DEFLU_LUCSE
ID DEFLU_LUCSE Reviewed; 92 AA.
AC P86471; D9J139;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 2.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Defensin Lucifensin {ECO:0000303|PubMed:19921400, ECO:0000303|PubMed:20542901};
DE AltName: Full=Sericasin {ECO:0000303|PubMed:19921400};
DE Flags: Precursor;
OS Lucilia sericata (Green bottle fly) (Phaenicia sericata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=13632;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Larva;
RX PubMed=20542901; DOI=10.1093/jac/dkq165;
RA Andersen A.S., Sandvang D., Schnorr K.M., Kruse T., Neve S., Joergensen B.,
RA Karlsmark T., Krogfelt K.A.;
RT "A novel approach to the antimicrobial activity of maggot debridement
RT therapy.";
RL J. Antimicrob. Chemother. 65:1646-1654(2010).
RN [2]
RP PROTEIN SEQUENCE OF 53-92, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Larval gut;
RX PubMed=19921400; DOI=10.1007/s00018-009-0194-0;
RA Cerovsky V., Zdarek J., Fucik V., Monincova L., Voburka Z., Bem R.;
RT "Lucifensin, the long-sought antimicrobial factor of medicinal maggots of
RT the blowfly Lucilia sericata.";
RL Cell. Mol. Life Sci. 67:455-466(2010).
RN [3]
RP FUNCTION, AND BINDING TO LIPID II.
RX PubMed=20508130; DOI=10.1126/science.1185723;
RA Schneider T., Kruse T., Wimmer R., Wiedemann I., Sass V., Pag U.,
RA Jansen A., Nielsen A.K., Mygind P.H., Raventos D.S., Neve S., Ravn B.,
RA Bonvin A.M., De Maria L., Andersen A.S., Gammelgaard L.K., Sahl H.G.,
RA Kristensen H.H.;
RT "Plectasin, a fungal defensin, targets the bacterial cell wall precursor
RT Lipid II.";
RL Science 328:1168-1172(2010).
RN [4]
RP FUNCTION, SYNTHESIS, MASS SPECTROMETRY, AND DISULFIDE BONDS.
RX PubMed=21560219; DOI=10.1002/cbic.201100066;
RA Cerovsky V., Slaninova J., Fucik V., Monincova L., Bednarova L., Malon P.,
RA Stokrova J.;
RT "Lucifensin, a novel insect defensin of medicinal maggots: synthesis and
RT structural study.";
RL ChemBioChem 12:1352-1361(2011).
RN [5]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=23624615; DOI=10.1007/s00441-013-1626-6;
RA Valachova I., Bohova J., Palosova Z., Takac P., Kozanek M., Majtan J.;
RT "Expression of lucifensin in Lucilia sericata medicinal maggots in infected
RT environments.";
RL Cell Tissue Res. 353:165-171(2013).
RN [6]
RP SUBCELLULAR LOCATION, INDUCTION, AND MASS SPECTROMETRY.
RX PubMed=25182719; DOI=10.12980/apjtb.4.2014c1134;
RA Valachova I., Prochazka E., Bohova J., Novak P., Takac P., Majtan J.;
RT "Antibacterial properties of lucifensin in Lucilia sericata maggots after
RT septic injury.";
RL Asian Pac. J. Trop. Biomed. 4:358-361(2014).
RN [7] {ECO:0007744|PDB:2LLD}
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=22322867; DOI=10.1007/s10858-012-9608-7;
RA Nygaard M.K., Andersen A.S., Kristensen H.H., Krogfelt K.A., Fojan P.,
RA Wimmer R.;
RT "The insect defensin lucifensin from Lucilia sericata.";
RL J. Biomol. NMR 52:277-282(2012).
CC -!- FUNCTION: Shows strong antibacterial activity against numerous Gram-
CC positive bacteria. It selectively inhibits peptidoglycan biosynthesis
CC through complex formation with the cell wall precursor lipid II (1:1
CC molar ratio) thus inhibiting cell wall synthesis (PubMed:20508130).
