ID   TXM11_MACGS             Reviewed;          81 AA.
AC   Q75WH2;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=U12-hexatoxin-Mg1a;
DE            Short=U12-HXTX-Mg1a;
DE   AltName: Full=Neurotoxin magi-11;
DE   AltName: Full=Peptide toxin 5;
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MASS SPECTROMETRY, AMIDATION AT
RP   PRO-78, SYNTHESIS OF 51-78, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=15246762; DOI=10.1016/j.toxicon.2004.05.012;
RA   Satake H., Villegas E., Oshiro N., Terada K., Shinada T., Corzo G.;
RT   "Rapid and efficient identification of cysteine-rich peptides by random
RT   screening of a venom gland cDNA library from the hexathelid spider
RT   Macrothele gigas.";
RL   Toxicon 44:149-156(2004).
CC   -!- FUNCTION: Blocks voltage-gated sodium channels (Nav) (By similarity).
CC       Intracranial injection into mice causes lacrimation, slow breathing and
CC       death. Intrathorax injection into crickets causes death. {ECO:0000250,
CC       ECO:0000269|PubMed:15246762}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15246762}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15246762}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P83561}.
CC   -!- MASS SPECTROMETRY: Mass=3227.1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15246762};
CC   -!- SIMILARITY: Belongs to the neurotoxin 15 family. 01 (magi-5) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB121199; BAD13406.1; -; mRNA.
DR   AlphaFoldDB; Q75WH2; -.
DR   SMR; Q75WH2; -.
DR   ArachnoServer; AS000363; U12-hexatoxin-Mg1a.
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; IPR012628; Toxin_23.
DR   Pfam; PF08093; Toxin_23; 1.
PE   1: Evidence at protein level;
KW   Amidation; Disulfide bond; Ion channel impairing toxin; Knottin;
KW   Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..50
FT                   /evidence="ECO:0000250|UniProtKB:P83561"
FT                   /id="PRO_0000284761"
FT   PEPTIDE         51..78
FT                   /note="U12-hexatoxin-Mg1a"
FT                   /id="PRO_0000284762"
FT   MOD_RES         78
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:15246762"
FT   DISULFID        52..66
FT                   /evidence="ECO:0000250|UniProtKB:P83561"
FT   DISULFID        59..71
FT                   /evidence="ECO:0000250|UniProtKB:P83561"
FT   DISULFID        65..75
FT                   /evidence="ECO:0000250|UniProtKB:P83561"
SQ   SEQUENCE   81 AA;  9266 MW;  C7B17543642FF9C0 CRC64;
     MKAPATIVIL IMSLISVLWA TADTEDGNLL FPIEDFIRKF DEYPVQPKER SCKLTFWRCK
     KDKECCGWNI CTGLCIPPGK K