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Entry version 59 (07 Nov 2018)
Sequence version 1 (26 Apr 2005)
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Protein

Alpha-conotoxin Vc1A

Gene
N/A
Organism
Conus victoriae (Queen Victoria cone)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 (IC50=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).2 Publications
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, IC50=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) (IC50=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) (IC50=140 nM) and alpha-6/alpha-3-beta-4 (CHRNA6/CHRNA3-CHRNB4) (IC50=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).10 Publications

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 (IC50=7.2 µM), alpha-3-beta-2/CHRNA3-CHRNB2 (IC50=5.5-7.3 µM), alpha-3-beta-4/CHRNA3-CHRNB4 (IC50=4.2 µM), alpha-3-alpha-5-beta-4/CHRNA3-CHRNA5-CHRNB4 (IC50>30 µM), alpha-4-beta-2/CHRNA4-CHRNB2 (IC50>30 µM), alpha-4-beta-4/CHRNA4-CHRNB4 (IC50>30 µM), rat alpha-7/CHRNA7 (IC50=7.1 µM) and alpha-1-beta-1-gamma-delta/CHRNA1-CHRNB1-CHRNG-CHRND (IC50>30 µM) subunits.2 Publications
cVc1.1 is a cyclic peptide with inhibitory activity on alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs (IC50=766 nM) and a high potency at inhibiting HVA calcium channels in mice DRG neurons (IC50=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 (IC50>17 µM) and a high potency at inhibiting HVA calcium channels in mice DRG neurons (IC50=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).3 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcetylcholine receptor inhibiting toxin, Ion channel impairing toxin, Neurotoxin, Postsynaptic neurotoxin, Toxin

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Alpha-conotoxin Vc1A1 Publication
Short name:
Alpha-Vc1A
Alternative name(s):
ACV11 Publication
Vc1.11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiConus victoriae (Queen Victoria cone)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri319920 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaNeogastropodaConoideaConidaeConusCylinder

Organism-specific databases

ConoServer: Cone snail toxin database

More...
ConoServeri
499 VcIA precursor

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

Failed in phase II clinical trial. Was tested by Metabolic under the name ACV1 to treat neuropathic pain.1 Publication
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).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi50G → A or 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. 2 Publications1
Mutagenesisi50G → 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. 2 Publications1
Mutagenesisi52C → 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. 1 Publication1
Mutagenesisi53S → 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. 2 Publications1
Mutagenesisi53S → 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. 2 Publications1
Mutagenesisi53S → 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. 2 Publications1
Mutagenesisi54D → A or 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. 2 Publications1
Mutagenesisi55P → A, D or 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. 2 Publications1
Mutagenesisi56R → A, D or 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. 2 Publications1
Mutagenesisi58 – 65Missing 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. 1 Publication8
Mutagenesisi58N → 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. 2 Publications1
Mutagenesisi58N → 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. 2 Publications1
Mutagenesisi58N → G: Vc1.1; 1.9-fold increase in potency of inhibition of rat alpha-9-alpha-10/CHRNA9-CHRNA10 nAChR. 1 Publication1
Mutagenesisi58N → 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. 1 Publication1
Mutagenesisi58N → 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. 2 Publications1
Mutagenesisi58N → 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. 1 Publication1
Mutagenesisi59Y → A or 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. 2 Publications1
Mutagenesisi59Y → 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. 2 Publications1
Mutagenesisi60D → 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. 2 Publications1
Mutagenesisi60D → 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. 2 Publications1
Mutagenesisi61H → 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. 2 Publications1
Mutagenesisi61H → D or 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. 2 Publications1
Mutagenesisi62P → 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. 2 Publications1
Mutagenesisi62P → D or 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. 2 Publications1
Mutagenesisi63E → 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. 2 Publications1
Mutagenesisi63E → 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. 2 Publications1
Mutagenesisi63E → 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. 2 Publications1
Mutagenesisi64I → 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. 2 Publications1
Mutagenesisi64I → 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. 2 Publications1
Mutagenesisi64I → 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. 2 Publications1
Mutagenesisi66G → 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. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000003489626 – 47CuratedAdd BLAST22
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_000003489750 – 65Alpha-conotoxin Vc1A1 PublicationAdd BLAST16

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi51 ↔ 573 PublicationsImported
Disulfide bondi52 ↔ 653 PublicationsImported
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei554-hydroxyproline1 Publication1
Modified residuei634-carboxyglutamate1 Publication1
Modified residuei65Cysteine amide1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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).2 Publications
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 (IC50=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).2 Publications
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 (IC50=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).2 Publications
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 µM 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).1 Publication
[C3S]Vc1.11-8 mutant is C-terminally amidated.1 Publication

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Hydroxylation

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed by the venom duct.1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

166
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H8SNMR-A50-65[»]
2MFXNMR-A50-65[»]
2MFYNMR-A50-65[»]
2MG6NMR-A50-65[»]
2N07NMR-X50-65[»]
4TTLX-ray1.70A50-65[»]
6CGXNMR-A50-65[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P69747

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P69747

Database of comparative protein structure models

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ModBasei
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P69747

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni54 – 56Key region for inhibition of alpha-9-alpha-10/CHRNA9-CHRNA10 nAChR1 Publication3
Regioni60 – 64Key region for inhibition of alpha-9-alpha-10/CHRNA9-CHRNA10 nAChR1 Publication5

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The cysteine framework is I (CC-C-C). Alpha4/7 pattern.Curated

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the conotoxin A superfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR009958 Conotoxin_a-typ
IPR018072 Conotoxin_a-typ_CS

Pfam protein domain database

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Pfami
View protein in Pfam
PF07365 Toxin_8, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS60014 ALPHA_CONOTOXIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P69747-1 [UniParc]FASTAAdd to basket
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MGMRMMFTVF LLVVLATTVV SSTSGRREFR GRNAAAKASD LVSLTDKKRG
60
CCSDPRCNYD HPEICG
Length:66
Mass (Da):7,258
Last modified:April 26, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC55B0951D5E7A28D
GO

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 1866.5 Da from positions 50 - 65. Determined by ESI. 1 Publication
Molecular mass is 1866 Da from positions 50 - 65. Determined by ESI. 1 Publication

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H8SNMR-A50-65[»]
2MFXNMR-A50-65[»]
2MFYNMR-A50-65[»]
2MG6NMR-A50-65[»]
2N07NMR-X50-65[»]
4TTLX-ray1.70A50-65[»]
6CGXNMR-A50-65[»]
ProteinModelPortaliP69747
SMRiP69747
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri499 VcIA precursor

Miscellaneous databases

EvolutionaryTraceiP69747

Family and domain databases

InterProiView protein in InterPro
IPR009958 Conotoxin_a-typ
IPR018072 Conotoxin_a-typ_CS
PfamiView protein in Pfam
PF07365 Toxin_8, 1 hit
PROSITEiView protein in PROSITE
PS60014 ALPHA_CONOTOXIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCA1A_CONVC
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P69747
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: November 7, 2018
This is version 59 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Pharmaceutical

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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