ID   SCX5_CENSC              Reviewed;          59 AA.
AC   P58779;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Alpha-like toxin CsEv5;
DE            Short=CsE v5;
DE            Short=CsE-v5;
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.
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, FUNCTION, AND DISULFIDE BONDS.
RX   PubMed=11444973; DOI=10.1021/bi010223h;
RA   Jablonsky M.J., Jackson P.L., Krishna N.R.;
RT   "Solution structure of an insect-specific neurotoxin from the New World
RT   scorpion Centruroides sculpturatus Ewing.";
RL   Biochemistry 40:8273-8282(2001).
RN   [3]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=11133274; DOI=10.1006/jmre.2000.2220;
RA   Xu Y., Jablonsky M.J., Jackson P.L., Braun W., Krishna N.R.;
RT   "Automatic assignment of NOESY cross peaks and determination of the protein
RT   structure of a new world scorpion neurotoxin using NOAH/DIAMOD.";
RL   J. Magn. Reson. 148:35-46(2001).
CC   -!- FUNCTION: Binds voltage-independently sodium channels (Nav) and
CC       inhibits the inactivation of the activated channels, thereby blocking
CC       neuronal transmission. Is highly toxic to insects and barely toxic to
CC       mammals. As it does not compete with the classical alpha-toxin AaH2,
CC       this toxin is considered as an alpha-like toxin.
CC       {ECO:0000269|PubMed:11444973}.
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   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. {ECO:0000305}.
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DR   PDB; 1I6F; NMR; -; A=1-59.
DR   PDB; 1I6G; NMR; -; A=1-59.
DR   PDB; 1NH5; NMR; -; A=1-59.
DR   PDBsum; 1I6F; -.
DR   PDBsum; 1I6G; -.
DR   PDBsum; 1NH5; -.
DR   AlphaFoldDB; P58779; -.
DR   BMRB; P58779; -.
DR   SMR; P58779; -.
DR   EvolutionaryTrace; P58779; -.
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..59
FT                   /note="Alpha-like toxin CsEv5"
FT                   /id="PRO_0000066774"
FT   DOMAIN          1..59
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        11..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        15..35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        21..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        25..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:1I6F"
FT   STRAND          7..11
FT                   /evidence="ECO:0007829|PDB:1NH5"
FT   HELIX           18..27
FT                   /evidence="ECO:0007829|PDB:1I6F"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:1I6F"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:1I6F"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:1I6F"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:1NH5"
SQ   SEQUENCE   59 AA;  6305 MW;  D6BFB7253C94A593 CRC64;
     KDGYPVDSKG CKLSCVANNY CDNQCKMKKA SGGHCYAMSC YCEGLPENAK VSDSATNIC