ID   KAX72_PANIM             Reviewed;          35 AA.
AC   P55928;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   02-SEP-2026, entry version 101.
DE   RecName: Full=Potassium channel toxin alpha-KTx 7.2;
DE   AltName: Full=Pandinotoxin-beta;
DE   AltName: Full=Potassium channel-blocking toxin 3;
DE            Short=Pi-3;
DE            Short=Pi3;
DE   AltName: Full=Toxin PiTX-K-beta;
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.
RC   TISSUE=Venom;
RX   PubMed=8913348; DOI=10.1016/s0026-895x(25)09545-8;
RA   Rogowski R.S., Collins J.H., O'Neill T.J., Gustafson T.A., Werkman T.R.,
RA   Rogawski M.A., Tenenholz T.C., Weber D.J., Blaustein M.P.;
RT   "Three new toxins from the scorpion Pandinus imperator selectively block
RT   certain voltage-gated K+ channels.";
RL   Mol. Pharmacol. 50:1167-1177(1996).
RN   [2]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=8660410; DOI=10.1007/s002329900084;
RA   Gomez-Lagunas F., Olamendi-Portugal T., Zamudio F.Z., Possani L.D.;
RT   "Two novel toxins from the venom of the scorpion Pandinus imperator show
RT   that the N-terminal amino acid sequence is important for their affinities
RT   towards Shaker B K+ channels.";
RL   J. Membr. Biol. 152:49-56(1996).
RN   [3]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=10707030;
RX   DOI=10.1002/(sici)1097-0134(20000301)38:4<441::aid-prot9>3.0.co;2-l;
RA   Klenk K.C., Tenenholz T.C., Matteson D.R., Rogowski R.S., Blaustein M.P.,
RA   Weber D.J.;
RT   "Structural and functional differences of two toxins from the scorpion
RT   Pandinus imperator.";
RL   Proteins 38:441-449(2000).
CC   -!- FUNCTION: Potent inhibitor of the A-type voltage-gated potassium
CC       channels. Most potent inhibitor of Kv1.2/KCNA2 channels. Reversibly
CC       block the Shaker B potassium-channels (Kv1.1 sub-family), but with a
CC       lower affinity than PiTX-K alpha. {ECO:0000269|PubMed:8660410}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CSalpha/beta).
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 07 subfamily. {ECO:0000305}.
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DR   PDB; 1C49; NMR; -; A=1-35.
DR   AlphaFoldDB; P55928; -.
DR   BMRB; P55928; -.
DR   SMR; P55928; -.
DR   EvolutionaryTrace; P55928; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
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.
DR   PDBsum; 1C49; -.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Toxin; Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..35
FT                   /note="Potassium channel toxin alpha-KTx 7.2"
FT                   /id="PRO_0000044911"
FT   SITE            24
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   SITE            33
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   DISULFID        4..25
FT                   /evidence="ECO:0000269|PubMed:10707030"
FT   DISULFID        10..30
FT                   /evidence="ECO:0000269|PubMed:10707030"
FT   DISULFID        14..32
FT                   /evidence="ECO:0000269|PubMed:10707030"
FT   HELIX           7..10
FT                   /evidence="ECO:0007829|PDB:1C49"
FT   HELIX           11..17
FT                   /evidence="ECO:0007829|PDB:1C49"
FT   STRAND          23..26
FT                   /evidence="ECO:0007829|PDB:1C49"
FT   STRAND          29..32
FT                   /evidence="ECO:0007829|PDB:1C49"
SQ   SEQUENCE   35 AA;  4072 MW;  DFCC26880D4C792A CRC64;
     TISCTNEKQC YPHCKKETGY PNAKCMNRKC KCFGR
//