ID   TXMG1_MACGS             Reviewed;          38 AA.
AC   P83557;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Mu-hexatoxin-Mg1b;
DE            Short=Mu-HXTX-Mg1b;
DE   AltName: Full=Neurotoxin magi-1 {ECO:0000303|PubMed:12860384};
OS   Macrothele gigas (Japanese funnel web spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Macrothelidae; Macrothele.
OX   NCBI_TaxID=223896 {ECO:0000305};
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP   AMIDATION AT SER-38, AND DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=12860384; DOI=10.1016/s0014-5793(03)00666-5;
RA   Corzo G., Gilles N., Satake H., Villegas E., Dai L., Nakajima T., Haupt J.;
RT   "Distinct primary structures of the major peptide toxins from the venom of
RT   the spider Macrothele gigas that bind to sites 3 and 4 in the sodium
RT   channel.";
RL   FEBS Lett. 547:43-50(2003).
CC   -!- FUNCTION: Insecticidal neurotoxin. Shows competition for site 3 of
CC       insect voltage-gated sodium channels (Nav).
CC       {ECO:0000269|PubMed:12860384}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12860384,
CC       ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:12860384, ECO:0000305}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=4563.0; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12860384};
CC   -!- MISCELLANEOUS: Has no effect on lepidopteran larvae when injected at 20
CC       pmol/g, or on mice when injected intracranially at 32.8 nmol/g.
CC       {ECO:0000269|PubMed:12860384}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. 09 (magi-1)
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P83557; -.
DR   SMR; P83557; -.
DR   ArachnoServer; AS000376; mu-hexatoxin-Mg1b.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012627; Toxin_22.
DR   Pfam; PF08092; Toxin_22; 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-hexatoxin-Mg1b"
FT                   /id="PRO_0000045035"
FT   MOD_RES         38
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000269|PubMed:12860384"
FT   DISULFID        1..15
FT                   /evidence="ECO:0000250"
FT   DISULFID        8..20
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..34
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   38 AA;  4602 MW;  F77D05A218675600 CRC64;
     CMGYDIHCTD RLPCCFGLEC VKTSGYWWYK KTYCRRKS