KAX52_ANDMA
ID KAX52_ANDMA Reviewed; 31 AA.
AC P31719;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Potassium channel toxin alpha-KTx 5.2;
DE AltName: Full=AmPO5;
DE Short=P05 {ECO:0000303|PubMed:11527975, ECO:0000303|PubMed:8385026};
DE Short=PO5 {ECO:0000303|PubMed:11527975, ECO:0000303|PubMed:8385026};
DE AltName: Full=Leiurotoxin I-like toxin P05 {ECO:0000303|PubMed:8385026, ECO:0000303|PubMed:8457543};
OS Androctonus mauritanicus mauritanicus (Scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX NCBI_TaxID=6860;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=8385026; DOI=10.1016/0014-5793(93)80583-g;
RA Zerrouk H., Mansuelle P., Benslimane A., Rochat H., Martin-Eauclaire M.-F.;
RT "Characterization of a new leiurotoxin I-like scorpion toxin. PO5 from
RT Androctonus mauretanicus mauretanicus.";
RL FEBS Lett. 320:189-192(1993).
RN [2]
RP FUNCTION, AND SYNTHESIS.
RX PubMed=8457543; DOI=10.1021/bi00062a005;
RA Sabatier J.-M., Zerrouk H., Darbon H., Mabrouk K., Benslimane A.,
RA Rochat H., Martin-Eauclaire M.-F., van Rietschoten J.;
RT "P05, a new leiurotoxin I-like scorpion toxin: synthesis and structure-
RT activity relationships of the alpha-amidated analog, a ligand of Ca(2+)-
RT activated K+ channels with increased affinity.";
RL Biochemistry 32:2763-2770(1993).
RN [3]
RP FUNCTION, MUTAGENESIS OF THR-1; VAL-2; ARG-7 AND VAL-24, AND SITES ALA-1;
RP PHE-6; ARG-7 AND VAL-24.
RX PubMed=11527975; DOI=10.1074/jbc.m106981200;
RA Shakkottai V.G., Regaya I., Wulff H., Fajloun Z., Tomita H., Fathallah M.,
RA Cahalan M.D., Gargus J.J., Sabatier J.M., Chandy K.G.;
RT "Design and characterization of a highly selective peptide inhibitor of the
RT small conductance calcium-activated K+ channel, SkCa2.";
RL J. Biol. Chem. 276:43145-43151(2001).
RN [4]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=8218272; DOI=10.1021/bi00096a005;
RA Meunier S., Bernassau J.-M., Sabatier J.-M., Martin-Eauclaire M.-F.,
RA van Rietschoten J., Cambillau C., Darbon H.;
RT "Solution structure of P05-NH2, a scorpion toxin analog with high affinity
RT for the apamin-sensitive potassium channel.";
RL Biochemistry 32:11969-11976(1993).
CC -!- FUNCTION: Blocker for the small conductance calcium-activated potassium
CC channels (PubMed:8385026, PubMed:8457543, PubMed:11527975). Shows
CC similar affinities for KCa2.2/KCNN2 (Kd=22 nM) and KCa2.3/KCNN3 (Kd=25
CC nM) (PubMed:11527975). {ECO:0000269|PubMed:11527975,
CC ECO:0000269|PubMed:8385026, ECO:0000269|PubMed:8457543}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8385026}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:8385026}.
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:8218272}.
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Alpha-KTx 05 subfamily. {ECO:0000305}.
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DR PIR; A49078; A49078.
DR PDB; 1PNH; NMR; -; A=1-31.
DR PDBsum; 1PNH; -.
DR AlphaFoldDB; P31719; -.
DR SMR; P31719; -.
DR EvolutionaryTrace; P31719; -.
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 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 Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin.
FT PEPTIDE 1..31
FT /note="Potassium channel toxin alpha-KTx 5.2"
FT /evidence="ECO:0000269|PubMed:8385026"
FT /id="PRO_0000044928"
FT REGION 6..9
FT /note="[R/K]XCQ motif"
FT /evidence="ECO:0000305"
FT SITE 1
FT /note="Interacts with KCa2.2/KCNN2 and KCa2.3/KCNN3"
FT /evidence="ECO:0000305|PubMed:11527975"
FT SITE 2
FT /note="Interacts with KCa2.2/KCNN2 and KCa2.3/KCNN3"
FT /evidence="ECO:0000305|PubMed:11527975"
FT SITE 7
FT /note="Interacts with KCa2.2/KCNN2 and KCa2.3/KCNN3"
FT /evidence="ECO:0000305|PubMed:11527975"
FT SITE 24
FT /note="Interacts with KCa2.2/KCNN2 and KCa2.3/KCNN3"
FT /evidence="ECO:0000305|PubMed:11527975"
FT DISULFID 3..21
FT /evidence="ECO:0000269|PubMed:8218272,
FT ECO:0000312|PDB:1PNH"
FT DISULFID 8..26
FT /evidence="ECO:0000269|PubMed:8218272,
FT ECO:0000312|PDB:1PNH"
FT DISULFID 12..28
FT /evidence="ECO:0000269|PubMed:8218272,
FT ECO:0000312|PDB:1PNH"
FT MUTAGEN 1
FT /note="T->A: 50-fold and 3-fold increase in potency of
FT inhibition of KCa2.2/KCNN2 and KCa2.3/KCNN3, respectively."
FT /evidence="ECO:0000269|PubMed:11527975"
FT MUTAGEN 2
FT /note="V->F: 50-fold and 6-fold increase in potency of
FT inhibition of KCa2.2/KCNN2 and KCa2.3/KCNN3, respectively."
FT /evidence="ECO:0000269|PubMed:11527975"
FT MUTAGEN 7
FT /note="R->M: 35-fold and 2-fold increase in potency of
FT inhibition of KCa2.2/KCNN2 and KCa2.3/KCNN3, respectively."
FT /evidence="ECO:0000269|PubMed:11527975"
FT MUTAGEN 24
FT /note="V->D: No change in potency of inhibition of
FT KCa2.2/KCNN2 and KCa2.3/KCNN3."
FT /evidence="ECO:0000269|PubMed:11527975"
FT HELIX 5..13
FT /evidence="ECO:0007829|PDB:1PNH"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:1PNH"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1PNH"
SQ SEQUENCE 31 AA; 3421 MW; 94B06CDC5CFB46FE CRC64;
TVCNLRRCQL SCRSLGLLGK CIGVKCECVK H
