ID   T4G1H_AGEOR             Reviewed;          74 AA.
AC   Q5Y4V1;
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-Ao1h {ECO:0000305};
DE            Short=U3-AGTX-Ao1h {ECO:0000305};
DE   AltName: Full=Mu-2Aaga_09 {ECO:0000312|EMBL:AAU87893.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY681333; AAU87893.1; -; mRNA.
DR   AlphaFoldDB; Q5Y4V1; -.
DR   SMR; Q5Y4V1; -.
DR   TCDB; 8.B.6.1.6; the ca(2+) channel-targeting spider toxin (cst) family.
DR   ArachnoServer; AS000079; U3-agatoxin-Ao1h.
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_5000093669"
FT   CHAIN           35..72
FT                   /note="U3-agatoxin-Ao1h"
FT                   /evidence="ECO:0000305|PubMed:15688451"
FT                   /id="PRO_5000093670"
FT   MOD_RES         72
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000250|UniProtKB:Q5Y4V3"
FT   DISULFID        37..53
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
FT   DISULFID        44..58
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
FT   DISULFID        52..68
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
FT   DISULFID        60..66
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
SQ   SEQUENCE   74 AA;  8200 MW;  FB4D4D22E14267BF CRC64;
     MRAIISLLLI STMVFGVIEA VSVQKSLKIF EGERGDCVGE SQQCADWSGP YCCKGYYCTC
     QYFPKCICVN DNGK