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