SCXN4_MESEU
ID SCXN4_MESEU Reviewed; 86 AA.
AC P86404; E4VP51;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 2.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Sodium channel neurotoxin MeuNaTxalpha-4 {ECO:0000303|Ref.2};
DE Flags: Precursor;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 20-25,
RP FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and 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).
RN [2]
RP PROTEIN SEQUENCE OF 20-85, FUNCTION, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RA Zhu S.Y., Gao B.;
RT "Characterization of a sodium channel toxin from the scorpion Mesobuthus
RT eupeus venom.";
RL Submitted (NOV-2009) to UniProtKB.
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. This toxin inhibits
CC inactivation of drosophila DmNav1 (EC(50)=130 nM) (PubMed:21969612,
CC Ref.2). {ECO:0000269|PubMed:21969612, ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.2}.
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 -!- MASS SPECTROMETRY: Mass=7193; Method=MALDI;
CC Evidence={ECO:0000269|Ref.2};
CC -!- MASS SPECTROMETRY: Mass=7199.55; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21969612};
CC -!- MISCELLANEOUS: Shows no effect on Nav1.2/SCN2A, Nav1.3/SCN3A,
CC Nav1.4/SCN4A, Nav1.5/SCN5A, Nav1.6/SCN8A, Nav1.7/SCN9A and
CC Nav1.8/SCN10A (PubMed:21969612). {ECO:0000269|PubMed:21969612}.
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Alpha subfamily. {ECO:0000255}.
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DR EMBL; EF445093; ABR21068.1; -; mRNA.
DR AlphaFoldDB; P86404; -.
DR BMRB; P86404; -.
DR SMR; P86404; -.
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 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:21969612, ECO:0000269|Ref.2"
FT CHAIN 20..85
FT /note="Sodium channel neurotoxin MeuNaTxalpha-4"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000401121"
FT PROPEP 86
FT /note="Removed by a carboxypeptidase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000447443"
FT DOMAIN 21..85
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 31..84
FT /evidence="ECO:0000250|UniProtKB:P86405"
FT DISULFID 35..57
FT /evidence="ECO:0000250|UniProtKB:P86405"
FT DISULFID 43..67
FT /evidence="ECO:0000250|UniProtKB:P86405"
FT DISULFID 47..69
FT /evidence="ECO:0000250|UniProtKB:P86405"
FT CONFLICT 62
FT /note="T -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="V -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 86 AA; 9442 MW; B67D44396A8AE0CD CRC64;
MNYLILISFA LLVITGVESA RDAYIAKPHN CVYECFDAFS SYCNGVCTKN GAKSGYCQIL
GTYGNGCWCI VLPDNVPIRI PGKCHR
