SCX3_CENEX
ID SCX3_CENEX Reviewed; 69 AA.
AC Q68PH2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Neurotoxin Cex3;
DE Flags: Precursor; Fragment;
OS Centruroides exilicauda (Bark scorpion) (Buthus exilicauda).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX NCBI_TaxID=6879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=15358055; DOI=10.1016/j.biochi.2004.05.005;
RA Valdez-Cruz N.A., Davila S., Licea A., Corona M., Zamudio F.Z.,
RA Garcia-Valdes J., Boyer L., Possani L.D.;
RT "Biochemical, genetic and physiological characterization of venom
RT components from two species of scorpions: Centruroides exilicauda Wood and
RT Centruroides sculpturatus Ewing.";
RL Biochimie 86:387-396(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:0000250}.
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 -!- 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; AY649861; AAT97994.1; -; mRNA.
DR AlphaFoldDB; Q68PH2; -.
DR SMR; Q68PH2; -.
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 2: Evidence at transcript level;
KW Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Secreted; Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL <1..1
FT /evidence="ECO:0000255"
FT CHAIN 2..66
FT /note="Neurotoxin Cex3"
FT /id="PRO_0000254066"
FT PROPEP 67..69
FT /id="PRO_0000254067"
FT DOMAIN 2..67
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 66
FT /note="Cysteine amide"
FT /evidence="ECO:0000255"
FT DISULFID 13..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 17..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 26..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 30..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT NON_TER 1
SQ SEQUENCE 69 AA; 7745 MW; 0233380932AD3236 CRC64;
AKDGYLVNKS TGCKYECFWL GKNEFCDKEC KAKNQGGSYG YCYSFACWCE GLPESTSTYP
LPNKSCGRK