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UniProtKB - P01391 (3L21_NAJKA)
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>sp|P01391|3L21_NAJKA Alpha-cobratoxin OS=Naja kaouthia OX=8649 PE=1 SV=1 IRCFITPDITSKDCPNGHVCYTKTWCDAFCSIRGKRVDLGCAATCPTVKTGVDIQCCSTD NCNPFPTRKRPCommunity curation ()Add a publicationFeedback
Protein
Alpha-cobratoxin
Gene
N/A
Organism
Naja kaouthia (Monocled cobra) (Naja siamensis)
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>Select a section on the left to see content.
<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
Monomer: binds with high affinity to muscular (alpha-1-beta-1-gamma-delta/CHRNA1-CHRNB1-CHRNG-CHRND) nAChR (tested on Torpedo californica, Kd=0.2-4.5 nM) and neuronal alpha-7/CHRNA7 nicotinic acetylcholine receptors (Kd=13-105 nM) (PubMed:18381281, PubMed:9305882, PubMed:22223648).
Also inhibits GABA(A) channels (PubMed:26221036).
Heteropentamer targets studied are composed of alpha-1-beta-3-gamma-2 (GABRA1-GABRB3-GABRG2) subunits (IC50=236 nM), alpha-1-beta-2-gamma-2 (GABRA1-GABRB2-GABRG2) subunits (IC50=469 nM), alpha-2-beta-2-gamma-2 (GABRA2-GABRB2-GABRG2) subunits (IC50=485 nM), alpha-5-beta-3-gamma-2 (GABRA5-GABRB3-GABRG2) subunits (IC50=635 nM), and alpha-2-beta-3-gamma-2 (GABRA2-GABRB3-GABRG2) subunits (IC50=1099 nM) (activated by 10 µM GABA) (PubMed:26221036).
4 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Naturally occurring disulfide-bound dimers of three-fingered toxins: a paradigm for biological activity diversification."
Osipov A.V., Kasheverov I.E., Makarova Y.V., Starkov V.G., Vorontsova O.V., Ziganshin R.K., Andreeva T.V., Serebryakova M.V., Benoit A., Hogg R.C., Bertrand D., Tsetlin V.I., Utkin Y.N.
J. Biol. Chem. 283:14571-14580(2008) [PubMed] [Europe PMC] [Abstract] - Ref.11"Neurotoxins from snake venoms and alpha-conotoxin ImI inhibit functionally active ionotropic gamma-aminobutyric acid (GABA) receptors."
Kudryavtsev D.S., Shelukhina I.V., Son L.V., Ojomoko L.O., Kryukova E.V., Lyukmanova E.N., Zhmak M.N., Dolgikh D.A., Ivanov I.A., Kasheverov I.E., Starkov V.G., Ramerstorfer J., Sieghart W., Tsetlin V.I., Utkin Y.N.
J. Biol. Chem. 290:22747-22758(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.12"Species specificity of rat and human alpha7 nicotinic acetylcholine receptors towards different classes of peptide and protein antagonists."
Yu J., Zhu X., Zhang L., Kudryavtsev D., Kasheverov I., Lei Y., Zhangsun D., Tsetlin V., Luo S.
Neuropharmacology 139:226-237(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION ON ALPHA-7/CHRNA7 NACHR, SYNTHESIS. - Ref.21"Dimeric alpha-cobratoxin X-ray structure: localization of intermolecular disulfides and possible mode of binding to nicotinic acetylcholine receptors."
Osipov A.V., Rucktooa P., Kasheverov I.E., Filkin S.Y., Starkov V.G., Andreeva T.V., Sixma T.K., Bertrand D., Utkin Y.N., Tsetlin V.I.
J. Biol. Chem. 287:6725-6734(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), DISULFIDE BOND (HOMODIMER), FUNCTION, SUBUNIT.
Homodimer: binds with high affinity (but lower than the monomeric form) to muscular (IC50=9.7 nM) and with low affinity to neuronal alpha-7/CHRNA7 nAChRs (IC50=1370 nM) (PubMed:22223648).
