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Psalmotoxin-1 (PcTx1) (Pi-theraphotoxin-Pc1a) (Pi-TRTX-Pc1a)

 TXP1_PSACA              Reviewed;          40 AA.
P60514;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 1.
28-FEB-2018, entry version 69.
RecName: Full=Psalmotoxin-1 {ECO:0000303|PubMed:10829030, ECO:0000303|PubMed:12824480, ECO:0000303|PubMed:15955877, ECO:0000303|PubMed:16505147};
AltName: Full=PcTx1 {ECO:0000303|PubMed:10829030, ECO:0000303|PubMed:12824480};
AltName: Full=Pi-theraphotoxin-Pc1a {ECO:0000303|PubMed:21825095};
Short=Pi-TRTX-Pc1a {ECO:0000303|PubMed:21825095};
Psalmopoeus cambridgei (Trinidad chevron tarantula).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
Araneae; Mygalomorphae; Theraphosidae; Psalmopoeus.
NCBI_TaxID=179874;
[1]
PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, MASS SPECTROMETRY, AND
SUBCELLULAR LOCATION.
TISSUE=Venom;
PubMed=10829030; DOI=10.1074/jbc.M003643200;
Escoubas P., de Weille J.R., Lecoq A., Diochot S., Waldmann R.,
Champigny G., Moinier D., Menez A., Lazdunski M.;
"Isolation of a tarantula toxin specific for a class of proton-gated
Na+ channels.";
J. Biol. Chem. 275:25116-25121(2000).
[2]
FUNCTION.
PubMed=15955877; DOI=10.1085/jgp.200509303;
Chen X., Kalbacher H., Gruender S.;
"The tarantula toxin psalmotoxin 1 inhibits acid-sensing ion channel
(ASIC) 1a by increasing its apparent H+ affinity.";
J. Gen. Physiol. 126:71-79(2005).
[3]
FUNCTION.
PubMed=16505147; DOI=10.1085/jgp.200509409;
Chen X., Kalbacher H., Gruender S.;
"Interaction of acid-sensing ion channel (ASIC) 1 with the tarantula
toxin psalmotoxin 1 is state dependent.";
J. Gen. Physiol. 127:267-276(2006).
[4]
FUNCTION ON CHICKEN ASIC1.
PubMed=19185346; DOI=10.1016/j.ceca.2008.12.002;
Samways D.S., Harkins A.B., Egan T.M.;
"Native and recombinant ASIC1a receptors conduct negligible Ca2+
entry.";
Cell Calcium 45:319-325(2009).
[5]
FUNCTION.
PubMed=21036899; DOI=10.1074/jbc.M110.171330;
Hoagland E.N., Sherwood T.W., Lee K.G., Walker C.J., Askwith C.C.;
"Identification of a calcium permeable human acid-sensing ion channel
1 transcript variant.";
J. Biol. Chem. 285:41852-41862(2010).
[6]
FUNCTION.
PubMed=21715637; DOI=10.1523/JNEUROSCI.1665-11.2011;
Sherwood T.W., Lee K.G., Gormley M.G., Askwith C.C.;
"Heteromeric acid-sensing ion channels (ASICs) composed of ASIC2b and
ASIC1a display novel channel properties and contribute to acidosis-
induced neuronal death.";
J. Neurosci. 31:9723-9734(2011).
[7]
FUNCTION.
PubMed=24262969; DOI=10.4161/chan.26978;
Smith R.N., Gonzales E.B.;
"Protons and Psalmotoxin-1 reveal nonproton ligand stimulatory sites
in chicken acid-sensing ion channel: Implication for simultaneous
modulation in ASICs.";
Channels 8:49-61(2014).
[8]
FUNCTION, MUTAGENESIS OF 1-GLU-ASP-2; LYS-6; TRP-7; LYS-8; ARG-28;
SER-29; PHE-30; GLU-31; VAL-32; VAL-34; PRO-35; LYS-36; THR-37; PRO-38
AND 38-PRO--THR-40, AND SITES TRP-7; ARG-28; PHE-30.
