ID   SCNA5_TITDI             Reviewed;          83 AA.
AC   C9X4K3;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Toxin TdNa5;
DE   AltName: Full=T-Arthr*-beta* NaTx2.5;
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: Inhibits the sodium currents (Nav) in an apparent
CC       irreversible manner (By similarity). Produces small depolarization and
CC       induces repetitive firing in squid axons (By similarity). Is specific
CC       for arthropods (crickets, triatomides, crabs and squids), but is non-
CC       toxic to mice (By similarity). Shows antibacterial activity against
CC       both Gram-positive and Gram-negative bacteria (By similarity).
CC       {ECO:0000250|UniProtKB:P0C1X7, ECO:0000250|UniProtKB:P0CF39}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:19470401}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:19470401}.
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}.
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DR   EMBL; FN392281; CAY61935.1; -; mRNA.
DR   AlphaFoldDB; C9X4K3; -.
DR   SMR; C9X4K3; -.
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; Antibiotic; Antimicrobial; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..81
FT                   /note="Toxin TdNa5"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1X7"
FT                   /id="PRO_5000525369"
FT   DOMAIN          21..82
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         81
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1X7"
FT   DISULFID        31..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        35..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        43..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        47..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   83 AA;  9382 MW;  36C3E084DA74E644 CRC64;
     MKTIIFFIAC LMLIDVVVES KDGYIIEHRG CKYSCFFGTN SWCNTECTLK KGSSGYCAWP
     ACWCYGLPDN VKIFDSNNNK CGK