However, it acquires (compared to the monomeric form) the capacity to block alpha-3/beta-2 (CHRNA3/CHRNB2) nAChRs (PubMed:18381281).
2 PublicationsManual assertion based on experiment ini
- Ref.2"Naturally occurring disulfide-bound dimers of three-fingered toxins: a paradigm for biological activity diversification."
Osipov A.V., Kasheverov I.E., Makarova Y.V., Starkov V.G., Vorontsova O.V., Ziganshin R.K., Andreeva T.V., Serebryakova M.V., Benoit A., Hogg R.C., Bertrand D., Tsetlin V.I., Utkin Y.N.
J. Biol. Chem. 283:14571-14580(2008) [PubMed] [Europe PMC] [Abstract] - Ref.21"Dimeric alpha-cobratoxin X-ray structure: localization of intermolecular disulfides and possible mode of binding to nicotinic acetylcholine receptors."
Osipov A.V., Rucktooa P., Kasheverov I.E., Filkin S.Y., Starkov V.G., Andreeva T.V., Sixma T.K., Bertrand D., Utkin Y.N., Tsetlin V.I.
J. Biol. Chem. 287:6725-6734(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), DISULFIDE BOND (HOMODIMER), FUNCTION, SUBUNIT.
Heterodimer with cytotoxin 3 (AC P01446): is slightly more active than the homodimer in inhibiting alpha-7/CHRNA7 nAChR and is considerably more active in blocking the alpha-3-beta-2/CHRNA3-CHRNB2 nAChR.
1 PublicationManual assertion based on experiment ini
- Ref.21"Dimeric alpha-cobratoxin X-ray structure: localization of intermolecular disulfides and possible mode of binding to nicotinic acetylcholine receptors."
Osipov A.V., Rucktooa P., Kasheverov I.E., Filkin S.Y., Starkov V.G., Andreeva T.V., Sixma T.K., Bertrand D., Utkin Y.N., Tsetlin V.I.
J. Biol. Chem. 287:6725-6734(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), DISULFIDE BOND (HOMODIMER), FUNCTION, SUBUNIT.
Miscellaneous
The monomeric form has no effect on alpha-3/beta-2 (CHRNA3/CHRNB2) nAChR (PubMed:18381281). It does not show any blockade of the nicotine-evoked release of dopamine (PubMed:9840221) and does not affect ACh release.2 Publications
Manual assertion based on experiment ini
- Ref.2"Naturally occurring disulfide-bound dimers of three-fingered toxins: a paradigm for biological activity diversification."
Osipov A.V., Kasheverov I.E., Makarova Y.V., Starkov V.G., Vorontsova O.V., Ziganshin R.K., Andreeva T.V., Serebryakova M.V., Benoit A., Hogg R.C., Bertrand D., Tsetlin V.I., Utkin Y.N.
J. Biol. Chem. 283:14571-14580(2008) [PubMed] [Europe PMC] [Abstract] - Ref.8"Effects of alpha-erabutoxin, alpha-bungarotoxin, alpha-cobratoxin and fasciculin on the nicotine-evoked release of dopamine in the rat striatum in vivo."
Dajas-Bailador F., Costa G., Dajas F., Emmett S.
Neurochem. Int. 33:307-312(1998) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.
Exists in two forms, due to cis-trans isomerization at 6-Thr-Pro-7 (Probable). In the dimeric form, the Pro-7 is extended away from the toxin core whereas in the monomeric form, Pro-7 makes a turn (PubMed:22223648).Curated1 Publication
Manual assertion based on experiment ini
- Ref.21"Dimeric alpha-cobratoxin X-ray structure: localization of intermolecular disulfides and possible mode of binding to nicotinic acetylcholine receptors."
Osipov A.V., Rucktooa P., Kasheverov I.E., Filkin S.Y., Starkov V.G., Andreeva T.V., Sixma T.K., Bertrand D., Utkin Y.N., Tsetlin V.I.