PubMed=26248594; DOI=10.1111/bph.13267;
Saez N.J., Deplazes E., Cristofori-Armstrong B., Chassagnon I.R.,
Lin X., Mobli M., Mark A.E., Rash L.D., King G.F.;
"Molecular dynamics and functional studies define a hot spot of
crystal contacts essential for psalmotoxin-1 inhibition of acid-
sensing ion channel 1a.";
Br. J. Pharmacol. 172:4985-4995(2015).
[9]
PHARMACEUTICAL.
PubMed=26320544; DOI=10.1016/j.neuropharm.2015.08.040;
McCarthy C.A., Rash L.D., Chassagnon I.R., King G.F., Widdop R.E.;
"PcTx1 affords neuroprotection in a conscious model of stroke in
hypertensive rats via selective inhibition of ASIC1a.";
Neuropharmacology 99:650-657(2015).
[10]
FUNCTION.
PubMed=27277303; DOI=10.1038/srep27647;
Joeres N., Augustinowski K., Neuhof A., Assmann M., Gruender S.;
"Functional and pharmacological characterization of two different
ASIC1a/2a heteromers reveals their sensitivity to the spider toxin
PcTx1.";
Sci. Rep. 6:27647-27659(2016).
[11]
FUNCTION.
TISSUE=Venom;
PubMed=28320941; DOI=10.1073/pnas.1614728114;
Chassagnon I.R., McCarthy C.A., Chin Y.K., Pineda S.S., Keramidas A.,
Mobli M., Pham V., De Silva T.M., Lynch J.W., Widdop R.E., Rash L.D.,
King G.F.;
"Potent neuroprotection after stroke afforded by a double-knot spider-
venom peptide that inhibits acid-sensing ion channel 1a.";
Proc. Natl. Acad. Sci. U.S.A. 114:3750-3755(2017).
[12]
REVIEW, AND PHARMACEUTICAL.
PubMed=28457973; DOI=10.1016/j.neuropharm.2017.04.042;
Cristofori-Armstrong B., Rash L.D.;
"Acid-sensing ion channel (ASIC) structure and function: insights from
spider, snake and sea anemone venoms.";
Neuropharmacology 127:173-184(2017).
[13]
STRUCTURE BY NMR, DISULFIDE BONDS, AND MASS SPECTROMETRY.
PubMed=12824480; DOI=10.1110/ps.0307003;
Escoubas P., Bernard C., Lambeau G., Lazdunski M., Darbon H.;
"Recombinant production and solution structure of PcTx1, the specific
peptide inhibitor of ASIC1a proton-gated cation channels.";
Protein Sci. 12:1332-1343(2003).
[14]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS, MUTAGENESIS OF
HIS-14; TRP-24; LYS-25; ARG-26 AND ARG-27, SITES TRP-24; ARG-26 AND
ARG-27, AND 3D-STRUCTURE MODELING OF THE TOXIN IN COMPLEX WITH RAT
ASIC1A.
PubMed=21825095; DOI=10.1124/mol.111.072207;
Saez N.J., Mobli M., Bieri M., Chassagnon I.R., Malde A.K.,
Gamsjaeger R., Mark A.E., Gooley P.R., Rash L.D., King G.F.;
"A dynamic pharmacophore drives the interaction between Psalmotoxin-1
and the putative drug target acid-sensing ion channel 1a.";
Mol. Pharmacol. 80:796-808(2011).
[15]
STRUCTURE BY NMR IN COMPLEX WITH CHICKEN ASIC1, AND DISULFIDE BOND.
PubMed=22842900; DOI=10.1038/nature11375;
Baconguis I., Gouaux E.;
"Structural plasticity and dynamic selectivity of acid-sensing ion
channel-spider toxin complexes.";
Nature 489:400-405(2012).
