ID   WTX1B_NEOAP             Reviewed;          25 AA.
AC   P0DSM4;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=M-poneritoxin-Na1b {ECO:0000303|PubMed:34302796};
DE            Short=M-PONTX-Na1b {ECO:0000303|PubMed:34302796};
DE   AltName: Full=Poneratoxin {ECO:0000305};
DE   AltName: Full=Ponericin Pa II2 {ECO:0000303|PubMed:25448389};
DE   AltName: Full=U1-poneritoxin-Na1b {ECO:0000303|PubMed:26805882};
DE            Short=U1-PONTX-Na1b {ECO:0000303|PubMed:26805882};
OS   Neoponera apicalis (Ant) (Pachycondyla apicalis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Neoponera.
OX   NCBI_TaxID=2320211;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, SYNTHESIS, TOXIC
RP   DOSE, AND BIOASSAY.
RC   TISSUE=Venom;
RX   PubMed=34302796; DOI=10.1016/j.bcp.2021.114693;
RA   Nixon S.A., Robinson S.D., Agwa A.J., Walker A.A., Choudhary S.,
RA   Touchard A., Undheim E.A.B., Robertson A., Vetter I., Schroeder C.I.,
RA   Kotze A.C., Herzig V., King G.F.;
RT   "Multipurpose peptides: the venoms of Amazonian stinging ants contain
RT   anthelmintic ponericins with diverse predatory and defensive activities.";
RL   Biochem. Pharmacol. 192:114693-114693(2021).
RN   [2]
RP   REVIEW, AND PROTEIN SEQUENCE.
RX   PubMed=25448389; DOI=10.1016/j.toxicon.2014.10.021;
RA   Aili S.R., Touchard A., Escoubas P., Padula M.P., Orivel J., Dejean A.,
RA   Nicholson G.M.;
RT   "Diversity of peptide toxins from stinging ant venoms.";
RL   Toxicon 92:166-178(2014).
RN   [3]
RP   REVIEW, AND NOMENCLATURE.
RX   PubMed=26805882; DOI=10.3390/toxins8010030;
RA   Touchard A., Aili S.R., Fox E.G., Escoubas P., Orivel J., Nicholson G.M.,
RA   Dejean A.;
RT   "The biochemical toxin arsenal from ant venoms.";
RL   Toxins 8:1-28(2016).
CC   -!- FUNCTION: Membrane-perturbating peptide with multiple activities
CC       (PubMed:34302796). It is insecticidal, since it induces reversible
CC       paralysis in insects (L.cuprina) after 1 hour, but fails to kill flies
CC       (PubMed:34302796). It shows a relatively strong and broad-spectrum
CC       antibacterial activity against both Gram-positive and Gram-negative
CC       bacteria (MIC<20 uM) (PubMed:34302796). It is also anthelmintic, since
CC       it potently inhibits the larval development of the major pathogenic
CC       nematode of ruminants (H.contortus, IC(50)=2.8 uM) (PubMed:34302796).
CC       Interestingly, only at 10 uM, it increases adult males motility of the
CC       other nematode B.malayi for 24 hours post-treatment, followed by a
CC       reduction in motility for the rest of the experiment (PubMed:34302796).
CC       It shows cytotoxic activity against HEK293 cells (EC(50)=4-6 uM) and
CC       induces hemolysis in human erythrocytes (EC(50)=40-62 uM)
CC       (PubMed:34302796). In addition, it causes an important increase in
CC       intracellular calcium concentration on neuronal and epithelial cell
CC       lines, which supports a non-specific membrane perturbation mechanism of
CC       action (PubMed:34302796). In vivo, it induces pain by intraplantar
CC       injection into mice, suggesting a defensive function against vertebrate
CC       predators (PubMed:34302796). {ECO:0000269|PubMed:34302796}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34302796}. Target
CC       cell membrane {ECO:0000305|PubMed:34302796}. Note=Adopts an alpha-
CC       helical conformation in membrane-mimetic environments.
CC       {ECO:0000305|PubMed:34302796}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:25448389}.
CC   -!- MASS SPECTROMETRY: Mass=2695.6; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:34302796};
CC   -!- TOXIC DOSE: PD(50) is 25.8 nmol/g 1 hour after injection into
CC       L.cuprina. LD(50) is >100 nmol/g 24 hours after injection into
CC       L.cuprina. {ECO:0000269|PubMed:34302796}.
CC   -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC       superfamily. Medium-length antimicrobial peptide (group 3) family.
CC       Ponericin-W subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DSM4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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   InterPro; IPR012523; Antimicrobial_4.
DR   Pfam; PF08024; Antimicrobial_4; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Hemolysis;
KW   Membrane; Secreted; Target cell membrane; Target membrane; Toxin.
FT   PEPTIDE         1..25
FT                   /note="M-poneritoxin-Na1b"
FT                   /evidence="ECO:0000305|PubMed:25448389"
FT                   /id="PRO_0000447119"
SQ   SEQUENCE   25 AA;  2697 MW;  3A37CB4C7846D70C CRC64;
     FLGALLKIGA KLLPSVVGLF KKKQQ