SCXA_MESMA
ID SCXA_MESMA Reviewed; 84 AA.
AC O61705;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Neurotoxin BmK-M10;
DE AltName: Full=Alpha-neurotoxin TX9;
DE AltName: Full=BmK AngM1 {ECO:0000303|PubMed:15200476};
DE AltName: Full=BmK-X;
DE Short=BmKX;
DE AltName: Full=BmK10;
DE AltName: Full=BmKalphaTx9;
DE AltName: Full=Bmk M10;
DE Short=BmkM10;
DE AltName: Full=Neurotoxin M10;
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].
RC TISSUE=Venom gland;
RA Xiong Y.-M., Ling M.-H., Wang D.-C., Chi C.-W.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 20-83, FUNCTION, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RX PubMed=15200476; DOI=10.1111/j.1399-3011.2004.00164.x;
RA Cao Z.Y., Mi Z.M., Cheng G.F., Shen W.Q., Xiao X., Liu X.M., Liang X.T.,
RA Yu D.Q.;
RT "Purification and characterization of a new peptide with analgesic effect
RT from the scorpion Buthus martensi Karch.";
RL J. Pept. Res. 64:33-41(2004).
CC -!- FUNCTION: Binds to voltage-dependent sodium channels (Nav) and voltage-
CC dependent delayed rectifier potassium channels and inhibits the
CC inactivation of the activated channels, thereby blocking neuronal
CC transmission. Administration to mice at a dosage of 0.8 mg/kg produces
CC an analgesic effect. {ECO:0000269|PubMed:15200476}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15200476}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:15200476}.
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=7040.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15200476};
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; AF062563; AAC16697.1; -; Genomic_DNA.
DR EMBL; AF164203; AAK06898.1; -; mRNA.
DR PDB; 2KBK; NMR; -; A=20-83.
DR PDBsum; 2KBK; -.
DR AlphaFoldDB; O61705; -.
DR SMR; O61705; -.
DR PRIDE; O61705; -.
DR EvolutionaryTrace; O61705; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0019870; F:potassium channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR GO; GO:0044489; P:negative regulation of voltage-gated sodium channel activity in another organism; IDA:UniProtKB.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:15200476"
FT CHAIN 20..83
FT /note="Neurotoxin BmK-M10"
FT /evidence="ECO:0000269|PubMed:15200476"
FT /id="PRO_0000035240"
FT PROPEP 84
FT /note="Removed by a carboxypeptidase"
FT /id="PRO_0000035241"
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:0007744|PDB:2KBK"
FT DISULFID 35..55
FT /evidence="ECO:0007744|PDB:2KBK"
FT DISULFID 41..65
FT /evidence="ECO:0007744|PDB:2KBK"
FT DISULFID 45..67
FT /evidence="ECO:0007744|PDB:2KBK"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2KBK"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:2KBK"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2KBK"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:2KBK"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:2KBK"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:2KBK"
SQ SEQUENCE 84 AA; 9346 MW; 62D3FD255F7E2D61 CRC64;
MNYLVMISFA LLLMKGVESV RDAYIAKPEN CVYECGITQD CNKLCTENGA ESGYCQWGGK
YGNACWCIKL PDSVPIRVPG KCQR
