ID   LYT2_HOGCA              Reviewed;          27 AA.
AC   P61508;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=M-lycotoxin-Hc2a;
DE            Short=M-LCTX-Hc2a;
DE   AltName: Full=Lycotoxin II;
DE   AltName: Full=Lycotoxin-2;
OS   Hogna carolinensis (Carolina wolf spider) (Lycosa carolinensis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Lycosoidea; Lycosidae; Hogna.
OX   NCBI_TaxID=278031;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SYNTHESIS, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=9442044; DOI=10.1074/jbc.273.4.2059;
RA   Yan L., Adams M.E.;
RT   "Lycotoxins, antimicrobial peptides from venom of the wolf spider Lycosa
RT   carolinensis.";
RL   J. Biol. Chem. 273:2059-2066(1998).
RN   [2]
RP   FUNCTION.
RX   PubMed=18098329; DOI=10.1002/psc.993;
RA   Adao R., Seixas R., Gomes P., Pessoa J.C., Bastos M.;
RT   "Membrane structure and interactions of a short Lycotoxin I analogue.";
RL   J. Pept. Sci. 14:528-534(2008).
CC   -!- FUNCTION: Forms pore that permeabilize the cell membrane. Promotes
CC       efflux of calcium from synaptosomes, causes hemolysis, and dissipates
CC       voltage gradients across muscle membrane. Potently inhibits the growth
CC       of bacteria, yeast and Leishmania. May function both in the prey
CC       capture strategy as well as protection from infectious organisms
CC       arising from prey ingestion (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:18098329, ECO:0000269|PubMed:9442044}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=3206.0; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:9442044};
CC   -!- SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 05
CC       subfamily.
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DR   AlphaFoldDB; P61508; -.
DR   ArachnoServer; AS000066; M-lycotoxin-Hc2a.
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   Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Hemolysis;
KW   Neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..27
FT                   /note="M-lycotoxin-Hc2a"
FT                   /id="PRO_0000044559"
SQ   SEQUENCE   27 AA;  3207 MW;  E4039D6948D46DB8 CRC64;
     KIKWFKTMKS IAKFIAKEQM KKHLGGE