{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0DPK1","uniProtkbId":"BXX_CLOBO","entryAudit":{"firstPublicDate":"2018-07-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-07-18","entryVersion":27,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Clostridium botulinum","taxonId":1491,"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Eubacteriales","Clostridiaceae","Clostridium","Clostridium botulinum group"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Botulinum neurotoxin type X"},"shortNames":[{"value":"BoNT/X"}]},"alternativeNames":[{"fullName":{"value":"Bontoxilysin-X"}}],"contains":[{"recommendedName":{"fullName":{"value":"Botulinum neurotoxin X light chain"},"shortNames":[{"value":"LC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28770820"}],"value":"3.4.24.69"}]}},{"recommendedName":{"fullName":{"value":"Botulinum neurotoxin X heavy chain"},"shortNames":[{"value":"HC"}]}}]},"genes":[{"orfNames":[{"value":"CBB2_0680"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28770820"}],"value":"Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin X which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. 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 HC forms pores that allows the light chain (LC) to translocate into the cytosol. 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). Artificially assembled BoNT/X cleaves synaptobrevin-2/VAMP2 and VAMP4 in cultured rat neurons and causes flaccid paralysis in mice (PubMed:28770820)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin type X"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28770820"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29540745"}],"value":"Has proteolytic activity. After translocation into the eukaryotic host cytosol, LC hydrolyzes the '66-Arg-|-Ala-67' bond in synaptobrevin-2/VAMP2, and the equivalent bonds in 'Arg-|-Ala' bonds in VAMP1 and VAMP3, thus blocking neurotransmitter release (PubMed:28770820). Has a wider target range than most BoNTs, as it also cleaves the '87-Arg-|-Ser-89' bond in VAMP4, the '40-Arg-|-Ser-41' bond in VAMP5 and the '173-Lys-|-Ser-174' bond in YKT6; whether these are physiologically relevant substrates is unknown (PubMed:28770820). BoNT/X is 10-fold more efficient than BoNT/B and 40-fold more efficient than TeTX on an artificial human VAMP1 substrate (PubMed:29540745)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin X light chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P10844"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28770820"}],"value":"Responsible for epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into 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 cell surface. It simultaneously recognizes 2 coreceptors; polysialated gangliosides and an unknown receptor protein in close proximity on host synaptic vesicles. The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) in the active site (By similarity). The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol (By similarity). Protein ligation of the RBD to the rest of the toxin (creates an artificial whole toxin) greatly increases VAMP2 degradation, and thus neuron uptake (PubMed:28770820)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin X heavy chain"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. 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The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) 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"}],"commentType":"DOMAIN","molecule":"Botulinum neurotoxin X heavy chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28770820"}],"value":"An interchain disulfide bond is required for toxin stability in an artificial construct with the light chain and translocation domain; which of Cys-461 or Cys-467 forms the disulfide bond with Cys-423 in vivo is unknown"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28770820"}],"value":"The inactive construct (Ala-360--363-Tyr) can be used to generate antibodies against this serotype. Additionally the enlarged substrate specificity can be used to understand the function of VAMP4, VAMP5 and YKT6"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28770820"}],"value":"There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C, D, E, F, and G; new subtypes are quite frequent. This toxin is not recognized or neutralized by any of the antisera against the standard serotypes (PubMed:28770820)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}],"value":"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"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8942019"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28770820"}],"value":"This strain was isolated from an infant botulism patient in Japan in 1996; toxicity of this strain is due to a type B neurotoxin (PubMed:8942019). This locus has includes a number of other genes usually associated with the botulinum neurotoxin cluster in Clostridia (p47, hemagglutinin genes and the OrfX cluster), which should permit the toxin to survive in a host. 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heart or respiratory failure (PubMed:15123599). Precursor of botulinum neurotoxin G which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles (PubMed:15123599). Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. 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 HC forms pores that allows the light chain (LC) to translocate into the cytosol. 