ID   KAX81_ANDMA             Reviewed;          29 AA.
AC   P56215;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Potassium channel toxin alpha-KTx 8.1 {ECO:0000305};
DE   AltName: Full=AmP01;
DE            Short=P01;
DE            Short=PO1 {ECO:0000303|PubMed:11527975, ECO:0000303|PubMed:8985784};
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 SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=8985784; DOI=10.1111/j.1399-3011.1996.tb00870.x;
RA   Zerrouk H., Laraba-Djebari F., Fremont V., Meki A., Darbon H.,
RA   Mansuelle P., Oughideni R., van Rietschoten J., Rochat H.,
RA   Martin-Eauclaire M.-F.;
RT   "Characterization of PO1, a new peptide ligand of the apamin-sensitive Ca2+
RT   activated K+ channel.";
RL   Int. J. Pept. Protein Res. 48:514-521(1996).
RN   [2]
RP   FUNCTION.
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   [3]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=8778783;
RX   DOI=10.1002/(sici)1097-0134(199603)24:3<359::aid-prot9>3.0.co;2-b;
RA   Blanc E., Fremont V., Sizun P., Meunier S., van Rietschoten J., Thevand A.,
RA   Bernassau J.-M., Darbon H.;
RT   "Solution structure of P01, a natural scorpion peptide structurally
RT   analogous to scorpion toxins specific for apamin-sensitive potassium
RT   channel.";
RL   Proteins 24:359-369(1996).
CC   -!- FUNCTION: Blocker for the small conductance calcium-activated potassium
CC       channels (KCa2). {ECO:0000269|PubMed:8985784}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8985784}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:8985784}.
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:8778783}.
CC   -!- MISCELLANEOUS: does not or very weakly inhibits KCa2.2/KCNN2 (Kd >1 uM)
CC       and KCa2.3/KCNN3 (Kd >1 uM). {ECO:0000269|PubMed:11527975}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 08 subfamily. {ECO:0000305}.
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DR   PDB; 1ACW; NMR; -; A=1-29.
DR   PDBsum; 1ACW; -.
DR   AlphaFoldDB; P56215; -.
DR   SMR; P56215; -.
DR   EvolutionaryTrace; P56215; -.
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; IPR008911; Toxin_alpha-KTx_8/9.
DR   Pfam; PF05453; Toxin_6; 1.
DR   SUPFAM; SSF57095; SSF57095; 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..29
FT                   /note="Potassium channel toxin alpha-KTx 8.1"
FT                   /evidence="ECO:0000269|PubMed:8985784"
FT                   /id="PRO_0000044945"
FT   DISULFID        3..19
FT                   /evidence="ECO:0000269|PubMed:8778783,
FT                   ECO:0000312|PDB:1ACW"
FT   DISULFID        6..24
FT                   /evidence="ECO:0000269|PubMed:8778783,
FT                   ECO:0000312|PDB:1ACW"
FT   DISULFID        10..26
FT                   /evidence="ECO:0000269|PubMed:8778783,
FT                   ECO:0000312|PDB:1ACW"
FT   HELIX           5..11
FT                   /evidence="ECO:0007829|PDB:1ACW"
FT   TURN            12..14
FT                   /evidence="ECO:0007829|PDB:1ACW"
FT   STRAND          16..20
FT                   /evidence="ECO:0007829|PDB:1ACW"
FT   STRAND          23..27
FT                   /evidence="ECO:0007829|PDB:1ACW"
SQ   SEQUENCE   29 AA;  3185 MW;  BC5F650C196E01C8 CRC64;
     VSCEDCPEHC STQKAQAKCD NDKCVCEPI