SCX2_CENLI
ID SCX2_CENLI Reviewed; 66 AA.
AC P59898;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Beta-toxin Cll2 {ECO:0000305};
DE Short=Cll 2 {ECO:0000303|PubMed:8653586};
DE Short=Cll2 {ECO:0000303|PubMed:22200496};
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, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8653586; DOI=10.1016/0305-0491(95)02031-4;
RA Dehesa-Davila M., Ramirez A.N., Zamudio F.Z., Gurrola-Briones G.,
RA Lievano A., Darszon A., Possani L.D.;
RT "Structural and functional comparison of toxins from the venom of the
RT scorpions Centruroides infamatus infamatus, Centruroides limpidus limpidus
RT and Centruroides noxius.";
RL Comp. Biochem. Physiol. 113B:331-339(1996).
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),
CC reduces peak current (observed on Nav1.6/SCN8A (IC(50)=172 nM),
CC Nav1.1/SCN1A, Nav1.4/SCN4A (weak) and Nav1.5/SCN5A (weak)), shifts the
CC voltage of activation toward more negative potentials (observed on
CC Nav1.6 and Nav1.2 (weak)), and induces resurgent currents at negative
CC voltages following brief and strong depolarizations (observed on
CC Nav1.6, Nav1.1 (weak), Nav1.2 (weak), and Nav1.4 (weak))
CC (PubMed:22200496). {ECO:0000269|PubMed:22200496,
CC ECO:0000269|PubMed:8653586}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8653586}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:8653586}.
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 of Nav1.2,
CC Nav1.3 and Nav1.7 (at 460 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 AlphaFoldDB; P59898; -.
DR SMR; P59898; -.
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="Beta-toxin Cll2"
FT /evidence="ECO:0000269|PubMed:8653586"
FT /id="PRO_0000066763"
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:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 16..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 25..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 29..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 66 AA; 7584 MW; DF159C4C7175B0C2 CRC64;
KEGYLVNHST GCKYECFKLG DNDYCLRECK QQYGKGAGGY CYAFGCWCNH LYEQAVVWPL
PKKTCN
