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Entry version 23 (25 May 2022)
Sequence version 1 (11 Jun 2014)
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Protein

Alpha-conotoxin GI

Gene
N/A
Organism
Conus geographus (Geography cone) (Nubecula geographus)
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. Both globular (with C1-C3; C2-C4 disulfide pattern) and ribbon (C1-C4; C2-C3) isomers reversibly inhibit mammalian muscle-type alpha-1-beta-1-delta-epsilon/CHRNA1-CHRNB1-CHRND-CHRNE nAChRs (IC50=5.86-19.9 nM and IC50=701 nM, respectively) (PubMed:30551685, PubMed:34062129).

The higher affinity site is the alpha/delta site on mouse muscle-derived BC3H-1 receptor, and the other site (alpha/gamma site) on nicotinic receptors from Torpedo californica electric organ (PubMed:7623764).

Miscellaneous

Both globular (with C1-C3; C2-C4 disulfide pattern) and ribbon (C1-C4; C2-C3) isomers show no or very weak inhibitory activity on alpha-3-beta-2/CHRNA3-CHRNB2, alpha-3-beta-4/CHRNA3-CHRNB4, alpha-4-beta-2/CHRNA4-CHRNB2, alpha-7/CHRNA7, and alpha-9-alpha-10/CHRNA9-CHRNA10.2 Publications
This toxin is a substrate for a cone snail multienzyme complex that regulates its folding and assembly. This complex is composed of protein-disulfide isomerase (PDI), peptidyl-prolyl cis-trans isomerase (PPI) and immunoglobulin-binding protein (BiP). PDI catalyzes the oxidation and reduction of disulfide bonds. Oxidative folding rates are further increased in the presence of PPI with the maximum effect observed in the presence of both enzymes. In contrast, BiP is only observed to assist folding in the presence of microsomes, suggesting that additional cofactors are involved. This toxin has been only observed in the globular form (disulfide pattern C1-C3 and C2-C4).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei60Key residue that binds to three hydrophobic amino acids of the delta subunit of muscle-type acetylcholine receptor1 Publication1

<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%5Fand%5Ftaxonomy%5Fsection">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 GI1 Publication
Alternative name(s):
G1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 geographus (Geography cone) (Nubecula geographus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri6491 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaSpiraliaLophotrochozoaMolluscaGastropodaCaenogastropodaNeogastropodaConoideaConidaeConusGastridium

Organism-specific databases

ConoServer: Cone snail toxin database

More...
ConoServeri
74, GI
22, GIA

<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

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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi50E → A: 3-fold increase in inhibitory potency towards mouse muscle-type acetylcholine receptor. No increase in inhibitory potency towards alpha-3-beta-2/CHRNA3-CHRNB2, alpha-3-beta-4/CHRNA3-CHRNB4, alpha-4-beta-4/CHRNA4-CHRNB4, alpha-7/CHRNA7, and alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs. 1 Publication1
Mutagenesisi53N → A: No significant change in inhibitory potency towards mouse muscle-type acetylcholine receptor. 1 Publication1
Mutagenesisi54P → A: 10-fold decrease in inhibitory potency towards mouse muscle-type acetylcholine receptor. 2-fold increase in inhibitory potency towards rat alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs. No increase in inhibitory potency towards alpha-3-beta-2/CHRNA3-CHRNB2, alpha-3-beta-4/CHRNA3-CHRNB4, alpha-4-beta-4/CHRNA4-CHRNB4, and alpha-7/CHRNA7 nAChRs. 1 Publication1
Mutagenesisi57G → A: 30-fold decrease in inhibitory potency towards mouse muscle-type acetylcholine receptor. 2-fold increase in inhibitory potency towards rat alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs. No increase in inhibitory potency towards alpha-3-beta-2/CHRNA3-CHRNB2, alpha-3-beta-4/CHRNA3-CHRNB4, alpha-4-beta-4/CHRNA4-CHRNB4, and alpha-7/CHRNA7 nAChRs. 1 Publication1
Mutagenesisi58R → A: 8.5-fold decrease in inhibitory potency towards mouse muscle-type acetylcholine receptor. No increase in inhibitory potency towards alpha-3-beta-2/CHRNA3-CHRNB2, alpha-3-beta-4/CHRNA3-CHRNB4, alpha-4-beta-4/CHRNA4-CHRNB4, alpha-7/CHRNA7, and alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs. Decrease in affinity for both alpha/delta and alpha/gamma sites on BC3H-50 receptors and loss of affinity for both alpha/delta and alpha/gamma sites on Torpedo receptors. 2 Publications1
Mutagenesisi59H → A: No significant change in inhibitory potency towards mouse muscle-type acetylcholine receptor. 1 Publication1
Mutagenesisi60Y → A: 65-fold decrease in inhibitory potency towards mouse muscle-type acetylcholine receptor. No increase in inhibitory potency towards alpha-3-beta-2/CHRNA3-CHRNB2, alpha-3-beta-4/CHRNA3-CHRNB4, alpha-4-beta-4/CHRNA4-CHRNB4, alpha-7/CHRNA7, and alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs. 1 Publication1
Mutagenesisi61S → A: No significant change in inhibitory potency towards mouse muscle-type acetylcholine receptor. 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 – 21Sequence analysisAdd BLAST21
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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_000045409422 – 491 PublicationAdd BLAST28
<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_000003487450 – 62Alpha-conotoxin GI1 PublicationAdd BLAST13

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 ↔ 569 Publications
Disulfide bondi52 ↔ 629 Publications
<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 residuei62Cysteine amide1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Not hydroxylated; hydroxylation, on a synthetic hydroxylated GI, improves its folding but impairs its activity against target receptors.

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, 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

Secondary structure

164
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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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 cysteine framework is I (CC-C-C). Alpha3/5 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

More...
InterProi
View protein in InterPro
IPR009958, Conotoxin_a-typ
IPR018072, Conotoxin_a-typ_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07365, Toxin_8, 1 hit

PROSITE; a protein domain and family database

More...
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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

X5I9Y2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGMRMMFTVF LLVVLATTVV SFPSERASDG RDDTAKDEGS DMDKLVEKKE
60
CCNPACGRHY SCGR
Length:64
Mass (Da):7,094
Last modified:June 11, 2014 - 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:iA15D550E4BA7E140
GO

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

More...
DDBJi
Links Updated
AB910809 mRNA Translation: BAO65577.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A01782, NTKNAG

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB910809 mRNA Translation: BAO65577.1
PIRiA01782, NTKNAG

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NOTX-ray1.20A50-62[»]
1QS3NMR-A51-61[»]
1XGANMR-A50-62[»]
1XGBNMR-A50-62[»]
1XGCNMR-A50-62[»]
2FR9NMR-A50-60[»]
2FRBNMR-A50-62[»]
ModBaseiSearch...
SWISS-MODEL-WorkspaceiSubmit a new modelling project...
PDBe-KBiSearch...

Organism-specific databases

ConoServeri74, GI
22, GIA

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

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 nameiCA1_CONGE
<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: X5I9Y2
Secondary accession number(s): P01519
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 23, 2022
Last sequence update: June 11, 2014
Last modified: May 25, 2022
This is version 23 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
  2. SIMILARITY comments
    Index of protein domains and families
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