ID   KAX69_OPICA             Reviewed;          61 AA.
AC   Q6XLL6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Potassium channel toxin alpha-KTx 6.9 {ECO:0000303|PubMed:14696198};
DE   AltName: Full=OcKTx4 {ECO:0000303|PubMed:14696198};
DE   Flags: Precursor;
OS   Opistophthalmus carinatus (African yellow leg scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Opistophthalminae;
OC   Opistophthalmus.
OX   NCBI_TaxID=190115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=14696198; DOI=10.1002/prot.10588;
RA   Zhu S.-Y., Huys I., Dyason K., Verdonck F., Tytgat J.;
RT   "Evolutionary trace analysis of scorpion toxins specific for K-channels.";
RL   Proteins 54:361-370(2004).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 24-61, SYNTHESIS OF 24-61, AND
RP   DISULFIDE BONDS.
RX   PubMed=29483648; DOI=10.1038/s41594-018-0033-9;
RA   Correnti C.E., Gewe M.M., Mehlin C., Bandaranayake A.D., Johnsen W.A.,
RA   Rupert P.B., Brusniak M.Y., Clarke M., Burke S.E., De Van Der Schueren W.,
RA   Pilat K., Turnbaugh S.M., May D., Watson A., Chan M.K., Bahl C.D.,
RA   Olson J.M., Strong R.K.;
RT   "Screening, large-scale production and structure-based classification of
RT   cystine-dense peptides.";
RL   Nat. Struct. Mol. Biol. 25:270-278(2018).
CC   -!- FUNCTION: Inhibits Kv1.2/KCNA2 and Kv1.3/KCNA3 voltage-gated potassium
CC       channels (PubMed:29483648). {ECO:0000269|PubMed:29483648}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:14696198}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:14696198}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 06 subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY225782; AAP73820.1; -; mRNA.
DR   PDB; 6AVD; X-ray; 1.80 A; A=24-61.
DR   PDBsum; 6AVD; -.
DR   AlphaFoldDB; Q6XLL6; -.
DR   SMR; Q6XLL6; -.
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; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..61
FT                   /note="Potassium channel toxin alpha-KTx 6.9"
FT                   /id="PRO_0000227034"
FT   SITE            49
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   SITE            58
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        29..50
FT                   /evidence="ECO:0000269|PubMed:29483648,
FT                   ECO:0000312|PDB:6AVD"
FT   DISULFID        35..55
FT                   /evidence="ECO:0000269|PubMed:29483648,
FT                   ECO:0000312|PDB:6AVD"
FT   DISULFID        39..57
FT                   /evidence="ECO:0000269|PubMed:29483648,
FT                   ECO:0000312|PDB:6AVD"
FT   DISULFID        45..60
FT                   /evidence="ECO:0000269|PubMed:29483648,
FT                   ECO:0000312|PDB:6AVD"
FT   HELIX           32..34
FT                   /evidence="ECO:0007829|PDB:6AVD"
FT   HELIX           36..43
FT                   /evidence="ECO:0007829|PDB:6AVD"
FT   STRAND          48..51
FT                   /evidence="ECO:0007829|PDB:6AVD"
FT   STRAND          54..57
FT                   /evidence="ECO:0007829|PDB:6AVD"
SQ   SEQUENCE   61 AA;  6589 MW;  E6F9A5179E74C640 CRC64;
     MNAKFILLLL VVTTTTLLPD AKGAEIIRCS GTRECYAPCQ KLTGCLNAKC MNKACKCYGC
     V