ID   TOP1_OXYTA              Reviewed;          48 AA.
AC   P83247;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=M-oxotoxin-Ot1a;
DE            Short=M-OXTX-Ot1a;
DE   AltName: Full=Oxki1;
DE   AltName: Full=Oxyopinin-1;
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).
RN   [2]
RP   FUNCTION, AND CIRCULAR DICHROISM.
RX   PubMed=15328050; DOI=10.1016/j.bbamem.2004.05.007;
RA   Belokoneva O.S., Satake H., Mal'tseva E.L., Pal'mina N.P., Villegas E.,
RA   Nakajima T., Corzo G.;
RT   "Pore formation of phospholipid membranes by the action of two hemolytic
RT   arachnid peptides of different size.";
RL   Biochim. Biophys. Acta 1664:182-188(2004).
CC   -!- FUNCTION: Disrupts cell membranes, particularly those rich in
CC       phosphocholine, through formation of pores. Has antimicrobial activity
CC       against Gram-negative bacterium E.coli, Gram-positive bacteria
CC       B.subtilis and S.aureus, and hemolytic activity against sheep, pig and
CC       guinea pig erythrocytes. Has insecticidal activity against S.frugiperda
CC       ovarian cells by opening non-selective ion channels. Enhances the
CC       insecticidal activity of spider venom neurotoxic peptides.
CC       {ECO:0000269|PubMed:11976325, ECO:0000269|PubMed:15328050}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11976325}. Target
CC       cell membrane {ECO:0000269|PubMed:11976325}. Note=Forms a transmembrane
CC       alpha-helix in the target cell membrane. Forms a membrane channel in
CC       the prey.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:11976325}.
CC   -!- MASS SPECTROMETRY: Mass=5221.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11976325};
CC   -!- SIMILARITY: Belongs to the cationic peptide 02 (oxyopinin-2) family.
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DR   AlphaFoldDB; P83247; -.
DR   SMR; P83247; -.
DR   ArachnoServer; AS000185; M-oxotoxin-Ot1a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Hemolysis;
KW   Ion transport; Membrane; Secreted; Target cell membrane; Target membrane;
KW   Toxin; Transmembrane; Transport.
FT   CHAIN           1..48
FT                   /note="M-oxotoxin-Ot1a"
FT                   /id="PRO_0000087675"
SQ   SEQUENCE   48 AA;  5221 MW;  58439CB5942C9C53 CRC64;
     FRGLAKLLKI GLKSFARVLK KVLPKAAKAG KALAKSMADE NAIRQQNQ