ID   SCX8_CENEL              Reviewed;          64 AA.
AC   P0CH40;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Beta-toxin CeII8;
OS   Centruroides elegans (Bark scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=217897;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, TOXIN TARGET, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=20600228; DOI=10.1016/j.toxicon.2010.06.008;
RA   Vandendriessche T., Olamendi-Portugal T., Zamudio F.Z., Possani L.D.,
RA   Tytgat J.;
RT   "Isolation and characterization of two novel scorpion toxins: The alpha-
RT   toxin-like CeII8, specific for Na(v)1.7 channels and the classical anti-
RT   mammalian CeII9, specific for Na(v)1.4 channels.";
RL   Toxicon 56:613-623(2010).
CC   -!- FUNCTION: Beta toxins bind at site-4 of sodium channels and shift the
CC       voltage of activation toward more negative potentials thereby affecting
CC       sodium channel activation and promoting spontaneous and repetitive
CC       firing. Has a selective effect toward Nav1.7/SCN9A which plays a role
CC       in pain mechanisms, and especially in the development of inflammatory
CC       pain. Shows no lethality toward mice. {ECO:0000269|PubMed:20600228}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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   -!- MASS SPECTROMETRY: Mass=7450.0; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:20600228};
CC   -!- MISCELLANEOUS: The protein sequence seems to be related to the alpha-
CC       toxins, however experimental data show that it has a clear beta-toxin
CC       activity. {ECO:0000305|PubMed:20600228}.
CC   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Alpha subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0CH40; -.
DR   SMR; P0CH40; -.
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   CDD; cd00107; Knot1; 1.
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..64
FT                   /note="Beta-toxin CeII8"
FT                   /id="PRO_0000398149"
FT   DOMAIN          2..61
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        12..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        16..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        22..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        26..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   64 AA;  7459 MW;  A10BAB2727124CEB CRC64;
     KKDGYPVNME ECRYNCWKNA YCDKLCKEKK GQSGYCYGWN LSCWCIGLPD NTNTKMNPFC
     QTAD