ID   TXC1_HOLCU              Reviewed;          36 AA.
AC   P15967;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Mu-agatoxin-Hc1a;
DE            Short=Mu-AGTX-Hc1a;
DE   AltName: Full=Curtatoxin-1 {ECO:0000303|PubMed:2298738};
DE            Short=CT-I {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, AMIDATION AT ASN-36, FUNCTION, AND 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).
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.
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   -!- TOXIC DOSE: LD(50) is 20 mg/kg in house crickets (Acheta domesticus).
CC       {ECO:0000269|PubMed:2298738}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. 04
CC       (aga-5) 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   PIR; A35030; A35030.
DR   AlphaFoldDB; P15967; -.
DR   SMR; P15967; -.
DR   TCDB; 8.B.6.1.3; the ca(2+) channel-targeting spider toxin (cst) family.
DR   ArachnoServer; AS000294; mu-agatoxin-Hc1a.
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..36
FT                   /note="Mu-agatoxin-Hc1a"
FT                   /id="PRO_0000044953"
FT   MOD_RES         36
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:2298738"
FT   DISULFID        2..17
FT                   /evidence="ECO:0000250"
FT   DISULFID        9..22
FT                   /evidence="ECO:0000250"
FT   DISULFID        16..32
FT                   /evidence="ECO:0000250"
FT   DISULFID        24..30
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   36 AA;  4111 MW;  617C02D23ED95147 CRC64;
     SCVGEYGRCR SAYEDCCDGY YCNCSQPPYC LCRNNN