ID   LYS2_LYCSI              Reviewed;          23 AA.
AC   P0DV71;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 1.
DT   03-AUG-2022, entry version 2.
DE   RecName: Full=Lycosin-II {ECO:0000303|PubMed:27128941, ECO:0000303|PubMed:34506798};
DE   Flags: Precursor;
OS   Lycosa singoriensis (Wolf spider) (Aranea singoriensis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Lycosoidea; Lycosidae; Lycosa.
OX   NCBI_TaxID=434756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-22, FUNCTION, MASS
RP   SPECTROMETRY, SUBCELLULAR LOCATION, SYNTHESIS OF 1-22, AND PROBABLE
RP   AMIDATION AT LEU-21.
RC   TISSUE=Venom;
RX   PubMed=27128941; DOI=10.3390/toxins8050119;
RA   Wang Y., Wang L., Yang H., Xiao H., Farooq A., Liu Z., Hu M., Shi X.;
RT   "The spider venom peptide Lycosin-II has potent antimicrobial activity
RT   against clinically isolated bacteria.";
RL   Toxins 8:0-0(2016).
RN   [2]
RP   SYNTHESIS OF 1-22, AND FUNCTION.
RX   PubMed=34506798; DOI=10.1016/j.bbamem.2021.183769;
RA   Oh J.H., Park J., Park Y.;
RT   "Anti-biofilm and anti-inflammatory effects of Lycosin-II isolated from
RT   spiders against multi-drug resistant bacteria.";
RL   Biochim. Biophys. Acta 1864:183769-183769(2022).
CC   -!- FUNCTION: Has strong antibacterial activity and biofilm inhibition
CC       effects against Gram-positive and -negative bacteria including E.coli,
CC       S.epidermidis, and A.baumannii and oxacillin-resistant S.aureus and
CC       meropenem-resistant P.aeruginosa (PubMed:27128941, PubMed:34506798). Is
CC       not cytotoxic against human foreskin fibroblast Hs27 or hemolytic
CC       against mammalian red blood cells (PubMed:27128941, PubMed:34506798).
CC       Its mechanism of action involves binding to lipoteichoic acid and
CC       lipopolysaccharide of Gram-positive and Gram-negative bacterial
CC       membranes, respectively, to destroy the bacterial membrane
CC       (PubMed:34506798). In addition, it shows anti-inflammatory effects by
CC       inhibiting the expression of pro-inflammatory cytokines that are
CC       increased during bacterial infection in Hs27 cells (PubMed:34506798).
CC       {ECO:0000269|PubMed:27128941, ECO:0000269|PubMed:34506798}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27128941}. Target
CC       cell membrane {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:27128941}.
CC   -!- MASS SPECTROMETRY: Mass=2418.65; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:27128941};
CC   -!- SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 05
CC       subfamily. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Direct protein sequencing; Membrane;
KW   Secreted; Target cell membrane; Target membrane.
FT   PEPTIDE         1..21
FT                   /note="Lycosin-II"
FT                   /evidence="ECO:0000269|PubMed:27128941"
FT                   /id="PRO_0000455435"
FT   MOD_RES         21
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000305|PubMed:27128941"
SQ   SEQUENCE   23 AA;  2631 MW;  1FCA212A1CD3B34A CRC64;
     VWLSALKFIG KHLAKHQLSK LGR