PON1A_ANOEM
ID PON1A_ANOEM Reviewed; 16 AA.
AC C0HJY4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=U1-poneritoxin-Ae1a {ECO:0000303|PubMed:27474999};
DE Short=U1-PONTX-Ae1a {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, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC
RP DOSE, DISULFIDE BONDS, AMIDATION AT CYS-16, AND STRUCTURE BY NMR OF 1-16.
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 -!- FUNCTION: Weakly inhibits human L-type voltage-gated calcium channel
CC Cav1 (CACNA1S, CACNA1C, CACNA1D, CACNA1F) (IC(50)=4.6 uM). In vivo, it
CC induces reversible paralysis in blowfly L.cuprina.
CC {ECO:0000269|PubMed:27474999}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27474999}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:27474999}.
CC -!- PTM: C-terminal amidation is necessary for channel blocking activity.
CC {ECO:0000269|PubMed:27474999}.
CC -!- MASS SPECTROMETRY: Mass=1733.64; Mass_error=0.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:27474999};
CC -!- TOXIC DOSE: PD(50) is 8.9 nmol/g by injection in blowfly.
CC {ECO:0000269|PubMed:27474999}.
CC -!- MISCELLANEOUS: Does not inhibit human L-type voltage-gated calcium
CC channel Cav2 (CACNA1A, CACNA1B, CACNA1E).
CC {ECO:0000269|PubMed:27474999}.
CC -!- SIMILARITY: Belongs to the poneritoxin-Ae1 family. {ECO:0000305}.
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DR PDB; 2NBC; NMR; -; A=1-16.
DR PDBsum; 2NBC; -.
DR AlphaFoldDB; C0HJY4; -.
DR BMRB; C0HJY4; -.
DR SMR; C0HJY4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium 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; Calcium channel impairing toxin;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Secreted; Toxin; Voltage-gated calcium channel impairing toxin.
FT PEPTIDE 1..16
FT /note="U1-poneritoxin-Ae1a"
FT /evidence="ECO:0000269|PubMed:27474999"
FT /id="PRO_0000437873"
FT MOD_RES 16
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:27474999"
FT DISULFID 2..14
FT /evidence="ECO:0000269|PubMed:27474999"
FT DISULFID 6..16
FT /evidence="ECO:0000269|PubMed:27474999"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2NBC"
SQ SEQUENCE 16 AA; 1739 MW; FA157660A5FEA3CF CRC64;
WCASGCRKKR HGGCSC