ID   KAX68_OPICA             Reviewed;          61 AA.
AC   Q6XLL7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   22-FEB-2023, entry version 50.
DE   RecName: Full=Potassium channel toxin alpha-KTx 6.8 {ECO:0000303|PubMed:14696198};
DE   AltName: Full=OcKTx3 {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).
CC   -!- FUNCTION: Blocker of voltage-gated potassium channels. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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; AY225781; AAP73819.1; -; mRNA.
DR   AlphaFoldDB; Q6XLL7; -.
DR   SMR; Q6XLL7; -.
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; Knottin, scorpion toxin-like; 1.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR001947; Scorpion_toxinS_K_inh.
DR   Pfam; PF00451; Toxin_2; 1.
DR   SUPFAM; SSF57095; Scorpion toxin-like; 1.
DR   PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..60
FT                   /note="Potassium channel toxin alpha-KTx 6.8"
FT                   /id="PRO_0000227033"
FT   MOD_RES         60
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        29..50
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        35..55
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        39..57
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        45..60
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
SQ   SEQUENCE   61 AA;  6747 MW;  D25F4D9774F55D01 CRC64;
     MNAKFILLLL VVTTTILLPD TQGAEVIKCR TPKDCADPCR KQTGCPHAKC MNKTCRCHRC
     G
//