T3G1C_AGEAP
ID T3G1C_AGEAP Reviewed; 38 AA.
AC P60178; P11059;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Mu-agatoxin-Aa1c;
DE Short=Mu-AGTX-Aa1c;
DE AltName: Full=Mu-agatoxin III {ECO:0000303|PubMed:2914898};
DE AltName: Full=Mu-agatoxin-3;
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, FUNCTION, SUBCELLULAR LOCATION, AMIDATION AT SER-38, 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 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 28 +-12 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. 02
CC (aga-3) subfamily. {ECO:0000305}.
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DR PIR; C32038; C32038.
DR AlphaFoldDB; P60178; -.
DR SMR; P60178; -.
DR ArachnoServer; AS000379; mu-agatoxin-Aa1c.
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..38
FT /note="Mu-agatoxin-Aa1c"
FT /id="PRO_0000044955"
FT MOD_RES 38
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:2914898"
FT DISULFID 3..19
FT /evidence="ECO:0000250"
FT DISULFID 10..24
FT /evidence="ECO:0000250"
FT DISULFID 18..34
FT /evidence="ECO:0000250"
FT DISULFID 26..32
FT /evidence="ECO:0000250"
SQ SEQUENCE 38 AA; 4197 MW; 6031DFF4DB386AD0 CRC64;
ADCVGDGQRC ADWAGPYCCS GYYCSCRSMP YCRCRSDS