ID   TX24A_MACGS             Reviewed;          77 AA.
AC   Q75WH3;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=U11-hexatoxin-Mg1a;
DE            Short=U11-HXTX-Mg1a;
DE   AltName: Full=Neurotoxin magi-10 {ECO:0000303|PubMed:15246762};
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, SUBCELLULAR
RP   LOCATION, AND BIOASSAY.
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).
RN   [2]
RP   FUNCTION, AND SYNTHESIS OF 43-77.
RX   PubMed=29483648; DOI=10.1038/s41594-018-0033-9;
RA   Correnti C.E., Gewe M.M., Mehlin C., Bandaranayake A.D., Johnsen W.A.,
RA   Rupert P.B., Brusniak M.Y., Clarke M., Burke S.E., De Van Der Schueren W.,
RA   Pilat K., Turnbaugh S.M., May D., Watson A., Chan M.K., Bahl C.D.,
RA   Olson J.M., Strong R.K.;
RT   "Screening, large-scale production and structure-based classification of
RT   cystine-dense peptides.";
RL   Nat. Struct. Mol. Biol. 25:270-278(2018).
CC   -!- FUNCTION: Inhibits Kv11.1/KCNH2/ERG1, Kv1.1/KCNA1 and Kv1.3/KCNA3
CC       voltage-gated potassium channels and Nav1.7/SCN9A voltage-gated sodium
CC       channels (PubMed:29483648). In vivo, intracranial injection into mice
CC       causes lack of coordination for 10 min, followed by fast recovery.
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. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=3734.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15246762};
CC   -!- SIMILARITY: Belongs to the neurotoxin 02 (plectoxin) family. 04 (U16-
CC       lycotoxin) subfamily.
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DR   EMBL; AB121198; BAD13405.1; -; mRNA.
DR   AlphaFoldDB; Q75WH3; -.
DR   ArachnoServer; AS000361; U11-hexatoxin-Mg1a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
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   Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..42
FT                   /id="PRO_0000285709"
FT   CHAIN           43..77
FT                   /note="U11-hexatoxin-Mg1a"
FT                   /id="PRO_0000285710"
FT   DISULFID        44..59
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..64
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..75
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   77 AA;  8342 MW;  95F30A150CB476A1 CRC64;
     MKVFSFTVVV VMILSLSAFV LAGDEGDVMK KIVAMEEAVE ERACLAEYQK CEGSTVPCCP
     GLSCSAGRFR KTKLCTK