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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.
22-NOV-2017, entry version 55.
RecName: Full=Alpha-conotoxin Vc1A;
Short=ACV1;
Short=Alpha-Vc1A;
AltName: Full=Vc1.1;
Flags: Precursor;
Conus victoriae (Queen Victoria cone).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae;
Conus.
NCBI_TaxID=319920;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 50-65, AND FUNCTION.
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, AND GAMMA-CARBOXYGLUTAMATION AT GLU-63.
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.
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]
PHARMACEUTICAL.
PubMed=16182258; DOI=10.1016/j.brainres.2005.08.009;
Satkunanathan N., Livett B., Gayler K., Sandall D., Down J.,
Khalil Z.;
"Alpha-conotoxin Vc1.1 alleviates neuropathic pain and accelerates
functional recovery of injured neurones.";
Brain Res. 1059:149-158(2005).
[5]
SYNTHESIS OF NON-POST-TRANSLATIONALLY MODIFIED PEPTIDE, DISULFIDE,
BONDS, MASS SPECTROMETRY, AND STRUCTURE BY NMR.
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).
-!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they
bind to the nicotinic acetylcholine receptors (nAChR) and thus
inhibit them. This synthetic peptide (produced without
hydroxyproline, nor 4-carboxyglutamate) is a neuronal nAChR
antagonist that acts as a powerful analgesic. It blocks nAChRs
composed of alpha-3 or -5/beta-2 (IC(50)=7.2 uM), alpha-3/beta-2
(IC(50)=7.3 uM), alpha-3/beta-4 (IC(50)=4.2 uM), alpha-3 or
-5/beta-4 (IC(50)<30 uM), alpha-4/beta-2 (IC(50)<30 uM), alpha-
4/beta-4 (IC(50)<30 uM) and alpha/beta/gamma/delta (IC(50)<30 uM)
subunits. {ECO:0000269|PubMed:12779345,
ECO:0000269|PubMed:15770155}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom duct.
-!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
-!- 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};
-!- MASS SPECTROMETRY: Mass=1809.7; Method=Electrospray; Range=50-65;
Note=Without hydroxyPro-55, nor gamma-carboxyglutamic acid.;
Evidence={ECO:0000269|PubMed:16754662};
-!- MASS SPECTROMETRY: Mass=1821.6; Method=Electrospray; Range=50-65;
Note=With hydroxyPro-55, but without gamma-carboxyglutamic acid.;
Evidence={ECO:0000269|PubMed:16754662};
-!- PHARMACEUTICAL: Failed in phase II clinical trial. Was tested by
Metabolic under the name ACV1 to treat neuropathic pain.
-!- 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=50-66.
PDB; 4TTL; X-ray; 1.70 A; A=50-66.
PDBsum; 2H8S; -.
PDBsum; 2MFX; -.
PDBsum; 2MFY; -.
PDBsum; 2MG6; -.
PDBsum; 2N07; -.
PDBsum; 4TTL; -.
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
/FTId=PRO_0000034896.
PEPTIDE 50 65 Alpha-conotoxin Vc1A.
/FTId=PRO_0000034897.
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
DISULFID 52 65
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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