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Alpha-conotoxin Vc1A (ACV1) (Alpha-Vc1A) (Vc1.1)

 CA1A_CONVC              Reviewed;          66 AA.
P69747;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
07-NOV-2018, entry version 59.
RecName: Full=Alpha-conotoxin Vc1A {ECO:0000303|PubMed:15170751};
Short=Alpha-Vc1A;
AltName: Full=ACV1 {ECO:0000303|PubMed:15770155};
AltName: Full=Vc1.1 {ECO:0000303|PubMed:12779345};
Flags: Precursor;
Conus victoriae (Queen Victoria cone).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
NCBI_TaxID=319920;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION OF VC1.1, AND SYNTHESIS OF 50-65
(VC1.1).
TISSUE=Venom duct;
PubMed=12779345; DOI=10.1021/bi034043e;
Sandall D.W., Satkunanathan N., Keays D.A., Polidano M.A., Liping X.,
Pham V., Down J.G., Khalil Z., Livett B.G., Gayler K.R.;
"A novel alpha-conotoxin identified by gene sequencing is active in
suppressing the vascular response to selective stimulation of sensory
nerves in vivo.";
Biochemistry 42:6904-6911(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, AMIDATION AT CYS-65,
HYDROXYLATION AT PRO-55, GAMMA-CARBOXYGLUTAMATION AT GLU-63, AND
SUBCELLULAR LOCATION.
TISSUE=Venom, and Venom duct;
PubMed=15170751; DOI=10.1002/jms.624;
Jakubowski J.A., Keays D.A., Kelley W.P., Sandall D.W., Bingham J.-P.,
Livett B.G., Gayler K.R., Sweedler J.V.;
"Determining sequences and post-translational modifications of novel
conotoxins in Conus victoriae using cDNA sequencing and mass
spectrometry.";
J. Mass Spectrom. 39:548-557(2004).
[3]
FUNCTION OF VC1.1, AND SYNTHESIS OF 50-65 (VC1.1).
PubMed=15770155; DOI=10.1097/00001756-200504040-00012;
Lang P.M., Burgstahler R., Haberberger R.V., Sippel W., Grafe P.;
"A conus peptide blocks nicotinic receptors of unmyelinated axons in
human nerves.";
NeuroReport 16:479-483(2005).
[4]
FUNCTION OF VC1.1, AND SYNTHESIS OF 50-65 (VC1.1).
PubMed=17101979; DOI=10.1073/pnas.0608715103;
Vincler M., Wittenauer S., Parker R., Ellison M., Olivera B.M.,
McIntosh J.M.;
"Molecular mechanism for analgesia involving specific antagonism of
alpha9alpha10 nicotinic acetylcholine receptors.";
Proc. Natl. Acad. Sci. U.S.A. 103:17880-17884(2006).
[5]
FUNCTION OF VC1A AND VC1.1, AND SYNTHESIS OF 50-65 (VC1A AND VC1.1).
PubMed=17804600; DOI=10.1124/mol.107.040568;
Nevin S.T., Clark R.J., Klimis H., Christie M.J., Craik D.J.,
Adams D.J.;
"Are alpha9alpha10 nicotinic acetylcholine receptors a pain target for
alpha-conotoxins?";
Mol. Pharmacol. 72:1406-1410(2007).
[6]
FUNCTION OF VC1A AND VC1.1 ON GABA(B) RECEPTOR, AND SYNTHESIS OF 50-65
(VC1A AND VC1.1).
PubMed=18945902; DOI=10.1523/JNEUROSCI.3594-08.2008;
Callaghan B., Haythornthwaite A., Berecki G., Clark R.J., Craik D.J.,
Adams D.J.;
"Analgesic alpha-conotoxins Vc1.1 and Rg1A inhibit N-type calcium
channels in rat sensory neurons via GABAB receptor activation.";
J. Neurosci. 28:10943-10951(2008).
[7]
FUNCTION OF VC1.1, SYNTHESIS OF 50-65 (VC1.1), AND MUTAGENESIS OF
GLY-50; SER-53; ASP-54; PRO-55; ARG-56; ASN-58; TYR-59; ASP-60;
HIS-61; PRO-62; GLU-63 AND ILE-64.
