T3C2_HOLCU
ID T3C2_HOLCU Reviewed; 38 AA.
AC P60177; P11059;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Mu-agatoxin-Hc1b;
DE Short=Mu-AGTX-Hc1b;
DE AltName: Full=Curtatoxin-2 {ECO:0000303|PubMed:2298738};
DE Short=CT-II {ECO:0000303|PubMed:2298738};
OS Hololena curta (Funnel-web spider) (Agelena curta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Agelenidae; Hololena.
OX NCBI_TaxID=6910;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AMIDATION AT SER-38, AND
RP TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=2298738; DOI=10.1016/s0021-9258(19)39939-9;
RA Stapleton A., Blankenship D.T., Ackermann D.L., Chen T.-M., Gorder G.W.,
RA Manley G.D., Palfreyman M.G., Coutant J.E., Cardin A.D.;
RT "Curtatoxins. Neurotoxic insecticidal polypeptides isolated from the
RT funnel-web spider Hololena curta.";
RL J. Biol. Chem. 265:2054-2059(1990).
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).
RN [3]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=2048147; DOI=10.1016/0041-0101(91)90286-z;
RA Quistad G.B., Reuter C.C., Skinner W.S., Dennis P.A., Suwanrumpha S.,
RA Fu E.W.;
RT "Paralytic and insecticidal toxins from the funnel web spider, Hololena
RT curta.";
RL Toxicon 29:329-336(1991).
CC -!- FUNCTION: Insecticidal neurotoxin that induces irreversible
CC neuromuscular blockade in house crickets (A.domesticus). Modifies
CC presynaptic voltage-gated sodium channels (Nav), causing them to open
CC at the normal resting potential of the nerve. This leads to spontaneous
CC release of neurotransmitter and repetitive action potentials in motor
CC neurons. {ECO:0000269|PubMed:2298738}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2298738}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:2298738}.
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 4 mg/kg in house crickets (Acheta domesticus).
CC {ECO:0000269|PubMed:2298738}.
CC -!- SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. 02
CC (aga-3) subfamily. {ECO:0000305}.
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DR PIR; B35030; B35030.
DR AlphaFoldDB; P60177; -.
DR SMR; P60177; -.
DR PRIDE; P60177; -.
DR ArachnoServer; AS000295; mu-agatoxin-Hc1b.
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; Secreted; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT PEPTIDE 1..38
FT /note="Mu-agatoxin-Hc1b"
FT /id="PRO_0000044956"
FT MOD_RES 38
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:2298738"
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
