TX31A_SCODE
ID TX31A_SCODE Reviewed; 70 AA.
AC A0A0R4I951;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 2.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Kappa-scoloptoxin(03)-Ssd1a {ECO:0000250|UniProtKB:I6RU32};
DE Short=Kappa-SLPTX(03)-Ssd1a {ECO:0000250|UniProtKB:I6RU32};
DE AltName: Full=Toxin SSD609 {ECO:0000303|PubMed:26307551};
DE Flags: Precursor;
OS Scolopendra dehaani (Thai centipede) (Scolopendra subspinipes dehaani).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Scolopendromorpha; Scolopendridae; Scolopendra.
OX NCBI_TaxID=2609776;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-49, FUNCTION, MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=23148443; DOI=10.1021/pr300881d;
RA Liu Z.C., Zhang R., Zhao F., Chen Z.M., Liu H.W., Wang Y.J., Jiang P.,
RA Zhang Y., Wu Y., Ding J.P., Lee W.H., Zhang Y.;
RT "Venomic and transcriptomic analysis of centipede Scolopendra subspinipes
RT dehaani.";
RL J. Proteome Res. 11:6197-6212(2012).
RN [2]
RP STRUCTURE BY NMR OF 24-70, SYNTHESIS OF 24-70, AND DISULFIDE BONDS.
RX PubMed=26307551; DOI=10.1038/srep13399;
RA Sun P., Wu F., Wen M., Yang X., Wang C., Li Y., He S., Zhang L., Zhang Y.,
RA Tian C.;
RT "A distinct three-helix centipede toxin SSD609 inhibits I(ks) channels by
RT interacting with the KCNE1 auxiliary subunit.";
RL Sci. Rep. 5:13399-13399(2015).
CC -!- FUNCTION: Toxin that acts on KCNE1 and to a lesser extent KCNE3, the
CC auxiliary subunits of potassium channel Kv7.1/KNCQ1 (PubMed:26307551).
CC The toxin reversibly inhibits the slow delayed rectifier potassium
CC currents (IKs) exhibited by the complex KCNQ1-KCNE1 (IC(50)=652 nM) and
CC by the complex KCNQ1-KCNE3 (30% inhibition at 1 uM) (PubMed:26307551).
CC The positively charged part of toxin binds to the negatively charged
CC residues of the N-terminal amphipathic helix from the KCNE1
CC extracellular region (PubMed:26307551). {ECO:0000269|PubMed:26307551}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23148443}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:23148443}.
CC -!- MASS SPECTROMETRY: Mass=5624.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:23148443};
CC -!- MISCELLANEOUS: The toxin does not inhibit the slow delayed rectifier
CC potassium current (IKs) exhibited by the following channels: KCNQ1
CC alone, the complex KCNQ1-KCNE2, the complex KCNQ1-KCNE4 and the complex
CC KCNMA1-KCNMB1 (KCa1.1-beta-1 subunit) (PubMed:26307551).
CC {ECO:0000269|PubMed:26307551}.
CC -!- SIMILARITY: Belongs to the scoloptoxin-03 family. {ECO:0000305}.
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DR EMBL; KC144606; -; NOT_ANNOTATED_CDS; mRNA.
DR PDB; 2MVT; NMR; -; A=24-70.
DR PDBsum; 2MVT; -.
DR AlphaFoldDB; A0A0R4I951; -.
DR SMR; A0A0R4I951; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Potassium channel impairing toxin; Secreted;
KW Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:23148443"
FT CHAIN 24..70
FT /note="Kappa-scoloptoxin(03)-Ssd1a"
FT /evidence="ECO:0000305"
FT /id="PRO_0000444605"
FT DISULFID 28..55
FT /evidence="ECO:0000269|PubMed:26307551,
FT ECO:0000312|PDB:2MVT"
FT DISULFID 38..54
FT /evidence="ECO:0000269|PubMed:26307551,
FT ECO:0000312|PDB:2MVT"
FT DISULFID 41..64
FT /evidence="ECO:0000269|PubMed:26307551,
FT ECO:0000312|PDB:2MVT"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:2MVT"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:2MVT"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:2MVT"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:2MVT"
SQ SEQUENCE 70 AA; 8253 MW; 49130659792F7EB8 CRC64;
MKFSMAILLV MAPIMFSLDK CYSADDKCED SLRREIACTK CRDRVRTDDY FYECCTSEST
FKKCQTMLHQ