PubMed=19447885; DOI=10.1074/jbc.M109.015339;
Halai R., Clark R.J., Nevin S.T., Jensen J.E., Adams D.J., Craik D.J.;
"Scanning mutagenesis of alpha-conotoxin Vc1.1 reveals residues
crucial for activity at the alpha9alpha10 nicotinic acetylcholine
receptor.";
J. Biol. Chem. 284:20275-20284(2009).
[8]
FUNCTION OF VC1.1, SYNTHESIS OF 50-65 (VC1.1), AND MUTAGENESIS OF
ASN-58.
PubMed=23566299; DOI=10.1021/jm400041h;
Yu R., Kompella S.N., Adams D.J., Craik D.J., Kaas Q.;
"Determination of the alpha-conotoxin Vc1.1 binding site on the
alpha9alpha10 nicotinic acetylcholine receptor.";
J. Med. Chem. 56:3557-3567(2013).
[9]
FUNCTION OF VC1.1, SYNTHESIS OF 50-65 (VC1.1), AND MUTAGENESIS OF
CYS-52 AND 58-ASN--CYS-65.
PubMed=26948522; DOI=10.1002/anie.201600297;
Carstens B.B., Berecki G., Daniel J.T., Lee H.S., Jackson K.A.,
Tae H.S., Sadeghi M., Castro J., O'Donnell T., Deiteren A.,
Brierley S.M., Craik D.J., Adams D.J., Clark R.J.;
"Structure-activity studies of cysteine-rich alpha-conotoxins that
inhibit high-voltage-activated calcium channels via GABA(B) receptor
activation reveal a minimal functional motif.";
Angew. Chem. Int. Ed. 55:4692-4696(2016).
[10]
FUNCTION OF CYCLIC VC1.1, SYNTHESIS OF 50-65 (VC1.1), AND
PHARMACEUTICAL.
PubMed=29194563; DOI=10.1111/bph.14115;
Castro J., Grundy L., Deiteren A., Harrington A.M., O'Donnell T.,
Maddern J., Moore J., Garcia-Caraballo S., Rychkov G.Y., Yu R.,
Kaas Q., Craik D.J., Adams D.J., Brierley S.M.;
"Cyclic analogues of alpha-conotoxin Vc1.1 inhibit colonic nociceptors
and provide analgesia in a mouse model of chronic abdominal pain.";
Br. J. Pharmacol. 175:2384-2398(2018).
[11]
STRUCTURE BY NMR OF 50-65 (VC1.1).
PubMed=16754662; DOI=10.1074/jbc.M604550200;
Clark R.J., Fischer H., Nevin S.T., Adams D.J., Craik D.J.;
"The synthesis, structural chracterisation and receptor specificity of
the alpha-conotoxin Vc1.1.";
J. Biol. Chem. 281:23254-23263(2006).
[12]
STRUCTURE BY NMR OF 50-66 (CYCLIC VC1.1), AND MUTAGENESIS OF GLY-66.
PubMed=20533477; DOI=10.1002/anie.201000620;
Clark R.J., Jensen J., Nevin S.T., Callaghan B.P., Adams D.J.,
Craik D.J.;
"The engineering of an orally active conotoxin for the treatment of
neuropathic pain.";
Angew. Chem. Int. Ed. 49:6545-6548(2010).
[13]
STRUCTURE BY NMR OF 50-65 (VC1.1 AND DICARBA ANALOGS), AND FUNCTION OF
VC1.1 AND DICARBA ANALOGS.
PubMed=23768016; DOI=10.1021/cb4002393;
van Lierop B.J., Robinson S.D., Kompella S.N., Belgi A.,
McArthur J.R., Hung A., MacRaild C.A., Adams D.J., Norton R.S.,
Robinson A.J.;
"Dicarba alpha-conotoxin Vc1.1 analogues with differential selectivity
for nicotinic acetylcholine and GABAB receptors.";
ACS Chem. Biol. 8:1815-1821(2013).
[14]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF L- AND D-CYCLIC VC1.1.
PubMed=25168664; DOI=10.1002/anie.201406563;
Wang C.K., King G.J., Northfield S.E., Ojeda P.G., Craik D.J.;
"Racemic and quasi-racemic X-ray structures of cyclic disulfide-rich
peptide drug scaffolds.";
Angew. Chem. Int. Ed. 53:11236-11241(2014).
[15]
STRUCTURE BY NMR OF 50-66 (CYCLIC VC1.1).
PubMed=26290113; DOI=10.1038/srep13264;
Yu R., Seymour V.A., Berecki G., Jia X., Akcan M., Adams D.J.,
Kaas Q., Craik D.J.;
"Less is more: design of a highly stable disulfide-deleted mutant of
analgesic cyclic alpha-conotoxin Vc1.1.";
Sci. Rep. 5:13264-13264(2015).
