SCXND_MESEU
ID SCXND_MESEU Reviewed; 73 AA.
AC G4WFQ2;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Sodium channel neurotoxin MeuNaTxalpha-13 {ECO:0000303|PubMed:21969612};
DE Flags: Precursor; Fragment;
OS Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=34648 {ECO:0000312|EMBL:ADW41694.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=21969612; DOI=10.1074/mcp.m111.012054;
RA Zhu S., Peigneur S., Gao B., Lu X., Cao C., Tytgat J.;
RT "Evolutionary diversification of Mesobuthus alpha-scorpion toxins affecting
RT sodium channels.";
RL Mol. Cell. Proteomics 11:M111.012054-M111.012054(2012).
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:P86405}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21969612}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:21969612}.
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; HQ332129; ADW41694.1; -; Genomic_DNA.
DR AlphaFoldDB; G4WFQ2; -.
DR SMR; G4WFQ2; -.
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 2: Evidence at transcript level;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL <1..5
FT /evidence="ECO:0000305"
FT CHAIN 6..71
FT /note="Sodium channel neurotoxin MeuNaTxalpha-13"
FT /evidence="ECO:0000305|PubMed:21969612"
FT /id="PRO_0000447459"
FT PROPEP 72..73
FT /note="Removed by a carboxypeptidase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000447460"
FT DOMAIN 7..71
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 17..70
FT /evidence="ECO:0000250|UniProtKB:P86405"
FT DISULFID 21..43
FT /evidence="ECO:0000250|UniProtKB:P86405"
FT DISULFID 29..53
FT /evidence="ECO:0000250|UniProtKB:P86405"
FT DISULFID 33..55
FT /evidence="ECO:0000250|UniProtKB:P86405"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:ADW41694.1"
SQ SEQUENCE 73 AA; 8081 MW; CFDDF3BFB0CA4725 CRC64;
TGVESARDAY IAKPHNCVYE CFDAFSSYCN DLCTENGAKS GYCQIAGKYG NGCWCIELPD
NVPIRIPGKC HRR