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Beta/omega-theraphotoxin-Tp2a (Beta/omega-TRTX-Tp2a) (ProTx-II) (PT-II) (Protoxin-2) (ProTx-2) (ProTx2)

 TXPR2_THRPR             Reviewed;          30 AA.
P83476;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
15-NOV-2002, sequence version 1.
20-JUN-2018, entry version 63.
RecName: Full=Beta/omega-theraphotoxin-Tp2a {ECO:0000305};
Short=Beta/omega-TRTX-Tp2a {ECO:0000305};
AltName: Full=ProTx-II {ECO:0000303|PubMed:12475222, ECO:0000303|PubMed:15632158};
Short=PT-II {ECO:0000303|PubMed:15632158};
AltName: Full=Protoxin-2 {ECO:0000305};
Short=ProTx-2 {ECO:0000305};
Short=ProTx2 {ECO:0000305};
Thrixopelma pruriens (Peruvian green velvet tarantula).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
Araneae; Mygalomorphae; Theraphosidae; Thrixopelma.
NCBI_TaxID=213387;
[1]
PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, SUBCELLULAR LOCATION, MASS
SPECTROMETRY, AND DISULFIDE BONDS.
TISSUE=Venom;
PubMed=12475222; DOI=10.1021/bi026546a;
Middleton R.E., Warren V.A., Kraus R.L., Hwang J.C., Liu C.J., Dai G.,
Brochu R.M., Kohler M.G., Gao Y.-D., Garsky V.M., Bogusky M.J.,
Mehl J.T., Cohen C.J., Smith M.M.;
"Two tarantula peptides inhibit activation of multiple sodium
channels.";
Biochemistry 41:14734-14747(2002).
[2]
FUNCTION.
PubMed=15632158; DOI=10.1074/jbc.M412552200;
Smith J.J., Alphy S., Seibert A.L., Blumenthal K.M.;
"Differential phospholipid binding by site 3 and site 4 toxins.
Implications for structural variability between voltage-sensitive
sodium channel domains.";
J. Biol. Chem. 280:11127-11133(2005).
[3]
FUNCTION.
PubMed=17339321; DOI=10.1074/jbc.M610462200;
Smith J.J., Cummins T.R., Alphy S., Blumenthal K.M.;
"Molecular interactions of the gating modifier toxin ProTx-II with NaV
1.5: implied existence of a novel toxin binding site coupled to
activation.";
J. Biol. Chem. 282:12687-12697(2007).
[4]
FUNCTION, SYNTHESIS, AND MUTAGENESIS OF TYR-1; GLN-3; TRP-5; MET-6;
TRP-7; THR-8; ASP-10; SER-11; GLU-12; LEU-23 AND TRP-24.
PubMed=17087985; DOI=10.1016/j.toxicon.2006.09.014;
Priest B.T., Blumenthal K.M., Smith J.J., Warren V.A., Smith M.M.;
"ProTx-I and ProTx-II: gating modifiers of voltage-gated sodium
channels.";
Toxicon 49:194-201(2007).
[5]
FUNCTION.
PubMed=18156314; DOI=10.1124/mol.107.041046;
Sokolov S., Kraus R.L., Scheuer T., Catterall W.A.;
"Inhibition of sodium channel gating by trapping the domain II voltage
sensor with protoxin II.";
Mol. Pharmacol. 73:1020-1028(2008).
[6]
FUNCTION.
PubMed=18728100; DOI=10.1124/mol.108.047670;
Schmalhofer W.A., Calhoun J., Burrows R., Bailey T., Kohler M.G.,
Weinglass A.B., Kaczorowski G.J., Garcia M.L., Koltzenburg M.,
Priest B.T.;
"ProTx-II, a selective inhibitor of NaV1.7 sodium channels, blocks
action potential propagation in nociceptors.";
Mol. Pharmacol. 74:1476-1484(2008).
[7]
FUNCTION.
PubMed=18657562; DOI=10.1016/j.toxicon.2008.06.023;
Edgerton G.B., Blumenthal K.M., Hanck D.A.;
"Evidence for multiple effects of ProTxII on activation gating in
Na(V)1.5.";
Toxicon 52:489-500(2008).
[8]
FUNCTION.
PubMed=20855463; DOI=10.1124/mol.110.066332;
Xiao Y., Blumenthal K., Jackson J.O. II, Liang S., Cummins T.R.;
"The tarantula toxins ProTx-II and huwentoxin-IV differentially
interact with human Nav1.7 voltage sensors to inhibit channel
activation and inactivation.";
Mol. Pharmacol. 78:1124-1134(2010).
