KAX72_PANIM
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 25-MAY-2022, entry version 97.
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;
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 PDBsum; 1C49; -.
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 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 PRINTS; PR00286; CHARYBDTOXIN.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
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
