SCX2A_ANDCR
ID SCX2A_ANDCR Reviewed; 85 AA.
AC D5HR51;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Alpha-toxin Ac2;
DE AltName: Full=Neurotoxin 2;
DE Flags: Precursor;
OS Androctonus crassicauda (Arabian fat-tailed scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX NCBI_TaxID=122909;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=20018978; DOI=10.1093/molbev/msp310;
RA Weinberger H., Moran Y., Gordon D., Turkov M., Kahn R., Gurevitz M.;
RT "Positions under positive selection--key for selectivity and potency of
RT scorpion alpha-toxins.";
RL Mol. Biol. Evol. 27:1025-1034(2010).
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|UniProtKB:P01484}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01484}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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}.
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 EMBL; GQ335451; ADE42760.1; -; Genomic_DNA.
DR AlphaFoldDB; D5HR51; -.
DR SMR; D5HR51; -.
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 3: Inferred from homology;
KW Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Secreted; Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:P01484"
FT CHAIN 20..83
FT /note="Alpha-toxin Ac2"
FT /id="PRO_5000585057"
FT DOMAIN 21..83
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 83
FT /note="Lysine amide"
FT /evidence="ECO:0000250|UniProtKB:P01480"
FT DISULFID 31..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 35..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 41..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 45..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 85 AA; 9545 MW; C0DEB5FE939EB0CE CRC64;
MNYLVMISLA LLFMTGVESI KDGYIVDDRN CTYFCGTKSY CNGECTKLKG ESGYCQWASP
YGNACYCYKL PDHVRTKGPG RCKGR