J. Biol. Chem. 287:6725-6734(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), DISULFIDE BOND (HOMODIMER), FUNCTION, SUBUNIT.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Sitei | 23 | Binds to Torpedo AChR1 Publication Manual assertion based on experiment ini
| 1 | |
| Sitei | 25 | Binds to both neuronal alpha-7/CHRNA7 and Torpedo AChRs2 Publications Manual assertion based on experiment ini
| 1 | |
| Sitei | 27 | Binds to both neuronal alpha-7/CHRNA7 and Torpedo AChRs2 Publications Manual assertion based on experiment ini
| 1 | |
| Sitei | 28 | Binds to alpha-7/CHRNA7 AChR1 Publication Manual assertion based on experiment ini
| 1 | |
| Sitei | 29 | Binds to both neuronal alpha-7/CHRNA7 and Torpedo AChRs2 Publications Manual assertion based on experiment ini
| 1 | |
| Sitei | 33 | Binds to both neuronal alpha-7/CHRNA7 and Torpedo AChRs2 Publications Manual assertion based on experiment ini
| 1 | |
| Sitei | 35 | Binds to alpha-7/CHRNA7 AChR1 Publication Manual assertion based on experiment ini
| 1 | |
| Sitei | 36 | Binds to both neuronal alpha-7/CHRNA7 and Torpedo AChRs, may be important for inhibition of GABA(A) receptors1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| 1 | |
| Sitei | 49 | Binds to Torpedo AChR1 Publication Manual assertion based on experiment ini
| 1 | |
| Sitei | 65 | Binds to both neuronal alpha-7/CHRNA7 and Torpedo AChRs2 Publications Manual assertion based on experiment ini
| 1 |
<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
- acetylcholine receptor inhibitor activity Source: UniProtKB-KW
- ion channel regulator activity Source: UniProtKB-KW
- toxin activity Source: UniProtKB-KW
<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 function | Acetylcholine 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-cobratoxin7 Publications<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Short name: Alpha-CT2 Publications Manual assertion based on opinion ini
Short name: Alpha-CbT1 Publication Manual assertion based on opinion ini
Short name: Alpha-Cbtx6 Publications Manual assertion based on opinion ini
Short name: Alpha-CtxCurated Alternative name(s): Alpha-elapitoxin-Nk2aCurated Short name: Alpha-EPTX-Nk2aCurated Long neurotoxin 1 Siamensis 31 Publication Manual assertion based on opinion ini
|
| <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>Organismi | Naja kaouthia (Monocled cobra) (Naja siamensis) |
| <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 identifieri | 8649 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Sauropsida › Sauria › Lepidosauria › Squamata › Bifurcata › Unidentata › Episquamata › Toxicofera › Serpentes › Colubroidea › Elapidae › Elapinae › Naja |
<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
- Secreted 1 Publication
Manual assertion based on experiment ini
- Ref.1Cited for: PROTEIN SEQUENCE, SUBCELLULAR LOCATION.
- Secreted 1 Publication
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Mutagenesisi | 23 | K → E: 2-fold and 28-fold decrease in affinity for Torpedo AChRs. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 25 | W → A: 11-fold decrease in affinity for Torpedo AChRs and 6-fold decrease in affinity for neuronal alpha-7/CHRNA7 AChR. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 27 | D → R: 31-fold decrease in affinity for Torpedo AChRs and 50-fold decrease in affinity for neuronal alpha-7/CHRNA7 AChR. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 28 | A → G: 5-fold decrease in affinity for neuronal alpha-7/CHRNA7 AChR. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 29 | F → A: 12-fold decrease in affinity for Torpedo AChRs and 74-fold decrease in affinity for neuronal alpha-7/CHRNA7 AChR. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 33 | R → E: 767-fold decrease in affinity for Torpedo AChRs and 339-fold decrease in affinity for neuronal alpha-7/CHRNA7 AChR. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 35 | K → A: 11-fold decrease in affinity for neuronal alpha-7/CHRNA7 AChR. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 36 | R → A: 16-fold decrease in affinity for Torpedo AChRs. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 49 | K → E: 3-fold and 53-fold decrease in affinity for Torpedo AChRs. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 65 | F → A: 7-fold decrease in affinity for Torpedo AChRs and 15-fold decrease in affinity for neuronal alpha-7/CHRNA7 AChR. 2 Publications Manual assertion based on experiment ini
