ID   TOP2C_OXYTA             Reviewed;          37 AA.
AC   P83250;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=M-oxotoxin-Ot2c;
DE            Short=M-OXTX-Ot2c;
DE   AltName: Full=Oxki2c;
DE   AltName: Full=Oxyopinin-2c;
OS   Oxyopes takobius (Lynx spider) (Oxyopes foliiformis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Lycosoidea; Oxyopidae; Oxyopes.
OX   NCBI_TaxID=666126;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MASS
RP   SPECTROMETRY, AND CIRCULAR DICHROISM ANALYSIS.
RC   TISSUE=Venom;
RX   PubMed=11976325; DOI=10.1074/jbc.m200511200;
RA   Corzo G., Villegas E., Gomez-Lagunas F., Possani L.D., Belokoneva O.S.,
RA   Nakajima T.;
RT   "Oxyopinins, large amphipathic peptides isolated from the venom of the wolf
RT   spider Oxyopes kitabensis with cytolytic properties and positive
RT   insecticidal cooperativity with spider neurotoxins.";
RL   J. Biol. Chem. 277:23627-23637(2002).
CC   -!- FUNCTION: Disrupts biological membranes, particularly those rich in
CC       phosphocholine. Has antimicrobial activity against Gram-negative
CC       bacterium E.coli, Gram-positive bacteria B.subtilis and S.aureus, and
CC       hemolytic activity against sheep, pig and guinea pig red blood cells.
CC       Has insecticidal activity against S.frugiperda ovarian cells by opening
CC       non-selective ion channels. Enhances the insecticidal activity of
CC       spider venom neurotoxic peptides. {ECO:0000269|PubMed:11976325}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11976325}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:11976325}.
CC   -!- MASS SPECTROMETRY: Mass=4064.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11976325};
CC   -!- SIMILARITY: Belongs to the cationic peptide 02 (oxyopinin-2) family.
CC       {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   AlphaFoldDB; P83250; -.
DR   SMR; P83250; -.
DR   TCDB; 1.C.68.1.2; the channel-forming oxyopinin peptide (oxyopinin) family.
DR   ArachnoServer; AS000188; M-oxotoxin-Ot2c.
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:0019836; P:hemolysis by symbiont of host erythrocytes; IEA:InterPro.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR012522; Antimicrobial_3.
DR   Pfam; PF08025; Antimicrobial_3; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Hemolysis;
KW   Secreted; Toxin.
FT   PEPTIDE         1..37
FT                   /note="M-oxotoxin-Ot2c"
FT                   /id="PRO_0000045033"
SQ   SEQUENCE   37 AA;  4065 MW;  EEE88975C9884F4E CRC64;
     GKLSGISKVL RAIAKFFKGV GKARKQFKEA SDLDKNQ