[16]
X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 2-38 IN COMPLEX WITH CHICKEN
ASIC1, AND DISULFIDE BOND.
PubMed=22760635; DOI=10.1038/ncomms1917;
Dawson R.J., Benz J., Stohler P., Tetaz T., Joseph C., Huber S.,
Schmid G., Hugin D., Pflimlin P., Trube G., Rudolph M.G., Hennig M.,
Ruf A.;
"Structure of the acid-sensing ion channel 1 in complex with the
gating modifier Psalmotoxin 1.";
Nat. Commun. 3:936-943(2012).
-!- FUNCTION: This toxin is a gating modifier that acts principally as
an inhibitor on ASIC1a (ASIC isoform 2) and a potentiator on
ASIC1b (ASIC isoform 3) (PubMed:10829030, PubMed:15955877,
PubMed:21036899). This toxin potently and selectively inhibits
rat, mouse and human ASIC1a (IC(50)=0.35-3.7 nM) (PubMed:10829030,
PubMed:15955877, PubMed:21715637, PubMed:26248594,
PubMed:21825095). The blockade is rapidly reversible
(PubMed:10829030, PubMed:28320941). The toxin acts by shifting its
steady-state desensitization to more alkaline pH (0.27 pH unit)
(PubMed:15955877, PubMed:16505147). At higher concentrations, it
potentiates rat and human ASIC1b and activates chicken ASIC1 by
stabilizing the open state of these subtypes (PubMed:16505147,
PubMed:21036899, PubMed:19185346, PubMed:24262969,
PubMed:22842900). The toxin binds most tightly to the open and the
desensitized states of ASIC1a (promoting desensitization), whereas
it binds most tightly to the open state of ASIC1b (promoting
opening) (PubMed:16505147). The toxin also inhibits mouse ASIC1a-
ASIC2b (IC(50)=2.64 nM) and rat ASIC1a-ASIC2a (PubMed:21715637,
PubMed:27277303). It binds to the extracellular domain at subunit
interfaces in the acidic pocket with the majority of contacts on
the thumb domain of the channel (PubMed:21825095, PubMed:22842900,
PubMed:22760635). It is also noteworthy that calcium competes with
the toxin, probably by inhibiting binding of the toxin to the
channel (PubMed:15955877). {ECO:0000269|PubMed:10829030,
ECO:0000269|PubMed:15955877, ECO:0000269|PubMed:16505147,
ECO:0000269|PubMed:19185346, ECO:0000269|PubMed:21036899,
ECO:0000269|PubMed:21715637, ECO:0000269|PubMed:21825095,
ECO:0000269|PubMed:22760635, ECO:0000269|PubMed:22842900,
ECO:0000269|PubMed:24262969, ECO:0000269|PubMed:26248594,
ECO:0000269|PubMed:27277303, ECO:0000269|PubMed:28320941}.
-!- INTERACTION:
Q1XA76:ASIC1 (xeno); NbExp=2; IntAct=EBI-16002043, EBI-15659618;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10829030}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000305|PubMed:10829030}.
-!- DOMAIN: The presence of a 'disulfide through disulfide knot'
structurally defines this protein as a knottin.
{ECO:0000269|PubMed:12824480, ECO:0000269|PubMed:21825095,
ECO:0000269|PubMed:22760635, ECO:0000269|PubMed:22842900}.
-!- MASS SPECTROMETRY: Mass=4689.25; Method=MALDI; Range=1-40;
Evidence={ECO:0000269|PubMed:10829030};
-!- MASS SPECTROMETRY: Mass=4690; Method=MALDI; Range=1-40;
Evidence={ECO:0000269|PubMed:12824480};
-!- PHARMACEUTICAL: This toxin has been shown to be neuroprotective in
both rodent and porcine models of cerebral ischemia when
administered 30 minutes prior to induction of stroke
(PubMed:28457973). In addition, a single dose of this toxin (1
ng/kg, i.c.v. 2 h post stroke) does indeed provide substantial
neuronal and functional protection in ischemic stroke in conscious
hypertensive rats (PubMed:26320544). {ECO:0000269|PubMed:26320544,
ECO:0000269|PubMed:28457973}.