| 1 |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000093554 | 1 – 71 | Alpha-cobratoxin1 Publication Manual assertion based on experiment ini
| 71 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 bondi | 3 ↔ 20 | In monomer, partialCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 6 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 3 | Interchain (with C-20); in homodimer; partialCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 14 ↔ 41 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 7 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 20 | Interchain (with C-3); in homodimer; partialCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 26 ↔ 30 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 7 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 45 ↔ 56 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 7 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 57 ↔ 62 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 7 PublicationsManual assertion based on experiment ini
|
<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
In homodimer alpha-cobratoxin, selective reduction of Cys(26)-Cys(30) in one subunit does not affect the activity against the alpha-7/CHRNA7 nAChR, whereas its reduction in both subunits almost prevents alpha-7/CHRNA7 nAChR recognition. On the contrary, reduction of one or both Cys(26)-Cys(30) disulfide bonds in the homodimer considerably potentiates inhibition of the alpha-3-beta-2/CHRNA3-CHRNB2 nAChR by the toxin.1 Publication
Manual assertion based on experiment ini
- Ref.21"Dimeric alpha-cobratoxin X-ray structure: localization of intermolecular disulfides and possible mode of binding to nicotinic acetylcholine receptors."
Osipov A.V., Rucktooa P., Kasheverov I.E., Filkin S.Y., Starkov V.G., Andreeva T.V., Sixma T.K., Bertrand D., Utkin Y.N., Tsetlin V.I.
J. Biol. Chem. 287:6725-6734(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), DISULFIDE BOND (HOMODIMER), FUNCTION, SUBUNIT.
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 gland.Curated
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Monomer, homo- or heterodimer with cytotoxins 1 (P60305), 2 (AC P01445), and 3 (AC P01446); disulfide-linked.
8 PublicationsManual assertion based on experiment ini
- Ref.2"Naturally occurring disulfide-bound dimers of three-fingered toxins: a paradigm for biological activity diversification."
Osipov A.V., Kasheverov I.E., Makarova Y.V., Starkov V.G., Vorontsova O.V., Ziganshin R.K., Andreeva T.V., Serebryakova M.V., Benoit A., Hogg R.C., Bertrand D., Tsetlin V.I., Utkin Y.N.
J. Biol. Chem. 283:14571-14580(2008) [PubMed] [Europe PMC] [Abstract] - Ref.14"Three-dimensional structure of the 'long' neurotoxin from cobra venom."
Walkinshaw M.D., Saenger W., Maelicke A.
Proc. Natl. Acad. Sci. U.S.A. 77:2400-2404(1980) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS. - Ref.15"The refined crystal structure of alpha-cobratoxin from Naja naja siamensis at 2.4-A resolution."
Betzel C., Lange G., Pal G.P., Wilson K.S., Maelicke A., Saenger W.
J. Biol. Chem. 266:21530-21536(1991) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), DISULFIDE BONDS. - Ref.16"Rapid determination and NMR assignments of antiparallel sheets and helices of a scorpion and a cobra toxin."
Laplante S.R., Mikou A., Robin M., Guittet E., Delsuc M.-A., Charpentier I., Lallemand J.-Y.
Int. J. Pept. Protein Res. 36:227-230(1990) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR, DISULFIDE BONDS. - Ref.17"Alpha-cobratoxin: proton NMR assignments and solution structure."
le Goas R., Laplante S.R., Mikou A., Delsuc M.-A., Guittet E., Robin M., Charpentier I., Lallemand J.-Y.
Biochemistry 31:4867-4875(1992) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR, DISULFIDE BONDS. - Ref.18"NMR-based binding screen and structural analysis of the complex formed between alpha-cobratoxin and an 18-mer cognate peptide derived from the alpha-1 subunit of the nicotinic acetylcholine receptor from Torpedo californica."
Zeng H., Hawrot E.
