ID   SCNA1_TITCE             Reviewed;          64 AA.
AC   C0HLZ2;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 1.
DT   03-AUG-2022, entry version 1.
DE   RecName: Full=Toxin Tce3 {ECO:0000303|PubMed:35024608};
OS   Tityus cerroazul (Scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=2684170 {ECO:0000303|PubMed:35024608};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-25, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland {ECO:0000303|PubMed:35024608};
RX   PubMed=35024608; DOI=10.1016/j.toxcx.2021.100090;
RA   Salazar M.H., Clement H., Corrales-Garcia L.L., Sanchez J., Cleghorn J.,
RA   Zamudio F., Possani L.D., Acosta H., Corzo G.;
RT   "Heterologous expression of four recombinant toxins from Panamanian
RT   scorpions of the genus Tityus and Centruroides for production of
RT   antivenom.";
RL   Toxicon X 13:100090-100090(2022).
CC   -!- FUNCTION: Inhibits the sodium (Nav) currents in an apparent
CC       irreversible manner (By similarity). Produces small depolarization and
CC       induces repetitive firing in squid axons (By similarity). Is specific
CC       for arthropods (crickets, triatomides, crabs and squids), but is non-
CC       toxic to mice (By similarity). Shows antibacterial activity against
CC       both Gram-positive and Gram-negative bacteria (By similarity).
CC       {ECO:0000250|UniProtKB:P0C1X7, ECO:0000250|UniProtKB:P0CF39}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:35024608}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:35024608}.
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   -!- MASS SPECTROMETRY: Mass=6966.9; Method=Electrospray; Note=Average
CC       mass.; Evidence={ECO:0000269|PubMed:35024608};
CC   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..64
FT                   /note="Toxin Tce3"
FT                   /id="PRO_0000456090"
FT   DOMAIN          1..62
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        11..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        15..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        23..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        27..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   64 AA;  7231 MW;  EE09D7A725C720B0 CRC64;
     KDGYIIEHRG CKYSCFFGSS SWCNKECTLK KGSSGYCAWP ACWCYGLPDS VKIFDSNNNK
     CSKK