ID   KA157_ANDAM             Reviewed;          59 AA.
AC   Q5K0E0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Potassium channel toxin alpha-KTx 15.7;
DE   AltName: Full=Neurotoxin AamTX {ECO:0000303|PubMed:15808902};
DE   Flags: Precursor;
OS   Androctonus amoreuxi (African fattail scorpion) (Scorpio amoreuxi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX   NCBI_TaxID=112024;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-41, MASS SPECTROMETRY,
RP   PYROGLUTAMATE FORMATION AT GLN-23, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=15808902; DOI=10.1016/j.peptides.2004.12.002;
RA   Chen T., Walker B., Zhou M., Shaw C.;
RT   "Molecular cloning of a novel putative potassium channel-blocking
RT   neurotoxin from the venom of the North African scorpion, Androctonus
RT   amoreuxi.";
RL   Peptides 26:731-736(2005).
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). {ECO:0000250|UniProtKB:P60208,
CC       ECO:0000250|UniProtKB:Q867F4}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15808902}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15808902}.
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   -!- MASS SPECTROMETRY: Mass=3751.48; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15808902};
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; AJ850860; CAH65474.1; -; mRNA.
DR   AlphaFoldDB; Q5K0E0; -.
DR   SMR; Q5K0E0; -.
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; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:15808902"
FT   CHAIN           23..59
FT                   /note="Potassium channel toxin alpha-KTx 15.7"
FT                   /evidence="ECO:0000305|PubMed:15808902"
FT                   /id="PRO_0000231493"
FT   SITE            49
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   SITE            58
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         23
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:15808902"
FT   DISULFID        30..50
FT                   /evidence="ECO:0000250|UniProtKB:Q86BX0"
FT   DISULFID        35..55
FT                   /evidence="ECO:0000250|UniProtKB:Q86BX0"
FT   DISULFID        39..57
FT                   /evidence="ECO:0000250|UniProtKB:Q86BX0"
SQ   SEQUENCE   59 AA;  6146 MW;  503665804F6E7024 CRC64;
     MKFSSIILLT LLICSMSIFG NGQVQTNKKC KGGSCASVCA KEIGVAAGKC INGRCVCYP