ID   TX1A_PARCV              Reviewed;          25 AA.
AC   P41736;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Delta-paraponeritoxin-Pc1a {ECO:0000305|PubMed:26805882};
DE            Short=Delta-PPOTX-Pc1a {ECO:0000305|PubMed:26805882};
DE   AltName: Full=Pac-TX;
DE   AltName: Full=Poneratoxin {ECO:0000303|PubMed:1685424, ECO:0000303|PubMed:1685425};
DE            Short=PoTX {ECO:0000303|PubMed:1685424, ECO:0000303|PubMed:1685425};
DE   AltName: Full=Poneritoxin {ECO:0000305};
OS   Paraponera clavata (Bullet ant) (Izuela).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Paraponerinae; Paraponera.
OX   NCBI_TaxID=55425;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT ARG-25, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=1685424; DOI=10.1016/0742-8413(91)90275-x;
RA   Piek T., Hue B., Mantel P., Nakajima T., Schmidt J.O.;
RT   "Pharmacological characterization and chemical fractionation of the venom
RT   of the ponerine ant, Paraponera clavata (F.).";
RL   Comp. Biochem. Physiol. 99C:481-486(1991).
RN   [2]
RP   PROTEIN SEQUENCE, AND SYNTHESIS.
RC   TISSUE=Venom;
RA   Konopinska D., Lombarska-Sliwinska D., Plech A., Rosinski G., Lisowski M.;
RT   "Poneratoxin, neurotoxic pentacosapeptide from ant venom: synthetic,
RT   biological and conformational studies.";
RL   (In) Schneider C.H., Eberles A.N. (eds.);
RL   Peptides 1992, pp.759-760, Escom Science Publishers, Leiden (1993).
RN   [3]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=1685425; DOI=10.1016/0742-8413(91)90276-y;
RA   Piek T., Duval A., Hue B., Karst H., Lapied B., Mantel P., Nakajima T.,
RA   Pelhate M., Schmidt J.O.;
RT   "Poneratoxin, a novel peptide neurotoxin from the venom of the ant,
RT   Paraponera clavata.";
RL   Comp. Biochem. Physiol. 99C:487-495(1991).
RN   [4]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=1317947; DOI=10.1007/bf00374453;
RA   Duval A., Malecot C.O., Pelhate M., Piek T.;
RT   "Poneratoxin, a new toxin from an ant venom, reveals an interconversion
RT   between two gating modes of the Na channels in frog skeletal muscle
RT   fibres.";
RL   Pflugers Arch. 420:239-247(1992).
RN   [5]
RP   FUNCTION.
RX   PubMed=12097919;
RA   Hendrich A.B., Mozrzymas J.W., Konopinska D., Scuka M.;
RT   "The effect of poneratoxin on neuromuscular transmission in the rat
RT   diaphragm.";
RL   Cell. Mol. Biol. Lett. 7:195-202(2002).
RN   [6]
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).
RN   [7]
RP   STRUCTURE BY NMR, AND SYNTHESIS.
RX   PubMed=15153103; DOI=10.1111/j.1432-1033.2004.04128.x;
RA   Szolajska E., Poznanski J., Ferber M.L., Michalik J., Gout E., Fender P.,
RA   Bailly I., Dublet B., Chroboczek J.;
RT   "Poneratoxin, a neurotoxin from ant venom. Structure and expression in
RT   insect cells and construction of a bio-insecticide.";
RL   Eur. J. Biochem. 271:2127-2136(2004).
CC   -!- FUNCTION: Blocks nicotinic synaptic transmission in insect CNS and
CC       affects voltage-gated sodium channels (Nav). It is a strong, but very
CC       slowly acting agonist for smooth muscles and its blocks synaptic
CC       transmission in the insect CNS in a concentration-dependent manner and
CC       depolarizes giant interneurons. Also affects neuromuscular transmission
CC       in rat tissue. {ECO:0000269|PubMed:12097919}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1685424}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:1685424}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Princess Bala's sting
CC       - Issue 14 of September 2001;
CC       URL="https://web.expasy.org/spotlight/back_issues/014";
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DR   PDB; 1G92; NMR; -; A=1-25.
DR   PDBsum; 1G92; -.
DR   AlphaFoldDB; P41736; -.
DR   BMRB; P41736; -.
DR   SMR; P41736; -.
DR   EvolutionaryTrace; P41736; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Direct protein sequencing;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..25
FT                   /note="Delta-paraponeritoxin-Pc1a"
FT                   /evidence="ECO:0000269|PubMed:1685424"
FT                   /id="PRO_0000044538"
FT   MOD_RES         25
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|PubMed:1685424"
FT   HELIX           2..8
FT                   /evidence="ECO:0007829|PDB:1G92"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:1G92"
FT   TURN            16..18
FT                   /evidence="ECO:0007829|PDB:1G92"
FT   HELIX           19..24
FT                   /evidence="ECO:0007829|PDB:1G92"
SQ   SEQUENCE   25 AA;  2757 MW;  EEA403CC125E7BB0 CRC64;
     FLPLLILGSL LMTPPVIQAI HDAQR