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UniProtKB - P18640 (BXC_CBCP)

Entry version 172 (29 Sep 2021)
Sequence version 3 (18 Jul 2018)
Previous versions | rss
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Protein

Botulinum neurotoxin type C

Gene
N/A
Organism
Clostridium botulinum C phage (Clostridium botulinum C bacteriophage)
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

Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure (PubMed:16252491, PubMed:7901002, PubMed:8611567).

Is unique among characterized BoNTs in having 2 substrates, syntaxin (STX) and SNAP25 (PubMed:7901002, PubMed:7737992, PubMed:8611567, PubMed:9886085, PubMed:17718519).

Precursor of botulinum neurotoxin C which unlike most BoNTs seems not to have a proteinaceous coreceptor, and instead recognizes 2 different complex polysialylated gangliosides found on neural tissue probably found in synaptic vesicles (PubMed:21483489, PubMed:23027864).

Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the heavy chain (HC) forms pores that allows the light chain (LC) to translocate into the cytosol (By similarity).

Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release (By similarity).

In vitro the whole toxin only has protease activity after reduction (PubMed:8611567).

Electrical stimulation increases uptake of toxin, presumably by transiently exposing a receptor usually found in eukaryotic target synaptic vesicles (PubMed:19650874).

Forms ion-conducting channels at around pH 6.1 (PubMed:2424493).

Requires complex eukaryotic host polysialogangliosides for full neurotoxicity (PubMed:19650874, PubMed:21483489).

Synaptic vesicle glycoproteins (SV2) do not seem to act as its receptor (PubMed:21483489).

By similarity2 Publications8 Publications

Has proteolytic activity. After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that cleaves syntaxin-1A/STX1A and syntaxin-1B/STX1B (PubMed:7901002, PubMed:7737992, PubMed:8611567).

Cleaves the '253-Arg-|-Ala-254' bond of STX1 and the '252-Arg-|-Ala-253' bond of STX2; also acts on syntaxin 3 (STX3) but not 4 (STX4) (PubMed:7737992).

Cleaves the '198-Arg-|-Ala-199' bond of SNAP25 (PubMed:8611567, PubMed:9886085, PubMed:17718519).

Recognizes the '93-Asn--Met-202' region of SNAP25 (PubMed:9886085).

5 Publications

Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into eukaryotic host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The RBD is responsible for the adherence of the toxin to the eukaryotic target cell surface. It simultaneously recognizes 2 polysialated gangliosides coreceptors in close proximity on host synaptic vesicles (PubMed:23027864, PubMed:21542861).

The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn2+ in the active site; it may also prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation (By similarity).

The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol (Probable). The C-terminal half of the HC (residues 864-1291) binds neurons in a dose-dependent manner (PubMed:20731382).

The C-terminal half of the HC (residues 863-1291) binds eukaryotic host gangliosides in the order GD1b > GT1b > GD1a > GM1a (PubMed:16115873, PubMed:20731382, PubMed:23027864, PubMed:19650874).

Has 2 ganglioside binding sites; Sia-1 prefers a sia7 sialic acid and sugars within the ganglioside (GD1b > GT1b), whereas GBP2 recognizes a sia5 sialic acid (GT1b and GD1a) (PubMed:23027864, PubMed:21542861).

Both sites are required for HC to enter neurons, acting via different gangliosides (PubMed:23027864).

This suggests that 2 gangliosides serve as toxin receptors (PubMed:16115873, PubMed:20731382, PubMed:21542861, PubMed:23027864).

Synaptic activity (depolarization with K+) increases uptake by neurons (PubMed:23027864).

Treatment of synaptosomes with proteinase K does not reduce HC binding, suggesting there is no protein receptor or it is protected from extracellular proteases (PubMed:16115873).

Decreases uptake and toxicity of whole BoNT/A, but also interferes with uptake of BoNT/E and BoNT/F (PubMed:19650874).

HC also binds phosphoinositides, which might play a role in membrane-binding (PubMed:22120109).