-!- MISCELLANEOUS: This peptide is present at only 0.4% abundance in
P.cambridgei venom. {ECO:0000269|PubMed:26320544}.
-!- MISCELLANEOUS: Does not act on rat and mouse ASIC1a-ASIC2a
(PubMed:10829030, PubMed:21715637). Does not act on rat ASIC1a-
ASIC3 (PubMed:10829030). {ECO:0000269|PubMed:10829030,
ECO:0000269|PubMed:21715637}.
-!- SIMILARITY: Belongs to the psalmotoxin-1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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PDB; 1LMM; NMR; -; A=1-40.
PDB; 2KNI; NMR; -; A=1-40.
PDB; 3S3X; X-ray; 2.99 A; D/E/F=2-38.
PDB; 4FZ0; X-ray; 2.80 A; M/N/O=1-40.
PDB; 4FZ1; X-ray; 3.36 A; D=1-40.
PDBsum; 1LMM; -.
PDBsum; 2KNI; -.
PDBsum; 3S3X; -.
PDBsum; 4FZ0; -.
PDBsum; 4FZ1; -.
ProteinModelPortal; P60514; -.
SMR; P60514; -.
DIP; DIP-59909N; -.
IntAct; P60514; 1.
TCDB; 8.B.10.1.1; the psalmotoxin-1 (pctx1) family.
ArachnoServer; AS000400; pi-theraphotoxin-Pc1a.
EvolutionaryTrace; P60514; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Knottin; Pharmaceutical;
Proton-gated sodium channel impairing toxin; Secreted; Toxin.
PEPTIDE 1 40 Psalmotoxin-1.
{ECO:0000269|PubMed:10829030}.
/FTId=PRO_0000044965.
SITE 7 7 Key residue for interaction with ASIC1a.
{ECO:0000269|PubMed:22760635,
ECO:0000269|PubMed:22842900,
ECO:0000269|PubMed:26248594}.
SITE 24 24 Key residue for interaction with ASIC1a.
{ECO:0000269|PubMed:21825095,
ECO:0000269|PubMed:22760635,
ECO:0000269|PubMed:22842900}.
SITE 26 26 Key residue for interaction with ASIC1a.
{ECO:0000269|PubMed:21825095,
ECO:0000269|PubMed:22760635,
ECO:0000269|PubMed:22842900}.
SITE 27 27 Key residue for interaction with ASIC1a.
{ECO:0000269|PubMed:21825095,
ECO:0000269|PubMed:22760635,
ECO:0000269|PubMed:22842900}.
SITE 28 28 Key residue for interaction with ASIC1a.
{ECO:0000269|PubMed:22760635,
ECO:0000269|PubMed:22842900,
ECO:0000269|PubMed:26248594}.
SITE 30 30 Key residue for interaction with ASIC1a.
{ECO:0000269|PubMed:22760635,
ECO:0000269|PubMed:22842900,
ECO:0000269|PubMed:26248594}.
DISULFID 3 18 {ECO:0000269|PubMed:12824480,
ECO:0000269|PubMed:21825095,
ECO:0000269|PubMed:22760635,
ECO:0000269|PubMed:22842900,
ECO:0000312|PDB:1LMM,
ECO:0000312|PDB:2KNI,
ECO:0000312|PDB:3S3X,
ECO:0000312|PDB:4FZ0,
ECO:0000312|PDB:4FZ1}.
DISULFID 10 23 {ECO:0000269|PubMed:12824480,
ECO:0000269|PubMed:21825095,
ECO:0000269|PubMed:22760635,
ECO:0000269|PubMed:22842900,
ECO:0000312|PDB:1LMM,
ECO:0000312|PDB:2KNI,
ECO:0000312|PDB:3S3X,
ECO:0000312|PDB:4FZ0,
ECO:0000312|PDB:4FZ1}.
