SCX2_TITST
ID SCX2_TITST Reviewed; 62 AA.
AC P68411; P23814;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Toxin Tst2;
DE AltName: Full=P-Mice-beta* NaTx5.2;
DE AltName: Full=Tityustoxin II;
DE Short=TsTX-II;
DE AltName: Full=Toxin III-8;
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 PROTEIN SEQUENCE, AND BIOASSAY.
RC TISSUE=Venom;
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: 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 similarity). Is toxic to
CC mice (PubMed:8611151). {ECO:0000250, 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=6989.2; 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}.
CC -!- CAUTION: This toxin is functionally similar to alpha toxins and
CC structurally similar to beta toxins. {ECO:0000305}.
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DR PIR; S62866; S62866.
DR AlphaFoldDB; P68411; -.
DR SMR; P68411; -.
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 Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..62
FT /note="Toxin Tst2"
FT /id="PRO_0000066825"
FT DOMAIN 1..62
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 62
FT /note="Cysteine amide"
FT /evidence="ECO:0000250|UniProtKB:P56612"
FT DISULFID 11..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 15..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 23..43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 27..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 62 AA; 6998 MW; E1564914002FD3E3 CRC64;
KEGYAMDHEG CKFSCFIRPA GFCDGYCKTH LKASSGYCAW PACYCYGVPD HIKVWDYATN
KC