By similarity1 Publication6 Publications

Miscellaneous

There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C, D, E, F, and G; new subtypes are quite frequent. Types C and D can undergo domain swapping to create hybrid types.
Botulism poisoning is usually food-borne, either by ingesting toxin or bacterial-contaminated food, or less frequently by inhalation poisoning. In both cases the neurotoxin binds to the apical surface of epithelial cells in the gut or airway. Toxin undergoes receptor-mediated endocytosis (using a different receptor than on target nerve cells), transcytosis across the epithelial cells and release into the general circulation. Once in the general circulation it binds to its target cells.By similarity
Botulinum neurotoxin type C is synthesized by C strains of C.botulinum which carry the appropriate bacteriophage.4 Publications
Strain CB-19 was isolated from mink (PubMed:16252491). BoNT/C usually causes animal and avian botulism; it is less toxic to chicken than is BoNT/CD (PubMed:16115873). One case of human infant botulism caused by this serotype is known (PubMed:1978909).1 Publication2 Publications
This protein can also be encoded on a prophage.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+2 PublicationsNote: Binds 2 zinc ions per subunit (PubMed:7737992). The catalytic Zn2+ is bound by LC, the other Zn2+ must bind to another region (PubMed:17718519).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

1,10-phenanthroline, EDTA and partially captopril block cleavage of syntaxin in brain synaptosomes (PubMed:7901002, PubMed:7737992). Treatment of synaptosomes with a mild detergent also inhibits cleavage (PubMed:7737992). 1,10-phenanthroline partially antagonizes inhibitions of neurotransmitter release (PubMed:8611567).3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.391 min(-1), for isolated botulinum neurotoxin C light chain.1 Publication
  1. KM=18.6 µM for purified SNAP25 with isolated botulinum neurotoxin C light chain1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi229Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei230PROSITE-ProRule annotation1
Metal bindingi233Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi269Zinc; catalyticCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1119Ganglioside GD1a; GBP2 binding site1 Publication1
Binding sitei1146Ganglioside GD1b; Sia-1 binding siteCombined sources1 Publication1
Binding sitei1281Ganglioside GD1a; GBP2 binding site1 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionHydrolase, Metalloprotease, Neurotoxin, Protease, Toxin
Biological processVirulence
LigandLipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.24.69, 1462

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-5250971, Toxicity of botulinum toxin type C (botC)

Protein family/group databases

UniLectin database of carbohydrate-binding proteins

More...UniLectini		P18640

<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:
Botulinum neurotoxin type C
Short name:
BoNT/C
Alternative name(s):
Bontoxilysin-C1
Short name:
BoNT/C11 Publication
Botulinum neurotoxin type C1
Cleaved into the following 2 chains:
Botulinum neurotoxin C light chain (EC:3.4.24.691 Publication)
Short name:
LC
Botulinum neurotoxin C heavy chain
Short name:
HC
<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>OrganismiClostridium botulinum C phage (Clostridium botulinum C bacteriophage)
<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 identifieri12336 [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 lineageiViruses › Duplodnaviria › Heunggongvirae › Uroviricota › Caudoviricetes › Caudovirales › Siphoviridae ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiClostridium botulinum C [TaxID: 36828]

<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

<p>This subsection of the 'Pathology and Biotech' section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

Has been used to treat human idiopathic facial hemispasm and blepharospasm; improvement is seen in 2-3 days and the effects last up to 12-13 weeks, making it a viable option in BoNT/A non-responders (PubMed:9086464).1 Publication