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). Binds to host peripheral neuronal presynaptic membranes via synaptotagmins 1 and 2 (SYT1 and SYT2) (PubMed:15123599). Toxin binds to the membrane proximal extra-cytoplasmic region of SYT1 and SYT2 that is transiently exposed outside of cells during exocytosis; exogenous gangliosides do not enhance binding and subsequent uptake of toxin into host cells (PubMed:15123599). Toxin activity can be blocked by the appropriate synaptotagmin protein fragments in cell culture (PubMed:15123599)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin type G"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7910017"}],"value":"Has proteolytic activity. After translocation into the eukaryotic host cytosol acts as a zinc endopeptidase that cleaves synaptobrevins-1, -2 and -3 (also called VAMP1, VAMP2 and VAMP3) (PubMed:7910017). Hydrolyzes the '81-Ala-|-Ala-82' bond of VAMP2, and probably also the equivalent 'Ala-|-Ala' sites in VAMP1 and VAMP3 (PubMed:7910017). Has low activity on A.californica synaptobrevin and none on D.melanogaster synaptobrevin or cellubrevin, have a slightly different sequence (PubMed:7910017)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin G light chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15123599"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17185412"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19650874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20219474"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20507178"}],"value":"Responsible for host cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (N-RBD, C-RBD). The RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously recognizes 2 coreceptors; polysialated gangliosides and the receptor proteins SYT1 and SYT2 in close proximity on host synaptic vesicles (PubMed:17185412). The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) 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 (By similarity). Has 2 coreceptors; complex gangliosides found primarily on neural tissue and host synaptotagmin-1 and -2 (SYT1 and SYT2) which bind to separate sites at the tip of the HC (PubMed:17185412). HC alone binds to host receptors SYT1 and SYT2; C-RBD interacts with host SYT2 (PubMed:15123599). Has equal affinity for SYT1 and SYT2; gangliosides are not required for (or only very slightly improve) binding to a membrane-anchored receptor fragment (PubMed:17185412, PubMed:20219474). Has also been shown to only bind SYT1; the assay methods were different (PubMed:20507178). Binds ganglioside GT1b (PubMed:20507178). Significantly decreases uptake and toxicity of whole BoNT/B and BoNT/G (PubMed:19650874)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin G heavy chain"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.","ecNumber":"3.4.24.69","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7910017"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16008342"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16008342"}],"value":"Binds 1 zinc ion per subunit (PubMed:16008342)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15123599"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17185412"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20219474"}],"value":"Heterodimer; disulfide-linked heterodimer of a light chain (LC) and a heavy chain (HC). The LC has the proteolytic/pharmacological activity, while the N- and C-termini of the HC mediate channel formation and toxin binding, respectively. Interacts with host receptors synaptotagmin-1 and -2 (SYT1 and SYT2) (PubMed:15123599, PubMed:17185412, PubMed:20219474)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin type G","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"74236"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"4922309"}],"value":"Secreted","id":"SL-0243"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin G light chain","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"74236"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7910017"}],"value":"Host cytoplasm, host cytosol","id":"SL-0384"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin G heavy chain","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"74236"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}],"value":"Host synapse, host presynaptic cell membrane","id":"SL-0434"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}],"value":"Host cytoplasmic vesicle, host secretory vesicle, host synaptic vesicle membrane","id":"SL-0503"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7910017"}],"value":"Has protease activity (PubMed:7910017)"}],"commentType":"DOMAIN","molecule":"Botulinum neurotoxin G light chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20219474"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20507178"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7910017"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15123599"}],"value":"Has 3 functional domains. The translocation domain (TD) which probably forms membrane channels to allow light chain (LC) into the host cytosol (Probable). The C-terminal receptor-binding domain (RBD) has 2 further subdomains, N-RBD (Hcn) and C-RBD (Hcc) (PubMed:20219474, PubMed:20507178). The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) 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 (By similarity). The RBD binds transiently exposed coreceptors on the host presynaptic cell membrane (Probable)"}],"commentType":"DOMAIN","molecule":"Botulinum neurotoxin G heavy chain"},{"texts":[{"value":"There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C, D, E, F, and G; new subtypes are quite frequent"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}],"value":"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"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4922309"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"74236"},{"evidenceCode":"ECO:0000305","source":"Reference","id":"Ref.4"}],"value":"Type G toxin has been isolated from soil samples and human autopsy specimens but has not been clearly implicated as the cause of human paralytic illness or death (Ref.4). Strain 89 was isolated from soil in Mendoza province, Argentiana (PubMed:4922309). Administration of strain 89 toxin to mouse, chicken, guinea pig and rhesus monkeys causes botulism symptoms and in most cases death, while dog and sheep show no signs of botulism (PubMed:74236). In the original report 5-fold higher levels of toxin caused botulism and death in sheep (PubMed:4922309)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"4922309"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"74236"}],"value":"Trypsinization of purified toxin increases its toxicity, suggesting it is released as a single chain (PubMed:4922309, PubMed:74236)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the peptidase M27 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":1297,"modifier":"EXACT"}},"description":"Botulinum neurotoxin type 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ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":3,"DOMAIN":2,"MISCELLANEOUS":4,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":3,"Region":4,"Motif":1,"Active site":1,"Binding site":3,"Site":1,"Disulfide bond":1,"Mutagenesis":7,"Beta strand":51,"Turn":8,"Helix":19},"uniParcId":"UPI000016EA78"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q00496","secondaryAccessions":["Q45862"],"uniProtkbId":"BXE_CLOBO","entryAudit":{"firstPublicDate":"1993-07-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-01-23","entryVersion":192,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Clostridium botulinum","taxonId":1491,"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Eubacteriales","Clostridiaceae","Clostridium","Clostridium botulinum group"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Botulinum neurotoxin type E"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8408542"}],"value":"BoNT/E"}]},"alternativeNames":[{"fullName":{"value":"Bontoxilysin-E"}}],"contains":[{"recommendedName":{"fullName":{"value":"Botulinum neurotoxin E light chain"},"shortNames":[{"value":"LC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8243676"}],"value":"3.4.24.69"}]}},{"recommendedName":{"fullName":{"value":"Botulinum neurotoxin E heavy chain"},"shortNames":[{"value":"HC"}]}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1541280"}],"value":"botE"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18815274"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19476346"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19650874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22720883"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8294407"}],"value":"Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin E which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them (PubMed:19476346, PubMed:19650874). 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 HC forms pores that allows the light chain (LC) to translocate into the cytosol (PubMed:22720883). 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). Electrical stimulation increases uptake of toxin, probably by transiently exposing a receptor found in eukaryotic target synaptic vesicles (PubMed:19476346, PubMed:19650874). Uses the large lumenal domain of synaptic vesicle glycoproteins 2A and 2B (SV2A and SV2B) but not SV2C as receptor; an N-linked glycan of SV2 is essential for receptor function (PubMed:18815274, PubMed:19476346). Host cell gangliosides are also required for neurotoxin uptake and full toxicity (PubMed:18815274, PubMed:19650874). BoNT/E is a 'coincidence detector'; it requires simultaneous binding to coreceptor GT1b and low pH to transform into a membrane-bound, oligomeric channel (PubMed:22720883). Requires trypsinization and reduction before it can be used in assays in vitro (PubMed:8294407)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin type E"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15157097"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15938619"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17666397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8243676"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8294407"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9886085"}],"value":"Has proteolytic activity (PubMed:8243676, PubMed:8294407, PubMed:9886085). After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '180-Arg-|-Ile-181' bond in SNAP25 (PubMed:8243676, PubMed:8294407, PubMed:9886085). Hydrolyzes the '185-Arg-|-Ile-186' bond of mouse SNAP23, but not in human which has a different sequence (PubMed:9886085). Recognizes the '146-Met--Asp-186' region of SNAP25 (PubMed:9886085). The reaction mechanism probably has a nucleophilic water held in place by Glu-213 (PubMed:15157097, PubMed:15938619). Reduction of the interchain disulfide bond occurs in the host cytosol and probably prevents retrotranslocation into the synaptic vesicle (PubMed:17666397)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin E light chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10413679"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17666397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18815274"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19476346"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19650874"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17907800"}],"value":"Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol (PubMed:17666397). 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 cell surface (PubMed:10413679). It probably simultaneously recognizes 2 coreceptors; polysialated gangliosides and either of the receptor proteins SV2A and SV2B in close proximity on host synaptic vesicles (PubMed:18815274, PubMed:19476346, PubMed:19650874). The N-terminus of the TD wraps an extended belt around the perimeter of the light chain (LC), protecting Zn(2+) in the active site (PubMed:19118561). The belt may also prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation (PubMed:17907800). The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol (By similarity). Responsible for adherence of the toxin to the cell surface; HC alone prevents uptake of whole toxin by neural cells, and delays paralysis onset by 154% (PubMed:10413679). Significantly decreases uptake and toxicity of whole BoNT/E, but also interferes with uptake of BoNT/C; binds GT1b in vitro (PubMed:19650874). Binds to synaptic vesicle glycoproteins SV2A and SV2B which serve as coreceptors with gangliosides (PubMed:18815274, PubMed:19650874). Interaction