ID   SCNA9_TITDI             Reviewed;          85 AA.
AC   C9X4K7;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Toxin TdNa9;
DE   AltName: Full=PT-alpha* NaTx7.1;
DE   Flags: Precursor;
OS   Tityus discrepans (Venezuelan scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=57059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-47.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=19470401; DOI=10.1016/j.biochi.2009.05.005;
RA   D'Suze G., Schwartz E.F., Garcia-Gomez B.I., Sevcik C., Possani L.D.;
RT   "Molecular cloning and nucleotide sequence analysis of genes from a cDNA
RT   library of the scorpion Tityus discrepans.";
RL   Biochimie 91:1010-1019(2009).
RN   [2]
RP   NOMENCLATURE.
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).
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. This toxin binds, in vitro, to
CC       sodium channels and inhibits the inactivation of the activated
CC       channels. Seems not toxic to mice, crickets and sweet-water shrimps (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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. Beta subfamily. {ECO:0000305}.
CC   -!- CAUTION: The Cys-43 indicated here is taken from the partial sequence
CC       in amino acid, and not from the translation of the transcript in which
CC       a Ser is found. {ECO:0000305}.
CC   -!- CAUTION: This toxin sequence resembles the beta scorpion toxin class,
CC       although patch-clamp experiments shows the induction of supplementary
CC       slow inactivation of sodium channels, which means that it behaves like
CC       an alpha scorpion toxin. {ECO:0000305}.
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DR   EMBL; FN392285; CAY61944.1; -; mRNA.
DR   AlphaFoldDB; C9X4K7; -.
DR   SMR; C9X4K7; -.
DR   TCDB; 8.B.1.1.11; the long (4c-c) scorpion toxin (l-st) superfamily.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
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   SUPFAM; SSF57095; SSF57095; 1.
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; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:19470401"
FT   CHAIN           22..85
FT                   /note="Toxin TdNa9"
FT                   /id="PRO_5000525373"
FT   DOMAIN          22..84
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        33..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        37..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        43..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        47..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   CONFLICT        43
FT                   /note="C -> S (in Ref. 1; CAY61944)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   85 AA;  9439 MW;  6F9FD3995206BE31 CRC64;
     MLKFAIAVAL LLFIGLELRE ARDGYPQSKV NYCKIYCPNT TVCQWTCKNR AGATDGDCRW
     SSCYCFNVAP DTVLYGDPGT KPCMA