ID   SCX30_TITSE             Reviewed;          89 AA.
AC   A0A7S8RFY1; A0A218QXD4;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   03-AUG-2022, entry version 5.
DE   RecName: Full=Putative sodium channel toxin Ts30 {ECO:0000303|PubMed:33181162};
DE   AltName: Full=Putative NaTx {ECO:0000303|PubMed:33181162};
DE   AltName: Full=Tityustoxin-30 {ECO:0000305};
DE   Flags: Precursor;
OS   Tityus serrulatus (Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=6887;
RN   [1] {ECO:0000312|EMBL:QPD99024.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Telson;
RX   PubMed=33181162; DOI=10.1016/j.toxicon.2020.11.001;
RA   Kalapothakis Y., Miranda K., Pereira A.H., Witt A.S.A., Marani C.,
RA   Martins A.P., Leal H.G., Campos-Junior E., Pimenta A.M.C., Borges A.,
RA   Chavez-Olortegui C., Kalapothakis E.;
RT   "Novel components of Tityus serrulatus venom: a transcriptomic approach.";
RL   Toxicon 189:91-104(2021).
RN   [2] {ECO:0000312|EMBL:JAW07013.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-89.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:29561852,
CC       ECO:0000305|PubMed:33181162}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:29561852, ECO:0000305|PubMed:33181162}.
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}.
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DR   EMBL; MT081342; QPD99024.1; -; mRNA.
DR   EMBL; GEUW01000032; JAW07013.1; -; mRNA.
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:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
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   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW   Toxin; Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..89
FT                   /note="Putative sodium channel toxin Ts30"
FT                   /id="PRO_5031043448"
FT   DOMAIN          21..85
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        31..84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        35..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        44..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        48..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   89 AA;  9934 MW;  E549B4D0F4496C5C CRC64;
     MFKLAIILAL LFFGARAGAV RDGYPILSDG CKYTCKPLGE NQNCSRICKE KAGSWYGYCY
     MWACYCTDVS KKAVLFGDSG TPECHVWIK