with SV2 proteins requires SV2 glycosylation (PubMed:19476346). HC alone significantly decreases uptake and toxicity of whole BoNT/E (PubMed:19650874). HC is responsible for translocation of LC into the host cytosol; an intact disulfide bond between the 2 subunits is required for translocation, which is reduced upon contact with the host cytosol (PubMed:17666397)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin E heavy chain"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.","ecNumber":"3.4.24.69","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8243676"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8294407"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9886085"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1429690"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15157097"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15938619"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19118561"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1429690"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15157097"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15938619"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19118561"}],"value":"Binds 1 zinc ion per subunit (PubMed:1429690, PubMed:15157097, PubMed:15938619, PubMed:19118561)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8294407"}],"value":"Proteolysis of SNAP25 by whole toxin inhibited by dipicolinic acid, 1,10-phenanthroline and EDTA (PubMed:8294407)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":7.9,"unit":"uM","substrate":"purified SNAP25 with botulinum neurotoxin E light chain","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15938619"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15938619"}],"value":"kcat is 257 min(-1) with botulinum neurotoxin E light chain."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18815274"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19118561"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19476346"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19650874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22720883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4030755"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6353669"}],"value":"Heterodimer; disulfide-linked heterodimer of a light chain (LC) and a heavy chain (HC); cleavage occurs after bacterial export by host proteases (PubMed:19118561, PubMed:4030755, PubMed:6353669). The LC has the proteolytic/pharmacological activity, while the N- and C-terminal of the HC mediate channel formation and toxin binding, respectively. Oligomerizes in the presence of coreceptor ganglioside GT1b between pH 4.4 and 8.0; it might oligomerize on host cell surface (PubMed:22720883). Interacts with host synaptic vesicle glycoproteins SV2A and SV2B (PubMed:18815274, PubMed:19650874). HC interacts with a complex including at least host SV2 and synaptotagmin-1 (SYT1); copurification depends on glycosylation of SV2 (PubMed:19476346)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin type E","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22720883"}],"value":"At pH 4.4 in the presence of ganglioside GT1b, becomes a membrane-associated hydrophobic protein (PubMed:22720883)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8294407"}],"value":"Secreted","id":"SL-0243"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin E light chain","subcellularLocations":[{"location":{"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8243676"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8294407"}],"value":"Host cytoplasm, host cytosol","id":"SL-0384"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin E heavy chain","subcellularLocations":[{"location":{"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10413679"}],"value":"Host synapse, host presynaptic cell membrane","id":"SL-0434"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}],"value":"Host cytoplasmic vesicle, host secretory vesicle, host synaptic vesicle membrane","id":"SL-0503"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8243676"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8294407"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9886085"}],"value":"Has protease activity (PubMed:8243676, PubMed:8294407, PubMed:9886085)"}],"commentType":"DOMAIN","molecule":"Botulinum neurotoxin E light chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18815274"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19118561"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19476346"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19650874"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17907800"}],"value":"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) (PubMed:19118561). In BoNT/E the domains are arranged differently than BoNT/A and BoNT/B; in BoNT/E the LC and RBD are on the same side of the TD and are in contact, whereas in BoNT/A and BoNT/B the LC is separated from the RBD by the TD (PubMed:19118561). The putative transmembrane region is closer to the receptor-binding regions in this toxin, which may explain why it acts faster than BoNT/A and BoNT/B (PubMed:19118561). The N-terminus of the TD wraps an extended belt around the perimeter of the LC, partially protecting Zn(2+) in the active site (PubMed:19118561). The belt may be a pseudosubstrate inhibitor which serves as an intramolecular chaperone for the LC prior to its translocation into the host cytosol (PubMed:17907800). The RBD binds transiently exposed coreceptors on the host presynaptic cell membrane (PubMed:18815274, PubMed:19476346, PubMed:19650874)"}],"commentType":"DOMAIN","molecule":"Botulinum neurotoxin E heavy chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15938619"}],"value":"Double mutants Gln-213/Gln-336 or Gln-213/Ala-351 might be suitable as vaccine candiates (PubMed:15938619)"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"value":"There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C, D, E, F, and G; new