ID   KA151_ANDAU             Reviewed;          37 AA.
AC   P60233;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Potassium channel toxin alpha-KTx 15.1 {ECO:0000305};
DE   AltName: Full=Peptide Aa1 {ECO:0000303|PubMed:11018665};
OS   Androctonus australis (Sahara scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX   NCBI_TaxID=6858;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=11018665; DOI=10.1016/s0005-2736(00)00259-5;
RA   Pisciotta M., Coronas F.I., Bloch C. Jr., Prestipino G., Possani L.D.;
RT   "Fast K(+) currents from cerebellum granular cells are completely blocked
RT   by a peptide purified from Androctonus australis Garzoni scorpion venom.";
RL   Biochim. Biophys. Acta 1468:203-212(2000).
RN   [2]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=18687312; DOI=10.1016/j.bcp.2008.07.008;
RA   Abdel-Mottaleb Y., Corzo G., Martin-Eauclaire M.F., Satake H., Ceard B.,
RA   Peigneur S., Nambaru P., Bougis P.E., Possani L.D., Tytgat J.;
RT   "A common 'hot spot' confers hERG blockade activity to alpha-scorpion
RT   toxins affecting K+ channels.";
RL   Biochem. Pharmacol. 76:805-815(2008).
CC   -!- FUNCTION: Blocker of voltage-gated potassium channels (600 nM of the
CC       toxin induces a block of 25% of hERG currents) (PubMed:18687312). May
CC       also inhibit Kv4/KCND when coexpressed with DPP6 or DPP10 (By
CC       similarity). In adult rat brain, it blocks the transient potassium
CC       channels in cerebellum granular cells. Blocks potassium channels by a
CC       simple 'plugging mechanism', in which a single toxin molecule finds a
CC       specific receptor site in the external vestibule of the potassium
CC       channel and thereby occludes the outer entry to the potassium
CC       conducting pore (PubMed:11018665). {ECO:0000250|UniProtKB:P60208,
CC       ECO:0000269|PubMed:11018665, ECO:0000269|PubMed:18687312}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11018665}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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   AlphaFoldDB; P60233; -.
DR   SMR; P60233; -.
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; -; 1.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR001947; Scorpion_toxinS_K_inh.
DR   Pfam; PF00451; Toxin_2; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Potassium channel impairing toxin; Pyrrolidone carboxylic acid;
KW   Secreted; Toxin; Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..37
FT                   /note="Potassium channel toxin alpha-KTx 15.1"
FT                   /evidence="ECO:0000269|PubMed:11018665"
FT                   /id="PRO_0000044896"
FT   SITE            6
FT                   /note="Hot spot basic residue in hERG blocking currents"
FT                   /evidence="ECO:0000305|PubMed:18687312"
FT   SITE            18
FT                   /note="Hot spot basic residue in hERG blocking currents"
FT                   /evidence="ECO:0000305|PubMed:18687312"
FT   SITE            19
FT                   /note="Hot spot basic residue in hERG blocking currents"
FT                   /evidence="ECO:0000305|PubMed:18687312"
FT   SITE            27
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   SITE            36
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I0L5"
FT   DISULFID        8..28
FT                   /evidence="ECO:0000250|UniProtKB:Q86BX0"
FT   DISULFID        13..33
FT                   /evidence="ECO:0000250|UniProtKB:Q86BX0"
FT   DISULFID        17..35
FT                   /evidence="ECO:0000250|UniProtKB:Q86BX0"
SQ   SEQUENCE   37 AA;  3875 MW;  29C0647D522001C4 CRC64;
     QNETNKKCQG GSCASVCRRV IGVAAGKCIN GRCVCYP