SCX_ANDMA
ID SCX_ANDMA Reviewed; 16 AA.
AC P0C911;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 23-FEB-2022, entry version 20.
DE RecName: Full=Alpha-toxin;
DE Flags: Fragment;
OS Androctonus mauritanicus mauritanicus (Scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX NCBI_TaxID=6860;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=18243273; DOI=10.1016/j.toxicon.2007.12.012;
RA Oukkache N., Rosso J.-P., Alami M., Ghalim N., Saile R., Hassar M.,
RA Bougis P.E., Martin-Eauclaire M.-F.;
RT "New analysis of the toxic compounds from the Androctonus mauretanicus
RT mauretanicus scorpion venom.";
RL Toxicon 51:835-852(2008).
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. {ECO:0000250}.
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. Alpha subfamily. {ECO:0000305}.
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Ion channel impairing toxin; Neurotoxin;
KW Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..>16
FT /note="Alpha-toxin"
FT /id="PRO_0000368019"
FT NON_TER 16
SQ SEQUENCE 16 AA; 1816 MW; F2AFA421F02B58CA CRC64;
GRDGYIAQPE NXVYXX