SCNA1_TITDI
ID SCNA1_TITDI Reviewed; 80 AA.
AC C9X4J9;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Toxin TdNa1;
DE AltName: Full=PT-Arthr*-beta* NaTx2.2;
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], AND PROTEIN SEQUENCE OF 21-46.
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: Inhibits the sodium (Nav) currents in an apparent
CC irreversible manner. Produces small depolarization and induces
CC repetitive firing in squid axons. Is specific for arthropods (crickets,
CC triatomides, crabs and squids), but is non-toxic to mice (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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN392277; CAY61927.1; -; mRNA.
DR AlphaFoldDB; C9X4J9; -.
DR SMR; C9X4J9; -.
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 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 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..20
FT /evidence="ECO:0000269|PubMed:19470401"
FT CHAIN 21..80
FT /note="Toxin TdNa1"
FT /id="PRO_5000525366"
FT DOMAIN 21..79
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 31..78
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 80 AA; 9067 MW; 42382873612F89BA CRC64;
MKGIILFISC LMLIDVVVES RDAYPADWRG CKFSCFWGSS SWCNEECTSL GGSSGYCAWP
ACWCYGLPDS VRYYNNKCHK
