ID   TX22A_MACGS             Reviewed;          46 AA.
AC   P83559;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Mu-hexatoxin-Mg2a {ECO:0000305};
DE            Short=Mu-HXTX-Mg2a {ECO:0000305};
DE   AltName: Full=Neurotoxin magi-3 {ECO:0000303|PubMed:12860384, ECO:0000303|PubMed:29247580};
OS   Macrothele gigas (Japanese funnel web spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Macrothelidae; Macrothele.
OX   NCBI_TaxID=223896;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   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).
RN   [2]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=29247580; DOI=10.1002/pro.3363;
RA   Titaux-Delgado G., Carrillo E., Mendoza A., Mayorga-Flores M.,
RA   Escobedo-Gonzalez F.C., Cano-Sanchez P., Lopez-Vera E., Corzo G.,
RA   Del Rio-Portilla F.;
RT   "Successful refolding and NMR structure of rMagi3: a disulfide-rich
RT   insecticidal spider toxin.";
RL   Protein Sci. 27:692-701(2018).
CC   -!- FUNCTION: Competes for binding at site 3 of the insect voltage-gated
CC       sodium channel (Nav) (PubMed:12860384). Insecticidal neurotoxin
CC       (PubMed:12860384, PubMed:29247580). Causes temporary paralysis to
CC       lepidopteran larvae (10.3 nmol/g) or to crickets (doses from 0.93 to
CC       119 ug/g) (PubMed:12860384, PubMed:29247580). Is not toxic to mice when
CC       injected intracranially (high doses) (PubMed:12860384,
CC       PubMed:29247580). {ECO:0000269|PubMed:12860384,
CC       ECO:0000269|PubMed:29247580}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12860384}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:12860384}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000269|PubMed:29247580}.
CC   -!- MASS SPECTROMETRY: Mass=5222.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12860384};
CC   -!- MISCELLANEOUS: Shows very weak inhibition on rat Nav1.4/SCN4A sodium
CC       channels (23% at 50 uM of toxin and 35% at 100 uM).
CC       {ECO:0000269|PubMed:29247580}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 02 (plectoxin) family. 02
CC       (plectoxin) subfamily.
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DR   PDB; 6AX2; NMR; -; A=1-46.
DR   PDBsum; 6AX2; -.
DR   AlphaFoldDB; P83559; -.
DR   BMRB; P83559; -.
DR   SMR; P83559; -.
DR   ArachnoServer; AS000380; mu-hexatoxin-Mg2a.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..46
FT                   /note="Mu-hexatoxin-Mg2a"
FT                   /evidence="ECO:0000269|PubMed:12860384"
FT                   /id="PRO_0000087679"
FT   DISULFID        3..18
FT                   /evidence="ECO:0000269|PubMed:29247580,
FT                   ECO:0007744|PDB:6AX2"
FT   DISULFID        10..24
FT                   /evidence="ECO:0000269|PubMed:29247580,
FT                   ECO:0007744|PDB:6AX2"
FT   DISULFID        17..36
FT                   /evidence="ECO:0000269|PubMed:29247580,
FT                   ECO:0007744|PDB:6AX2"
FT   DISULFID        21..43
FT                   /evidence="ECO:0000269|PubMed:29247580,
FT                   ECO:0007744|PDB:6AX2"
FT   DISULFID        26..34
FT                   /evidence="ECO:0000269|PubMed:29247580,
FT                   ECO:0007744|PDB:6AX2"
FT   STRAND          17..19
FT                   /evidence="ECO:0007829|PDB:6AX2"
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:6AX2"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:6AX2"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:6AX2"
SQ   SEQUENCE   46 AA;  5233 MW;  CC2AB39F1C53DD52 CRC64;
     GGCIKWNHSC QTTTLKCCGK CVVCYCHTPW GTNCRCDRTR LFCTED