ID   SCX10_TITPA             Reviewed;          66 AA.
AC   C0HLZ1;
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 Tppa2 {ECO:0000303|PubMed:35024608};
DE   AltName: Full=Toxin Cocle-A1 {ECO:0000303|PubMed:29196122};
OS   Tityus pachyurus (Colombian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=288781 {ECO:0000303|PubMed:35024608};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROBABLE AMIDATION AT CYS-62.
RC   STRAIN=Cocle area; TISSUE=Venom gland;
RX   PubMed=29196122; DOI=10.1016/j.toxicon.2017.11.013;
RA   Salazar M.H., Arenas I., Corrales-Garcia L.L., Miranda R., Velez S.,
RA   Sanchez J., Mendoza K., Cleghorn J., Zamudio F.Z., Castillo A.,
RA   Possani L.D., Corzo G., Acosta H.;
RT   "Venoms of Centruroides and Tityus species from Panama and their main toxic
RT   fractions.";
RL   Toxicon 141:79-87(2018).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   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: 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|UniProtKB:Q2NME3}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29196122,
CC       ECO:0000269|PubMed:35024608}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:29196122, ECO:0000305|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=7099.1; 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}.
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DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   1: Evidence at protein level;
KW   Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..62
FT                   /note="Toxin Tppa2"
FT                   /id="PRO_0000456089"
FT   DOMAIN          1..63
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         62
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000305|PubMed:29196122"
FT   DISULFID        11..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        15..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        23..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        27..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   66 AA;  7578 MW;  502794B9C4DD7385 CRC64;
     KDGYLVGNDG CKYSCLTRPG HYCASECSRV KGKDGYCYAW MACYCYNMPN WVKTWSRATN
     KCGKRK