SCX1_ANDAU
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 03-AUG-2022, entry version 108.
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; -; 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; 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