[16]
STRUCTURE BY NMR OF CYCLIC [D11A; E14A]VC1.1, AND MUTAGENESIS OF
ASP-60 AND GLU-63.
PubMed=29746088; DOI=10.1021/acschembio.8b00190;
Sadeghi M., Carstens B.B., Callaghan B.P., Daniel J.T., Tae H.S.,
O'Donnell T., Castro J., Brierley S.M., Adams D.J., Craik D.J.,
Clark R.J.;
"Structure-activity studies reveal the molecular basis for GABAB-
receptor mediated inhibition of high voltage-activated calcium
channels by alpha-conotoxin Vc1.1.";
ACS Chem. Biol. 13:1577-1587(2018).
-!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they
bind to the nicotinic acetylcholine receptors (nAChR) and thus
inhibit them. This toxin (native toxin Vc1a; hydroxylated and
gamma-carboxylated) blocks alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs
(IC(50)=62.9 nM) (PubMed:17804600). In contrast to the non-post-
translationally modified analog Vc1.1, Vc1a does not inhibit high
voltage-activated (HVA) calcium channel currents
(PubMed:18945902). In vivo, in contrast to Vc1.1, Vc1a does not
show analgesic effects in rat models of neuropathic pain
(PubMed:17804600). {ECO:0000269|PubMed:17804600,
ECO:0000269|PubMed:18945902}.
-!- FUNCTION: The synthetic peptide Vc1.1 (a non-hydroxylated and non-
gamma-carboxylated analog of Vc1a) has two types of targets. It
blocks alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs (on rat receptors,
IC(50)=19-109 nM) (with preference for rat over human receptors)
and inhibits high voltage-activated (HVA) calcium channel (Cav2.2,
Cav2.3) currents by acting on GABA(B) receptors (GABBR1 and
GABBR2) (IC(50)=1.7 nM) (PubMed:17101979, PubMed:17804600,
PubMed:18945902, PubMed:19447885, PubMed:23566299,
PubMed:26948522, PubMed:20533477, PubMed:23768016). It also shows
moderate inhibition on alpha-6/alpha-3-beta-2-beta-3
(CHRNA6/CHRNA3-CHRNB2-CHRNB3) (IC(50)=140 nM) and alpha-6/alpha-3-
beta-4 (CHRNA6/CHRNA3-CHRNB4) (IC(50)=980 nM) (PubMed:17101979).
On alpha-9-alpha-10/CHRNA9-CHRNA10 nAChR, it most likely interacts
with the alpha-10(+)/alpha-9(-)interface of the receptor
(PubMed:23566299). In vivo, it acts as a powerful analgesic in rat
models of neuropathic pain (PubMed:17804600).
{ECO:0000269|PubMed:12779345, ECO:0000269|PubMed:15770155,
ECO:0000269|PubMed:17101979, ECO:0000269|PubMed:17804600,
ECO:0000269|PubMed:18945902, ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:20533477, ECO:0000269|PubMed:23566299,
ECO:0000269|PubMed:23768016, ECO:0000269|PubMed:26948522}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15170751}.
-!- TISSUE SPECIFICITY: Expressed by the venom duct.
{ECO:0000305|PubMed:15170751}.
-!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
{ECO:0000305}.
-!- PTM: Vc1.1 is described as having no post-translational
modifications (except C-terminal amidation), whereas Vc1a contains
an hydroxyproline at Pro-55 and a 4-carboxyglutamate at Glu-63
(and a C-terminal amidation) (PubMed:17101979, PubMed:17804600).
{ECO:0000305|PubMed:17101979, ECO:0000305|PubMed:17804600}.
-!- PTM: Hydroxylation of Pro-55 is not important for inhibition of
alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs, since [P6O]Vc1.1 (Pro-55
hydroxylated) shows similar inhibition than native toxin
(IC(50)=99.1 nM) (PubMed:17804600). In contrast, hydroxylation of
Pro-55 seems to impair inhibition of HVA calcium channel currents,
since [P6O]Vc1.1 has no effect on HVA calcium channel currents
(PubMed:18945902). In vivo, hydroxylation of Pro-55 seems to
induce the loss of analgesic effects in rat models of neuropathic
pain, since [P6O]Vc1.1 has no effect on mechanical allodynia
(PubMed:17804600). {ECO:0000269|PubMed:17804600,
ECO:0000269|PubMed:18945902}.