DISULFID 17 33 {ECO:0000269|PubMed:12824480,
ECO:0000269|PubMed:21825095,
ECO:0000269|PubMed:22760635,
ECO:0000269|PubMed:22842900,
ECO:0000312|PDB:1LMM,
ECO:0000312|PDB:2KNI,
ECO:0000312|PDB:3S3X,
ECO:0000312|PDB:4FZ0,
ECO:0000312|PDB:4FZ1}.
MUTAGEN 1 2 Missing: 1.6-fold decrease in ability to
inhibit rASIC1a channel.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 6 6 K->A: 97.7-fold decrease in ability to
inhibit rASIC1a channel, probably due to
structural perturbations.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 7 7 W->A: Complete loss in ability to inhibit
rASIC1a channel.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 8 8 K->A: 1.7-fold decrease in ability to
inhibit rASIC1a channel.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 14 14 H->A: No change in ability to inhibit
rASIC1a channel.
{ECO:0000269|PubMed:21825095}.
MUTAGEN 24 24 W->A: 170-fold decrease in ability to
inhibit rASIC1a channel.
{ECO:0000269|PubMed:21825095}.
MUTAGEN 25 25 K->A: No change in ability to inhibit
rASIC1a channel.
{ECO:0000269|PubMed:21825095}.
MUTAGEN 26 26 R->A: Loss of ability to inhibit rASIC1a
at low concentration and gain of function
as a positive modulator at high
concentrations (>100 nM), probably by
stabilizing the open state of the
channel. {ECO:0000269|PubMed:21825095}.
MUTAGEN 27 27 R->A: 165-fold decrease in ability to
inhibit rASIC1a channel.
{ECO:0000269|PubMed:21825095}.
MUTAGEN 28 28 R->A: 14.5-fold decrease in ability to
inhibit rASIC1a channel.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 29 29 S->A: Does not significantly modify the
ability to inhibit rASIC1a channel.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 30 30 F->A: Loss of ability to inhibit rASIC1a
at low concentration and gain of function
as a positive modulator at high
concentrations, probably by stabilizing
the open state of the channel.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 31 31 E->A: 2.2-fold decrease in ability to
inhibit rASIC1a channel.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 32 32 V->A: 17.9-fold decrease in ability to
inhibit rASIC1a channel, probably due to
structural perturbations.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 34 34 V->A: 1.4-fold decrease in ability to
inhibit rASIC1a channel.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 35 35 P->A: 2.7-fold increase in ability to
inhibit rASIC1a channel.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 36 36 K->A: 1.8-fold increase in ability to
inhibit rASIC1a channel.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 37 37 T->A: Does not significantly modify the
ability to inhibit rASIC1a channel.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 38 40 Missing: 4.1-fold decrease in ability to
inhibit rASIC1a channel, probably due to
the deletion of P-38.
{ECO:0000269|PubMed:26248594}.
MUTAGEN 38 38 P->A: 3.9-fold decrease in ability to
inhibit rASIC1a channel.
{ECO:0000269|PubMed:26248594}.
STRAND 2 4 {ECO:0000244|PDB:2KNI}.
STRAND 6 8 {ECO:0000244|PDB:2KNI}.
TURN 11 14 {ECO:0000244|PDB:1LMM}.
STRAND 18 20 {ECO:0000244|PDB:1LMM}.
STRAND 21 24 {ECO:0000244|PDB:4FZ0}.
STRAND 27 29 {ECO:0000244|PDB:4FZ0}.
STRAND 32 35 {ECO:0000244|PDB:4FZ0}.
SEQUENCE 40 AA; 4695 MW; A52DC98962D9598C CRC64;
EDCIPKWKGC VNRHGDCCEG LECWKRRRSF EVCVPKTPKT


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