ID   SCX3_TITFA              Reviewed;          67 AA.
AC   P0DSO4;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Beta-toxin Tf3 {ECO:0000303|PubMed:25817000};
OS   Tityus fasciolatus (Central Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=203543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=25817000; DOI=10.1016/j.toxicon.2015.03.018;
RA   Mendes T.M., Guimaraes-Okamoto P.T., Machado-de-Avila R.A., Oliveira D.,
RA   Melo M.M., Lobato Z.I., Kalapothakis E., Chavez-Olortegui C.;
RT   "General characterization of Tityus fasciolatus scorpion venom. Molecular
RT   identification of toxins and localization of linear B-cell epitopes.";
RL   Toxicon 99:109-117(2015).
CC   -!- FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium
CC       channels (Nav) and inhibit the inactivation of the activated channels,
CC       thereby blocking neuronal transmission. {ECO:0000250|UniProtKB:P01496}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25817000}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:25817000}.
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. Alpha subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DSO4; -.
DR   SMR; P0DSO4; -.
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   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   CDD; cd00107; Knot1; 1.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR   InterPro; IPR003614; Scorpion_toxin-like.
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   SMART; SM00505; Knot1; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   3: Inferred from homology;
KW   Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..64
FT                   /note="Beta-toxin Tf3"
FT                   /evidence="ECO:0000305|PubMed:25817000"
FT                   /id="PRO_0000447417"
FT   DOMAIN          2..63
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         64
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000250|UniProtKB:P01484"
FT   DISULFID        12..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        16..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        24..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        28..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   67 AA;  7616 MW;  E853741681299341 CRC64;
     KKDGYPVEGD NCAFVCFGYD NAYCDKLCKD KKADSGYCYW VHILCYCYGL PDKEPTKTNG
     RCKPGKK