ID   SCX13_TITOB             Reviewed;          89 AA.
AC   H1ZZI2; A0A1E1WWD6;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Sodium channel toxin To13 {ECO:0000303|PubMed:22355312};
DE   AltName: Full=T NaTx8.1;
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], NOMENCLATURE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and 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).
RN   [2] {ECO:0000312|EMBL:JAT91106.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Telson;
RX   PubMed=29561852; DOI=10.1371/journal.pone.0193739;
RA   de Oliveira U.C., Nishiyama M.Y. Jr., Dos Santos M.B.V.,
RA   Santos-da-Silva A.P., Chalkidis H.M., Souza-Imberg A., Candido D.M.,
RA   Yamanouye N., Dorce V.A.C., Junqueira-de-Azevedo I.L.M.;
RT   "Proteomic endorsed transcriptomic profiles of venom glands from Tityus
RT   obscurus and T. serrulatus scorpions.";
RL   PLoS ONE 13:e0193739-e0193739(2018).
CC   -!- FUNCTION: Inhibits voltage-gated sodium channels (Nav). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22355312}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:22355312}.
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. {ECO:0000305}.
CC   -!- CAUTION: The fragment sequence AC P84683 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 P84683 does not
CC       correspond to theoretical mass of the peptide presented here.
CC       {ECO:0000305}.
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DR   EMBL; HE585236; CCD31430.1; -; mRNA.
DR   EMBL; GEMQ01000083; JAT91106.1; -; mRNA.
DR   AlphaFoldDB; H1ZZI2; -.
DR   SMR; H1ZZI2; -.
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; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW   Toxin; Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..89
FT                   /note="Sodium channel toxin To13"
FT                   /id="PRO_5000851438"
FT   DOMAIN          20..87
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        30..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        34..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        45..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        49..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   CONFLICT        33
FT                   /note="E -> K (in Ref. 2; JAT91106)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   89 AA;  10112 MW;  A53B575D961679F0 CRC64;
     MKTLFLIITS FILLEVEGIK NGYPRDSKGC TFECGQDAKH GDDYCDKMCK TTLKGEGGDC
     DFEYAECWCD NIPDTVVTWK NKEPKCKQI