SCX5_TITSE
ID SCX5_TITSE Reviewed; 64 AA.
AC P46115;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Alpha-toxin Ts5 {ECO:0000303|PubMed:19689419};
DE AltName: Full=P-alpha* NaTx3.2;
DE AltName: Full=Tityustoxin V;
DE Short=Toxin V;
DE Short=Ts V;
DE Short=TsTX-V;
DE Short=TsV;
DE AltName: Full=Tityustoxin-5;
OS Tityus serrulatus (Brazilian scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=6887;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=7727504; DOI=10.1016/0304-4165(94)00142-k;
RA Marangoni S., Toyama M.H., Arantes E.C., Giglio J.R., da Silva C.A.,
RA Carneiro E.M., Goncalves A.A., Oliveira B.;
RT "Amino acid sequence of TsTX-V, an alpha-toxin from Tityus serrulatus
RT scorpion venom, and its effect on K+ permeability of beta-cells from
RT isolated rat islets of Langerhans.";
RL Biochim. Biophys. Acta 1243:309-314(1995).
RN [2]
RP PROTEIN SEQUENCE OF 6-20, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom {ECO:0000303|PubMed:25199494};
RX PubMed=25199494; DOI=10.1016/j.toxicon.2014.08.064;
RA Pucca M.B., Amorim F.G., Cerni F.A., Bordon K.C.F., Cardoso I.A.,
RA Anjolette F.A., Arantes E.C.;
RT "Influence of post-starvation extraction time and prey-specific diet in
RT Tityus serrulatus scorpion venom composition and hyaluronidase activity.";
RL Toxicon 90:326-336(2014).
RN [3]
RP AMINO ACID COMPOSITION, FUNCTION, AND TOXIC DOSE.
RX PubMed=8280757; DOI=10.1016/0304-4165(94)90098-1;
RA Arantes E.C., Riccioppo Neto F., Sampaio S.V., Vieira C.A., Giglio J.R.;
RT "Isolation and characterization of TsTX-V, a new neurotoxin from Tityus
RT serrulatus scorpion venom which delays the inactivation of Na+ channels.";
RL Biochim. Biophys. Acta 1199:69-75(1994).
RN [4]
RP FUNCTION, AND 3D-STRUCTURE MODELING.
RX PubMed=12875879; DOI=10.1016/s0041-0101(03)00086-2;
RA Goncalves A.A., Toyama M.H., Carneiro E.M., Marangoni S., Arantes E.C.,
RA Giglio J.R., Boschero A.C.;
RT "Participation of Na(+) channels in the potentiation by Tityus serrulatus
RT alpha-toxin TsTx-V of glucose-induced electrical activity and insulin
RT secretion in rodent islet beta-cells.";
RL Toxicon 41:1039-1045(2003).
RN [5]
RP NOMENCLATURE.
RX PubMed=19689419; DOI=10.2174/092986609788923329;
RA Cologna C.T., Marcussi S., Giglio J.R., Soares A.M., Arantes E.C.;
RT "Tityus serrulatus scorpion venom and toxins: an overview.";
RL Protein Pept. Lett. 16:920-932(2009).
RN [6]
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. By extending the depolarized
CC period it indirectly affects beta-cell voltage-dependent potassium
CC channels, thus increasing potassium permeability.
CC {ECO:0000269|PubMed:12875879, ECO:0000269|PubMed:8280757}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25199494,
CC ECO:0000269|PubMed:7727504}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:25199494}.
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 -!- TOXIC DOSE: LD(50) is 94 +/- 7 ug/kg by intravenous injection into
CC mice. {ECO:0000269|PubMed:8280757}.
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 PIR; S60352; S60352.
DR AlphaFoldDB; P46115; -.
DR SMR; P46115; -.
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 Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..64
FT /note="Alpha-toxin Ts5"
FT /evidence="ECO:0000269|PubMed:7727504"
FT /id="PRO_0000066826"
FT DOMAIN 2..64
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 12..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 16..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 24..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 28..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 64 AA; 7200 MW; 14BA04DE1EE103EF CRC64;
KKDGYPVEGD NCAFACFGYD NAYCDKLCKD KKADDGYCVW SPDCYCYGLP EHILKEPTKT
SGRC
