KAX64_PANIM
ID KAX64_PANIM Reviewed; 38 AA.
AC P58498;
DT 19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Potassium channel toxin alpha-KTx 6.4;
DE AltName: Full=Potassium channel-blocking toxin 4;
DE Short=Pi-4;
DE Short=Pi4;
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 FUNCTION, TOXIC DOSE, DISULFIDE BONDS, AND SYNTHESIS.
RX PubMed=12919322; DOI=10.1046/j.1432-1033.2003.03743.x;
RA M'Barek S., Mosbah A., Sandoz G., Fajloun Z., Olamendi-Portugal T.,
RA Rochat H., Sampieri F., Guijarro J.I., Mansuelle P., Delepierre M.,
RA De Waard M., Sabatier J.-M.;
RT "Synthesis and characterization of Pi4, a scorpion toxin from Pandinus
RT imperator that acts on K+ channels.";
RL Eur. J. Biochem. 270:3583-3592(2003).
RN [3]
RP STRUCTURE BY NMR, DOMAIN, DISULFIDE BONDS, AND SYNTHESIS.
RX PubMed=12930984; DOI=10.1110/ps.03186703;
RA Guijarro J.I., M'Barek S., Gomez-Lagunas F., Garnier D., Rochat H.,
RA Sabatier J.-M., Possani L.D., Delepierre M.;
RT "Solution structure of Pi4, a short four-disulfide-bridged scorpion toxin
RT specific of potassium channels.";
RL Protein Sci. 12:1844-1854(2003).
RN [4]
RP ERRATUM OF PUBMED:12930984.
RA Guijarro J.I., M'Barek S., Gomez-Lagunas F., Garnier D., Rochat H.,
RA Sabatier J.-M., Possani L., Delepierre M.;
RL Protein Sci. 12:2651-2651(2003).
CC -!- FUNCTION: Potently, completely and reversibly blocks voltage-gated
CC potassium channel Kv1.2/KCNA2 and Shaker B (Sh). Also blocks small
CC conductance (SK) calcium-activated potassium channel (KCNN).
CC {ECO:0000269|PubMed:12919322}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9655636}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:9655636}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC beta-sheet by disulfide bonds (CSalpha/beta).
CC {ECO:0000269|PubMed:12930984}.
CC -!- TOXIC DOSE: LD(50) is 10 ug/kg by intracerebroventricular injection
CC into mice. {ECO:0000269|PubMed:12919322}.
CC -!- MISCELLANEOUS: This toxin has no effect on voltage-gated potassium
CC channel Kv1.1/KCNA1 and Kv1.3/KCNA3. {ECO:0000305|PubMed:12919322}.
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; 1N8M; NMR; -; A=1-38.
DR PDBsum; 1N8M; -.
DR AlphaFoldDB; P58498; -.
DR SMR; P58498; -.
DR EvolutionaryTrace; P58498; -.
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 3D-structure; Calcium-activated potassium channel impairing toxin;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Potassium channel impairing toxin; Secreted; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT PEPTIDE 1..38
FT /note="Potassium channel toxin alpha-KTx 6.4"
FT /evidence="ECO:0000269|PubMed:9655636"
FT /id="PRO_0000044913"
FT SITE 10
FT /note="Important for the interaction with Kv1.2/KCNA2
FT channel"
FT /evidence="ECO:0000303|PubMed:12919322"
FT SITE 19
FT /note="Important for the interaction with Kv1.2/KCNA2
FT channel"
FT /evidence="ECO:0000303|PubMed:12919322"
FT SITE 26
FT /note="Basic residue of the functional dyad, important for
FT the interaction with Kv1.2/KCNA2 channel"
FT /evidence="ECO:0000303|PubMed:12919322"
FT SITE 28
FT /note="Important for the interaction with Kv1.2/KCNA2
FT channel"
FT /evidence="ECO:0000303|PubMed:12919322"
FT SITE 30
FT /note="Important for the interaction with Kv1.2/KCNA2
FT channel"
FT /evidence="ECO:0000303|PubMed:12919322"
FT SITE 33
FT /note="Important for the interaction with Kv1.2/KCNA2
FT channel"
FT /evidence="ECO:0000303|PubMed:12919322"
FT SITE 35
FT /note="Aromatic residue of the functional dyad, important
FT for the interaction with Kv1.2/KCNA2 channel"
FT /evidence="ECO:0000303|PubMed:12919322"
FT DISULFID 6..27
FT /evidence="ECO:0000269|PubMed:12919322,
FT ECO:0000269|PubMed:12930984, ECO:0007744|PDB:1N8M"
FT DISULFID 12..32
FT /evidence="ECO:0000269|PubMed:12919322,
FT ECO:0000269|PubMed:12930984, ECO:0007744|PDB:1N8M"
FT DISULFID 16..34
FT /evidence="ECO:0000269|PubMed:12919322,
FT ECO:0000269|PubMed:12930984, ECO:0007744|PDB:1N8M"
FT DISULFID 22..37
FT /evidence="ECO:0000269|PubMed:12919322,
FT ECO:0000269|PubMed:12930984, ECO:0007744|PDB:1N8M"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:1N8M"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1N8M"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1N8M"
SQ SEQUENCE 38 AA; 4188 MW; 1C1F402B8DF2EEFF CRC64;
IEAIRCGGSR DCYRPCQKRT GCPNAKCINK TCKCYGCS
