SC15_MESMA
ID SC15_MESMA Reviewed; 85 AA.
AC Q9GNG8; Q1H5L1;
DT 19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Toxin BmKaTX15;
DE AltName: Full=Alpha-neurotoxin Tx15;
DE AltName: Full=BmKalphaTx15;
DE AltName: Full=KTc;
DE AltName: Full=Na+ channel toxin BmKT';
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 [MRNA].
RC TISSUE=Venom gland;
RX PubMed=10858508; DOI=10.1016/s0041-0101(00)00081-7;
RA Zhu S.-Y., Li W.-X., Zeng X.-C., Liu H., Jiang D.-H., Mao X.;
RT "Nine novel precursors of Buthus martensii scorpion alpha-toxin
RT homologues.";
RL Toxicon 38:1653-1661(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16150513; DOI=10.1016/j.peptides.2005.07.016;
RA Zeng X.C., Luo F., Li W.X.;
RT "Characterization of a novel cDNA encoding a short venom peptide derived
RT from venom gland of scorpion Buthus martensii Karsch: trans-splicing may
RT play an important role in the diversification of scorpion venom peptides.";
RL Peptides 27:675-681(2006).
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}.
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 (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Alpha subfamily. {ECO:0000305}.
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DR EMBL; AF163017; AAG39643.1; -; mRNA.
DR EMBL; AF163016; AAG39642.1; -; mRNA.
DR EMBL; AY786186; AAX11389.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9GNG8; -.
DR SMR; Q9GNG8; -.
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..19
FT /evidence="ECO:0000250"
FT CHAIN 20..85
FT /note="Toxin BmKaTX15"
FT /id="PRO_0000035250"
FT DOMAIN 21..83
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
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; 9398 MW; 3312B422EC1C57E1 CRC64;
MNYLVFFSLA LLVMTGVESV RDGYIADDKN CAYFCGRNAY CDDECKKNGA ESGYCQWAGV
YGNACWCYKL PDKVPIRVPG KCNGG
