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Huwentoxin-IV (HwTx-IV) (Huwentoxin-4) (Huwentoxin-IVa) (HWTX-IVa) (Huwentoxin-IVb) (HWTX-IVb) (Huwentoxin-IVc) (HWTX-IVc) (Mu-theraphotoxin-Hs2a) (Mu-TRTX-Hs2a)

 TXH4_CYRSC              Reviewed;          89 AA.
P83303; B3FIU7; B3FIU8; B3FIU9; Q86C52;
20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 2.
05-DEC-2018, entry version 87.
RecName: Full=Huwentoxin-IV {ECO:0000303|PubMed:14757201};
Short=HwTx-IV {ECO:0000303|PubMed:14757201};
AltName: Full=Huwentoxin-4 {ECO:0000305};
AltName: Full=Huwentoxin-IVa {ECO:0000312|EMBL:ABY77744.1};
Short=HWTX-IVa {ECO:0000312|EMBL:ABY77744.1};
AltName: Full=Huwentoxin-IVb {ECO:0000312|EMBL:ABY77745.1};
Short=HWTX-IVb {ECO:0000312|EMBL:ABY77745.1};
AltName: Full=Huwentoxin-IVc {ECO:0000312|EMBL:ABY77746.1};
Short=HWTX-IVc {ECO:0000312|EMBL:ABY77746.1};
AltName: Full=Mu-theraphotoxin-Hs2a {ECO:0000303|PubMed:23760503};
Short=Mu-TRTX-Hs2a {ECO:0000303|PubMed:23760503};
Flags: Precursor;
Cyriopagopus schmidti (Chinese bird spider) (Haplopelma schmidti).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
Araneae; Mygalomorphae; Theraphosidae; Haplopelma.
NCBI_TaxID=29017;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=14757201; DOI=10.1016/j.toxicon.2003.08.007;
Diao J., Lin Y., Tang J., Liang S.-P.;
"cDNA sequence analysis of seven peptide toxins from the spider
Selenocosmia huwena.";
Toxicon 42:715-723(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-89.
TISSUE=Venom gland;
PubMed=18482741; DOI=10.1016/j.toxicon.2008.03.024;
Jiang L., Peng L., Chen J., Zhang Y., Xiong X., Liang S.;
"Molecular diversification based on analysis of expressed sequence
tags from the venom glands of the Chinese bird spider Ornithoctonus
huwena.";
Toxicon 51:1479-1489(2008).
[3]
PROTEIN SEQUENCE OF 53-87, STRUCTURE BY NMR OF 53-87, FUNCTION,
DISULFIDE BONDS, AMIDATION AT ILE-87, AND SUBCELLULAR LOCATION.
TISSUE=Venom;
PubMed=12228241; DOI=10.1074/jbc.M204063200;
Peng K., Shu Q., Liang S.-P.;
"Function and solution structure of huwentoxin-IV, a potent neuronal
tetrodotoxin (TTX)-sensitive sodium channel antagonist from Chinese
bird spider Selenocosmia huwena.";
J. Biol. Chem. 277:47564-47571(2002).
[4]
PROTEIN SEQUENCE OF 53-59, PYROGLUTAMATE FORMATION AT GLU-53, AND MASS
SPECTROMETRY.
TISSUE=Venom;
PubMed=23826086; DOI=10.1371/journal.pone.0065984;
Rong M., Duan Z., Chen J., Li J., Xiao Y., Liang S.;
"Native pyroglutamation of huwentoxin-IV: a post-translational
modification that increases the trapping ability to the sodium
channel.";
PLoS ONE 8:E65984-E65984(2013).
[5]
FUNCTION.
TISSUE=Venom;
PubMed=18628201; DOI=10.1074/jbc.M708447200;
Xiao Y., Bingham J.-P., Zhu W., Moczydlowski E., Liang S.,
Cummins T.R.;
"Tarantula huwentoxin-IV inhibits neuronal sodium channels by binding
to receptor site 4 and trapping the domain II voltage sensor in the
closed configuration.";
J. Biol. Chem. 283:27300-27313(2008).
[6]
FUNCTION, SYNTHESIS OF 53-87, AND MASS SPECTROMETRY.
TISSUE=Venom;
PubMed=18054060; DOI=10.1016/j.toxicon.2007.09.008;
Xiao Y., Luo X., Kuang F., Deng M., Wang M., Zeng X., Liang S.;
"Synthesis and characterization of huwentoxin-IV, a neurotoxin
inhibiting central neuronal sodium channels.";
Toxicon 51:230-239(2008).