-!- PTM: Gamma-carboxylation of Glu-63 is not important for inhibition
of alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs, since [E14gamma]Vc1.1
(carboxyglutamate at Glu-63) shows similar inhibition than native
toxin (IC(50)=65.3 nM) (PubMed:17804600). In contrast, gamma-
carboxylation of Glu-63 seems to impair inhibition of HVA calcium
channel currents, since [E14gamma]Vc1.1 has no effect on HVA
calcium channel currents (PubMed:18945902).
{ECO:0000269|PubMed:17804600, ECO:0000269|PubMed:18945902}.
-!- PTM: Non-native isomers 'ribbon' (with disulfide connectivity C1-
C4; C2-C3) and 'beads' (with disulfide connectivity C1-C2; C3-C4)
of Vc1.1 also inhibit HVA calcium channel currents in rat DRG
neurons (20-30% inhibition at 1 uM toxin) (PubMed:26948522). It
has been shown that both reduced and alkylated Vc1.1 have no
effect on HVA calcium channel currents. The observed activity can
be attributed to specific isomers (PubMed:26948522).
{ECO:0000269|PubMed:26948522}.
-!- PTM: [C3S]Vc1.1(1-8) mutant is C-terminally amidated.
{ECO:0000269|PubMed:26948522}.
-!- MASS SPECTROMETRY: Mass=1866.5; Method=Electrospray; Range=50-65;
Evidence={ECO:0000269|PubMed:15170751};
-!- MASS SPECTROMETRY: Mass=1866; Method=Electrospray; Range=50-65;
Evidence={ECO:0000269|PubMed:16754662};
-!- PHARMACEUTICAL: Failed in phase II clinical trial. Was tested by
Metabolic under the name ACV1 to treat neuropathic pain.
{ECO:0000305|PubMed:29194563}.
-!- PHARMACEUTICAL: Cyclic versions of Vc1.1 evoke significant anti-
nociceptive actions in animal model of chronic visceral
hypersensitivity (CVH), suggesting that they could be novel
candidates for treatment of chronic visceral pain (CVP).
{ECO:0000305|PubMed:29194563}.
-!- MISCELLANEOUS: The synthetic peptide Vc1.1 (a non-hydroxylated and
non-gamma-carboxylated analog of Vc1a) shows weak inhibition on
nAChRs composed of alpha-3-alpha-5-beta-2/CHRNA3-CHRNA5-CHRNB2
(IC(50)=7.2 uM), alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=5.5-7.3 uM),
alpha-3-beta-4/CHRNA3-CHRNB4 (IC(50)=4.2 uM), alpha-3-alpha-5-
beta-4/CHRNA3-CHRNA5-CHRNB4 (IC(50)>30 uM), alpha-4-beta-2/CHRNA4-
CHRNB2 (IC(50)>30 uM), alpha-4-beta-4/CHRNA4-CHRNB4 (IC(50)>30
uM), rat alpha-7/CHRNA7 (IC(50)=7.1 uM) and alpha-1-beta-1-gamma-
delta/CHRNA1-CHRNB1-CHRNG-CHRND (IC(50)>30 uM) subunits.
{ECO:0000269|PubMed:16754662, ECO:0000269|PubMed:19447885}.
-!- MISCELLANEOUS: cVc1.1 is a cyclic peptide with inhibitory activity
on alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs (IC(50)=766 nM) and a
high potency at inhibiting HVA calcium channels in mice DRG
neurons (IC(50)=0.3 nM) (PubMed:20533477). Toxin cVc1.1[D11A;
E14A] is a cyclic peptide with a very low inhibitory activity on
alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs (IC(50)>17 uM) and a high
potency at inhibiting HVA calcium channels in mice DRG neurons
(IC(50)=3.3 nM) (PubMed:29746088). Both of them show
antinociceptive actions, with greater efficacy in a model of
animal chronic visceral hypersensitivity (CVH) (PubMed:29194563,
PubMed:29746088). {ECO:0000269|PubMed:20533477,
ECO:0000269|PubMed:29194563, ECO:0000269|PubMed:29746088}.
-!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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PDB; 2H8S; NMR; -; A=50-65.
PDB; 2MFX; NMR; -; A=50-65.
PDB; 2MFY; NMR; -; A=50-65.
PDB; 2MG6; NMR; -; A=50-65.
PDB; 2N07; NMR; -; X=50-65.
PDB; 4TTL; X-ray; 1.70 A; A=50-65.