J. Biol. Chem. 277:37439-37445(2002) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR, DISULFIDE BONDS. - Ref.19"Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors."
Bourne Y., Talley T.T., Hansen S.B., Taylor P., Marchot P.
EMBO J. 24:1512-1522(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS), DISULFIDE BONDS. - Ref.21"Dimeric alpha-cobratoxin X-ray structure: localization of intermolecular disulfides and possible mode of binding to nicotinic acetylcholine receptors."
Osipov A.V., Rucktooa P., Kasheverov I.E., Filkin S.Y., Starkov V.G., Andreeva T.V., Sixma T.K., Bertrand D., Utkin Y.N., Tsetlin V.I.
J. Biol. Chem. 287:6725-6734(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), DISULFIDE BOND (HOMODIMER), FUNCTION, SUBUNIT.
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 2 – 4 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 10 – 13 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 19 – 25 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 27 – 29 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 30 – 33 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 36 – 44 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 52 – 57 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 59 – 63 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 |
3D structure databases
AlphaFold Protein Structure Database More...AlphaFoldDBi | P01391 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P01391 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P01391 |
<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 information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily.Curated
Family and domain databases
Conserved Domains Database More...CDDi | cd00206, snake_toxin, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.10.60.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR003571, Snake_3FTx IPR045860, Snake_toxin-like_sf IPR018354, Snake_toxin_con_site |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF57302, SSF57302, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00272, SNAKE_TOXIN, 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.
P01391-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
IRCFITPDIT SKDCPNGHVC YTKTWCDAFC SIRGKRVDLG CAATCPTVKT
60 70
GVDIQCCSTD NCNPFPTRKR P
Length:71
Mass (Da):7,831
Last modified:July 21, 1986 - 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:i6F07ADD885E9AC33
Sequence databases
Protein sequence database of the Protein Information Resource More...PIRi | A01662, N2NJ1S |
<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
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P01391 | Long neurotoxin 2 | 71 | UniRef90_P01391 | |||
| Long neurotoxin 3 | ) | 71 | ||||
| Long neurotoxin 4 | 71 | |||||
| Long neurotoxin 1 | 71 | |||||
| Long neurotoxin 5 | 71 | |||||
| +1 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P01391 | Long neurotoxin 3 | ) | 71 | UniRef50_P01391 | ||
| Alpha-elapitoxin-Djk2a | 72 | |||||
| Long neurotoxin 3 | 73 | |||||
| Long neurotoxin 1 | 71 | |||||
| Long neurotoxin Tx-NM3-1 | 71 | |||||
| +29 | ||||||
<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
| PIRi | A01662, N2NJ1S |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1CTX | X-ray | 2.80 | A | 1-71 | [»] | |
| 1LXG | NMR | - | A | 1-71 | [»] | |
| 1LXH | NMR | - | A | 1-71 | [»] | |
| 1YI5 | X-ray | 4.20 | F/G/H/I/J | 1-71 | [»] | |
| 4AEA | X-ray | 1.94 | A/B | 1-71 | [»] | |
| 6ZFM | X-ray | 1.90 | A/B/D/E | 1-71 | [»] | |
| AlphaFoldDBi | P01391 | |||||
| SMRi | P01391 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Miscellaneous databases
| EvolutionaryTracei | P01391 |
Family and domain databases
| CDDi | cd00206, snake_toxin, 1 hit |
| Gene3Di | 2.10.60.10, 1 hit |
| InterProi | View protein in InterPro IPR003571, Snake_3FTx IPR045860, Snake_toxin-like_sf IPR018354, Snake_toxin_con_site |
| SUPFAMi | SSF57302, SSF57302, 1 hit |
| PROSITEi | View protein in PROSITE PS00272, SNAKE_TOXIN, 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 namei | 3L21_NAJKA | |
| <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>Accessioni | P01391Primary (citable) accession number: P01391 | |
| <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 historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
| Last sequence update: | July 21, 1986 | |
| Last modified: | May 25, 2022 | |
| This is version 129 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Animal Toxin Annotation Program | |
| Annotation program | Chordata Protein 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 sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