CC Shows antibacterial activity against the Gram-positive bacteria
CC M.luteus, E.fecalis (MIC=32 mg/L), S.aureus (MIC=16 mg/L), S.carnosus
CC (MIC=2 mg/L), S.pneumoniae (MIC=2 mg/L) and S.pyogenes (MIC=2 mg/L) and
CC against a number of methicillin-resistant S.aureus and glycopeptide-
CC intermediate S.aureus isolates (PubMed:20542901, PubMed:19921400,
CC PubMed:21560219). Does not show antibacterial activity against Gram-
CC negative bacteria or antifungal activity against C.utilis
CC (PubMed:20542901). Shows slight antifungal activity against C.albicans
CC (PubMed:21560219). {ECO:0000269|PubMed:19921400,
CC ECO:0000269|PubMed:20542901, ECO:0000269|PubMed:21560219,
CC ECO:0000305|PubMed:20508130}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00710,
CC ECO:0000269|PubMed:19921400, ECO:0000269|PubMed:21560219,
CC ECO:0000269|PubMed:25182719}. Host cell membrane
CC {ECO:0000305|PubMed:20508130}.
CC -!- TISSUE SPECIFICITY: Larval fat body, hemolymph and salivary glands (at
CC protein level) (PubMed:19921400). Expressed in the salivary glands of
CC all larval stages (PubMed:23624615). {ECO:0000269|PubMed:19921400,
CC ECO:0000269|PubMed:23624615}.
CC -!- DEVELOPMENTAL STAGE: In the salivary glands, there is no expression in
CC early larval stages with expression beginning 5-6 hours after hatching
CC (PubMed:23624615). Maximum expression is reached about 24 hours after
CC hatching, remains strong during the second and third instars and
CC declines at the end of the third instar before the wandering stage
CC (PubMed:23624615). No expression is detected at the wandering stage
CC (PubMed:23624615). {ECO:0000269|PubMed:23624615}.
CC -!- INDUCTION: Induced in the hemolymph by septic injury caused by
CC dorsolateral puncturing with a needle contaminated with
CC lipopolysaccharide (LPS) solution (PubMed:25182719). Induced in the
CC salivary glands by feeding (PubMed:23624615). Induced in the fat body
CC and the grease coupler of the salivary glands in response to oral
CC ingestion of S.aureus and P.aeruginosa (PubMed:23624615).
CC {ECO:0000269|PubMed:23624615, ECO:0000269|PubMed:25182719}.
CC -!- PTM: The disulfide bonds are essential for antimicrobial activity.
CC {ECO:0000269|PubMed:21560219}.
CC -!- MASS SPECTROMETRY: Mass=4113.8783; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:20542901};
CC -!- MASS SPECTROMETRY: Mass=4113.6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19921400};
CC -!- MASS SPECTROMETRY: Mass=4113.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:21560219};
CC -!- MASS SPECTROMETRY: Mass=4114.8951; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:25182719};
CC -!- MISCELLANEOUS: During maggot debridement therapy which involves the
CC controlled application of cultured sterile larvae to an infected
CC chronic non-healing wound, one of the key factors which protects larvae
CC against the infectious wound environment and contributes to wound
CC healing through its antimicrobial activity.
CC {ECO:0000269|PubMed:19921400}.
CC -!- SIMILARITY: Belongs to the invertebrate defensin family. Type 1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00710}.
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DR EMBL; HM243535; ADI87383.1; -; mRNA.
DR PDB; 2LLD; NMR; -; A=53-92.
DR PDBsum; 2LLD; -.
DR AlphaFoldDB; P86471; -.
DR BMRB; P86471; -.
DR SMR; P86471; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR001542; Defensin_invertebrate/fungal.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR Pfam; PF01097; Defensin_2; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Defensin;
KW Direct protein sequencing; Disulfide bond; Fungicide; Host cell membrane;
KW Host membrane; Immunity; Innate immunity; Lipid-binding; Membrane;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..52
FT /evidence="ECO:0000305"
FT /id="PRO_0000445006"
FT PEPTIDE 53..92
FT /note="Defensin Lucifensin"
FT /evidence="ECO:0000269|PubMed:19921400"
FT /id="PRO_0000392967"
FT DISULFID 55..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT ECO:0000269|PubMed:21560219, ECO:0000269|PubMed:22322867,
FT ECO:0007744|PDB:2LLD"
FT DISULFID 68..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT ECO:0000269|PubMed:21560219, ECO:0000269|PubMed:22322867,
FT ECO:0007744|PDB:2LLD"
FT DISULFID 72..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT ECO:0000269|PubMed:21560219, ECO:0000269|PubMed:22322867,
FT ECO:0007744|PDB:2LLD"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:2LLD"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:2LLD"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2LLD"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2LLD"
SQ SEQUENCE 92 AA; 9996 MW; 4DA6C576BCE898D6 CRC64;
MKFFMVFAVT FCLALSFVSQ SLALPADDEA HFVDGLEALK TIEPELHGRY KRATCDLLSG
TGVKHSACAA HCLLRGNRGG YCNGRAICVC RN
