBL
3. U19970 GenBank || EMBL
4. U48795 GenBank || EMBL
5. X96735 GenBank || EMBL
6. AY162210 GenBank || EMBL
7. AY251531 GenBank || EMBL
8. AF288284 GenBank || EMBL
9. CR457083 GenBank || EMBL
10. CR541961 GenBank || EMBL
11. BC055089 GenBank || EMBL
CCDS: CCDS2762.2
RefSeq: NP_004336.3
5.5 Protein-Protein Interaction Databases
STRING: 9606.ENSP00000296435
IntAct: P49913
MINT: Not found
DIP: Not found
BioGRID: 107270
5.6 Ligand Databases
BindingDB: Not found
DrugBank: DB02345
ChEMBL: Not found
5.7 Family & Domain Databases
InterPro: IPR001894, IPR018216, IPR022746, IPR046350
PANTHER: PTHR10206
PROSITE: PS00946, PS00947
5.8 Genome Annotation Databases
Ensembl: ENSGT00390000000410
KEGG: hsa:820
5.9 Phylogenomic Databases
GeneTree: ENSGT00390000000410
5.10 Enzyme & Pathway Databases
BRENDA: Not found
BioCyc: MetaCyc:ENSG00000164047-MON
5.11 Protein-RNA Interaction Databases
RNAct: P49913




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