SCX1_CENLI
ID SCX1_CENLI Reviewed; 66 AA.
AC P45667;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Toxin Cll1 {ECO:0000305};
DE AltName: Full=Cll toxin 1 {ECO:0000303|PubMed:7727365};
DE AltName: Full=Crustacean toxin 1 {ECO:0000303|PubMed:7727365};
OS Centruroides limpidus (Mexican scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX NCBI_TaxID=6876;
RN [1]
RP PROTEIN SEQUENCE, DISULFIDE BONDS, STRUCTURE BY NMR, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom;
RX PubMed=7727365; DOI=10.1021/bi00203a010;
RA Lebreton F., Delepierre M., Ramirez A.N., Balderas C., Possani L.D.;
RT "Primary and NMR three-dimensional structure determination of a novel
RT crustacean toxin from the venom of the scorpion Centruroides limpidus
RT limpidus Karsch.";
RL Biochemistry 33:11135-11149(1994).
RN [2]
RP FUNCTION, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom;
RX PubMed=22200496; DOI=10.1016/j.toxicon.2011.12.003;
RA Schiavon E., Pedraza-Escalona M., Gurrola G.B., Olamendi-Portugal T.,
RA Corzo G., Wanke E., Possani L.D.;
RT "Negative-shift activation, current reduction and resurgent currents
RT induced by beta-toxins from Centruroides scorpions in sodium channels.";
RL Toxicon 59:283-293(2012).
RN [3]
RP NEUTRALIZATION BY ANTIBODY.
RX PubMed=30634620; DOI=10.3390/toxins11010032;
RA Riano-Umbarila L., Gomez-Ramirez I.V., Ledezma-Candanoza L.M.,
RA Olamendi-Portugal T., Rodriguez-Rodriguez E.R., Fernandez-Taboada G.,
RA Possani L.D., Becerril B.;
RT "Generation of a broadly cross-neutralizing antibody fragment against
RT several mexican scorpion venoms.";
RL Toxins 11:0-0(2019).
CC -!- FUNCTION: Beta toxin that binds site-4 of sodium channels (Nav) and
CC reduces peak current (observed on Nav1.1/SCN1A, Nav1.2/SCN2A,
CC Nav1.3/SCN3A, Nav1.4/SCN5A, Nav1.5/SCN4A, and Nav1.6/SCN8A (IC(50)=44.9
CC nM)), shifts the voltage of activation toward more negative potentials
CC (observed on Nav1.6, Nav1.1 (weak), Nav1.2 (weak), and Nav1.7 (weak)),
CC and induces resurgent currents at negative voltages following brief and
CC strong depolarizations (observed on Nav1.6, Nav1.1 (weak), Nav1.2
CC (weak), and Nav1.4 (weak)) (PubMed:22200496). This toxin is only active
CC on crustaceans (PubMed:7727365). {ECO:0000269|PubMed:22200496,
CC ECO:0000269|PubMed:7727365}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7727365}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:7727365}.
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 -!- MISCELLANEOUS: Does not show inhibition of peak current on Nav1.7/SCN9A
CC (at 560 nM). {ECO:0000269|PubMed:22200496}.
CC -!- MISCELLANEOUS: Is neutralized by the single-chain antibody fragment
CC 10FG2. {ECO:0000269|PubMed:30634620}.
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; A55869; A55869.
DR AlphaFoldDB; P45667; -.
DR SMR; P45667; -.
DR TCDB; 8.B.1.2.1; the long (4c-c) scorpion toxin (l-st) superfamily.
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 Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..66
FT /note="Toxin Cll1"
FT /evidence="ECO:0000269|PubMed:7727365"
FT /id="PRO_0000066765"
FT DOMAIN 1..66
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 12..65
FT /evidence="ECO:0000269|PubMed:7727365"
FT DISULFID 16..41
FT /evidence="ECO:0000269|PubMed:7727365"
FT DISULFID 25..46
FT /evidence="ECO:0000269|PubMed:7727365"
FT DISULFID 29..48
FT /evidence="ECO:0000269|PubMed:7727365"
SQ SEQUENCE 66 AA; 7338 MW; A478E63796F54DAA CRC64;
KEGYLVNKST GCKYGCFWLG KNENCDKECK AKNQGGSYGY CYSFACWCEG LPESTPTYPL
PNKSCS