subtypes are quite frequent"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}],"value":"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"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1431246"}],"value":"Types A, B and E are the most frequent cause of adult human foodborne botulism; type A is the most severe, while type E has the shortest incubation period (PubMed:1431246)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19118561"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4030755"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6353669"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8294407"}],"value":"Unlike botulinum neurotoxin type A, type E is released from bacteria as a single chain and cleaved by host proteases into the active dichain (PubMed:19118561, PubMed:4030755, PubMed:6353669, 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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:15394302, PubMed:7578132). Precursor of botulinum neurotoxin A which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins of synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. 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 HC forms pores that allows the light chain (LC) to translocate into the cytosol (PubMed:17666397, PubMed:19096517). 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. Toxin activity requires polysialylated gangliosides; GT1b supports activity better than GD1a (PubMed:12089155). Binds to host peripheral neuronal presynaptic membranes via the synaptic vesicle glycoproteins SV2A, SV2B and SV2C (PubMed:16543415). It binds directly to the largest lumenal (intravesicular) loop of SV2A, SV2B and SV2C that is transiently exposed outside of cells during exocytosis; gangliosides enhance binding (PubMed:16543415, PubMed:16545378, PubMed:18815274). Recognizes an N-linked glycan on SV2 proteins (PubMed:18815274, PubMed:27294781). May also use FGFR3 as a receptor (PubMed:23696738). Toxin uptake into neural cells requires stimulation (incubation with K(+) to stimulate receptor exposure) to be internalized by receptor-mediated endocytosis (PubMed:16543415, PubMed:19650874, PubMed:21632541, PubMed:21832053). Subsequently the toxin colocalizes with its receptor in host cells (PubMed:16543415, PubMed:19650874). Toxin uptake can be blocked by the appropriate SV2 protein fragments in cell culture (PubMed:16543415)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin type A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10694409"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11565902"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11700044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11827515"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15592454"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17666397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7578132"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8243676"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9886085"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19351593"}],"value":"Has proteolytic activity (PubMed:7578132). After translocation into the eukaryotic host cytosol LC hydrolyzes the '197-Gln-|-Arg-198' bond in SNAP25, blocking neurotransmitter release (PubMed:10694409, PubMed:11700044, PubMed:11827515, PubMed:19351593, PubMed:7578132, PubMed:8243676, PubMed:9886085). Recognizes the '146-Met--Gly-155' region of SNAP25, which confers substrate specificity (PubMed:15592454, PubMed:9886085). Hydrolyzes the '202-Thr-|-Arg-203' bond of mouse SNAP23, but not in human which has a different sequence (PubMed:9886085). Reduction of the interchain disulfide bond occurs in the host cytosol and probably prevents retrotranslocation into the synaptic vesicle (PubMed:17666397). Has slow (occurs over 4 weeks) autocatalytic cleavage, however it is not clear if this is physiologically relevant (PubMed:11565902)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin A light chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10413679"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14731268"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16545378"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17666397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18704164"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19096517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19161982"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19351593"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19650874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21106906"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22158863"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22363010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23471747"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24240280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27294781"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27313224"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27958736"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6694738"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17907800"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"2446925"}],"value":"Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of botulinum neurotoxin A light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD) (PubMed:19096517). The RBD is responsible for binding to host epithelial cells and transcytosis across them; this uses different receptors than those on nerve cells (PubMed:21106906). RBD is also responsible for adherence of toxin to host nerve cell surface; HC alone prevents uptake of whole toxin by neural cells, and delays paralysis onset by 75% (PubMed:10413679, PubMed:6694738). Isolated RBD also delays paralysis onset (PubMed:21106906). The N-terminus of the RBD binds to phosphatidylinositol, which might play a role in membrane-binding (PubMed:19161982). Binds to host protein receptor synaptic vesicle glycoproteins SV2A, SV2B and SV2C via lumenal