ID   KAX2E_HETGR             Reviewed;          37 AA.
AC   P0DL43;
DT   27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2015, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Potassium channel toxin alpha-KTx 2.14 {ECO:0000303|PubMed:24512947};
OS   Heteroctenus garridoi (Cuban scorpion) (Rhopalurus garridoi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Heteroctenus.
OX   NCBI_TaxID=2203757;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY PROFILE.
RC   TISSUE=Venom;
RX   PubMed=24512947; DOI=10.1016/j.peptides.2013.10.010;
RA   Rodriguez-Ravelo R., Restano-Cassulini R., Zamudio F.Z., Coronas F.I.,
RA   Espinosa-Lopez G., Possani L.D.;
RT   "A K+ channel blocking peptide from the Cuban scorpion Rhopalurus
RT   garridoi.";
RL   Peptides 53:42-47(2014).
CC   -!- FUNCTION: Reversibly blocks hKv1.1/KCNA1 (50% inhibition of current at
CC       1 uM). Seems not to be voltage-dependent.
CC       {ECO:0000269|PubMed:24512947}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24512947}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:24512947}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CSalpha/beta).
CC       {ECO:0000250|UniProtKB:P40755}.
CC   -!- MISCELLANEOUS: Does not block hKv1.4/KCNA4, hERG1/KCNH2 and EAG/KCNH1
CC       currents, at 1 uM. {ECO:0000269|PubMed:24512947}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 02 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DL43; -.
DR   SMR; P0DL43; -.
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   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   CHAIN           1..37
FT                   /note="Potassium channel toxin alpha-KTx 2.14"
FT                   /evidence="ECO:0000269|PubMed:24512947"
FT                   /id="PRO_0000433139"
FT   SITE            27
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   SITE            36
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   DISULFID        7..28
FT                   /evidence="ECO:0000250|UniProtKB:P40755"
FT   DISULFID        13..33
FT                   /evidence="ECO:0000250|UniProtKB:P40755"
FT   DISULFID        17..35
FT                   /evidence="ECO:0000250|UniProtKB:P40755"
SQ   SEQUENCE   37 AA;  3946 MW;  C99DEA3CBA0136FC CRC64;
     TIINVKCTSP KQCVPACKAA MGTVRAKCIN GKCKCYI