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Potassium channel toxin gamma-KTx 1.1 (Ergtoxin) (CnErg1) (CnErgTx1) (ErgTx) (ErgTx1)

 KGX11_CENNO             Reviewed;          62 AA.
Q86QT3; Q9GQ92;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
22-NOV-2017, entry version 72.
RecName: Full=Potassium channel toxin gamma-KTx 1.1 {ECO:0000303|PubMed:12459475};
AltName: Full=Ergtoxin {ECO:0000303|PubMed:10224238};
Short=CnErg1 {ECO:0000303|PubMed:12459475};
Short=CnErgTx1 {ECO:0000303|PubMed:12459475};
Short=ErgTx {ECO:0000303|PubMed:10224238};
Short=ErgTx1 {ECO:0000303|PubMed:12459475};
Flags: Precursor;
Centruroides noxius (Mexican scorpion).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
NCBI_TaxID=6878;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-62, AND
NOMENCLATURE.
TISSUE=Venom gland;
PubMed=12459475; DOI=10.1016/S0014-5793(02)03652-9;
Corona M., Gurrola G.B., Merino E., Cassulini R.R., Valdez-Cruz N.A.,
Garcia B., Ramirez-Dominguez M.E., Coronas F.I., Zamudio F.Z.,
Wanke E., Possani L.D.;
"A large number of novel Ergtoxin-like genes and ERG K+-channels
blocking peptides from scorpions of the genus Centruroides.";
FEBS Lett. 532:121-126(2002).
[2]
PROTEIN SEQUENCE OF 21-62, FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Venom;
PubMed=10224238;
Gurrola G.B., Rosati B., Rocchetti M., Pimienta G., Zaza A.,
Arcangeli A., Olivotto M., Possani L.D., Wanke E.;
"A toxin to nervous, cardiac, and endocrine ERG K+ channels isolated
from Centruroides noxius scorpion venom.";
FASEB J. 13:953-962(1999).
[3]
SEQUENCE REVISION TO 54 AND 61-62, AND MASS SPECTROMETRY.
PubMed=11023354; DOI=10.1016/S0014-5793(00)01891-3;
Scaloni A., Bottiglieri C., Ferrara L., Corona M., Gurrola G.B.,
Batista C.V.F., Wanke E., Possani L.D.;
"Disulfide bridges of ergtoxin, a member of a new sub-family of
peptide blockers of the ether-a-go-go-related K+ channel.";
FEBS Lett. 479:156-157(2000).
[4]
ERRATUM.
Scaloni A., Bottiglieri C., Ferrara L., Corona M., Gurrola G.B.,
Batista C.V.F., Wanke E., Possani L.D.;
FEBS Lett. 481:308-308(2000).
[5]
FUNCTION.
PubMed=11755529; DOI=10.1016/S0014-5793(01)03218-5;
Pardo-Lopez L., Garcia-Valdes J., Gurrola G.B., Robertson G.A.,
Possani L.D.;
"Mapping the receptor site for ergtoxin, a specific blocker of ERG
channels.";
FEBS Lett. 510:45-49(2002).
[6]
FUNCTION.
PubMed=11864985; DOI=10.1074/jbc.M200460200;
Pardo-Lopez L., Zhang M., Liu J., Jiang M., Possani L.D., Tseng G.N.;
"Mapping the binding site of a human ether-a-go-go-related gene-
specific peptide toxin (ErgTx) to the channel's outer vestibule.";
J. Biol. Chem. 277:16403-16411(2002).
[7]
FUNCTION.
PubMed=12860380; DOI=10.1016/S0014-5793(03)00662-8;
Milnes J.T., Dempsey C.E., Ridley J.M., Crociani O., Arcangeli A.,
Hancox J.C., Witchel H.J.;
"Preferential closed channel blockade of HERG potassium currents by
chemically synthesised BeKm-1 scorpion toxin.";
FEBS Lett. 547:20-26(2003).
[8]
FUNCTION.
PubMed=16497878; DOI=10.1124/mol.105.019729;
Restano-Cassulini R., Korolkova Y.V., Diochot S., Gurrola G.,
Guasti L., Possani L.D., Lazdunski M., Grishin E.V., Arcangeli A.,
Wanke E.;
"Species diversity and peptide toxins blocking selectivity of ether-a-
go-go-related gene subfamily K+ channels in the central nervous
system.";
Mol. Pharmacol. 69:1673-1683(2006).
[9]
FUNCTION, AND SYNTHESIS OF 21-62.
