ID   TX14B_SCODE             Reviewed;         197 AA.
AC   P0DPU6;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Scoloptoxin SSD20 {ECO:0000303|PubMed:23148443};
DE   Flags: Precursor; Fragment;
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 7-29, SUBCELLULAR LOCATION,
RP   MASS SPECTROMETRY, AND FUNCTION.
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).
CC   -!- FUNCTION: May act as a voltage-gated potassium channel inhibitor. Is
CC       highly similar to the subunit beta of SSD14 which, when complexed with
CC       subunit alpha, induces platelet aggregation and hemolysis.
CC       {ECO:0000305|PubMed:23148443}.
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=20667.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23148443};
CC   -!- SIMILARITY: Belongs to the scoloptoxin-11 family. {ECO:0000305}.
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DR   EMBL; KC144040; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DPU6; -.
DR   SMR; P0DPU6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0036374; F:glutathione hydrolase activity; IEA:InterPro.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.20.40; -; 1.
DR   InterPro; IPR000101; GGT_peptidase.
DR   InterPro; IPR043137; GGT_ssub.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   PANTHER; PTHR11686; PTHR11686; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hemostasis impairing toxin;
KW   Ion channel impairing toxin; Platelet aggregation activating toxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          <1..6
FT                   /evidence="ECO:0000269|PubMed:23148443"
FT   CHAIN           7..197
FT                   /note="Scoloptoxin SSD20"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000446692"
FT   CONFLICT        16
FT                   /note="E -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   197 AA;  21351 MW;  7B2978048D563E31 CRC64;
     PPMTTETAHI SVVSREGDAV VVTTTINYWF GSGLRSPSTG VILNDEMDDF SAHDIQNIYG
     VPPSKANFIV PGKRPQSSTC PSIFVNEGGD VVMAIGASGG TRITSSVSLT SMRVLWLGRN
     IKEAIDEPRL HHQLLPDEIE YEFKFPNEIL EKLKAIGHKT KPAGAFGSLV VGIKRMKGGT
     LTANYDYRRG GSVDGFK