[9]
FUNCTION.
PubMed=24886690; DOI=10.1186/1756-6606-7-36;
Bladen C., Hamid J., Souza I.A., Zamponi G.W.;
"Block of T-type calcium channels by protoxins I and II.";
Mol. Brain 7:36-36(2014).
[10]
DOMAIN.
PubMed=26843868; DOI=10.1155/2015/537508;
Kikuchi K., Sugiura M., Kimura T.;
"High proteolytic resistance of spider-derived inhibitor cystine
knots.";
Int. J. Pept. 2015:537508-537508(2015).
[11]
FUNCTION.
PubMed=25658507; DOI=10.1021/jm501765v;
Murray J.K., Ligutti J., Liu D., Zou A., Poppe L., Li H.,
Andrews K.L., Moyer B.D., McDonough S.I., Favreau P., Stoecklin R.,
Miranda L.P.;
"Engineering potent and selective analogues of GpTx-1, a tarantula
venom peptide antagonist of the Na(V)1.7 sodium channel.";
J. Med. Chem. 58:2299-2314(2015).
[12]
PHARMACEUTICAL, AND MUTAGENESIS OF TYR-1; TRP-7 AND TRP-30.
PubMed=28045073; DOI=10.1038/srep39662;
Flinspach M., Xu Q., Piekarz A.D., Fellows R., Hagan R., Gibbs A.,
Liu Y., Neff R.A., Freedman J., Eckert W.A., Zhou M., Bonesteel R.,
Pennington M.W., Eddinger K.A., Yaksh T.L., Hunter M., Swanson R.V.,
Wickenden A.D.;
"Insensitivity to pain induced by a potent selective closed-state
Nav1.7 inhibitor.";
Sci. Rep. 7:39662-39662(2017).
[13]
STRUCTURE BY NMR, DISULFIDE BOND, SYNTHESIS, AND MUTAGENESIS OF LYS-4;
TRP-5; TRP-7; LYS-14; GLU-17; TRP-24; LYS-26; LYS-27; LYS-28 AND
TRP-30.
PubMed=27311819; DOI=10.1074/jbc.M116.729095;
Henriques S.T., Deplazes E., Lawrence N., Cheneval O., Chaousis S.,
Inserra M., Thongyoo P., King G.F., Mark A.E., Vetter I., Craik D.J.,
Schroeder C.I.;
"Interaction of tarantula venom peptide ProTx-II with lipid membranes
is a prerequisite for its inhibition of human voltage-gated sodium
channel Nav1.7.";
J. Biol. Chem. 291:17049-17065(2016).
-!- FUNCTION: Gating-modifier toxin that targets voltage-gated sodium
channels with a preferential activity on Nav1.7/SCN9A. It inhibits
both activation and inactivation (PubMed:20855463). For inhibition
of activation, it is 100-fold more selective for Nav1.7/SCN9A
(IC(50)=0.3-3) than for other sodium channels (Nav1.2/SCN2A
IC(50)=40-540 nM, Nav1.3/SCN3A IC(50)=102 nM, Nav1.4/SCN4A
IC(50)=30-39 nM, Nav1.5/SCN5A IC(50)=19-90 nM, Nav1.6/SCN8A
IC(50)=26 nM, and Nav1.8/SCN10A IC(50)=146 nM) (PubMed:12475222,
PubMed:18156314, PubMed:18728100, PubMed:20855463,
PubMed:25658507, PubMed:27311819). For inhibition of inactivation,
it is 20-fold more potent in inhibiting inactivation on
Nav1.7/SCN9A (IC(50)=250 nM) than other channels (about 4.6 uM for
all channels) (PubMed:20855463). It also inhibits Cav1.2/CACNA1C
and Cav3.2/CACNA1H (29% block at 1 uM) (PubMed:17087985,
PubMed:24886690). It inhibits Nav1.7/SCN9A activation by
interacting with DII and impairs Nav1.7/SCN9A inactivation by
interacting with DIV (PubMed:20855463). This toxin binds to lipid
membrane (PubMed:15632158, PubMed:27311819). This ability
correlates with hNav1.7/SCN9A inhibition, showing that membrane
binding is the first step in the inhibitory mechanism of this
toxin (PubMed:27311819). {ECO:0000269|PubMed:12475222,
ECO:0000269|PubMed:15632158, ECO:0000269|PubMed:17087985,
ECO:0000269|PubMed:17339321, ECO:0000269|PubMed:18156314,
ECO:0000269|PubMed:18657562, ECO:0000269|PubMed:18728100,
ECO:0000269|PubMed:20855463, ECO:0000269|PubMed:24886690,
ECO:0000269|PubMed:25658507, ECO:0000269|PubMed:27311819}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12475222}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000305|PubMed:12475222}.
