SCXB_ANDAU
ID SCXB_ANDAU Reviewed; 83 AA.
AC Q9BLM3;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Toxin AahP985;
DE AltName: Full=Neurotoxin pcD-985;
DE Flags: Precursor;
OS Androctonus australis (Sahara scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX NCBI_TaxID=6858;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hector;
RX PubMed=11311249; DOI=10.1016/s0014-5793(01)02336-5;
RA Ceard B., Martin-Eauclaire M.-F., Bougis P.E.;
RT "Evidence for a position-specific deletion as an evolutionary link between
RT long- and short-chain scorpion toxins.";
RL FEBS Lett. 494:246-248(2001).
CC -!- FUNCTION: Binds voltage-independently at site-3 of sodium channels
CC (Nav) and inhibits the inactivation of the activated channels, thereby
CC 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 EMBL; AJ308441; CAC37322.1; -; mRNA.
DR AlphaFoldDB; Q9BLM3; -.
DR SMR; Q9BLM3; -.
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 2: Evidence at transcript level;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..83
FT /note="Toxin AahP985"
FT /id="PRO_0000035226"
FT DOMAIN 20..82
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 30..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 34..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 40..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 44..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 83 AA; 9083 MW; 4C6EB7BE25413FBF CRC64;
MNYLVMISLA LLIAGVDSAR DAYIAKNDNC VYECFQDSYC NDLCTKNGAK SGTCDWIGTY
GDACLCYALP DNVPIKLSGE CHR