[7]
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).
[8]
FUNCTION.
PubMed=21659528; DOI=10.1074/jbc.M111.246876;
Xiao Y., Jackson J.O. II, Liang S., Cummins T.R.;
"Common molecular determinants of tarantula huwentoxin-IV inhibition
of Na+ channel voltage sensors in domains II and IV.";
J. Biol. Chem. 286:27301-27310(2011).
[9]
FUNCTION, SYNTHESIS OF 53-87, AND MUTAGENESIS OF GLU-53; GLU-56 AND
TYR-85.
PubMed=23523779; DOI=10.1016/j.peptides.2013.03.011;
Revell J.D., Lund P.E., Linley J.E., Metcalfe J., Burmeister N.,
Sridharan S., Jones C., Jermutus L., Bednarek M.A.;
"Potency optimization of Huwentoxin-IV on hNav1.7: a neurotoxin TTX-S
sodium-channel antagonist from the venom of the Chinese bird-eating
spider Selenocosmia huwena.";
Peptides 44:40-46(2013).
[10]
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).
[11]
STRUCTURE BY NMR OF 53-87, FUNCTION, AND MUTAGENESIS OF GLU-56;
PHE-58; PRO-63; ASP-66; LEU-74; SER-77; TRP-82; LYS-84; TYR-85 AND
ILE-87.
PubMed=23760503; DOI=10.1074/jbc.M113.461392;
Minassian N.A., Gibbs A., Shih A.Y., Liu Y., Neff R.A., Sutton S.W.,
Mirzadegan T., Connor J., Fellows R., Husovsky M., Nelson S.,
Hunter M.J., Flinspach M., Wickenden A.D.;
"Analysis of the structural and molecular basis of voltage-sensitive
sodium channel inhibition by the spider toxin huwentoxin-IV (mu-TRTX-
Hh2a).";
J. Biol. Chem. 288:22707-22720(2013).
[12]
STRUCTURE BY NMR OF 53-87 OF HUWENTOXIN-IV; MHUWENTOXIN-IV AND
GHUWENTOXIN-IV, FUNCTION, SYNTHESIS OF 53-87 (HUWENTOXIN-IV;
MHUWENTOXIN-IV AND GHUWENTOXIN-IV), AND MUTAGENESIS OF GLU-53; GLU-56;
PHE-58 AND TYR-85.
PubMed=28115115; DOI=10.1016/j.bbamem.2017.01.020;
Agwa A.J., Lawrence N., Deplazes E., Cheneval O., Chen R.M.,
Craik D.J., Schroeder C.I., Henriques S.T.;
"Spider peptide toxin HwTx-IV engineered to bind to lipid membranes
has an increased inhibitory potency at human voltage-gated sodium
channel hNaV1.7.";
Biochim. Biophys. Acta 1859:835-844(2017).
[13]
STRUCTURE BY NMR OF M3-HUWENTOXIN-IV MUTANT, AND MUTAGENESIS OF
GLU-53; GLU-56 AND TYR-85.
PubMed=28301520; DOI=10.1371/journal.pone.0173551;
Rahnama S., Deuis J.R., Cardoso F.C., Ramanujam V., Lewis R.J.,
Rash L.D., King G.F., Vetter I., Mobli M.;
"The structure, dynamics and selectivity profile of a NaV1.7 potency-
optimised huwentoxin-IV variant.";
PLoS ONE 12:E0173551-E0173551(2017).
-!- FUNCTION: This lethal neurotoxin (without cyclization at position
53) inhibits neuronal voltage-gated sodium channel hNav1.7/SCN9A
(IC(50) is 22-33 nM), rNav1.2/SCN2A (IC(50) is 150 nM), and
rNav1.3/SCN3A (IC(50) is 338 nM) (PubMed:18628201,
PubMed:20855463, PubMed:25658507, PubMed:23760503). It inhibits
activation of sodium channel by trapping the voltage sensor of
domain II (DIIS4) in the closed configuration (PubMed:18628201,
PubMed:23760503). The toxin neither shifts the Nav1.7 activation
curve nor modifies the slope factor (PubMed:20855463). It does not
slow fast-inactivation of hNav1.7 channels (PubMed:20855463). In
addition, it has only a weak affinity for lipid membranes
(PubMed:18054060, PubMed:28115115). This toxin also exists with a
pyroglutamate at position 53 (PubMed:23826086). The sole
difference observed between modified (mHwTx-IV) and unmodified
toxins is that moderate or high depolarization voltages (200 mV)
permit the unmodified toxin to dissociate, whereas mHwTx-IV toxin
does not dissociate, even at high depolarization voltages
(PubMed:23826086). These data indicate that mHwTx-IV strongly
binds to voltage sensor of sodium channel even at extreme
depolarization voltages (PubMed:23826086).
