ID   KAX65_PANIM             Reviewed;          38 AA.
AC   P58490;
DT   19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   19-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Potassium channel toxin alpha-KTx 6.5;
DE   AltName: Full=Pi-7;
DE            Short=Pi7;
DE   AltName: Full=Toxin-7;
OS   Pandinus imperator (Emperor scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Pandininae; Pandinus.
OX   NCBI_TaxID=55084;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=9655636; DOI=10.1016/s0041-0101(97)00163-3;
RA   Olamendi-Portugal T., Gomez-Lagunas F., Gurrola G.B., Possani L.D.;
RT   "Two similar peptides from the venom of the scorpion Pandinus imperator,
RT   one highly effective blocker and the other inactive on K+ channels.";
RL   Toxicon 36:759-770(1998).
RN   [2]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=10606507; DOI=10.1021/bi991685m;
RA   Delepierre M., Prochnicka-Chalufour A., Boisbouvier J., Possani L.D.;
RT   "Pi7, an orphan peptide from the scorpion Pandinus imperator: a 1H-NMR
RT   analysis using a nano-NMR probe.";
RL   Biochemistry 38:16756-16765(1999).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9655636}.
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   -!- MISCELLANEOUS: Is inactive on voltage-gated potassium channels.
CC       {ECO:0000305|PubMed:9655636}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 06 subfamily. {ECO:0000305}.
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DR   PDB; 1QKY; NMR; -; A=1-38.
DR   PDBsum; 1QKY; -.
DR   AlphaFoldDB; P58490; -.
DR   SMR; P58490; -.
DR   EvolutionaryTrace; P58490; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Secreted; Toxin.
FT   PEPTIDE         1..38
FT                   /note="Potassium channel toxin alpha-KTx 6.5"
FT                   /id="PRO_0000044914"
FT   DISULFID        6..27
FT                   /evidence="ECO:0000269|PubMed:10606507"
FT   DISULFID        12..32
FT                   /evidence="ECO:0000269|PubMed:10606507"
FT   DISULFID        16..34
FT                   /evidence="ECO:0000269|PubMed:10606507"
FT   DISULFID        22..37
FT                   /evidence="ECO:0000269|PubMed:10606507"
FT   HELIX           9..19
FT                   /evidence="ECO:0007829|PDB:1QKY"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:1QKY"
FT   STRAND          31..34
FT                   /evidence="ECO:0007829|PDB:1QKY"
SQ   SEQUENCE   38 AA;  4291 MW;  101A3B3A95561FB8 CRC64;
     DEAIRCTGTK DCYIPCRYIT GCFNSRCINK SCKCYGCT