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>Mutagenesisi1119Y → A: Receptor-binding domain (RBD) no longer binds eukaryotic gangliosides GD1a or GM1a, reduced GT1b binding, GD1b binding unaffected. RBD fragment enters neurons but does not compartmentalize normally; uptake is not stimulated by K(+). 1 Publication1
Mutagenesisi1126A → K: Receptor-binding domain (RBD) no longer binds eukaryotic gangliosides GM1a, GD1b, reduced binding of GD1a and GT1b. RBD fragment does not enter neurons; uptake is not stimulated by K(+). 1 Publication1
Mutagenesisi1146Y → A: Whole toxin has dramatically reduced toxicity. 1 Publication1
Mutagenesisi1179Y → S: Receptor-binding domain (RBD) has decreased binding to neurons. Greatly decreased binding to neurons; when associated with L-1258. Whole toxin has greatly decreased toxicity, even less toxic; when associated with L-1258. Decreased binding to mixed gangliosides, even less binding to mixed gangliosides; when associated with L-1258. 1 Publication1
Mutagenesisi1193H → A: No effect on receptor-binding domain (RBD) binding to eukaryotic gangliosides. 1 Publication1
Mutagenesisi1203L → F: Receptor-binding domain (RBD) has decreased binding to neurons. Whole toxin has greatly decreased toxicity. Decreased binding to mixed gangliosides. 1 Publication1
Mutagenesisi1258 – 1259WY → AA: Whole toxin has greatly decreased toxicity. 1 Publication2
Mutagenesisi1258W → A: Receptor-binding domain (RBD) has greatly reduced binding of ganglioside GD1b, no longer binds neurons. 1 Publication1
Mutagenesisi1258W → L: Receptor-binding domain (RBD) has decreased binding to neurons (Ref.16). Greatly decreased binding to neurons; when associated with S-1179. Whole toxin has greatly decreased toxicity, even less toxic; when associated with S-1179. Decreased binding to mixed gangliosides, even less binding to mixed gangliosides; when associated with S-1179. 2 Publications1
Mutagenesisi1281S → Y: Receptor-binding domain (RBD) has decreased binding to neurons. Whole toxin has decreased toxicity and decreased binding to mixed gangliosides. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB13898, Equine Botulinum Neurotoxin C Immune FAB2

<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%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00004449052 – 1291Botulinum neurotoxin type CAdd BLAST1290
ChainiPRO_00000292172 – 449Botulinum neurotoxin C light chainAdd BLAST448
ChainiPRO_0000029218450 – 1291Botulinum neurotoxin C heavy chainAdd BLAST842

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 bondi437 ↔ 453Interchain (between light and heavy chains)By similarityCurated

Keywords - PTMi

Disulfide bond

<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

Heterodimer; disulfide-linked heterodimer of a light chain (LC) and a heavy chain (HC) (PubMed:16252491). The LC has the proteolytic/pharmacological activity (PubMed:7901002, PubMed:7737992, PubMed:8611567). The N- and C-terminal of the HC mediate channel formation and toxin binding, respectively. Can also be purified in complex with a non-toxic component that is larger than the HC (PubMed:16252491, PubMed:7802661). The stoichiometry of the whole complex has been modeled as one BoNT/C, one NTNHA, three HA-70, six HA-33 and three HA-17 (By similarity).

By similarity5 Publications

<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

11291
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P18640

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		P18640

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni450 – 865Translocation domain (TD)By similarityAdd BLAST416
Regioni490 – 541BeltBy similarityAdd BLAST52
Regioni866 – 1093N-terminus of receptor binding domain (N-RBD)By similarityAdd BLAST228
Regioni1094 – 1291C-terminus of receptor binding domain (C-RBD)By similarityAdd BLAST198
Regioni1126 – 1129Ganglioside GD1b; Sia-1 binding siteCombined sources1 Publication4
Regioni1247 – 1250Ganglioside GD1a; GBP2 binding site1 Publication4
Regioni1269 – 1283Ganglioside-binding loop2 PublicationsAdd BLAST15

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1256 – 1258Host ganglioside-binding motifBy similarity1 Publication3

<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

Has proteolytic activity (PubMed:7901002, PubMed:7737992, PubMed:8611567, PubMed:9886085, PubMed:17718519).5 Publications
Has 3 functional domains; the translocation domain (TD) and the receptor-binding domain (RBD) which is further subdivided into N- and C-terminal domains (N-RBD and C-RBD). The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn2+ in the active site and may be a pseudosubstrate inhibitor which serves as an intramolecular chaperone for the LC prior to its translocation into the host cytosol. The RBD binds transiently exposed coreceptors on the host presynaptic cell membrane (By similarity). Binds phosphoinositides, which might play a role in membrane-binding (PubMed:22120109).By similarity1 Publication

