ID   KA159_LYCMC             Reviewed;          60 AA.
AC   D9U2A8;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   22-FEB-2023, entry version 30.
DE   RecName: Full=Potassium channel toxin alpha-KTx 15.9;
DE   AltName: Full=Neurotoxin KTx9 {ECO:0000312|EMBL:ABY26664.1};
DE   Flags: Precursor;
OS   Lychas mucronatus (Chinese swimming scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Lychas.
OX   NCBI_TaxID=172552;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Hainan; TISSUE=Venom gland;
RX   PubMed=20663230; DOI=10.1186/1471-2164-11-452;
RA   Zhao R., Ma Y., He Y., Di Z., Wu Y.-L., Cao Z.-J., Li W.-X.;
RT   "Comparative venom gland transcriptome analysis of the scorpion Lychas
RT   mucronatus reveals intraspecific toxic gene diversity and new venomous
RT   components.";
RL   BMC Genomics 11:452-452(2010).
RN   [2]
RP   FUNCTION, AND SYNTHESIS OF 23-60.
RX   PubMed=29483648; DOI=10.1038/s41594-018-0033-9;
RA   Correnti C.E., Gewe M.M., Mehlin C., Bandaranayake A.D., Johnsen W.A.,
RA   Rupert P.B., Brusniak M.Y., Clarke M., Burke S.E., De Van Der Schueren W.,
RA   Pilat K., Turnbaugh S.M., May D., Watson A., Chan M.K., Bahl C.D.,
RA   Olson J.M., Strong R.K.;
RT   "Screening, large-scale production and structure-based classification of
RT   cystine-dense peptides.";
RL   Nat. Struct. Mol. Biol. 25:270-278(2018).
CC   -!- FUNCTION: Blocker of A-type voltage-gated potassium channels of
CC       cerebellar granular cells. May also inhibit Kv4/KCND when coexpressed
CC       with DPP6 or DPP10. The occlusion of the outer entry of the K(+)
CC       conducting pore is partially reversible and affects both open and
CC       closed channels. It shares the same target in rat brain than BmTX3 (AC
CC       Q8I0L5) and AmmTX3 (AC P60208). Has been shown to weakly inhibit TRPV1
CC       channels (PubMed:29483648). {ECO:0000250|UniProtKB:P60208,
CC       ECO:0000250|UniProtKB:Q867F4, ECO:0000269|PubMed:29483648}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20663230}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:20663230}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CSalpha/beta).
CC       {ECO:0000250|UniProtKB:P84777}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 15 subfamily. {ECO:0000305}.
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DR   EMBL; EU163855; ABY26664.1; -; mRNA.
DR   AlphaFoldDB; D9U2A8; -.
DR   SMR; D9U2A8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor 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   Gene3D; 3.30.30.10; Knottin, scorpion toxin-like; 1.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR001947; Scorpion_toxinS_K_inh.
DR   Pfam; PF00451; Toxin_2; 1.
DR   PRINTS; PR00286; CHARYBDTOXIN.
DR   SUPFAM; SSF57095; Scorpion toxin-like; 1.
DR   PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..60
FT                   /note="Potassium channel toxin alpha-KTx 15.9"
FT                   /id="PRO_0000403829"
FT   DISULFID        30..51
FT                   /evidence="ECO:0000250|UniProtKB:Q86BX0"
FT   DISULFID        36..56
FT                   /evidence="ECO:0000250|UniProtKB:Q86BX0"
FT   DISULFID        40..58
FT                   /evidence="ECO:0000250|UniProtKB:Q86BX0"
SQ   SEQUENCE   60 AA;  6526 MW;  F7B7FA7287261E01 CRC64;
     MKIFLPVLVM LILCSMCLLT EGQVSTNKKC SNTSQCYKTC EKVVGVAAGK CMNGKCICYP
//