ID   SCX2_ANDAM              Reviewed;          86 AA.
AC   Q86SE0;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Toxin Aam2;
DE   AltName: Full=AamH2;
DE   AltName: Full=Alpha-neurotoxin 2;
DE   Flags: Precursor;
OS   Androctonus amoreuxi (African fattail scorpion) (Scorpio amoreuxi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX   NCBI_TaxID=112024;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AMIDATION AT ASN-84, AND PROTEIN SEQUENCE OF
RP   21-84.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=12972326; DOI=10.1016/s0167-0115(03)00146-0;
RA   Chen T., Folan R., Kwok H., O'Kane E.J., Bjourson A.J., Shaw C.;
RT   "Isolation of scorpion (Androctonus amoreuxi) putative alpha neurotoxins
RT   and parallel cloning of their respective cDNAs from a single sample of
RT   venom.";
RL   Regul. Pept. 115:115-121(2003).
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   EMBL; AJ536596; CAD60540.1; -; mRNA.
DR   AlphaFoldDB; Q86SE0; -.
DR   SMR; Q86SE0; -.
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   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:12972326"
FT   CHAIN           21..84
FT                   /note="Toxin Aam2"
FT                   /id="PRO_0000035215"
FT   DOMAIN          22..84
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         84
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000305|PubMed:12972326"
FT   DISULFID        32..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        36..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        42..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        46..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   86 AA;  9283 MW;  40FBE2D61C8A62A8 CRC64;
     MNYLITISLA LLLMTGVASG VRDGYIADAG NCGYTCVAND YCNTECTKNG AESGYCQWFG
     RYGNACWCIK LPDKVPIKVP GKCNGR