ID   KGX1A_CENMA             Reviewed;          42 AA.
AC   C0HLM3;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 1.
DT   25-MAY-2022, entry version 2.
DE   RecName: Full=Potassium channel toxin gamma-KTx 1.10 {ECO:0000303|PubMed:34201318};
DE            Short=CmERG1 {ECO:0000303|PubMed:34201318};
OS   Centruroides margaritatus (Central American bark Scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=29018 {ECO:0000303|PubMed:34201318};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, NOMENCLATURE, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   STRAIN=Patia Valley {ECO:0000303|PubMed:34201318};
RC   TISSUE=Venom {ECO:0000303|PubMed:34201318};
RX   PubMed=34201318; DOI=10.3390/toxins13060407;
RA   Beltran-Vidal J., Carcamo-Noriega E., Pastor N., Zamudio-Zuniga F.,
RA   Guerrero-Vargas J.A., Castano S., Possani L.D., Restano-Cassulini R.;
RT   "Colombian Scorpion Centruroides margaritatus: Purification and
RT   Characterization of a Gamma Potassium Toxin with Full-Block Activity on the
RT   hERG1 Channel.";
RL   Toxins 13:0-0(2021).
CC   -!- FUNCTION: Blocks human Kv11.1/KCNH2/ERG1 potassium channels
CC       (reversible, IC(50)=3.4 nM) (PubMed:34201318). At high toxin
CC       concentrations, block of Kv11.1/KCNH2/ERG1 macroscopic current is
CC       almost complete (PubMed:34201318). Does not accelerate the kinetics of
CC       the closing process and has no effect on the activation and
CC       inactivation kinetics of the Kv11.1/KCNH2/ERG1 channels
CC       (PubMed:34201318). {ECO:0000269|PubMed:34201318}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34201318}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:34201318}.
CC   -!- DOMAIN: Has the CSalpha/beta fold, which comprises one or two short
CC       alpha helices connected to anti-parallel beta-sheets stabilized by
CC       three or four disulfide bonds. {ECO:0000250|UniProtKB:Q86QT3}.
CC   -!- MASS SPECTROMETRY: Mass=4792.88; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:34201318};
CC   -!- SIMILARITY: Belongs to the ergtoxin family. Gamma-KTx 1 subfamily.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0140628; F:outward rectifier potassium channel inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0044562; P:envenomation resulting in negative regulation of voltage-gated potassium channel activity in another organism; IDA:UniProtKB.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR012622; Ergtoxin.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   Pfam; PF08086; Toxin_17; 1.
DR   SUPFAM; SSF57095; SSF57095; 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..42
FT                   /note="Potassium channel toxin gamma-KTx 1.10"
FT                   /id="PRO_0000454472"
FT   DISULFID        5..23
FT                   /evidence="ECO:0000250|UniProtKB:Q86QT3"
FT   DISULFID        11..34
FT                   /evidence="ECO:0000250|UniProtKB:Q86QT3"
FT   DISULFID        20..39
FT                   /evidence="ECO:0000250|UniProtKB:Q86QT3"
FT   DISULFID        24..41
FT                   /evidence="ECO:0000250|UniProtKB:Q86QT3"
SQ   SEQUENCE   42 AA;  4802 MW;  F91B04FB4847AD7F CRC64;
     DRDSCVDKSR CAKYGYFQEC TDCCKKYGHN GGTCMFFKCK CA