-!- DOMAIN: The presence of a 'disulfide through disulfide knot'
structurally defines this protein as a knottin.
{ECO:0000269|PubMed:27311819}.
-!- MASS SPECTROMETRY: Mass=3827; Method=Electrospray; Range=1-30;
Evidence={ECO:0000269|PubMed:12475222};
-!- MASS SPECTROMETRY: Mass=3827; Method=MALDI; Range=1-30;
Evidence={ECO:0000269|PubMed:12475222};
-!- PHARMACEUTICAL: The derivative JNJ63955918 (Y1GPY; W7Q; W30L) is
under preclinical trial by Janssen Pharmaceutica as a non-opioid
alternative for the pharmacological treatment of severe pain.
{ECO:0000269|PubMed:28045073}.
-!- MISCELLANEOUS: Highly resistant to proteases, such as pepsin,
trypsin, chymotrypsin and elastase. The toxin is not degraded in
the plasma and shows fast clearance from the circulation.
{ECO:0000269|PubMed:26843868}.
-!- MISCELLANEOUS: Does not inhibit Kv1.2/KCNA2, Kv1.3/KCNA3,
Kv1.5/KCNA5, and Kv2.1/KCNB1 channels (PubMed:12475222). Does not
inhibit or only very weakly Cav3.1/CACNA1G and Cav3.3/CACNA1I
(PubMed:26843868). {ECO:0000269|PubMed:12475222,
ECO:0000269|PubMed:26843868}.
-!- SIMILARITY: Belongs to the neurotoxin 30 (phrixotoxin) family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
Note=JNJ63955918;
URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=30181";
-----------------------------------------------------------------------
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PDB; 2N9T; NMR; -; A=1-30.
PDB; 5O0U; X-ray; 0.99 A; A=1-30.
PDB; 5TCZ; NMR; -; A=1-29.
PDBsum; 2N9T; -.
PDBsum; 5O0U; -.
PDBsum; 5TCZ; -.
ProteinModelPortal; P83476; -.
SMR; P83476; -.
TCDB; 8.B.5.2.1; the na(+)/k(+)/ca(2+) channel targeting tarantula huwentoxin (tht) family.
ArachnoServer; AS000414; beta/omega-theraphotoxin-Tp2a.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
1: Evidence at protein level;
3D-structure; Calcium channel impairing toxin;
Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Knottin; Lipid-binding; Neurotoxin;
Pharmaceutical; Secreted; Toxin;
Voltage-gated calcium channel impairing toxin;
Voltage-gated sodium channel impairing toxin.
PEPTIDE 1 30 Beta/omega-theraphotoxin-Tp2a.
/FTId=PRO_0000044556.
DISULFID 2 16 {ECO:0000269|PubMed:12475222,
ECO:0000269|PubMed:27311819,
ECO:0000312|PDB:2N9T,
ECO:0000312|PDB:5O0U,
ECO:0000312|PDB:5TCZ}.
DISULFID 9 21 {ECO:0000269|PubMed:12475222,
ECO:0000269|PubMed:27311819,
ECO:0000312|PDB:2N9T,
ECO:0000312|PDB:5O0U,
ECO:0000312|PDB:5TCZ}.
DISULFID 15 25 {ECO:0000269|PubMed:12475222,
ECO:0000269|PubMed:27311819,
ECO:0000312|PDB:2N9T,
ECO:0000312|PDB:5O0U,
ECO:0000312|PDB:5TCZ}.
MUTAGEN 1 1 Y->A: No change in binding affinity.
{ECO:0000269|PubMed:17087985}.
MUTAGEN 1 1 Y->GPY: Important increase in selectivity
for Nav1.7/SCN9A; derivative JNJ63955918.
{ECO:0000269|PubMed:28045073}.
MUTAGEN 3 3 Q->A: No change in binding affinity.
{ECO:0000269|PubMed:17087985}.
MUTAGEN 4 4 K->R: In K/R, 30-fold decrease in ability
to inhibit Nav1.7/SCN9A, and change of
ability to bind membranes. In K/R,E17K,
110-fold decrease in ability to inhibit
Nav1.7/SCN9A, and change of ability to
bind membranes.
{ECO:0000269|PubMed:27311819}.
MUTAGEN 5 5 W->A: At least 10-fold decrease in
affinity with Nav1.5 sodium channel.
