ID   SCX1_ANDAU              Reviewed;          83 AA.
AC   P01479;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 3.
DT   22-FEB-2023, entry version 110.
DE   RecName: Full=Neurotoxin-1'';
DE   AltName: Full=AaH I'';
DE            Short=AaHI'';
DE   AltName: Full=Neurotoxin I'';
DE   Contains:
DE     RecName: Full=Neurotoxin-1/1';
DE     AltName: Full=AaH I/AaH I' {ECO:0000303|PubMed:2808423};
DE              Short=AaHI/AaHI';
DE     AltName: Full=Neurotoxin I/I';
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] (AAH I AND AAH I').
RC   STRAIN=Hector;
RX   PubMed=2808423; DOI=10.1016/s0021-9258(19)47295-5;
RA   Bougis P.E., Rochat H., Smith L.A.;
RT   "Precursors of Androctonus australis scorpion neurotoxins. Structures of
RT   precursors, processing outcomes, and expression of a functional recombinant
RT   toxin II.";
RL   J. Biol. Chem. 264:19259-19265(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (AAH I').
RC   STRAIN=Hector;
RX   PubMed=7756304; DOI=10.1021/bi00020a018;
RA   Delabre M.-L., Pasero P., Marilley M., Bougis P.E.;
RT   "Promoter structure and intron-exon organization of a scorpion alpha-toxin
RT   gene.";
RL   Biochemistry 34:6729-6736(1995).
RN   [3]
RP   PROTEIN SEQUENCE OF 20-82 (AAH I).
RC   STRAIN=Hector; TISSUE=Venom;
RX   PubMed=5500394; DOI=10.1111/j.1432-1033.1970.tb01162.x;
RA   Rochat H., Rochat C., Miranda F., Lissitzky S., Edman P.;
RT   "The amino acid sequence of neurotoxin I of Androctonus australis hector.";
RL   Eur. J. Biochem. 17:262-266(1970).
RN   [4]
RP   PROTEIN SEQUENCE OF 20-83 (AAH I'').
RC   STRAIN=Hector; TISSUE=Venom;
RX   PubMed=6523502; DOI=10.1016/0041-0101(84)90153-3;
RA   Martin M.-F., Rochat H.;
RT   "Purification and amino acid sequence of toxin I' from the venom of the
RT   North African scorpion Androctonus australis hector.";
RL   Toxicon 22:695-703(1984).
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. Is active against mammals and
CC       binds with high affinity rat brain synaptosomes.
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; M27701; AAA29946.1; -; mRNA.
DR   EMBL; M27702; AAA29947.1; -; mRNA.
DR   EMBL; X76135; CAA53740.1; -; Genomic_DNA.
DR   PIR; A34444; NTSRIA.
DR   PIR; B34444; NTSRI2.
DR   AlphaFoldDB; P01479; -.
DR   SMR; P01479; -.
DR   ABCD; P01479; 2 sequenced antibodies.
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; Knottin, scorpion toxin-like; 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; Scorpion toxin-like; 1.
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:5500394,
FT                   ECO:0000269|PubMed:6523502"
FT   CHAIN           20..83
FT                   /note="Neurotoxin-1"""
FT                   /id="PRO_0000035217"
FT   CHAIN           20..82
FT                   /note="Neurotoxin-1/1'"
FT                   /id="PRO_0000035218"
FT   PROPEP          83
FT                   /note="Removed by a carboxypeptidase (in neurotoxin-1/1')"
FT                   /id="PRO_0000035219"
FT   DOMAIN          21..82
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        31..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        35..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        39..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        43..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   VARIANT         36
FT                   /note="V -> I (in neurotoxin-1')"
SQ   SEQUENCE   83 AA;  9061 MW;  7B6F72F3CB98D1C6 CRC64;
     MNYLVMISLA LLLMIGVESK RDGYIVYPNN CVYHCVPPCD GLCKKNGGSS GSCSFLVPSG
     LACWCKDLPD NVPIKDTSRK CTR
//