ID   SCNAA_TITDI             Reviewed;          81 AA.
AC   C9X4K8;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Toxin TdNa10;
DE   AltName: Full=T-alpha* NaTx7.2;
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].
RC   TISSUE=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 {ECO:0000250}.
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: 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; FN392286; CAY61946.1; -; mRNA.
DR   AlphaFoldDB; C9X4K8; -.
DR   SMR; C9X4K8; -.
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   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW   Toxin; Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..81
FT                   /note="Toxin TdNa10"
FT                   /id="PRO_5000525374"
FT   DOMAIN          21..81
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        32..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        36..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        42..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        46..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   81 AA;  9107 MW;  C68F622EE5474243 CRC64;
     MWTFAIVLAF LLIGLDEGEA LDGYPLSKNN YCKIYCPNTE VCKDTCKRRA GATDGECRWD
     GCYCFNVAPD TKMYPGELPC H