loop 4 (PubMed:16545378, PubMed:19650874, PubMed:24240280, PubMed:27294781, PubMed:27313224, PubMed:6370252). Binding can be inhibited by protein fragments from either the HC or SV2C (PubMed:24240280). Isolated HC significantly decreases uptake and toxicity of whole BoNT/A, but also interferes with uptake of BoNT/E and to a lesser extent BoNT/F (PubMed:19650874). The RBD recognizes the N-linked glycan on 'Asn-559' of SV2A, SV2B and SV2C; hydrogen-bonding occurs via 10 well-defined water molecules and stacking of hydrophobic residues (PubMed:27294781). Binds one host GT1b ganglioside, which serves as a coreceptor (PubMed:14731268, PubMed:18704164, PubMed:27958736). Modeling shows the HC can bind both coreceptors (a ganglioside and SV2 protein) simultaneously at different sites (PubMed:24240280). Crystals of the RBD with a GT1b analog can be grown at pH 5.5, indicating the toxin-ganglioside complex could be stable within the endosome (PubMed:18704164). Isolated RBD binds NTNHA (a bacterial protein that protects toxin) with high affinity at pH 6.0 but not at pH 7.5 (PubMed:22363010). The N-terminal belt (residues 449-545) wraps around the perimeter of the LC, probably protecting Zn(2+) in the active site; it is not required for channel formation by the TD domain but may serve to prevent premature LC dissociation from the translocation channel and to protect toxin prior to translocation (PubMed:17907800, PubMed:19351593, PubMed:22158863). The isolated TD forms transmembrane channels of about 15 Angstroms in the absence of a pH gradient; LC translocation requires a pH and redox gradient (pH 5.0/oxidizing in the cis compartment, pH 7.0/reducing in the trans compartment), LC does not unfold unless the cis pH is 6.0 or less (PubMed:17666397, PubMed:19096517, PubMed:2446925). Pores are presumably made by 1-2 toxin molecules (PubMed:23471747). While interaction with the RBD modulates the pH threshold for membrane insertion, the RBD is not essential for toxin degradation of SNAP25 in neural cells (PubMed:19096517)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin A heavy chain"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.","ecNumber":"3.4.24.69","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10694409"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7578132"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8243676"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9886085"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11565902"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11700044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1429690"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15592454"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19351593"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22363010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7578132"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11700044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1429690"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15592454"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19351593"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22363010"}],"value":"Binds 1 zinc ion per subunit (PubMed:11700044, PubMed:1429690, PubMed:15592454, PubMed:19351593, PubMed:22363010)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21832053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6694738"}],"value":"Toxin internalization is inhibited by azide or dinitrophenol or at 4 degrees Celsius (PubMed:6694738). Dynamin (DNM) inhibitors abolish toxin uptake (PubMed:21832053)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":41.0,"unit":"uM","substrate":"purified SNAP25 with isolated botulinum neurotoxin A light chain","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10694409"}]},{"constant":9.8,"unit":"uM","substrate":"purified SNAP25 with isolated botulinum neurotoxin A light chain","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11827515"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10694409"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11827515"}],"value":"kcat is 140 min(-1) (PubMed:10694409). kcat is 1026 (-1) (PubMed:11827515)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16543415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16545378"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18815274"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19650874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22363010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24240280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27313224"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7578132"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22363010"}],"value":"Heterodimer; disulfide-linked heterodimer of a light chain (LC) and heavy chain (HC) (PubMed:7578132). Interacts with glycosylated host synaptic vesicle glycoproteins SV2A, SV2B and SV2C which serve as coreceptors (PubMed:16543415, PubMed:18815274, PubMed:19650874, PubMed:24240280, PubMed:27313224). Glycosylation of 'Asn-559' in SV2C contributes a 12-fold increase in affinity to this interaction (PubMed:27313224). Depolarization of target tissue with high levels of K(+) leads to greater levels of receptor exposure (PubMed:16543415). In vitro addition of gangliosides increases SV2-toxin interaction (PubMed:16543415). Forms a highly interlocked heterodimer with NTNHA at pH 6.0 but not at pH 7.5 called the minimally functional progenitor toxin complex (M-PTC) (PubMed:22363010). The PTC is thought to protect toxin in the host acidic gastrointestinal tract, facilitate transcytosis across the intestinal barrier and release at neutral pH as is found in the bloodstream (PubMed:22363010)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P0DPI0","intActId":"EBI-8178893"},"interactantTwo":{"uniProtKBAccession":"Q02563","geneName":"Sv2a","intActId":"EBI-466194"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P0DPI0","intActId":"EBI-8178893"},"interactantTwo":{"uniProtKBAccession":"Q496J9","geneName":"SV2C","intActId":"EBI-16081469"},"numberOfExperiments":4,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P0DPI0","intActId":"EBI-8178893"},"interactantTwo":{"uniProtKBAccession":"Q9Z2I6","geneName":"Sv2c","intActId":"EBI-8178859"},"numberOfExperiments":12,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin type A","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6694738"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7592120"}],"value":"Whole toxin may be released from the bacteria during cell wall exfoliation (PubMed:7592120). There are estimated to be 150-500 toxin molecules per um(2) of non-myelinated mouse hemidiaphragm nerve membrane (PubMed:6694738). In mouse hemidiaphragm binds only to nerve terminals, and not to muscle, blood vessels, connective tissue Schwann cells or myelin, toxin can be internalized by this preparation (PubMed:6694738)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7592120"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7592120"}],"value":"Secreted, cell wall","id":"SL-0041"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6694738"}],"value":"Host synapse, host presynaptic cell membrane","id":"SL-0434"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin A light chain","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6370252"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7578132"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8243676"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"9886085"}],"value":"Host cytoplasm, host cytosol","id":"SL-0384"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin A heavy chain","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21632541"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21832053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23471747"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24240280"}],"value":"Whole toxin may be released from the bacteria during cell wall exfoliation (PubMed:7592120). Colocalizes with its receptor SV2C (synaptic vesicle glycoprotein 2C) and VGAT (vesicular inhibitory amino acid transporter) in neurons (PubMed:24240280). In neurons HC colocalizes with synaptophysin or VAMP2 probably in synaptic vesicles, a portion also colocalizes with RAB5 and may be in synaptic vesicle protein sorting endosomes (PubMed:21632541, PubMed:21832053). Therefore there may be more than one uptake pathway at nerve terminals. Uptake of HC and whole toxin is slowed by dynamin inhibitors (PubMed:21832053). 1-2 molecules of HC are found in the host synaptic vesicle lumen, uptake and subsequent release of LC is very rapid (PubMed:21832053, PubMed:23471747)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6370252"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6694738"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10413679"}],"value":"Host synapse, host presynaptic cell membrane","id":"SL-0434"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23471747"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10413679"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21632541"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21832053"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24240280"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"6694738"}],"value":"Host cytoplasmic vesicle, host secretory vesicle, host synaptic vesicle membrane","id":"SL-0503"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17666397"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19096517"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"2446925"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7592120"}],"value":"In cultured bacteria, first detected in late exponential growth (17 hours), reaches maximal levels at 24-25 hours and remains nearly constant for 5 days (at protein level)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7578132"}],"value":"Has protease activity (PubMed:7578132)"}],"commentType":"DOMAIN","molecule":"Botulinum neurotoxin A light chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17666397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18032388"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19096517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19351593"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22363010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2446925"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17907800"}],"value":"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). Upon trypsin digestion the isolated TD forms channels in bilayers when the cis side is acidic/oxidizing and the trans side is pH 7.0/reducing (PubMed:17666397, PubMed:19096517, PubMed:2446925). The RBD rotates 140 degrees around the TD in the presence of NTNHA (PubMed:22363010). The 3 major domains each serve as a chaperone for the other 2 to ensure they act only in the correct host cell context (PubMed:19096517). In BoNT/A structures the LC is separated from the RBD by the TD; the belt wraps around the perimeter of the LC, protecting Zn(2+) in the active site (PubMed:18032388, PubMed:19351593, PubMed:22363010). The belt region (449-545) may be a pseudosubstrate inhibitor which serves as an intramolecular chaperone for the LC prior to its translocation into the host cytosol (PubMed:17907800)"}],"commentType":"DOMAIN","molecule":"Botulinum neurotoxin A heavy chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2126206"}],"value":"In a bacterial culture the precursor chain is initally cleaved on the amino side of Gly-445 and is processed more slowly between Lys-448 and Ala-449 to give the final mature heavy chain sequence"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11565902"}],"value":"Has slow autocatalytic activity, cleaves 250-Tyr-Tyr-251, 266-Phe-Gly-267, 419-Phe-Thr-420, 423-Phe-Glu-424, 430-Cys-Val-431, 432-Arg-Gly-433, 438-Lys-Thr-439, and probably 429-Leu-Cys-430 over a period of 4 weeks. Catalysis of the '197-Gln-|-Arg-198' bond in SNAP25 is estimated to be 10(5) more