{ECO:0000269|PubMed:17087985}.
MUTAGEN 5 5 W->Y: 290-fold decrease in ability to
inhibit Nav1.7/SCN9A, and decrease of
ability to bind membranes.
{ECO:0000269|PubMed:27311819}.
MUTAGEN 6 6 M->A: At least 10-fold decrease in
affinity with Nav1.5 sodium channel.
{ECO:0000269|PubMed:17087985}.
MUTAGEN 7 7 W->A: At least 10-fold decrease in
affinity with Nav1.5 sodium channel.
{ECO:0000269|PubMed:17087985}.
MUTAGEN 7 7 W->Q: Important increase in selectivity
for Nav1.7/SCN9A; derivative JNJ63955918.
{ECO:0000269|PubMed:28045073}.
MUTAGEN 7 7 W->Y: 111-fold decrease in ability to
inhibit Nav1.7/SCN9A, and decrease of
ability to bind membranes.
{ECO:0000269|PubMed:27311819}.
MUTAGEN 8 8 T->A: No change in binding affinity.
{ECO:0000269|PubMed:17087985}.
MUTAGEN 10 10 D->A: No change in binding affinity.
{ECO:0000269|PubMed:17087985}.
MUTAGEN 11 11 S->A: No change in binding affinity.
{ECO:0000269|PubMed:17087985}.
MUTAGEN 12 12 E->A: No change in binding affinity.
{ECO:0000269|PubMed:17087985}.
MUTAGEN 14 14 K->R: In K/R, 30-fold decrease in ability
to inhibit Nav1.7/SCN9A, and change of
ability to bind membranes. In K/R,E17K,
110-fold decrease in ability to inhibit
Nav1.7/SCN9A, and change of ability to
bind membranes.
{ECO:0000269|PubMed:27311819}.
MUTAGEN 17 17 E->K: No change in ability to inhibit
Nav1.7/SCN9A, and change of ability to
bind membranes. In K/R,E17K, 110-fold
decrease in ability to inhibit
Nav1.7/SCN9A, and change of ability to
bind membranes.
{ECO:0000269|PubMed:27311819}.
MUTAGEN 23 23 L->A: No change in binding affinity.
{ECO:0000269|PubMed:17087985}.
MUTAGEN 24 24 W->A: At least 10-fold decrease in
affinity with Nav1.5 sodium channel.
{ECO:0000269|PubMed:17087985}.
MUTAGEN 24 24 W->Y: 180-fold decrease in ability to
inhibit Nav1.7/SCN9A, and decrease of
ability to bind membranes.
{ECO:0000269|PubMed:27311819}.
MUTAGEN 26 26 K->R: In K/R, 30-fold decrease in ability
to inhibit Nav1.7/SCN9A, and change of
ability to bind membranes. In K/R,E17K,
110-fold decrease in ability to inhibit
Nav1.7/SCN9A, and change of ability to
bind membranes.
{ECO:0000269|PubMed:27311819}.
MUTAGEN 27 27 K->R: In K/R, 30-fold decrease in ability
to inhibit Nav1.7/SCN9A, and change of
ability to bind membranes. In K/R,E17K,
110-fold decrease in ability to inhibit
Nav1.7/SCN9A, and change of ability to
bind membranes.
{ECO:0000269|PubMed:27311819}.
MUTAGEN 28 28 K->R: In K/R, 30-fold decrease in ability
to inhibit Nav1.7/SCN9A, and change of
ability to bind membranes. In K/R,E17K,
110-fold decrease in ability to inhibit
Nav1.7/SCN9A, and change of ability to
bind membranes.
{ECO:0000269|PubMed:27311819}.
MUTAGEN 30 30 W->L: Important increase in selectivity
for Nav1.7/SCN9A; derivative JNJ63955918.
{ECO:0000269|PubMed:28045073}.
MUTAGEN 30 30 W->Y: 6-fold decrease in ability to
inhibit Nav1.7/SCN9A, and decrease of
ability to bind membranes.
{ECO:0000269|PubMed:27311819}.
STRAND 5 7 {ECO:0000244|PDB:2N9T}.
STRAND 11 13 {ECO:0000244|PDB:5O0U}.
TURN 16 18 {ECO:0000244|PDB:2N9T}.
STRAND 19 27 {ECO:0000244|PDB:5O0U}.
SEQUENCE 30 AA; 3833 MW; 5B8CF4C6338C1B9B CRC64;
YCQKWMWTCD SERKCCEGMV CRLWCKKKLW


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