ID   PON1D_ANOEM             Reviewed;          18 AA.
AC   C0HJY7;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=U1-poneritoxin-Ae1d {ECO:0000303|PubMed:27474999};
DE            Short=U1-PONTX-Ae1d {ECO:0000303|PubMed:27474999};
DE   AltName: Full=Poneratoxin {ECO:0000305};
OS   Anochetus emarginatus (Ant) (Stenomyrmex emarginatus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Anochetus.
OX   NCBI_TaxID=486636;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AMIDATION AT
RP   CYS-18, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=27474999; DOI=10.1016/j.bbagen.2016.07.027;
RA   Touchard A., Brust A., Cardoso F., Chin Y.-K., Herzig V., Jin A.-H.,
RA   Dejean A., Alewood P., King G., Orivel J., Escoubas P.;
RT   "Isolation and characterization of a structurally unique beta-hairpin venom
RT   peptide from the predatory ant Anochetus emarginatus.";
RL   Biochim. Biophys. Acta 1860:2553-2562(2016).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27474999}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:27474999}.
CC   -!- MASS SPECTROMETRY: Mass=1866.81; Mass_error=0.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:27474999};
CC   -!- SIMILARITY: Belongs to the poneritoxin-Ae1 family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HJY7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond; Secreted; Toxin.
FT   PEPTIDE         1..18
FT                   /note="U1-poneritoxin-Ae1d"
FT                   /evidence="ECO:0000269|PubMed:27474999"
FT                   /id="PRO_0000437876"
FT   MOD_RES         18
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:27474999"
FT   DISULFID        4..16
FT                   /evidence="ECO:0000250|UniProtKB:C0HJY4"
FT   DISULFID        8..18
FT                   /evidence="ECO:0000250|UniProtKB:C0HJY4"
SQ   SEQUENCE   18 AA;  1872 MW;  7FDC3B80BFC95AB2 CRC64;
     RSLCSNGCRP KPFGGCSC