ID   KGX41_CENLI             Reviewed;          43 AA.
AC   Q86QU9;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Potassium channel toxin gamma-KTx 4.1 {ECO:0000303|PubMed:12459475};
DE   AltName: Full=CllErgTx2 {ECO:0000305};
DE            Short=CllErg2 {ECO:0000303|PubMed:12459475};
DE            Short=ErgTx2 {ECO:0000303|PubMed:12459475};
DE   AltName: Full=Ergtoxin-like protein {ECO:0000303|PubMed:12459475};
OS   Centruroides limpidus (Mexican scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=6876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND
RP   NOMENCLATURE.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=12459475; DOI=10.1016/s0014-5793(02)03652-9;
RA   Corona M., Gurrola G.B., Merino E., Cassulini R.R., Valdez-Cruz N.A.,
RA   Garcia B., Ramirez-Dominguez M.E., Coronas F.I., Zamudio F.Z., Wanke E.,
RA   Possani L.D.;
RT   "A large number of novel Ergtoxin-like genes and ERG K+-channels blocking
RT   peptides from scorpions of the genus Centruroides.";
RL   FEBS Lett. 532:121-126(2002).
CC   -!- FUNCTION: Reversibly blocks Kv11/ERG potassium channels.
CC       {ECO:0000250|UniProtKB:P59940}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12459475}.
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   -!- SIMILARITY: Belongs to the ergtoxin family. Gamma-KTx 4 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY159344; AAO22222.1; -; mRNA.
DR   AlphaFoldDB; Q86QU9; -.
DR   SMR; Q86QU9; -.
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..43
FT                   /note="Potassium channel toxin gamma-KTx 4.1"
FT                   /evidence="ECO:0000269|PubMed:12459475"
FT                   /id="PRO_0000066851"
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   43 AA;  4840 MW;  D0651E1523CCE257 CRC64;
     DRDSCVDKSK CSKYGYYGQC DECCKKAGDR AGNCVYFKCK CNP