ID   TXR3_MACRV              Reviewed;          29 AA.
AC   P61232;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Beta-hexatoxin-Mr1a;
DE            Short=Beta-HXTX-Mr1a;
DE   AltName: Full=Raventoxin III;
DE   AltName: Full=Raventoxin-3;
OS   Macrothele raveni (Funnel-web spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Macrothelidae; Macrothele.
OX   NCBI_TaxID=269627;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=12727269; DOI=10.1016/s0041-0101(02)00361-6;
RA   Zeng X.-Z., Xiao Q.-B., Liang S.-P.;
RT   "Purification and characterization of raventoxin-I and raventoxin-III, two
RT   neurotoxic peptides from the venom of the spider Macrothele raveni.";
RL   Toxicon 41:651-656(2003).
CC   -!- FUNCTION: Insect and vertebrate active toxin. Binds at site 4 of
CC       mammalian voltage-gated sodium channels and shifts the activation
CC       voltage of the mammalian rNav1.2a (SCN2A) channel to more
CC       hyperpolarized voltages, whereas the insect channel, DmNav1 (para), is
CC       not affected. Causes temporary paralysis when injected into
CC       lepidopteran larvae at 8.6 nmol/g. A low intracranial injection dose
CC       into mice causes lacrimation, closure of the eyes and sweating. A high
CC       injection dose causes extensive lacrimation and death.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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   -!- MASS SPECTROMETRY: Mass=3287.58; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12727269};
CC   -!- MISCELLANEOUS: The primary structure of the mature toxin is identical
CC       to that of beta-hexatoxin-Mg1a (Magi-5) from Macrothele gigas (AC
CC       P83561).
CC   -!- SIMILARITY: Belongs to the neurotoxin 15 family. 01 (magi-5) subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P61232; -.
DR   SMR; P61232; -.
DR   ArachnoServer; AS000417; beta-hexatoxin-Mr1a.
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   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Knottin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..29
FT                   /note="Beta-hexatoxin-Mr1a"
FT                   /evidence="ECO:0000269|PubMed:12727269"
FT                   /id="PRO_0000044557"
FT   DISULFID        2..16
FT                   /evidence="ECO:0000250|UniProtKB:P83561"
FT   DISULFID        9..21
FT                   /evidence="ECO:0000250|UniProtKB:P83561"
FT   DISULFID        15..26
FT                   /evidence="ECO:0000250|UniProtKB:P83561"
SQ   SEQUENCE   29 AA;  3293 MW;  9143A6E21E4D09FE CRC64;
     GCKLTFWKCK NKKECCGWNA CALGICMPR