ID   SCXV_CENSC              Reviewed;          63 AA.
AC   P46066;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Alpha-toxin CsE5;
DE   AltName: Full=B140-1;
DE   AltName: Full=CsE-V {ECO:0000303|PubMed:7739052};
DE            Short=CsEV;
DE   AltName: Full=Neurotoxin V;
OS   Centruroides sculpturatus (Arizona bark scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=218467;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=1926166; DOI=10.1016/0041-0101(91)90057-x;
RA   David R.M., Krishna N.R., Watt D.D.;
RT   "Characterization of cationic binding sites of neurotoxins from venom of
RT   the scorpion (Centruroides sculpturatus Ewing) using lanthanides as binding
RT   probes.";
RL   Toxicon 29:645-662(1991).
RN   [2]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=7739052; DOI=10.1016/s0022-2836(95)80062-x;
RA   Jablonsky M.J., Watt D.D., Krishna N.R.;
RT   "Solution structure of an Old World-like neurotoxin from the venom of the
RT   New World scorpion Centruroides sculpturatus Ewing.";
RL   J. Mol. Biol. 248:449-458(1995).
CC   -!- FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium
CC       channels (Nav) and inhibit the inactivation of the activated channels,
CC       thereby blocking neuronal transmission.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1926166}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:1926166}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000269|PubMed:7739052}.
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   PDB; 1NRA; NMR; -; A=1-63.
DR   PDB; 1NRB; NMR; -; A=1-63.
DR   PDBsum; 1NRA; -.
DR   PDBsum; 1NRB; -.
DR   AlphaFoldDB; P46066; -.
DR   BMRB; P46066; -.
DR   SMR; P46066; -.
DR   EvolutionaryTrace; P46066; -.
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   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..63
FT                   /note="Alpha-toxin CsE5"
FT                   /evidence="ECO:0000269|PubMed:1926166"
FT                   /id="PRO_0000066775"
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                   ECO:0000269|PubMed:7739052, ECO:0000312|PDB:1NRA,
FT                   ECO:0000312|PDB:1NRB"
FT   DISULFID        16..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:7739052, ECO:0000312|PDB:1NRA,
FT                   ECO:0000312|PDB:1NRB"
FT   DISULFID        22..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:7739052, ECO:0000312|PDB:1NRA,
FT                   ECO:0000312|PDB:1NRB"
FT   DISULFID        26..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT                   ECO:0000269|PubMed:7739052, ECO:0000312|PDB:1NRA,
FT                   ECO:0000312|PDB:1NRB"
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:1NRA"
FT   STRAND          17..19
FT                   /evidence="ECO:0007829|PDB:1NRA"
FT   HELIX           20..28
FT                   /evidence="ECO:0007829|PDB:1NRA"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:1NRA"
FT   TURN            38..41
FT                   /evidence="ECO:0007829|PDB:1NRA"
FT   STRAND          42..48
FT                   /evidence="ECO:0007829|PDB:1NRA"
SQ   SEQUENCE   63 AA;  7076 MW;  8BFEB36915AD8467 CRC64;
     KKDGYPVDSG NCKYECLKDD YCNDLCLERK ADKGYCYWGK VSCYCYGLPD NSPTKTSGKC
     NPA