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 56 (12 Sep 2018)
Sequence version 1 (01 Jun 2003)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Mu-conotoxin SIIIA

Gene
N/A
Organism
Conus striatus (Striated 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

Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin moderately blocks rNav1.1/SCN1A, rNav1.2/SCN2A, rNav1.3/SCN3A, rNav1.4/SCN4A, and mNav1.6/SCN8A.6 Publications

Miscellaneous

Does not inhibit Nav1.5/SCN5A (PubMed:18522941), Nav1.7/SCN9A (PubMed:18522941) and Nav1.8/SCN10A (PubMed:18522941, PubMed:21652776).1 Publication

Caution

All results of mutagenesis experiments are compared with the mutant DEL-52.Curated

<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

Protein family/group databases

Transport Classification Database

More...
TCDBi
8.B.28.1.1 the mu-conotoxin (mu-conotoxin) family

<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:
Mu-conotoxin SIIIA
<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 striatus (Striated 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 identifieri6493 [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 lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaNeogastropodaConoideaConidaeConusPionoconus

Organism-specific databases

ConoServer: Cone snail toxin database

More...
ConoServeri
825 SIIIA 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 & 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>Mutagenesisi52Q → R: Increase of affinity for both Nav1.2/SCN2A and Nav1.4/SCN4A. 2 Publications1
Mutagenesisi52Missing : Increase of affinity at Nav1.2/SCN2A and decrease of affinity at Nav1.4/SCN4A. 2 Publications1
Mutagenesisi62K → A: 6-fold decrease of affinity to both Nav1.2/SCN2A and Nav1.4/SCN4A; when associated with DEL-52. 1 Publication1
Mutagenesisi62K → R: 10-fold increase of affinity at Nav1.2/SCN2A without affecting Nav1.4/SCN4A affinity; when associated with DEL-52 and A-66. 1 Publication1
Mutagenesisi63W → A: 22- and 87-fold decrease of affinity to Nav1.2/SCN2A and Nav1.4/SCN4A, respectively; when associated with DEL-52. 1 Publication1
Mutagenesisi65R → A: Decrease of affinity to both Nav1.2/SCN2A and Nav1.4/SCN4A; when associated with DEL-52. 1 Publication1
Mutagenesisi66D → A: 10-fold increase of affinity at Nav1.2/SCN2A without affecting Nav1.4/SCN4A affinity; when associated with DEL-52. 30-fold decrease of affinity to Nav1.4/SCN4A without affecting Nav1.2/SCN2A affinity; when associated with DEL-52 and R-67. 100,000- and 400-fold decrease in affinity to Nav1.2/SCN2A and Nav1.4/SCN4A, respectively; when associated with DEL-52 and D-67. Different changes when associated with C-terminal extension, see mutated Cys-71. 2 Publications1
Mutagenesisi66D → K: Decrease of affinity to both Nav1.2/SCN2A and Nav1.4/SCN4A; when associated with DEL-52. 2 Publications1
Mutagenesisi67H → A: Most important decrease of affinity to both Nav1.2/SCN2A and Nav1.4/SCN4A; when associated with DEL-52. 1 Publication1
Mutagenesisi67H → D: 100,000- and 400-fold decrease in affinity to Nav1.2/SCN2A and Nav1.4/SCN4A, respectively; when associated with DEL-52 and A-66. 1 Publication1
Mutagenesisi67H → R: 30-fold decrease of affinity at Nav1.4/SCN4A without affecting Nav1.2/SCN2A affinity; when associated with DEL-52 and A-66. 1 Publication1
Mutagenesisi69R → A: 30- and 500-fold decrease of affinity to Nav1.2/SCN2A and Nav1.4/SCN4A, respectively; when associated with DEL-52. 1 Publication1
Mutagenesisi71C → CA: Increase in affinity for Nav1.2/SCN2A, no change in affinity for Nav1.4/SCN4A; when associated with DEL-52 and A-66. 1 Publication1
Mutagenesisi71C → CAA: Increase in affinity for Nav1.2/SCN2A, little decrease in affinity for Nav1.4/SCN4A; when associated with DEL-52 and A-66. 1 Publication1
Mutagenesisi71C → CAD: Important decrease in affinity for both Nav1.2/SCN2A and Nav1.4/SCN4A; when associated with DEL-52 and A-66. 1 Publication1
Mutagenesisi71C → CAK: Little decrease in affinity for Nav1.4/SCN4A, no change in affinity for Nav1.2/SCN2A; when associated with DEL-52 and A-66. 1 Publication1
Mutagenesisi71C → CD: The second most selective for Nav1.2/SCN2A over Nav1.4/SCVN4A; when associated with DEL-52 and A-66. 1 Publication1
Mutagenesisi71C → CK: The most selective for Nav1.2/SCN2A over Nav1.4/SCVN4A; when associated with DEL-52 and A-66. 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 – 20Sequence analysisAdd BLAST20
<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_000003505721 – 49By similarityAdd BLAST29
<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_000003505852 – 71Mu-conotoxin SIIIAAdd BLAST20

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei52Pyrrolidone carboxylic acid1 Publication1
<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 bondi54 ↔ 641 Publication
Disulfide bondi55 ↔ 701 Publication
Disulfide bondi59 ↔ 711 Publication
Modified residuei71Cysteine amide1 Publication1

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond, Pyrrolidone carboxylic acid

<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 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 cysteine framework is III (CC-C-C-CC). Classified in the M-5 branch, since 5 residues stand between the fourth and the fifth cysteine residues.

<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 M superfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004214 Conotoxin
IPR008036 Conotoxin_mu-typ

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02950 Conotoxin, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS60013 MU_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.

Q86DU6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMSKLGVLLT VCPLLFPLTA LPPDGDQPAD RPAERMQDDI SSDEHPLFDK
60 70
RQNCCNGGCS SKWCRDHARC CGR
Length:73
Mass (Da):8,105
Last modified:June 1, 2003 - 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:i5AE22E12A64B9B57
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 2206.8 Da from positions 52 - 71. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY207469 mRNA Translation: AAO48588.1

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Biological Magnetic Resonance Data Bank

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY207469 mRNA Translation: AAO48588.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Protein family/group databases

TCDBi8.B.28.1.1 the mu-conotoxin (mu-conotoxin) family

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri825 SIIIA precursor

Family and domain databases

InterProiView protein in InterPro
IPR004214 Conotoxin
IPR008036 Conotoxin_mu-typ
PfamiView protein in Pfam
PF02950 Conotoxin, 1 hit
PROSITEiView protein in PROSITE
PS60013 MU_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 nameiCM3A_CONST
<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: Q86DU6
<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: January 16, 2004
Last sequence update: June 1, 2003
Last modified: September 12, 2018
This is version 56 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

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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