ID   T4G1D_AGEAP             Reviewed;          37 AA.
AC   P11060;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Mu-agatoxin-Aa1d {ECO:0000305};
DE            Short=Mu-AGTX-Aa1d {ECO:0000305};
DE   AltName: Full=Mu-agatoxin IV {ECO:0000303|PubMed:2914898};
DE            Short=Mu-Aga IV {ECO:0000303|PubMed:2914898};
DE   AltName: Full=Mu-agatoxin-4 {ECO:0000305};
OS   Agelenopsis aperta (North American funnel-web spider) (Agelenopsis
OS   gertschi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Agelenidae; Agelenopsis.
OX   NCBI_TaxID=6908;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT ASN-37, FUNCTION, SUBCELLULAR LOCATION, AND
RP   TOXIC DOSE.
RC   TISSUE=Venom;
RX   PubMed=2914898; DOI=10.1016/s0021-9258(18)94154-2;
RA   Skinner W.S., Adams M.E., Quistad G.B., Kataoka H., Cesarin B.J.,
RA   Enderlin F.E., Schooley D.A.;
RT   "Purification and characterization of two classes of neurotoxins from the
RT   funnel web spider, Agelenopsis aperta.";
RL   J. Biol. Chem. 264:2150-2155(1989).
RN   [2]
RP   3D-STRUCTURE MODELING.
RX   PubMed=8608119; DOI=10.1021/bi952605r;
RA   Omecinsky D.O., Holub K.E., Adams M.E., Reily M.D.;
RT   "Three-dimensional structure analysis of mu-agatoxins: further evidence for
RT   common motifs among neurotoxins with diverse ion channel specificities.";
RL   Biochemistry 35:2836-2844(1996).
RN   [3]
RP   REVIEW.
RX   PubMed=15066410; DOI=10.1016/j.toxicon.2004.02.004;
RA   Adams M.E.;
RT   "Agatoxins: ion channel specific toxins from the American funnel web
RT   spider, Agelenopsis aperta.";
RL   Toxicon 43:509-525(2004).
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.
CC       {ECO:0000269|PubMed:2914898}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2914898}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:2914898}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- TOXIC DOSE: LD(50) is 40 +-9 mg/kg into third stadium larvae of
CC       M.sexta. {ECO:0000269|PubMed:2914898}.
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   PIR; D32038; D32038.
DR   AlphaFoldDB; P11060; -.
DR   SMR; P11060; -.
DR   ArachnoServer; AS000381; mu-agatoxin-Aa1d.
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   PIRSF; PIRSF001882; Curtatoxin; 1.
DR   PROSITE; PS60015; MU_AGATOXIN; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Presynaptic neurotoxin;
KW   Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..37
FT                   /note="Mu-agatoxin-Aa1d"
FT                   /evidence="ECO:0000269|PubMed:2914898"
FT                   /id="PRO_0000044958"
FT   MOD_RES         37
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:2914898"
FT   DISULFID        2..18
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
FT   DISULFID        9..23
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
FT   DISULFID        17..33
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
FT   DISULFID        25..31
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
SQ   SEQUENCE   37 AA;  4208 MW;  1CA2F3A18C59A044 CRC64;
     ACVGENQQCA DWAGPHCCDG YYCTCRYFPK CICRNNN