{ECO:0000269|PubMed:12228241, ECO:0000269|PubMed:18054060,
ECO:0000269|PubMed:18628201, ECO:0000269|PubMed:20855463,
ECO:0000269|PubMed:21659528, ECO:0000269|PubMed:23523779,
ECO:0000269|PubMed:23760503, ECO:0000269|PubMed:25658507,
ECO:0000269|PubMed:28115115}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12228241}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000305|PubMed:12228241}.
-!- DOMAIN: The presence of a 'disulfide through disulfide knot'
structurally defines this protein as a knottin.
{ECO:0000269|PubMed:12228241, ECO:0000269|PubMed:23760503,
ECO:0000269|PubMed:28115115}.
-!- PTM: Two forms of huwentoxin-IV exist in the venom of H.schmidti,
a non-N-terminally modified (HwTx-IV) and a naturally modified
peptide with pyroglutamic acid residue at position 53 (mHwTx-IV).
mHwTx-IV shows no observable difference with the unmodified toxin
when applied to the TTX-S sodium channel of DRG neuron (IC(50)~50
nM) or when tested on hNav1.7/SCN9A (IC(50)=30.8 nM)
(PubMed:23826086, PubMed:28115115). In addition, similarly to the
unmodified toxin, mHwTx-IV has only a weak affinity for lipid
membranes (PubMed:28115115). However, in contrast with HwTx-IV,
which dissociates at moderate and high depolarization voltages
(50-200 mV), mHwTx-IV inhibition of TTX-sensitive sodium channels
is not reversed by strong depolarization voltages
(PubMed:23826086). {ECO:0000269|PubMed:23826086,
ECO:0000269|PubMed:28115115}.
-!- MASS SPECTROMETRY: Mass=4089.64; Method=MALDI; Range=53-87;
Note=mhuwentoxin-IV (with pyrrolidone carboxylic acid (Glu) at
position 53).; Evidence={ECO:0000269|PubMed:23826086};
-!- MASS SPECTROMETRY: Mass=4107.94; Method=MALDI; Range=53-87;
Note=huwentoxin-IV (with unmodified Glu at position 53).;
Evidence={ECO:0000269|PubMed:23826086};
-!- MASS SPECTROMETRY: Mass=4107.5; Method=MALDI; Range=53-87;
Note=huwentoxin-IV (with unmodified Glu at position 53).;
Evidence={ECO:0000269|PubMed:18054060};
-!- MISCELLANEOUS: Shows a weak or no inhibition on rNav1.4/SCN4A
(IC(50)=3.9 uM) and hNav1.5/SCN5A sodium channels (IC(50)=25->10
uM). {ECO:0000269|PubMed:18628201, ECO:0000269|PubMed:25658507}.
-!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 22 (Htx-
4) subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
Note=huwentoxin-IV;
URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=19026";
-!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
Note=Mutant W82A;
URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=19030";
-!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
Note=Mutant K84A;
URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=19032";
-----------------------------------------------------------------------
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EMBL; AY263707; AAP33074.1; -; mRNA.
EMBL; EU195291; ABY77744.1; -; mRNA.
EMBL; EU195292; ABY77745.1; -; mRNA.
EMBL; EU195293; ABY77746.1; -; mRNA.
PDB; 1MB6; NMR; -; A=53-87.
PDB; 2M4X; NMR; -; A=53-87.
PDB; 2M4Z; NMR; -; A=53-87.
PDB; 2M50; NMR; -; A=53-87.
PDB; 5T3M; NMR; -; A=53-87.
PDB; 5TLR; NMR; -; A=53-87.
PDBsum; 1MB6; -.
PDBsum; 2M4X; -.
PDBsum; 2M4Z; -.
PDBsum; 2M50; -.
PDBsum; 5T3M; -.
PDBsum; 5TLR; -.
ProteinModelPortal; P83303; -.
SMR; P83303; -.
TCDB; 8.B.3.1.3; the huwentoxin-1 (huwentoxin-1) family.
ArachnoServer; AS000332; mu-theraphotoxin-Hs2a.
EvolutionaryTrace; P83303; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0072556; C:other organism presynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR011696; Huwentoxin-1.
InterPro; IPR013140; Huwentoxin_CS1.
