ID   KKX21_OPIMA             Reviewed;          27 AA.
AC   P0C1Z3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Potassium channel toxin kappa-KTx 2.2 {ECO:0000303|PubMed:22305749};
DE   AltName: Full=Toxin OmTx2 {ECO:0000303|PubMed:15631621};
DE   Contains:
DE     RecName: Full=Potassium channel toxin kappa-KTx 2.1 {ECO:0000303|PubMed:22305749};
DE     AltName: Full=Toxin OmTx1 {ECO:0000303|PubMed:15631621};
DE   Contains:
DE     RecName: Full=Potassium channel toxin kappa-KTx 2.4 {ECO:0000303|PubMed:22305749};
DE     AltName: Full=Toxin OmTx4 {ECO:0000303|PubMed:15631621};
OS   Opisthacanthus madagascariensis (Scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Hemiscorpiidae; Opisthacanthus.
OX   NCBI_TaxID=167108;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION (OMTX1 AND OMTX2), SYNTHESIS (OMTX1; OMTX2 AND
RP   OMTX4), IDENTIFICATION BY MASS SPECTROMETRY, STRUCTURE BY NMR (OMTX1 AND
RP   OMTX2), DISULFIDE BONDS, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=15631621; DOI=10.1042/bj20041705;
RA   Chagot B., Pimentel C., Dai L., Pil J., Tytgat J., Nakajima T., Corzo G.,
RA   Darbon H., Ferrat G.;
RT   "An unusual fold for potassium channel blockers: NMR structure of three
RT   toxins from the scorpion Opisthacanthus madagascariensis.";
RL   Biochem. J. 388:263-271(2005).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=22305749; DOI=10.1016/j.bcp.2012.01.021;
RA   Vandendriessche T., Kopljar I., Jenkins D.P., Diego-Garcia E.,
RA   Abdel-Mottaleb Y., Vermassen E., Clynen E., Schoofs L., Wulff H.,
RA   Snyders D., Tytgat J.;
RT   "Purification, molecular cloning and functional characterization of HelaTx1
RT   (Heterometrus laoticus): the first member of a new kappa-KTX subfamily.";
RL   Biochem. Pharmacol. 83:1307-1317(2012).
CC   -!- FUNCTION: OmTx1 decreases the amplitude of the potassium current of the
CC       rat channels Kv1.1/KCNA1 by 17% and Kv1.2/KCNA2 by 12% as well as human
CC       Kv1.3/KCNA3 by 24%. {ECO:0000269|PubMed:15631621}.
CC   -!- FUNCTION: OmTx2 decreases the amplitude of the potassium current of the
CC       rat channels Kv1.1/KCNA1 by 8% and Kv1.2/KCNA2 by 10% as well as human
CC       Kv1.3/KCNA3 by 36%. Also alters glucose-induced insulin release from
CC       pancreatic islets. {ECO:0000269|PubMed:15631621}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15631621}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15631621}.
CC   -!- DOMAIN: Has the structural arrangement of two alpha-helices stabilized
CC       by disulfide bonds (CSalpha/alpha 2(S-S)).
CC       {ECO:0000269|PubMed:15631621}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor kappa-KTx family. Kappa-KTx 2 subfamily.
CC       {ECO:0000305}.
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DR   PDB; 1WQC; NMR; -; A=1-26.
DR   PDB; 1WQD; NMR; -; A=1-27.
DR   PDBsum; 1WQC; -.
DR   PDBsum; 1WQD; -.
DR   AlphaFoldDB; P0C1Z3; -.
DR   SMR; P0C1Z3; -.
DR   EvolutionaryTrace; P0C1Z3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Toxin; Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..27
FT                   /note="Potassium channel toxin kappa-KTx 2.2"
FT                   /evidence="ECO:0000303|PubMed:15631621"
FT                   /id="PRO_0000254058"
FT   PEPTIDE         1..26
FT                   /note="Potassium channel toxin kappa-KTx 2.1"
FT                   /evidence="ECO:0000303|PubMed:15631621"
FT                   /id="PRO_0000254059"
FT   PEPTIDE         1..24
FT                   /note="Potassium channel toxin kappa-KTx 2.4"
FT                   /evidence="ECO:0000303|PubMed:15631621"
FT                   /id="PRO_0000254060"
FT   DISULFID        3..21
FT                   /evidence="ECO:0000269|PubMed:15631621"
FT   DISULFID        7..17
FT                   /evidence="ECO:0000269|PubMed:15631621"
FT   HELIX           2..10
FT                   /evidence="ECO:0007829|PDB:1WQC"
FT   HELIX           15..22
FT                   /evidence="ECO:0007829|PDB:1WQC"
SQ   SEQUENCE   27 AA;  3152 MW;  888A2DA64298BC32 CRC64;
     DPCYEVCLQQ HGNVKECEEA CKHPVEY