SCXM1_MESMA
ID SCXM1_MESMA Reviewed; 86 AA.
AC A0F0C2; Q95P87;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Mesotoxin-1;
DE Flags: Precursor;
OS Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=34649;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MESOTOXIN-2 ASP-74, VARIANT
RP MESOTOXIN-3 ALA-77, AND 3D-STRUCTURE MODELING.
RX PubMed=17054952; DOI=10.1016/j.febslet.2006.09.071;
RA Zhu S., Gao B.;
RT "Molecular characterization of a possible progenitor sodium channel toxin
RT from the Old World scorpion Mesobuthus martensii.";
RL FEBS Lett. 580:5979-5987(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 41-86.
RC TISSUE=Venom gland;
RA Zhu S., Li W.;
RT "cDNA encoding a toxin-like peptide from BmK.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to sodium channels (Nav) and affects the channel
CC activation process. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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 (3 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR EMBL; DQ872676; ABJ09780.1; -; Genomic_DNA.
DR EMBL; AF159977; AAK61824.1; -; mRNA.
DR AlphaFoldDB; A0F0C2; -.
DR SMR; A0F0C2; -.
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; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51863; LCN_CSAB; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..86
FT /note="Mesotoxin-1"
FT /id="PRO_0000425735"
FT DOMAIN 24..86
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 37..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 47..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 51..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT VARIANT 74
FT /note="N -> D (in mesotoxin-2)"
FT /evidence="ECO:0000269|PubMed:17054952"
FT VARIANT 77
FT /note="T -> A (in mesotoxin-3)"
FT /evidence="ECO:0000269|PubMed:17054952"
SQ SEQUENCE 86 AA; 9959 MW; 5A4A568D0F361D8F CRC64;
MKILTVFMIF IANFLNMMQV FSVKDRFLII NGSYELCVYA ENLGEDCENL CKQQKATDGF
CRQPHCFCTD MPDNYATRPD TVDPIM