ID   T4G1E_AGEOR             Reviewed;          73 AA.
AC   Q5Y4V4;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=U3-agatoxin-Ao1e {ECO:0000305};
DE            Short=U3-AGTX-Ao1e {ECO:0000305};
DE   AltName: Full=Mu-2Aga_06 {ECO:0000312|EMBL:AAU87890.1};
DE   Flags: Precursor;
OS   Agelena orientalis (Funnel-web spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Agelenidae; Agelena.
OX   NCBI_TaxID=293813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15688451; DOI=10.1002/prot.20390;
RA   Kozlov S.A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R.,
RA   Grishin E.V.;
RT   "A novel strategy for the identification of toxinlike structures in spider
RT   venom.";
RL   Proteins 59:131-140(2005).
CC   -!- FUNCTION: Insecticidal neurotoxin that induces an irreversible spastic
CC       paralysis when injected into insects. Modifies presynaptic voltage-
CC       gated sodium channels (Nav), causing them to open at the normal resting
CC       potential of the nerve. This leads to spontaneous release of
CC       neurotransmitter and repetitive action potentials in motor neurons (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. 03
CC       (aga-4) subfamily. Aga sub-subfamily. {ECO:0000305}.
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DR   EMBL; AY681330; AAU87890.1; -; mRNA.
DR   AlphaFoldDB; Q5Y4V4; -.
DR   SMR; Q5Y4V4; -.
DR   ArachnoServer; AS000082; U3-agatoxin-Ao1e.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR016328; Beta/delta-agatoxin_fam.
DR   PROSITE; PS60015; MU_AGATOXIN; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Disulfide bond; Ion channel impairing toxin; Knottin;
KW   Neurotoxin; Presynaptic neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..34
FT                   /evidence="ECO:0000305|PubMed:15688451"
FT                   /id="PRO_5000093663"
FT   CHAIN           35..71
FT                   /note="U3-agatoxin-Ao1e"
FT                   /evidence="ECO:0000305|PubMed:15688451"
FT                   /id="PRO_5000093664"
FT   MOD_RES         71
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000250|UniProtKB:Q5Y4V3"
FT   DISULFID        36..52
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
FT   DISULFID        43..57
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
FT   DISULFID        51..67
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
FT   DISULFID        59..65
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
SQ   SEQUENCE   73 AA;  8070 MW;  E7711C265E8EE313 CRC64;
     MRTIISLLLL SAMVFAVIEA ISLEEGLQLF EGERGCVGEN QQCADWAGPH CCSGYYCTCR
     YFPKCICVND NGK