ID   SCX8_TITOB              Reviewed;          86 AA.
AC   H1ZZH7;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Toxin To8;
DE   AltName: Full=PT-beta* NaTx10.1;
DE   Flags: Precursor;
OS   Tityus obscurus (Amazonian scorpion) (Tityus cambridgei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=1221240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND NOMENCLATURE.
RC   TISSUE=Venom gland;
RX   PubMed=22355312; DOI=10.1371/journal.pone.0030478;
RA   Guerrero-Vargas J.A., Mourao C.B., Quintero-Hernandez V., Possani L.D.,
RA   Schwartz E.F.;
RT   "Identification and phylogenetic analysis of Tityus pachyurus and Tityus
RT   obscurus novel putative Na+-channel scorpion toxins.";
RL   PLoS ONE 7:E30478-E30478(2012).
CC   -!- FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium
CC       channels (Nav) and shift the voltage of activation toward more negative
CC       potentials thereby affecting sodium channel activation and promoting
CC       spontaneous and repetitive firing. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
CC   -!- CAUTION: The fragment sequence AC P84691 is identical to the sequence
CC       presented in this entry, but both peptides are probably different
CC       peptides, since the experimental molecular mass of AC P84691 does not
CC       correspond to theoretical mass of the peptide presented here.
CC       {ECO:0000305}.
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DR   EMBL; HE585231; CCD31425.1; -; mRNA.
DR   AlphaFoldDB; H1ZZH7; -.
DR   SMR; H1ZZH7; -.
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   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR018218; Scorpion_toxinL.
DR   InterPro; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 1.
DR   PRINTS; PR00285; SCORPNTOXIN.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Secreted; Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..82
FT                   /note="Toxin To8"
FT                   /id="PRO_5000851428"
FT   DOMAIN          21..83
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         82
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        35..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        43..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        47..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   86 AA;  9866 MW;  0EAF44DACD567065 CRC64;
     MTRFVLFISC FFLIGMVVEC KEGYLLGSRG CKMNCLTRPE KFCELECSLV GGENGYCAYW
     LACYCYNVPE SVKLWESDTN ECGKRK