<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 peptidase M27 family.Curated

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.1120.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000395, Bot/tetX_LC
IPR036248, Clostridium_toxin_transloc
IPR013320, ConA-like_dom_sf
IPR011065, Kunitz_inhibitor_STI-like_sf
IPR013104, Toxin_rcpt-bd_C
IPR012928, Toxin_rcpt-bd_N
IPR012500, Toxin_trans

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01742, Peptidase_M27, 1 hit
PF07951, Toxin_R_bind_C, 1 hit
PF07953, Toxin_R_bind_N, 1 hit
PF07952, Toxin_trans, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00760, BONTOXILYSIN

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49899, SSF49899, 1 hit
SSF50386, SSF50386, 1 hit
SSF58091, SSF58091, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00142, ZINC_PROTEASE, 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.

P18640-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPITINNFNY SDPVDNKNIL YLDTHLNTLA NEPEKAFRIT GNIWVIPDRF 
        60         70         80         90        100
SRNSNPNLNK PPRVTSPKSG YYDPNYLSTD SDKDTFLKEI IKLFKRINSR 
       110        120        130        140        150
EIGEELIYRL STDIPFPGNN NTPINTFDFD VDFNSVDVKT RQGNNWVKTG 
       160        170        180        190        200
SINPSVIITG PRENIIDPET STFKLTNNTF AAQEGFGALS IISISPRFML 
       210        220        230        240        250
TYSNATNDVG EGRFSKSEFC MDPILILMHE LNHAMHNLYG IAIPNDQTIS 
       260        270        280        290        300
SVTSNIFYSQ YNVKLEYAEI YAFGGPTIDL IPKSARKYFE EKALDYYRSI 
       310        320        330        340        350
AKRLNSITTA NPSSFNKYIG EYKQKLIRKY RFVVESSGEV TVNRNKFVEL 
       360        370        380        390        400
YNELTQIFTE FNYAKIYNVQ NRKIYLSNVY TPVTANILDD NVYDIQNGFN 
       410        420        430        440        450
IPKSNLNVLF MGQNLSRNPA LRKVNPENML YLFTKFCHKA IDGRSLYNKT 
       460        470        480        490        500
LDCRELLVKN TDLPFIGDIS DVKTDIFLRK DINEETEVIY YPDNVSVDQV 
       510        520        530        540        550
ILSKNTSEHG QLDLLYPSID SESEILPGEN QVFYDNRTQN VDYLNSYYYL 
       560        570        580        590        600
ESQKLSDNVE DFTFTRSIEE ALDNSAKVYT YFPTLANKVN AGVQGGLFLM 
       610        620        630        640        650
WANDVVEDFT TNILRKDTLD KISDVSAIIP YIGPALNISN SVRRGNFTEA 
       660        670        680        690        700
FAVTGVTILL EAFPEFTIPA LGAFVIYSKV QERNEIIKTI DNCLEQRIKR 
       710        720        730        740        750
WKDSYEWMMG TWLSRIITQF NNISYQMYDS LNYQAGAIKA KIDLEYKKYS 
       760        770        780        790        800
GSDKENIKSQ VENLKNSLDV KISEAMNNIN KFIRECSVTY LFKNMLPKVI 
       810        820        830        840        850
DELNEFDRNT KAKLINLIDS HNIILVGEVD KLKAKVNNSF QNTIPFNIFS 
       860        870        880        890        900
YTNNSLLKDI INEYFNNIND SKILSLQNRK NTLVDTSGYN AEVSEEGDVQ 
       910        920        930        940        950
LNPIFPFDFK LGSSGEDRGK VIVTQNENIV YNSMYESFSI SFWIRINKWV 
       960        970        980        990       1000
SNLPGYTIID SVKNNSGWSI GIISNFLVFT LKQNEDSEQS INFSYDISNN 
      1010       1020       1030       1040       1050
APGYNKWFFV TVTNNMMGNM KIYINGKLID TIKVKELTGI NFSKTITFEI 
      1060       1070       1080       1090       1100
NKIPDTGLIT SDSDNINMWI RDFYIFAKEL DGKDINILFN SLQYTNVVKD 
      1110       1120       1130       1140       1150
YWGNDLRYNK EYYMVNIDYL NRYMYANSRQ IVFNTRRNNN DFNEGYKIII 
      1160       1170       1180       1190       1200
KRIRGNTNDT RVRGGDILYF DMTINNKAYN LFMKNETMYA DNHSTEDIYA 
      1210       1220       1230       1240       1250
IGLREQTKDI NDNIIFQIQP MNNTYYYASQ IFKSNFNGEN ISGICSIGTY 
      1260       1270       1280       1290 
RFRLGGDWYR HNYLVPTVKQ GNYASLLEST STHWGFVPVS E
Length:1,291
Mass (Da):148,870
Last modified:July 18, 2018 - v3
<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:i4A21DB35B8743CF8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti85T → P in CAA37780 (PubMed:2204031).1

