SCNA8_TITDI
ID SCNA8_TITDI Reviewed; 85 AA.
AC C9X4K6;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Toxin TdNa8;
DE AltName: Full=P*T-alpha* NaTx3.6;
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 MASS SPECTROMETRY.
RX PubMed=16705749; DOI=10.1002/pmic.200500525;
RA Batista C.V.F., D'Suze G., Gomez-Lagunas F., Zamudio F.Z., Encarnacion S.,
RA Sevcik C., Possani L.D.;
RT "Proteomic analysis of Tityus discrepans scorpion venom and amino acid
RT sequence of novel toxins.";
RL Proteomics 6:3718-3727(2006).
RN [3]
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. {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 -!- MASS SPECTROMETRY: Mass=7090.8; Method=MALDI; Note=very likely
CC corresponds to the mass found for the peptide eluting at 35.93
CC minutes.; Evidence={ECO:0000269|PubMed:16705749};
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Alpha subfamily. {ECO:0000305}.
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DR EMBL; FN392284; CAY61941.1; -; mRNA.
DR AlphaFoldDB; C9X4K6; -.
DR SMR; C9X4K6; -.
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 1: Evidence at protein level;
KW Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Secreted; Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..82
FT /note="Toxin TdNa8"
FT /id="PRO_5000525372"
FT DOMAIN 21..81
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 82
FT /note="Proline amide"
FT /evidence="ECO:0000250"
FT DISULFID 31..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 35..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 42..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 46..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 85 AA; 9341 MW; 32C433B9E7A54929 CRC64;
MNYLTLIAAA SLLTAGTESK KDGYPVKEGD CAFPCGYDNA YCDKLCKERK ADSGYCYWGN
ILCYCYGLPD KAAIKGYGRC RPGKK