ID   SCX6_ANDAU              Reviewed;          66 AA.
AC   P56743;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Toxin Aah6;
DE   AltName: Full=AaH VI;
DE            Short=AaHVI;
DE   AltName: Full=Neurotoxin 6;
DE   AltName: Full=Neurotoxin VI;
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   PROTEIN SEQUENCE, TOXIC DOSE, GLYCOSYLATION AT ASN-9, AND STRUCTURE OF
RP   CARBOHYDRATE.
RC   STRAIN=Hector; TISSUE=Venom;
RX   PubMed=9989600; DOI=10.1016/s0014-5793(98)01710-4;
RA   Hassani O., Loew D., van Dorsselaer A., Papandreou M.J., Sorokine O.,
RA   Rochat H., Sampieri F., Mansuelle P.;
RT   "Aah VI, a novel, N-glycosylated anti-insect toxin from Androctonus
RT   australis hector scorpion venom: isolation, characterisation, and glycan
RT   structure determination.";
RL   FEBS Lett. 443:175-180(1999).
CC   -!- FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium
CC       channels 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 is active only on insects
CC       (By similarity). This toxin has very low anti-insect activity.
CC       {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   -!- PTM: N-glycans are core-fucosylated, heterogeneous and short which
CC       could be the result of extensive trimming.
CC   -!- TOXIC DOSE: LD(50) is 8.5 ug/g in Blattella germanica.
CC       {ECO:0000269|PubMed:9989600}.
CC   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P56743; -.
DR   SMR; P56743; -.
DR   GlyConnect; 434; 9 N-Linked glycans (1 site).
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   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; Glycoprotein; Secreted; Toxin.
FT   CHAIN           1..66
FT                   /note="Toxin Aah6"
FT                   /id="PRO_0000066724"
FT   DOMAIN          2..65
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   CARBOHYD        9
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:9989600"
FT                   /id="CAR_000157"
FT   DISULFID        13..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        17..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        26..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        30..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   66 AA;  7348 MW;  1A2F86D8CB3AA1F1 CRC64;
     GRDGYVVKNG TNCKYSCEIG SEYEYCGPLC KRKNAKTGYC YAFACWCIDV PDDVKLYGDD
     GTYCSS