PDB; 6CGX; NMR; -; A=50-65.
PDBsum; 2H8S; -.
PDBsum; 2MFX; -.
PDBsum; 2MFY; -.
PDBsum; 2MG6; -.
PDBsum; 2N07; -.
PDBsum; 4TTL; -.
PDBsum; 6CGX; -.
ProteinModelPortal; P69747; -.
SMR; P69747; -.
ConoServer; 499; VcIA precursor.
EvolutionaryTrace; P69747; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0035792; C:other organism postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR009958; Conotoxin_a-typ.
InterPro; IPR018072; Conotoxin_a-typ_CS.
Pfam; PF07365; Toxin_8; 1.
PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
1: Evidence at protein level;
3D-structure; Acetylcholine receptor inhibiting toxin; Amidation;
Cleavage on pair of basic residues; Disulfide bond;
Gamma-carboxyglutamic acid; Hydroxylation;
Ion channel impairing toxin; Neurotoxin; Pharmaceutical;
Postsynaptic neurotoxin; Secreted; Signal; Toxin.
SIGNAL 1 25 {ECO:0000255}.
PROPEP 26 47 {ECO:0000305}.
/FTId=PRO_0000034896.
PEPTIDE 50 65 Alpha-conotoxin Vc1A.
{ECO:0000305|PubMed:12779345}.
/FTId=PRO_0000034897.
REGION 54 56 Key region for inhibition of alpha-9-
alpha-10/CHRNA9-CHRNA10 nAChR.
{ECO:0000305|PubMed:19447885}.
REGION 60 64 Key region for inhibition of alpha-9-
alpha-10/CHRNA9-CHRNA10 nAChR.
{ECO:0000305|PubMed:19447885}.
MOD_RES 55 55 4-hydroxyproline.
{ECO:0000269|PubMed:15170751}.
MOD_RES 63 63 4-carboxyglutamate.
{ECO:0000269|PubMed:15170751}.
MOD_RES 65 65 Cysteine amide.
{ECO:0000269|PubMed:15170751}.
DISULFID 51 57 {ECO:0000269|PubMed:16754662,
ECO:0000269|PubMed:25168664,
ECO:0000269|PubMed:29746088,
ECO:0000312|PDB:2H8S,
ECO:0000312|PDB:4TTL,
ECO:0000312|PDB:6CGX}.
DISULFID 52 65 {ECO:0000269|PubMed:16754662,
ECO:0000269|PubMed:25168664,
ECO:0000269|PubMed:29746088,
ECO:0000312|PDB:2H8S,
ECO:0000312|PDB:4TTL,
ECO:0000312|PDB:6CGX}.
MUTAGEN 50 50 G->A,D: Vc1.1; No change in potency of
inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. No change in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 50 50 G->K: Vc1.1; No change in potency of
inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. Decrease in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 52 52 C->S: In [C3S]Vc1.1(1-8); Shows similar
potency of inhibition of HVA calcium
currents. Shows 95% inhibition of human
alpha-7/CHRNA7, but no inhibition of
human alpha-9-alpha-10/CHRNA9-CHRNA10
AChR. {ECO:0000269|PubMed:26948522}.
MUTAGEN 53 53 S->A: Vc1.1; 2.5-fold decrease in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. Decrease in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 53 53 S->D: Vc1.1; 1.7-fold decrease in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. No change in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 53 53 S->K: Vc1.1; 1.7-fold increase in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. No change in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons. 2-fold
increase in potency of inhibition of rat
alpha-9-alpha-10/CHRNA9-CHRNA10 nAChR;
when associated with A-58.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 54 54 D->A,K: Vc1.1; Almost complete loss of
potency of inhibition of rat alpha-9-
alpha-10/CHRNA9-CHRNA10 nAChR. Decrease
in potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 55 55 P->A,D,K: Vc1.1; Almost complete loss of
potency of inhibition of rat alpha-9-
alpha-10/CHRNA9-CHRNA10 nAChR. Decrease
in potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 56 56 R->A,D,K: Vc1.1; Almost complete loss of
potency of inhibition of rat alpha-9-
alpha-10/CHRNA9-CHRNA10 nAChR. Decrease
in potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 58 65 Missing: In [C3S]Vc1.1(1-8); Shows
similar potency of inhibition of HVA
calcium currents. Shows 95% inhibition of
human alpha-7/CHRNA7, but no inhibition
of human alpha-9-alpha-10/CHRNA9-CHRNA10
AChR. {ECO:0000269|PubMed:26948522}.