PubMed=17369411; DOI=10.1529/biophysj.106.101956;
Hill A.P., Sunde M., Campbell T.J., Vandenberg J.I.;
"Mechanism of block of the hERG K+ channel by the scorpion toxin
CnErg1.";
Biophys. J. 92:3915-3929(2007).
[10]
MUTAGENESIS OF MET-55, AND FUNCTION.
TISSUE=Venom;
PubMed=20600425; DOI=10.1016/j.peptides.2010.06.018;
Jimenez-Vargas J.M., Restano-Cassulini R., Quintero-Hernandez V.,
Gurrola G.B., Possani L.D.;
"Recombinant expression of the toxic peptide ErgTx1 and role of Met35
on its stability and function.";
Peptides 32:560-567(2011).
[11]
MUTAGENESIS OF GLN-38 AND ALA-62.
PubMed=23103547; DOI=10.1016/j.bbrc.2012.10.065;
Wang X., Jimenez-Vargas J.M., Xu C., Possani L.D., Zhu S.;
"Positive selection-guided mutational analysis revealing two key
functional sites of scorpion ERG K(+) channel toxins.";
Biochem. Biophys. Res. Commun. 429:111-116(2012).
[12]
STRUCTURE BY NMR OF 21-62, DISULFIDE BONDS, BINDING SITE LYS33, AND
SYNTHESIS OF 21-62.
PubMed=12650941; DOI=10.1016/S0014-5793(03)00216-3;
Torres A.M., Bansal P., Alewood P.F., Bursill J.A., Kuchel P.W.,
Vandenberg J.I.;
"Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion
toxin.";
FEBS Lett. 539:138-142(2003).
[13]
STRUCTURE BY NMR OF 21-62, AND DISULFIDE BONDS.
PubMed=15211519; DOI=10.1002/prot.20102;
Frenal K., Xu C.Q., Wolff N., Wecker K., Gurrola G.B., Zhu S.-Y.,
Chi C.W., Possani L.D., Tytgat J., Delepierre M.;
"Exploring structural features of the interaction between the scorpion
toxinCnErg1 and ERG K+ channels.";
Proteins 56:367-375(2004).
-!- FUNCTION: Blocks human and rat Kv11.1/KCNH2/ERG1 and
Kv11.3/KCNH7/ERG3, as well as rat (but not human)
Kv11.2/KCNH6/ERG2 (PubMed:11755529, PubMed:11864985,
PubMed:16497878, PubMed:17369411, PubMed:20600425) by binding to
channel outer vestibule (S5P domain) with a 1:1 stoichiometry
(PubMed:11755529, PubMed:11864985, PubMed:17369411,
PubMed:20600425). Inhibition data are the following: hERG1
(reversible, IC(50)~7 nM) (PubMed:11755529, PubMed:11864985,
PubMed:16497878, PubMed:17369411, PubMed:20600425), rERG1
(reversible, Kd=6.8 nM) (PubMed:16497878), rERG2 (irreversible,
Kd=2.8 nM) (PubMed:16497878), hERG3 (irreversible, Kd=4.05 nM)
(PubMed:16497878) and rERG3 (reversible, Kd=38.1 nM)
(PubMed:16497878) potassium channels. The toxin potency is not
affected by elevating potassium ion concentration from 2 to 98 mM
(PubMed:11864985). This toxin only blocks channels in a closed
state (PubMed:12860380). At high toxin concentrations, block of
Kv11.1/KCNH2/ERG1 macroscopic current is incomplete (93.5%). This
suggests a kinetic mechanism model with two different states of
toxin-channel binding (T+C=TC*=TC; in the TC* state, the toxin
binds the channel but does not occlude the pore, whereas in the TC
state the toxin binds and occludes the pore). In this model,
incomplete block is explained by the relatively fast dissociation
rate from the blocked channel conformation (TC) relative to the
rate of conversion of the toxin-channel encounter complex (TC*) to
the blocked channel conformation (TC) (PubMed:17369411).
{ECO:0000269|PubMed:10224238, ECO:0000269|PubMed:11755529,
ECO:0000269|PubMed:11864985, ECO:0000269|PubMed:12860380,
ECO:0000269|PubMed:16497878, ECO:0000269|PubMed:17369411,
ECO:0000269|PubMed:20600425}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10224238}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
-!- DOMAIN: The presence of a 'disulfide through disulfide knot'
structurally defines this protein as a knottin.
-!- DOMAIN: Has the CSalpha/beta fold, which comprises one or two
short alpha helices connected to anti-parallel beta-sheets
stabilized by three or four disulfide bonds.
{ECO:0000269|PubMed:12650941, ECO:0000269|PubMed:15211519}.
