SNA64_LYCMC
ID SNA64_LYCMC Reviewed; 87 AA.
AC P0CI58;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Neurotoxin LmNaTx64.1 {ECO:0000303|PubMed:20663230};
DE Flags: Precursor;
OS Lychas mucronatus (Chinese swimming scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Lychas.
OX NCBI_TaxID=172552;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Yunnan; TISSUE=Venom gland;
RX PubMed=20663230; DOI=10.1186/1471-2164-11-452;
RA Zhao R., Ma Y., He Y., Di Z., Wu Y.-L., Cao Z.-J., Li W.-X.;
RT "Comparative venom gland transcriptome analysis of the scorpion Lychas
RT mucronatus reveals intraspecific toxic gene diversity and new venomous
RT components.";
RL BMC Genomics 11:452-452(2010).
CC -!- FUNCTION: Binds voltage-independently at site-4 of sodium channels
CC (Nav) and shift the voltage of activation toward more negative
CC potentials thereby affecting sodium channel activation and promoting
CC spontaneous and repetitive firing. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20663230}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:20663230}.
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. Beta subfamily. {ECO:0000305}.
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DR EMBL; GT028975; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0CI58; -.
DR SMR; P0CI58; -.
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..18
FT /evidence="ECO:0000255"
FT PEPTIDE 19..84
FT /note="Neurotoxin LmNaTx64.1"
FT /evidence="ECO:0000305|PubMed:20663230"
FT /id="PRO_0000403818"
FT DOMAIN 19..85
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 84
FT /note="Cysteine amide"
FT /evidence="ECO:0000250|UniProtKB:P15226"
FT DISULFID 33..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 37..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 44..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 48..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 87 AA; 10167 MW; 676EF1ADE1F8052D CRC64;
MKILFLIILT AFFIGVHCKH GYPIIRAGRD KGCKVSCVIN NQYCDTECKQ LKGRRGYCYF
WRLACFCEYL PDYVPTWSRA TNKCKAK