MUTAGEN 58 58 N->A: Vc1.1; 2.2-fold increase in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. 30-fold increase
in potency of inhibition of rat alpha-3-
beta-2/CHRNA3-CHRNB2 nAChR. Decrease in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons. 2-fold
increase in potency of inhibition of rat
alpha-9-alpha-10/CHRNA9-CHRNA10 nAChR;
when associated with K-53.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 58 58 N->D: Vc1.1; No change in potency of
inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. No change in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 58 58 N->G: Vc1.1; 1.9-fold increase in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR.
{ECO:0000269|PubMed:19447885}.
MUTAGEN 58 58 N->I: Vc1.1; 1.7-fold increase in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. 25-fold increase
in potency of inhibition of rat alpha-3-
beta-2/CHRNA3-CHRNB2 nAChR. 7-fold
increase in potency of inhibition of rat
alpha-7/CHRNA7 nAChR.
{ECO:0000269|PubMed:19447885}.
MUTAGEN 58 58 N->K: Vc1.1; Complete loss of potency of
inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. No change in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 58 58 N->L: Vc1.1; 1.7-fold increase in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. 2-fold increase
in potency of inhibition of rat alpha-3-
beta-2/CHRNA3-CHRNB2 nAChR.
{ECO:0000269|PubMed:19447885}.
MUTAGEN 59 59 Y->A,K: Vc1.1; No change in potency of
inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. Decrease in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 59 59 Y->D: Vc1.1; 5-fold decrease in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. Decrease in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 60 60 D->A: Vc1.1; 5-fold decrease in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. No change in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons. Toxin
cVc1.1[D11A; E14A]; important decrease in
potency of inhibition of alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. Very potent in
inhibition of HVA calcium channels in
mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 60 60 D->K: Vc1.1; 5-fold decrease in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. No change in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 61 61 H->A: Vc1.1; 10-fold decrease in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. Decrease in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 61 61 H->D,K: Vc1.1; About 4.1-fold decrease in
potency of inhibition of rat alpha-9-
alpha-10/CHRNA9-CHRNA10 nAChR. Decrease
in potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 62 62 P->A: Vc1.1; 3.3-fold decrease in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. Decrease in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 62 62 P->D,K: Vc1.1; Complete loss of potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. Decrease in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 63 63 E->A: Vc1.1; About 3.3-fold decrease in
potency of inhibition of rat alpha-9-
alpha-10/CHRNA9-CHRNA10 nAChR. No change
in potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons. Toxin
cVc1.1[D11A; E14A]; important decrease in
potency of inhibition of alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. Very potent in
inhibition of HVA calcium channels in
mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 63 63 E->D: Vc1.1; About 2-fold decrease in
potency of inhibition of rat alpha-9-
alpha-10/CHRNA9-CHRNA10 nAChR. No change
in potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 63 63 E->K: Vc1.1; About 3-fold decrease in
potency of inhibition of rat alpha-9-
alpha-10/CHRNA9-CHRNA10 nAChR. Decrease
in potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 64 64 I->A: Vc1.1; 5-fold decrease in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. No change in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 64 64 I->D: Vc1.1; Complete loss of potency of
inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. No change in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 64 64 I->K: Vc1.1; 2.5-fold decrease in potency
of inhibition of rat alpha-9-alpha-
10/CHRNA9-CHRNA10 nAChR. Decrease in
potency of inhibition of HVA calcium
channels in rat/mouse DRG neurons.
{ECO:0000269|PubMed:19447885,
ECO:0000269|PubMed:29746088}.
MUTAGEN 66 66 G->GGAAGG: Toxin cVc1.1[D11A; E14A];
important decrease in potency of
inhibition of alpha-9-alpha-10/CHRNA9-
CHRNA10 nAChR. Very potent in inhibition
of HVA calcium channels in mouse DRG
neurons. {ECO:0000269|PubMed:29746088}.
HELIX 51 53 {ECO:0000244|PDB:4TTL}.
HELIX 55 60 {ECO:0000244|PDB:4TTL}.
HELIX 62 65 {ECO:0000244|PDB:4TTL}.
SEQUENCE 66 AA; 7258 MW; C55B0951D5E7A28D CRC64;
MGMRMMFTVF LLVVLATTVV SSTSGRREFR GRNAAAKASD LVSLTDKKRG CCSDPRCNYD
HPEICG


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