ID   KGX17_CENEL             Reviewed;          42 AA.
AC   P0C892;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Potassium channel toxin gamma-KTx 1.7 {ECO:0000303|PubMed:18338253};
DE   AltName: Full=CeErgTx4 {ECO:0000305};
DE            Short=CeErg4 {ECO:0000303|PubMed:18338253};
OS   Centruroides elegans (Bark scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=217897;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   NOMENCLATURE.
RC   TISSUE=Venom;
RX   PubMed=18338253; DOI=10.1007/s11064-008-9634-8;
RA   Restano-Cassulini R., Olamendi-Portugal T., Zamudio F., Becerril B.,
RA   Possani L.D.;
RT   "Two novel ergtoxins, blockers of K(+)-channels, purified from the Mexican
RT   scorpion Centruroides elegans elegans.";
RL   Neurochem. Res. 33:1525-1533(2008).
CC   -!- FUNCTION: Blocks in a reversible manner human and rat Kv11.1/KCNH2/ERG1
CC       potassium channels. Also completely and irreversibly blocks rat
CC       Kv11.2/KCNH6/ERG2 and human Kv11.3/KCNH7/ERG3 channels.
CC       {ECO:0000269|PubMed:18338253}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18338253}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
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=4761.3; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:18338253};
CC   -!- MISCELLANEOUS: Does not affect human Kv11.2/KCNH6/ERG2.
CC       {ECO:0000269|PubMed:18338253}.
CC   -!- SIMILARITY: Belongs to the ergtoxin family. Gamma-KTx 1 subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0C892; -.
DR   SMR; P0C892; -.
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.
DR   PROSITE; PS60026; ERGTX; 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   CHAIN           1..42
FT                   /note="Potassium channel toxin gamma-KTx 1.7"
FT                   /evidence="ECO:0000269|PubMed:18338253"
FT                   /id="PRO_0000352490"
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;  4768 MW;  9BE5F514484108F0 CRC64;
     DRDSCVDKSR CSKYGYYQEC QDCCKKAGHN GGTCMFFKCK CA