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
X66433 Genomic DNA Translation: CAA47060.1
X72793 Genomic DNA Translation: CAA51313.1
X53751 Genomic DNA Translation: CAA37780.1
D90210 Genomic DNA Translation: BAA14235.1
X62389 Genomic DNA Translation: CAA44263.1
AB200358 Genomic DNA Translation: BAD90566.1

NCBI Reference Sequences

More...RefSeqi		YP_398516.1, NC_007581.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3772941

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		vg:3772941

<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%5Freferences%5Fsection">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

BotDB - A Database Resource for Clostridial Neurotoxins

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66433 Genomic DNA Translation: CAA47060.1
X72793 Genomic DNA Translation: CAA51313.1
X53751 Genomic DNA Translation: CAA37780.1
D90210 Genomic DNA Translation: BAA14235.1
X62389 Genomic DNA Translation: CAA44263.1
AB200358 Genomic DNA Translation: BAD90566.1
RefSeqiYP_398516.1, NC_007581.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QN0X-ray1.75A1-427[»]
3DEBX-ray1.95A1-430[»]
3N7KX-ray2.50A/B866-1291[»]
3R4SX-ray2.15A/B867-1291[»]
3R4UX-ray2.20A/B867-1291[»]
SMRiP18640
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

DrugBankiDB13898, Equine Botulinum Neurotoxin C Immune FAB2

Protein family/group databases

UniLectiniP18640

Genome annotation databases

GeneIDi3772941
KEGGivg:3772941

Enzyme and pathway databases

BRENDAi3.4.24.69, 1462
ReactomeiR-HSA-5250971, Toxicity of botulinum toxin type C (botC)

Miscellaneous databases

EvolutionaryTraceiP18640

Family and domain databases

Gene3Di1.20.1120.10, 1 hit
InterProiView protein in InterPro
IPR000395, Bot/tetX_LC
IPR036248, Clostridium_toxin_transloc
IPR013320, ConA-like_dom_sf
IPR011065, Kunitz_inhibitor_STI-like_sf
IPR013104, Toxin_rcpt-bd_C
IPR012928, Toxin_rcpt-bd_N
IPR012500, Toxin_trans
PfamiView protein in Pfam
PF01742, Peptidase_M27, 1 hit
PF07951, Toxin_R_bind_C, 1 hit
PF07953, Toxin_R_bind_N, 1 hit
PF07952, Toxin_trans, 1 hit
PRINTSiPR00760, BONTOXILYSIN
SUPFAMiSSF49899, SSF49899, 1 hit
SSF50386, SSF50386, 1 hit
SSF58091, SSF58091, 1 hit
PROSITEiView protein in PROSITE
PS00142, ZINC_PROTEASE, 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 nameiBXC_CBCP
<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: P18640
<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: November 1, 1990
Last sequence update: July 18, 2018
Last modified: September 29, 2021
This is version 172 of the entry and version 3 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 programViral 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 sequencing, Pharmaceutical

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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