Pfam; PF07740; Toxin_12; 1.
PROSITE; PS60021; HWTX_1; 1.
1: Evidence at protein level;
3D-structure; Amidation; Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Knottin; Neurotoxin;
Presynaptic neurotoxin; Pyrrolidone carboxylic acid; Secreted; Signal;
Toxin; Voltage-gated sodium channel impairing toxin.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 52 {ECO:0000269|PubMed:12228241}.
/FTId=PRO_0000035560.
CHAIN 53 87 Huwentoxin-IV.
{ECO:0000269|PubMed:12228241}.
/FTId=PRO_0000035561.
SITE 58 58 Binds to the extracellular loop of
voltage sensor domain II of sodium
channels (Nav1.2/SCN2A and Nav1.7/SCN9A).
{ECO:0000305|PubMed:23760503}.
SITE 78 78 Binds to the extracellular loop of
voltage sensor domain II of sodium
channels (Nav1.2/SCN2A and Nav1.7/SCN9A).
{ECO:0000305|PubMed:23760503}.
SITE 79 79 Binds to the extracellular loop of
voltage sensor domain II of sodium
channels (Nav1.2/SCN2A and Nav1.7/SCN9A).
{ECO:0000305|PubMed:23760503}.
SITE 82 82 Binds to the extracellular loop of
voltage sensor domain II of sodium
channels (Nav1.2/SCN2A and Nav1.7/SCN9A).
{ECO:0000305|PubMed:23760503}.
SITE 84 84 Binds to the extracellular loop of
voltage sensor domain II of sodium
channels (Nav1.2/SCN2A and Nav1.7/SCN9A).
{ECO:0000305|PubMed:23760503}.
MOD_RES 53 53 Pyrrolidone carboxylic acid (Glu);
partial. {ECO:0000269|PubMed:23826086}.
MOD_RES 87 87 Isoleucine amide.
{ECO:0000269|PubMed:12228241}.
DISULFID 54 69 {ECO:0000269|PubMed:12228241,
ECO:0000312|PDB:1MB6,
ECO:0000312|PDB:2M4X,
ECO:0000312|PDB:5TLR}.
DISULFID 61 76 {ECO:0000269|PubMed:12228241,
ECO:0000312|PDB:1MB6,
ECO:0000312|PDB:2M4X,
ECO:0000312|PDB:5TLR}.
DISULFID 68 83 {ECO:0000269|PubMed:12228241,
ECO:0000312|PDB:1MB6,
ECO:0000312|PDB:2M4X,
ECO:0000312|PDB:5TLR}.
MUTAGEN 53 56 ECLE->ACLA: 6-fold increase in ability to
inhibit hNav1.7/SCN9A. 28-fold increase
in ability to inhibit hNav1.7/SCN9A; when
associated with W-85.
{ECO:0000269|PubMed:23523779}.
MUTAGEN 53 56 ECLE->GCLG: 34-fold increase in ability
to inhibit hNav1.7/SCN9A. In m3-
huwentoxin-IV; 43-fold increase in
ability to inhibit hNav1.7/SCN9A. In m3-
huwentoxin-IV; potently inhibits
Nav1.1/SCN1A, Nav1.2/SCN2A, Nav1.3/SCN3A,
Nav1.6/SCN8A and Nav1.7/SCN9A. In
gHuwentoxin-IV; shows higher affinity for
lipid membranes and a 4-fold increase in
ability to inhibit hNav1.7/SCN9A compared
to both huwentoxin-IV and mhuwentoxin-IV.
{ECO:0000269|PubMed:23523779,
ECO:0000269|PubMed:28115115,
ECO:0000269|PubMed:28301520}.
MUTAGEN 53 53 E->A: 2.8-fold increase in ability to
inhibit hNav1.7/SCN9A, and no change in
activity on hNav1.5/SCN5A.
{ECO:0000269|PubMed:23523779}.
MUTAGEN 56 56 E->A: No change in activity on both
Nav1.2/SCN2A and hNav1.5/SCN5A, and
contreversial activity on Nav1.7/SCN9A.
Small increase in ability to inhibit
Nav1.7/SCN9A (according to
PMID:23760503), and 1.5-fold decrease in
ability to inhibit hNav1.7/SCN9A
(according to PMID:23523779).
{ECO:0000269|PubMed:23523779,
ECO:0000269|PubMed:23760503}.
MUTAGEN 58 58 F->A: Important decrease in ability to
inhibit Nav1.2/SCN2A, and small decrease
in ability to inhibit Nav1.7/SCN9A.
