SCAA_MESMA
ID SCAA_MESMA Reviewed; 85 AA.
AC Q95P69;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Toxin BmKT;
DE Short=BmK T;
DE AltName: Full=Antitumor-analgesic peptide;
DE Short=AGAP;
DE Short=AGSP;
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], AND FUNCTION.
RC TISSUE=Venom gland;
RX PubMed=10728828; DOI=10.1016/s0041-0101(99)00192-0;
RA Zeng X.-C., Li W.-X., Zhu S.-Y., Peng F., Jiang D.-H., Yang F.-H.,
RA Wu K.-L.;
RT "Cloning and characterization of the cDNA sequences of two venom peptides
RT from Chinese scorpion Buthus martensii Karsch (BmK).";
RL Toxicon 38:893-899(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12597884; DOI=10.1016/s1046-5928(02)00609-5;
RA Liu Y.-F., Ma R.-L., Wang S.-L., Duan Z.-Y., Zhang J.-H., Wu L.-J.,
RA Wu C.-F.;
RT "Expression of an antitumor-analgesic peptide from the venom of Chinese
RT scorpion Buthus martensii karsch in Escherichia coli.";
RL Protein Expr. Purif. 27:253-258(2003).
CC -!- FUNCTION: Binds to sodium channels (Nav) and inhibits the inactivation
CC of the activated channels, thereby blocking neuronal transmission (By
CC similarity). Tested on mice, has antitumor effect and strong inhibitory
CC effect on pain. {ECO:0000250, ECO:0000269|PubMed:10728828}.
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; AF370023; AAK53809.1; -; mRNA.
DR EMBL; AF464898; AAP34332.1; -; mRNA.
DR AlphaFoldDB; Q95P69; -.
DR SMR; Q95P69; -.
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 BmKT"
FT /id="PRO_0000035259"
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; 9412 MW; 2FFC463E02EE57E1 CRC64;
MNYLVFFSLA LLLMTGVESV RDGYIADDKN CAYFCGRNAY CDDECKKNGA ESGYCQWAGV
YGNACWCYKL PDKVPIRVPG KCNGG
