ID   LYT1_LYCER              Reviewed;          25 AA.
AC   C0HJU9;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Toxin LyeTx 1 {ECO:0000303|PubMed:19946788};
OS   Lycosa erythrognatha (Wolf spider) (Scaptocosa raptoria).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Lycosoidea; Lycosidae; Lycosa.
OX   NCBI_TaxID=332789;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP   AMIDATION AT LEU-25, AND STRUCTURE BY NMR.
RC   TISSUE=Venom;
RX   PubMed=19946788; DOI=10.1007/s00726-009-0385-x;
RA   Santos D.M., Verly R.M., Pilo-Veloso D., de Maria M., de Carvalho M.A.,
RA   Cisalpino P.S., Soares B.M., Diniz C.G., Farias L.M., Moreira D.F.,
RA   Frezard F., Bemquerer M.P., Pimenta A.M., de Lima M.E.;
RT   "LyeTx I, a potent antimicrobial peptide from the venom of the spider
RT   Lycosa erythrognatha.";
RL   Amino Acids 39:135-144(2010).
CC   -!- FUNCTION: Has antimicrobial activity against Gram-positive bacterium
CC       S.aureus (MIC=3.79 uM), Gram-negative bacterium E.coli (MIC=7.81 uM)
CC       and yeasts C.krusei (MIC=26.3 uM) and C.neoformans (MIC=13.2 uM). Has
CC       hemolytic activity against rabbit erythrocytes. Forms pores in lipid
CC       bilayers in vitro; pore formation is reduced when cholesterol is
CC       present in the bilayers. {ECO:0000269|PubMed:19946788}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19946788}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:19946788}.
CC   -!- MASS SPECTROMETRY: Mass=2831.93; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:19946788};
CC   -!- SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 05
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PDB; 6CL3; NMR; -; A=1-25.
DR   PDB; 7MMM; NMR; -; A=1-25.
DR   PDBsum; 6CL3; -.
DR   PDBsum; 7MMM; -.
DR   AlphaFoldDB; C0HJU9; -.
DR   BMRB; C0HJU9; -.
DR   SMR; C0HJU9; -.
DR   TCDB; 8.B.10.2.3; the psalmotoxin-1 (pctx1) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Hemolysis; Secreted; Toxin.
FT   PEPTIDE         1..25
FT                   /note="Toxin LyeTx 1"
FT                   /evidence="ECO:0000269|PubMed:19946788"
FT                   /id="PRO_0000434015"
FT   MOD_RES         25
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:19946788"
FT   HELIX           2..15
FT                   /evidence="ECO:0007829|PDB:6CL3"
FT   HELIX           17..24
FT                   /evidence="ECO:0007829|PDB:6CL3"
SQ   SEQUENCE   25 AA;  2834 MW;  0BFFE912FECD7409 CRC64;
     IWLTALKFLG KNLGKHLAKQ QLAKL