{ECO:0000269|PubMed:23760503}.
MUTAGEN 58 58 F->W: In gHuwentoxin-IV; shows higher
affinity for lipid membranes and a 4-fold
increase in ability to inhibit
hNav1.7/SCN9A compared to both
huwentoxin-IV and mhuwentoxin-IV.
{ECO:0000269|PubMed:28115115}.
MUTAGEN 63 63 P->A: Important decrease in ability to
inhibit both Nav1.2/SCN2A and
Nav1.7/SCN9A.
{ECO:0000269|PubMed:23760503}.
MUTAGEN 66 66 D->A: Important decrease in ability to
inhibit both Nav1.2/SCN2A and
Nav1.7/SCN9A.
{ECO:0000269|PubMed:23760503}.
MUTAGEN 74 74 L->A: Important decrease in ability to
inhibit both Nav1.2/SCN2A and
Nav1.7/SCN9A.
{ECO:0000269|PubMed:23760503}.
MUTAGEN 77 77 S->A: Important decrease in ability to
inhibit both Nav1.2/SCN2A and
Nav1.7/SCN9A.
{ECO:0000269|PubMed:23760503}.
MUTAGEN 78 78 R->A: Important decrease in ability to
inhibit Nav1.2/SCN2A, and no change in
activity on Nav1.7/SCN9A.
{ECO:0000269|PubMed:23760503}.
MUTAGEN 79 79 K->A: Important decrease in ability to
inhibit Nav1.2/SCN2A, and no change in
activity on Nav1.7/SCN9A.
{ECO:0000269|PubMed:23760503}.
MUTAGEN 81 81 R->A: Small decrease in ability to
inhibit Nav1.2/SCN2A, and no change in
activity on Nav1.7/SCN9A.
{ECO:0000269|PubMed:23760503}.
MUTAGEN 82 82 W->A: Almost complete loss in ability to
inhibit both Nav1.2/SCN2A and
Nav1.7/SCN9A.
{ECO:0000269|PubMed:23760503}.
MUTAGEN 84 84 K->A: Almost complete loss in ability to
inhibit both Nav1.2/SCN2A and
Nav1.7/SCN9A.
{ECO:0000269|PubMed:23760503}.
MUTAGEN 85 85 Y->A: Important decrease in ability to
inhibit both Nav1.2/SCN2A and
Nav1.7/SCN9A.
{ECO:0000269|PubMed:23760503}.
MUTAGEN 85 85 Y->W: 12-fold increase in ability to
inhibit hNav1.7/SCN9A, and no change in
activity on hNav1.5/SCN5A. In m3-
huwentoxin-IV; 43-fold increase in
ability to inhibit hNav1.7/SCN9A. In m3-
huwentoxin-IV; potently inhibits
Nav1.1/SCN1A, Nav1.2/SCN2A, Nav1.3/SCN3A,
Nav1.6/SCN8A and Nav1.7/SCN9A. In
gHuwentoxin-IV; shows higher affinity for
lipid membranes and a 4-fold increase in
ability to inhibit hNav1.7/SCN9A compared
to both huwentoxin-IV and mhuwentoxin-IV.
{ECO:0000269|PubMed:23523779,
ECO:0000269|PubMed:28115115,
ECO:0000269|PubMed:28301520}.
MUTAGEN 87 87 I->A: Small decrease in ability to
inhibit both Nav1.2/SCN2A and
Nav1.7/SCN9A.
{ECO:0000269|PubMed:23760503}.
CONFLICT 17 17 L -> Q (in Ref. 2; ABY77746).
{ECO:0000305|PubMed:18482741}.
CONFLICT 85 85 Y -> C (in Ref. 2; ABY77745).
{ECO:0000305|PubMed:18482741}.
STRAND 57 60 {ECO:0000244|PDB:2M4Z}.
STRAND 63 65 {ECO:0000244|PDB:1MB6}.
TURN 70 73 {ECO:0000244|PDB:1MB6}.
STRAND 74 77 {ECO:0000244|PDB:1MB6}.
TURN 78 81 {ECO:0000244|PDB:1MB6}.
STRAND 82 85 {ECO:0000244|PDB:1MB6}.
SEQUENCE 89 AA; 9997 MW; 39CCC6FC1ADCBC75 CRC64;
MVNMKASMFL ALAGLVLLFV VCYASESEEK EFSNELLSSV LAVDDNSKGE ERECLEIFKA
CNPSNDQCCK SSKLVCSRKT RWCKYQIGK


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