ID   CEII9_CENEL             Reviewed;          67 AA.
AC   P0CH41;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Beta-mammal toxin CeII9 {ECO:0000303|PubMed:20600228};
DE   AltName: Full=Cell9 {ECO:0000305};
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, 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).
RN   [2]
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 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. This toxin is active against mammals and lethal to mice.
CC       Selectively modulates Nav1.4/SCN4A, a sodium channel present in both
CC       denervated and innervated skeletal muscle.
CC       {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=7590.0; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:20600228};
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; P0CH41; -.
DR   SMR; P0CH41; -.
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..67
FT                   /note="Beta-mammal toxin CeII9"
FT                   /id="PRO_0000398150"
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   67 AA;  7599 MW;  F70F0559679397D4 CRC64;
     KEGYLVNHST GCKYECFKLG DNDYCLRECR QGYGKGAGGY CYAFGCWCTH LYEQAVVWPL
     PKKTCNA