SCX1_TITST
ID SCX1_TITST Reviewed; 84 AA.
AC P56612;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Toxin Tst1;
DE AltName: Full=PT-Mice-beta* NaTx6.3;
DE AltName: Full=Tst-gamma;
DE Flags: Precursor;
OS Tityus stigmurus (Brazilian scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=50344;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-81, AMIDATION AT
RP CYS-81, AND BIOASSAY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=8611151; DOI=10.1042/bj3130753;
RA Becerril B., Corona M., Coronas F.I., Zamudio F.Z., Calderon-Aranda E.S.,
RA Fletcher P.L. Jr., Martin B.M., Possani L.D.;
RT "Toxic peptides and genes encoding toxin gamma of the Brazilian scorpions
RT Tityus bahiensis and Tityus stigmurus.";
RL Biochem. J. 313:753-760(1996).
RN [2]
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=17270501; DOI=10.1016/j.cbpc.2006.12.004;
RA Batista C.V.F., Roman-Gonzalez S.A., Salas-Castillo S.P., Zamudio F.Z.,
RA Gomez-Lagunas F., Possani L.D.;
RT "Proteomic analysis of the venom from the scorpion Tityus stigmurus:
RT biochemical and physiological comparison with other Tityus species.";
RL Comp. Biochem. Physiol. 146C:147-157(2007).
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: Beta toxins bind voltage-independently at site-4 of sodium
CC channels (Nav) and shift the voltage of activation toward more negative
CC potentials thereby affecting sodium channel activation and promoting
CC spontaneous and repetitive firing. This toxin is active only on mammals
CC (By similarity). Is toxic to mice (PubMed:8611151). {ECO:0000250,
CC ECO:0000269|PubMed:8611151}.
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 -!- MASS SPECTROMETRY: Mass=6983.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17270501};
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 PIR; S62867; S62867.
DR AlphaFoldDB; P56612; -.
DR SMR; P56612; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0051701; P:biological process involved in interaction with host; IDA:UniProtKB.
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; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:8611151"
FT CHAIN 20..81
FT /note="Toxin Tst1"
FT /id="PRO_0000035306"
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:0000305|PubMed:8611151"
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 84 AA; 9366 MW; 460653ABAE1F7877 CRC64;
MKGMILFISC LLLIDIVVGG KEGYLMDHEG CKLSCFIRPS GYCGRECTLK KGSSGYCAWP
ACYCYGLPNW VKVWDRATNK CGKK
