SC11_MESMA
ID SC11_MESMA Reviewed; 85 AA.
AC Q9NJC7; Q49S26; Q9NJP8;
DT 19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=BmK AGP-SYPU2;
DE AltName: Full=Alpha-neurotoxin Tx11;
DE AltName: Full=Alpha-toxin 2;
DE AltName: Full=BmKalpha2;
DE AltName: Full=BmKalphaTx11;
DE AltName: Full=BmKalphaTx11';
DE AltName: Full=Toxin BmTX11';
DE AltName: Full=Toxin Bmka2;
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 [MRNA].
RC TISSUE=Venom gland;
RX PubMed=11306129; DOI=10.1016/s0041-0101(00)00257-9;
RA Ye J.-G., Chen J., Zuo X.-P., Ji Y.-H.;
RT "Cloning and characterization of cDNA sequences encoding two novel alpha-
RT like-toxin precursors from the Chinese scorpion Buthus martensii Karsch.";
RL Toxicon 39:1191-1194(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ISOFORM TX11P 4-LEU--PHE-7.
RC TISSUE=Venom gland;
RX PubMed=16053704; DOI=10.5483/bmbrep.2005.38.4.386;
RA Xu X., Cao Z., Sheng J., Wu W., Luo F., Sha Y., Mao X., Liu H., Jiang D.,
RA Li W.;
RT "Genomic sequence analysis and organization of BmKalphaTx11 and
RT BmKalphaTx15 from Buthus martensii Karsch: molecular evolution of alpha-
RT toxin genes.";
RL J. Biochem. Mol. Biol. 38:386-390(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=22295565;
RA Zhang R., Yang Z., Liu Y.F., Cui Y., Zhang J.H.;
RT "Purification, characterization and cDNA cloning of an analgesic peptide
RT from the Chinese scorpion Buthus martensii Karsch (BmK AGP-SYPU2).";
RL Mol. Biol. (Mosk.) 45:956-962(2011).
RN [5]
RP FUNCTION, BIOASSAY, SITES GLY-84 AND GLY-85, AND MUTAGENESIS OF
RP 84-GLY-GLY-85 AND GLY-85.
RX PubMed=21189156; DOI=10.5483/bmbrep.2010.43.12.801;
RA Zhang R., Cui Y., Zhang X., Yang Z., Zhao Y., Song Y., Wu C., Zhang J.;
RT "Soluble expression, purification and the role of C-terminal glycine
RT residues in scorpion toxin BmK AGP-SYPU2.";
RL BMB Rep. 43:801-806(2010).
RN [6]
RP STRUCTURE BY NMR OF 20-85, AND DISULFIDE BONDS.
RX PubMed=19932686; DOI=10.1016/j.bbrc.2009.11.110;
RA Zhu J., Tong X., Cao C., Wu G., Zhang N., Wu H.;
RT "Solution structure of BmKalphaTx11, a toxin from the venom of the Chinese
RT scorpion Buthus martensii Karsch.";
RL Biochem. Biophys. Res. Commun. 391:627-633(2010).
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 (By similarity). Shows analgesic
CC activity when intraperitoneally injected into mice. {ECO:0000250,
CC ECO:0000269|PubMed:21189156, ECO:0000269|PubMed:22295565}.
CC -!- SUBCELLULAR LOCATION: Secreted.
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 -!- MISCELLANEOUS: Exists only in one form, with a trans isomerization at
CC 28-Asp-Arg-29. The cis isomere does not exist (PubMed:19932686).
CC {ECO:0000305|PubMed:19932686}.
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; AF155364; AAF31478.1; -; mRNA.
DR EMBL; AF132974; AAF31295.1; -; mRNA.
DR EMBL; AF288608; AAG00581.1; -; mRNA.
DR EMBL; AY647171; AAV64255.1; -; Genomic_DNA.
DR PDB; 2KBH; NMR; -; A=20-85.
DR PDB; 2KBJ; NMR; -; A=20-85.
DR PDBsum; 2KBH; -.
DR PDBsum; 2KBJ; -.
DR AlphaFoldDB; Q9NJC7; -.
DR SMR; Q9NJC7; -.
DR EvolutionaryTrace; Q9NJC7; -.
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 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:0000250"
FT CHAIN 20..85
FT /note="BmK AGP-SYPU2"
FT /id="PRO_0000035245"
FT DOMAIN 21..83
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT SITE 84
FT /note="Important for analgesic activity"
FT SITE 85
FT /note="Important for analgesic activity"
FT DISULFID 31..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:19932686"
FT DISULFID 35..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:19932686"
FT DISULFID 41..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:19932686"
FT DISULFID 45..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:19932686"
FT VARIANT 4..7
FT /note="MVII -> LVFF (in isoform TX11P)"
FT VARIANT 13
FT /note="V -> L (in isoform TX11P)"
FT MUTAGEN 84..85
FT /note="Missing: Important decrease in analgesic activity."
FT /evidence="ECO:0000269|PubMed:21189156"
FT MUTAGEN 85
FT /note="Missing: Significant decrease in analgesic
FT activity."
FT /evidence="ECO:0000269|PubMed:21189156"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:2KBH"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:2KBH"
FT STRAND 51..70
FT /evidence="ECO:0007829|PDB:2KBH"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:2KBJ"
SQ SEQUENCE 85 AA; 9524 MW; 565390BB6E71806E CRC64;
MNYMVIISLA LLVMTGVESV KDGYIADDRN CPYFCGRNAY CDGECKKNRA ESGYCQWASK
YGNACWCYKL PDDARIMKPG RCNGG
