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Entry version 22 (13 Feb 2019)
Sequence version 1 (06 Feb 2013)
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Protein

Alpha-conotoxin TxID

Gene
N/A
Organism
Conus textile (Cloth-of-gold 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 inhibits alpha-3-beta-4/CHRNA3-CHRNB4 (IC50=3.6-18.38 nM), alpha-6/alpha-3-beta-4 (CHRNA6/CHRNA3-CHRNB2-CHRNB4) (IC50=33.9-94.1 nM), and alpha-2-beta-4/CHRNA2-CHRNB4 (IC50=4550 nM) nAChRs (PubMed:24200193, PubMed:28603989, PubMed:29925760). The toxin competes with agonists in the orthosteric binding site of alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4 (PubMed:30252466).1 Publication3 Publications

Miscellaneous

This toxin does not show inhibition at neuronal alpha-4-beta-4/CHRNA4-CHRNB4, alpha-4-beta-2/CHRNA4-CHRNB2, alpha-6/alpha-3-beta-2-beta-3 (CHRNA6/CHRNA3-CHRNB2-CHRNB3), alpha-3-beta-2/CHRNA3-CHRNB2, alpha-2-beta-2/CHRNA2-CHRNB2, alpha-9-alpha-10/CHRNA9-CHRNA10, alpha-7/CHRNA7 nAChRs and muscle alpha-1-beta-1-delta-epsilon/CHRNA1-CHRNB1-CHRND-CHRNE nAChR (PubMed:24200193).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 functionAcetylcholine receptor inhibiting 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 TxID1 Publication
Alternative name(s):
Alpha-conotoxin TxICImported
<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 textile (Cloth-of-gold 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 identifieri6494 [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

<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

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>Mutagenesisi22G → A: 17-fold and 8-fold decrease in inhibitory potency on alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs, respectively. 1 Publication1
Mutagenesisi25S → A: 3-fold and 2-fold decrease in inhibitory potency on alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs, respectively. 1 Publication1
Mutagenesisi26H → A: Complete loss in inhibitory potency on both alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs. 1 Publication1
Mutagenesisi27P → A: Complete loss in inhibitory potency on both alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs. 1 Publication1
Mutagenesisi28V → A: Complete loss in inhibitory potency on both alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs. 1 Publication1
Mutagenesisi30S → A: 46-fold increase in selectivity for alpha-3-beta-4/CHRNA3-CHRNB4 over alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs. 1.1-fold and 5.2-fold decrease in inhibitory potency on alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs, respectively. 1 Publication1
Mutagenesisi30S → K: Become completely selective for alpha-3-beta-4/CHRNA3-CHRNB4 over alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs. 2-fold decrease in inhibitory potency on alpha-3-beta-4/CHRNA3-CHRNB4 and loss of activity on alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs, respectively. 1 Publication1
Mutagenesisi32M → A: Complete loss in inhibitory potency on both alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs. 1 Publication1
Mutagenesisi32M → E, K, Q or R: Complete loss in inhibitory potency on both alpha-3-beta-4/CHRNA3-CHRNB4 nAChRs. 1 Publication1
Mutagenesisi32M → I: 21-fold and 1.5-fold decrease in inhibitory potency on alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs, respectively. 1 Publication1
Mutagenesisi32M → L or V: Important decrease in inhibitory potency on alpha-3-beta-4/CHRNA3-CHRNB4. 1 Publication1
Mutagenesisi33S → A: 5-fold and 1.2-fold decrease in inhibitory potency on alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs, respectively. 1 Publication1
Mutagenesisi34P → A: Complete loss in inhibitory potency on both alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs. 1 Publication1
Mutagenesisi35I → A: 4.4-fold and 1.3-fold decrease in inhibitory potency on alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4 nAChRs, respectively. 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 <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_0000439430‹1 – 21CuratedAdd BLAST›21
<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_000043943122 – 36Alpha-conotoxin TxID1 PublicationAdd BLAST15

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 bondi23 ↔ 291 PublicationImported
Disulfide bondi24 ↔ 361 PublicationImported
<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 residuei36Cysteine 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

Unmodified Met-32 is essential for toxin binding to rat alpha-3-beta-4/CHRNA3-CHRNB4 nAChR. An oxidation of this methionine provokes a 13.3-fold decrease in inhibitory potency (IC50=245 nM instead of 18 nM). Owing to its potent activity, derivatives of this toxin have a potential in the development of a novel drug. Unfortunately, the oxidation of the methionine is readily to happen during toxin synthesis and oxidation steps as well as under oxidative environment in vivo, which should still be considered to find a solution to this major drawback.1 Publication

Keywords - PTMi

Amidation, 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

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
2M3INMR-A16-30[»]

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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 cysteine framework is I (CC-C-C). Alpha4/6 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

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

Pfam protein domain database

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Pfami
View protein in Pfam
PF07365 Toxin_8, 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: Fragment.

<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.

K8DWB5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30 
FDGRNAAGND KMSALMALTT RGCCSHPVCS AMSPICG
Length:37
Mass (Da):3,774
Last modified:February 6, 2013 - 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:i066ED035FF4B52F6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei11

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
HF543950 Genomic DNA Translation: CCN27219.1

<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
HF543950 Genomic DNA Translation: CCN27219.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M3INMR-A16-30[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiView protein in InterPro
IPR009958 Conotoxin_a-typ
PfamiView protein in Pfam
PF07365 Toxin_8, 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 nameiCA1D_CONTE
<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: K8DWB5
<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 12, 2017
Last sequence update: February 6, 2013
Last modified: February 13, 2019
This is version 22 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

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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