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SCX9_CENSU
ID   SCX9_CENSU              Reviewed;          82 AA.
AC   F1CGT6;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Beta-neurotoxin Css9 {ECO:0000305};
DE   AltName: Full=Beta-neurotoxin CssIX {ECO:0000303|PubMed:21329715};
DE            Short=Css IX {ECO:0000305};
DE   Flags: Precursor;
OS   Centruroides suffusus (Durango bark scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=6880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-49; 52-56 AND 59-75,
RP   MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TOXIC DOSE.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=21329715; DOI=10.1016/j.toxicon.2011.02.006;
RA   Espino-Solis G.P., Estrada G., Olamendi-Portugal T., Villegas E.,
RA   Zamudio F., Cestele S., Possani L.D., Corzo G.;
RT   "Isolation and molecular cloning of beta-neurotoxins from the venom of the
RT   scorpion Centruroides suffusus suffusus.";
RL   Toxicon 57:739-746(2011).
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. This toxin compete with high
CC       affinity with 125I-Css4 bound on rat brain synaptosome and may bind
CC       with high affinity to Nav1.1/SCN1A, Nav1.2/SCN2A and Nav1.6/SCN8A.
CC       {ECO:0000269|PubMed:21329715}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21329715}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:21329715}.
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=7524.9; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:21329715};
CC   -!- TOXIC DOSE: LD(100) is 4 ug/kg by intracranial injection into mice.
CC       {ECO:0000269|PubMed:21329715}.
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; HQ262494; ADY17426.1; -; mRNA.
DR   AlphaFoldDB; F1CGT6; -.
DR   SMR; F1CGT6; -.
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; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:21329715"
FT   CHAIN           18..82
FT                   /note="Beta-neurotoxin Css9"
FT                   /evidence="ECO:0000305|PubMed:21329715"
FT                   /id="PRO_5003266311"
FT   DOMAIN          18..81
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        28..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        32..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        39..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        43..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   82 AA;  9388 MW;  12C1A2D1BB8AE188 CRC64;
     MKLLMLIVAL MIIGVQSKDG YPMDHKGCKI SCVINNKYCE TECVTVLKGK KGYCYFWKLA
     CYCEGLPNWA KVWDRATNKC RA
 
 
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