-!- PTM: After protein storage at -20 Celsius degrees during a couple
of months, the Met-55 of a small number of toxins is naturally
oxidized. This oxidized form is about three orders of magnitude
less efficient (IC(50)=15 uM) than non-oxidized form.
{ECO:0000269|PubMed:20600425}.
-!- MASS SPECTROMETRY: Mass=4730.8; Mass_error=0.4; Method=MALDI;
Range=21-62; Evidence={ECO:0000269|PubMed:11023354};
-!- MISCELLANEOUS: The affinity of the toxin for the channel decreases
as temperature increases (Kd=7.3 nM and Kd=64 nM at 22 and 37
degrees Celsius, respectively), likely due to changes in the
structure of the channel binding site.
{ECO:0000269|PubMed:17369411}.
-!- MISCELLANEOUS: Does not affect the function of either mouse
EAG/KCNH1 or ELK1 channels at concentration of 200 nM
(PubMed:11755529). Does not inhibit hKv1.4/KCNA4, hKv4.3/KCND3,
hKv2.1/KCNB1 and rKv7.1/KCNQ1 potassium channels at concentration
of 50 nM (PubMed:11864985). Does not inhibit human
Kv11.2/KCNH6/ERG2 (PubMed:16497878). {ECO:0000269|PubMed:11755529,
ECO:0000269|PubMed:11864985, ECO:0000269|PubMed:16497878}.
-!- SIMILARITY: Belongs to the ergtoxin family. Gamma-KTx 1 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY164271; AAO22234.1; -; mRNA.
EMBL; AF288205; AAG38523.1; -; mRNA.
PDB; 1NE5; NMR; -; A=21-62.
PDB; 1PX9; NMR; -; A=21-62.
PDBsum; 1NE5; -.
PDBsum; 1PX9; -.
ProteinModelPortal; Q86QT3; -.
SMR; Q86QT3; -.
EvolutionaryTrace; Q86QT3; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0019870; F:potassium channel inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
Gene3D; 3.30.30.10; -; 1.
InterPro; IPR012622; Ergtoxin.
InterPro; IPR036574; Scorpion_toxin-like_sf.
Pfam; PF08086; Toxin_17; 1.
ProDom; PD736966; Ergtoxin; 1.
SUPFAM; SSF57095; SSF57095; 1.
PROSITE; PS60026; ERGTX; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Knottin; Neurotoxin;
Potassium channel impairing toxin; Secreted; Signal; Toxin;
Voltage-gated potassium channel impairing toxin.
SIGNAL 1 20 {ECO:0000269|PubMed:10224238}.
CHAIN 21 62 Potassium channel toxin gamma-KTx 1.1.
/FTId=PRO_0000035362.
SITE 33 33 May represent the binding site.
{ECO:0000305|PubMed:12650941}.
SITE 55 55 Key residue on the interacting surface
with the channel.
{ECO:0000305|PubMed:20600425}.
DISULFID 25 43 {ECO:0000269|PubMed:12650941,
ECO:0000269|PubMed:15211519}.
DISULFID 31 54 {ECO:0000269|PubMed:12650941,
ECO:0000269|PubMed:15211519}.
DISULFID 40 59 {ECO:0000269|PubMed:12650941,
ECO:0000269|PubMed:15211519}.
DISULFID 44 61 {ECO:0000269|PubMed:12650941,
ECO:0000269|PubMed:15211519}.
MUTAGEN 38 38 Q->A: 6-fold reduction in affinity for
Kv11.1/KCNH2/ERG1 potassium channel
(Kd=72.9 nM).
{ECO:0000269|PubMed:23103547}.
MUTAGEN 55 55 M->A: 30-fold reduction in affinity for
Kv11.1/KCNH2/ERG1 potassium channel
(Kd=303.4 nM).
{ECO:0000269|PubMed:20600425}.
MUTAGEN 62 62 A->T: No change in affinity for
Kv11.1/KCNH2/ERG1 potassium channel
(Kd=14.2 nM).
{ECO:0000269|PubMed:23103547}.
HELIX 25 27 {ECO:0000244|PDB:1NE5}.
STRAND 33 35 {ECO:0000244|PDB:1NE5}.
HELIX 38 47 {ECO:0000244|PDB:1NE5}.
STRAND 48 50 {ECO:0000244|PDB:1NE5}.
STRAND 52 57 {ECO:0000244|PDB:1NE5}.
STRAND 59 61 {ECO:0000244|PDB:1NE5}.
SEQUENCE 62 AA; 6970 MW; 53F88F4B9F187E37 CRC64;
MKVLILIMII ASLMIMGVEM DRDSCVDKSR CAKYGYYQEC QDCCKNAGHN GGTCMFFKCK
CA


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