Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 3 (18 Sep 2019)
Sequence version 1 (18 Jul 2018)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

MuO-conotoxin MfVIA

Gene
N/A
Organism
Conus magnificus (Magnificent cone) (Darioconus magnificus)
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

MuO-conotoxins are gating-modifier toxins that inhibit sodium current by trapping the domain II voltage sensor in the closed position to prevent opening of the sodium channel. This toxin shows high activity on Nav1.4/SCN4A (IC50=81 nM) and Nav1.8/SCN10A (IC50=96-529 nM). It also shows low activity on other sodium channels (Nav1.5/SCN5A, IC50=431-3900 nM > Nav1.1/SCN1A, IC50=3.3 µM; Nav1.2/SCN2A, IC50=5.1-6.3 µM; Nav1.3/SCN3A, IC50=2.2 µM; Nav1.6/SCN8A, IC50=1.2-4.6 µM; Nav1.7/SCN9A, IC50=2.3-5.5 µM) (PubMed:22609441). On Nav1.8/SCN10A, it causes a small left shift in the voltage dependence of activation and the voltage dependence of inactivation (PubMed:27026701). In addition, it has been shown to interact with lipid membranes (PubMed:27026701).2 Publications

Miscellaneous

On Nav1.8/SCN10A, the mutant (E5K,E8K)MfVIA causes a small left shift in the voltage dependence of activation and the voltage dependence of inactivation (PubMed:27026701). In addition, it inserts more deeply into the membranes than the wild-type toxin (PubMed:27026701). In vivo, the mutant (E5K,E8K)MfVIA is analgesic in a formalin-induced mouse pain model (PubMed:27026701).1 Publication

<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 functionIon channel impairing toxin, Neurotoxin, Toxin, Voltage-gated sodium channel impairing 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:
MuO-conotoxin MfVIA2 Publications
<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 magnificus (Magnificent cone) (Darioconus magnificus)
<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 identifieri257332 [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 lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaNeogastropodaConoideaConidaeConusDarioconus

<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 & Seán O’Donoghue; 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

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>Mutagenesisi5 – 8EKWE → KKWK: 3-fold increase in potency to inhibit human Nav1.8/SCN10A sodium channels, and important increase in interaction with lipid membrane. 1 Publication4
Mutagenesisi5E → A: 2-fold increase in potency to inhibit human Nav1.8/SCN10A sodium channels, and small decrease in interaction with lipid membrane. 1 Publication1
Mutagenesisi6K → A: 1.5-fold decrease in potency to inhibit human Nav1.8/SCN10A sodium channels. 1 Publication1
Mutagenesisi7W → A: 2.5-fold decrease in potency to inhibit human Nav1.8/SCN10A sodium channels, and important decrease in interaction with lipid membrane. 1 Publication1
Mutagenesisi8E → A: 2-fold increase in potency to inhibit human Nav1.8/SCN10A sodium channels, and small decrease in interaction with lipid membrane. 1 Publication1
Mutagenesisi14I → A: 5-fold decrease in potency to inhibit human Nav1.8/SCN10A sodium channels, and no change in interaction with lipid membrane. 1 Publication1
Mutagenesisi15L → A: 2.5-fold decrease in potency to inhibit human Nav1.8/SCN10A sodium channels. 1 Publication1
Mutagenesisi17F → A: 2-fold decrease in potency to inhibit human Nav1.8/SCN10A sodium channels. 1 Publication1
Mutagenesisi18V → A: 2-fold decrease in potency to inhibit human Nav1.8/SCN10A sodium channels. 1 Publication1
Mutagenesisi19Y → A: 12-fold decrease in potency to inhibit human Nav1.8/SCN10A sodium channels, and no change in interaction with lipid membrane. 1 Publication1
Mutagenesisi19Y → F: 1.3-fold decrease in potency to inhibit human Nav1.8/SCN10A sodium channels. 1 Publication1
Mutagenesisi19Y → W: 2-fold decrease in potency to inhibit human Nav1.8/SCN10A sodium channels, and no change in interaction with lipid membrane. 1 Publication1
Mutagenesisi29F → A: 6-fold decrease in potency to inhibit human Nav1.8/SCN10A sodium channels, and important decrease in interaction with lipid membrane. 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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004446911 – 32MuO-conotoxin MfVIA1 PublicationAdd BLAST32

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 bondi3 ↔ 212 PublicationsImported
Disulfide bondi10 ↔ 262 PublicationsImported
Disulfide bondi20 ↔ 312 PublicationsImported

Keywords - PTMi

Disulfide bond

<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

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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

<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 presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.1 Publication
The cysteine framework is VI/VII (C-C-CC-C-C).Curated

Keywords - Domaini

Knottin

<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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

P0DM15-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30 
RDCQEKWEYC IVPILGFVYC CPGLICGPFV CV
Length:32
Mass (Da):3,654
Last modified:July 18, 2018 - 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:i355B70AE0527FC2D
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 3647.7 Da from positions 1 - 32. Determined by MALDI. Average mass.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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N7FNMR-A1-32[»]
ModBaseiSearch...
SWISS-MODEL-WorkspaceiSubmit a new modelling project...
PDBe-KBiSearch...

Family and domain databases

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiCO6A_CONMF
<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: P0DM15
<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: July 18, 2018
Last sequence update: July 18, 2018
Last modified: September 18, 2019
This is version 3 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, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again