ID   KGX19_CENTE             Reviewed;          42 AA.
AC   C0HJW3;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Potassium channel gamma toxin gamma-KTx 1.9 {ECO:0000303|PubMed:26921461};
DE   AltName: Full=Toxin II.10.9 {ECO:0000303|PubMed:26921461};
OS   Centruroides tecomanus (Scorpion) (Centruroides limpidus tecomanus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=1028682;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=26921461; DOI=10.1016/j.toxicon.2016.02.017;
RA   Olamendi-Portugal T., Bartok A., Zamudio-Zuniga F., Balajthy A.,
RA   Becerril B., Panyi G., Possani L.D.;
RT   "Isolation, chemical and functional characterization of several new K(+)-
RT   channel blocking peptides from the venom of the scorpion Centruroides
RT   tecomanus.";
RL   Toxicon 115:1-12(2016).
CC   -!- FUNCTION: Blocks human voltage-gated potassium channel
CC       Kv11.1/KCNH2/ERG1 (IC(50)=16.9 nM). {ECO:0000269|PubMed:26921461}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26921461}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:26921461}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=4874.0; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:26921461};
CC   -!- MISCELLANEOUS: Has no effect on voltage-gated potassium channels
CC       Kv1.1/KCNA1, Kv1.2/KCNA2, Kv1.3/KCNA3, Kv10.1/KCNH1/EAG1 and Shaker IR
CC       (with inactivation domain removed) and on intermediate conductance
CC       calcium-activated potassium channel KCa3.1/KCNN4.
CC       {ECO:0000269|PubMed:26921461}.
CC   -!- SIMILARITY: Belongs to the ergtoxin family. Gamma-KTx 1 subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; C0HJW3; -.
DR   SMR; C0HJW3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019870; F:potassium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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   Knottin; Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..42
FT                   /note="Potassium channel gamma toxin gamma-KTx 1.9"
FT                   /evidence="ECO:0000269|PubMed:26921461"
FT                   /id="PRO_0000436541"
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;  4882 MW;  9BE5F5045AF93360 CRC64;
     DRDSCIDKSR CSKYGYYQEC QDCCKKAGHN RGTCMFFKCK CA