SCX5_TITOB
ID SCX5_TITOB Reviewed; 84 AA.
AC P84693; A0A1E1WVU6; H1ZZH4;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Toxin To5 {ECO:0000303|PubMed:22355312};
DE AltName: Full=PT-Arthr*-beta* NaTx2.7;
DE AltName: Full=Toxin Tc66 {ECO:0000303|PubMed:15025998};
DE AltName: Full=Toxin To66 {ECO:0000305};
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], NOMENCLATURE, MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom, and 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:JAT91094.1}
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] {ECO:0000305}
RP PROTEIN SEQUENCE OF 20-29, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:15025998};
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: 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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15025998,
CC ECO:0000269|PubMed:22355312}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:15025998, ECO:0000305|PubMed:22355312}.
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=6937.1; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:22355312};
CC -!- MASS SPECTROMETRY: Mass=6935.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15025998};
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 EMBL; HE585228; CCD31422.1; -; mRNA.
DR EMBL; GEMQ01000095; JAT91094.1; -; Transcribed_RNA.
DR AlphaFoldDB; P84693; -.
DR SMR; P84693; -.
DR GO; GO:0005576; C:extracellular region; HDA:UniProtKB.
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; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:15025998"
FT CHAIN 20..81
FT /note="Toxin To5"
FT /evidence="ECO:0000305|PubMed:15025998"
FT /id="PRO_5000851422"
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:0000250"
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"
FT CONFLICT 21
FT /note="R -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 84 AA; 9310 MW; 624C205659DC9244 CRC64;
MKAIIFFIGC LMLIDLVAGS RSGYPVTQKG CVYSCFWGSN WWCNAECTAL GGSSGYCAWP
SCWCYSLPDN RNIWGSYPNN CGKK
