ID   KAX1I_RHOJU             Reviewed;          37 AA.
AC   C0HJS9;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Potassium channel toxin alpha-KTx 1.18 {ECO:0000303|PubMed:26169670};
DE   AltName: Full=Peptide Rj1m1 {ECO:0000303|PubMed:26169670};
OS   Rhopalurus junceus (Caribbean blue scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Rhopalurus.
OX   NCBI_TaxID=419285 {ECO:0000303|PubMed:26169670};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:26169670};
RX   PubMed=26169670; DOI=10.1016/j.toxicon.2015.06.026;
RA   Rodriguez-Ravelo R., Batista C.V., Coronas F.I., Zamudio F.Z.,
RA   Hernandez-Orihuela L., Espinosa-Lopez G., Ruiz-Urquiola A., Possani L.D.;
RT   "Comparative proteomic analysis of male and female venoms from the Cuban
RT   scorpion Rhopalurus junceus.";
RL   Toxicon 107:327-334(2015).
CC   -!- FUNCTION: Blocks high conductance calcium-activated potassium channels.
CC       {ECO:0000250|UniProtKB:P0C182}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26169670}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:26169670}.
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   -!- MASS SPECTROMETRY: Mass=4029.94; Mass_error=1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:26169670};
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 01 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; C0HJS9; -.
DR   SMR; C0HJS9; -.
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.
PE   1: Evidence at protein level;
KW   Calcium-activated potassium channel impairing toxin;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..37
FT                   /note="Potassium channel toxin alpha-KTx 1.18"
FT                   /evidence="ECO:0000269|PubMed:26169670"
FT                   /id="PRO_0000441011"
FT   SITE            27
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:O46028"
FT   SITE            36
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:O46028"
FT   DISULFID        7..28
FT                   /evidence="ECO:0000250|UniProtKB:P24663"
FT   DISULFID        13..33
FT                   /evidence="ECO:0000250|UniProtKB:P24663"
FT   DISULFID        17..35
FT                   /evidence="ECO:0000250|UniProtKB:P24663"
SQ   SEQUENCE   37 AA;  4037 MW;  70E3E8F239A12E36 CRC64;
     IVIDVPCTVS KECWSACKKA VGTDRGKCMG KKCKCYP