SCX3_TITOB
ID SCX3_TITOB Reviewed; 86 AA.
AC P60213; A0A1E1WVN9; H1ZZH2; P84687;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 3.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Toxin To3 {ECO:0000303|PubMed:22355312};
DE AltName: Full=PT-alpha' NaTx14.2;
DE AltName: Full=Toxin Tc48b/Tc49a;
DE AltName: Full=Toxin To48b/To49a;
DE Flags: Precursor;
OS Tityus obscurus (Amazonian scorpion) (Tityus cambridgei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=1221240;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AMIDATION AT ARG-84, AND NOMENCLATURE.
RC TISSUE=Venom gland;
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).
RN [2] {ECO:0000312|EMBL:JAT91089.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Telson;
RX PubMed=29561852; DOI=10.1371/journal.pone.0193739;
RA de Oliveira U.C., Nishiyama M.Y. Jr., Dos Santos M.B.V.,
RA Santos-da-Silva A.P., Chalkidis H.M., Souza-Imberg A., Candido D.M.,
RA Yamanouye N., Dorce V.A.C., Junqueira-de-Azevedo I.L.M.;
RT "Proteomic endorsed transcriptomic profiles of venom glands from Tityus
RT obscurus and T. serrulatus scorpions.";
RL PLoS ONE 13:e0193739-e0193739(2018).
RN [3]
RP PROTEIN SEQUENCE OF 21-64, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=15109895; DOI=10.1016/j.toxicon.2004.02.014;
RA Murgia A.R., Batista C.V.F., Prestipino G., Possani L.D.;
RT "Amino acid sequence and function of a new alpha-toxin from the Amazonian
RT scorpion Tityus cambridgei.";
RL Toxicon 43:737-740(2004).
RN [4]
RP PROTEIN SEQUENCE OF 21-59, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=11821128; DOI=10.1016/s0041-0101(01)00252-5;
RA Batista C.V.F., Zamudio F.Z., Lucas S., Fox J.W., Frau A., Prestipino G.,
RA Possani L.D.;
RT "Scorpion toxins from Tityus cambridgei that affect Na(+)-channels.";
RL Toxicon 40:557-562(2002).
RN [5]
RP PROTEIN SEQUENCE OF 21-30, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=15025998; DOI=10.1016/j.jchromb.2003.09.002;
RA Batista C.V.F., del Pozo L., Zamudio F.Z., Contreras S., Becerril B.,
RA Wanke E., Possani L.D.;
RT "Proteomics of the venom from the Amazonian scorpion Tityus cambridgei and
RT the role of prolines on mass spectrometry analysis of toxins.";
RL J. Chromatogr. B 803:55-66(2004).
CC -!- FUNCTION: Affects sodium-permeability in pituitary GH3 cells in
CC culture. Inhibits the inactivation of sodium activated channels (Nav).
CC Slightly delays the activation time course, and consequently the time
CC to peak. Shifts the voltage dependence of the activation to more
CC negative potentials. Does not reduce the peak sodium-current amplitude.
CC {ECO:0000269|PubMed:15109895}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11821128,
CC ECO:0000269|PubMed:15025998}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:11821128, ECO:0000269|PubMed:15025998}.
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=7151; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11821128};
CC -!- MASS SPECTROMETRY: Mass=7152.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15025998};
CC -!- MASS SPECTROMETRY: Mass=7385.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15109895};
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 does not seem to be a typical beta-scorpion toxin,
CC but causes a rather alpha-scorpion toxin-like effect. {ECO:0000305}.
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DR EMBL; HE585226; CCD31420.1; -; mRNA.
DR EMBL; GEMQ01000100; JAT91089.1; -; mRNA.
DR AlphaFoldDB; P60213; -.
DR SMR; P60213; -.
DR GO; GO:0005576; C:extracellular region; HDA:UniProtKB.
DR GO; GO:0019871; F:sodium channel inhibitor activity; ISS:UniProtKB.
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; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:11821128,
FT ECO:0000269|PubMed:15025998, ECO:0000269|PubMed:15109895"
FT CHAIN 21..84
FT /note="Toxin To3"
FT /id="PRO_0000066810"
FT DOMAIN 21..83
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 84
FT /note="Arginine amide"
FT /evidence="ECO:0000269|PubMed:22355312"
FT DISULFID 31..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 35..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 43..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 47..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT CONFLICT 13
FT /note="V -> L (in Ref. 2; JAT91089)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="K -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 86 AA; 9903 MW; 9A205478D39E617E CRC64;
MTRFVLFISC FFVIGMVVEC KDGYLVGNDG CKYNCLTRPG HYCANECSRV KGKDGYCYAW
MACYCYSMPD WVKTWSRSTN RCGRGK