efficient than autocatalysis, leaving the physiological importance of autocatalysis in doubt (PubMed:11565902)"}],"commentType":"PTM","molecule":"Botulinum neurotoxin A light chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28584101"}],"value":"Ubiquitinated by host HECD2. Deubiquitination by host VCPIP1 prevents degradation by the proteasome"}],"commentType":"PTM","molecule":"Botulinum neurotoxin A light chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21832053"}],"value":"Dynamin inhibitors slow toxin uptake by nerve cells, and might be used to prolong the treatment window for antitoxins"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10768948"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19351593"}],"value":"Replacement of the RBD by other proteins (such as wheat germ agglutinin) allows the rest of the toxin to be taken up by other cell types, and can be used for investigating synaptic vesicle docking-dependent processes in BoNT resistant cells (PubMed:10768948). LC retains protease activity (PubMed:10768948, PubMed:19351593)"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21106906"}],"value":"Isolated receptor-binding domain (RBD) can be used as a vaccine; a mutated form that is transcytosed into the general circulation but does not enter nerve cells (Leu-1266-1267-Ser) is as efficient as wild-type RBD (PubMed:21106906)"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28356439"}],"value":"Available under the name Botox (onabotulinumtoxinA, Allergan), Dysport (abobotulinumtoxinA, Ipsen Biopharmaceuticals) and Xeomin (incobotulinumtoxinA, Merz Pharmaceuticals) for the treatment of strabismus and blepharospasm associated with dystonia and cervical dystonia. Also used for the treatment of hemifacial spasm and a number of other neurological disorders characterized by abnormal muscle contraction. It is also used cosmetically to smooth facial wrinkles"}],"commentType":"PHARMACEUTICAL"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C, D, E, F, and G; new subtypes are quite frequent"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1431246"}],"value":"Types A, B and E are the most frequent cause of adult human foodborne botulism; type A is the most severe, while type E has the shortest incubation period (PubMed:1431246)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2126206"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6370252"}],"value":"Neurotoxin type A is released from bacteria in the two-chain form (PubMed:2126206, PubMed:6370252)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21106906"}],"value":"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"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the peptidase M27 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16545378"}],"value":"Contradictory results show that only SV2C is the receptor; in these experiments gangliosides do not improve toxin-coreceptor interaction (PubMed:16545378)"}],"commentType":"CAUTION"},{"commentType":"WEB RESOURCE","resourceName":"BOTOX product information Web site","resourceUrl":"https://www.botox.com/","ftp":false},{"commentType":"WEB RESOURCE","resourceName":"Protein Spotlight","resourceUrl":"https://www.proteinspotlight.org/back_issues/019","ftp":false,"note":"From sausages to wrinkles - Issue 19 of February 2002"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2126206"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6370252"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.6"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11565902"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":1296,"modifier":"EXACT"}},"description":"Botulinum neurotoxin type A","featureId":"PRO_0000444902"},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"Botulinum neurotoxin A light chain","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6370252"}],"featureId":"PRO_0000029211"},{"type":"Chain","location":{"start":{"value":449,"modifier":"EXACT"},"end":{"value":1296,"modifier":"EXACT"}},"description":"Botulinum neurotoxin A heavy chain","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6370252"}],"featureId":"PRO_0000029212"},{"type":"Transmembrane","location":{"start":{"value":627,"modifier":"EXACT"},"end":{"value":647,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":656,"modifier":"EXACT"},"end":{"value":676,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":449,"modifier":"EXACT"},"end":{"value":870,"modifier":"EXACT"}},"description":"Translocation domain (TD); not required to bind NTNHA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22363010"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19096517"}]},{"type":"Region","location":{"start":{"value":492,"modifier":"EXACT"},"end":{"value":545,"modifier":"EXACT"}},"description":"Belt; not required for channel 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Precursor of botulinum neurotoxin F which may have 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. 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 HC forms pores that allows the light chain (LC) to translocate into the cytosol. 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). Whole toxin only has protease activity after reduction, which releases LC (PubMed:8505288). Requires complex eukaryotic host polysialogangliosides for full neurotoxicity (By similarity). It is not clear whether a synaptic vesicle protein acts as its receptor; there is evidence for and against SV2 fulfilling this function (By similarity)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin type F"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8175689"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8197120"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8505288"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"16128577"}],"value":"Has proteolytic activity (PubMed:8175689, PubMed:8197120, PubMed:8505288). After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '60-Gln-|-Lys-61' bond of synaptobrevin-1/VAMP1 and the equivalent 'Gln-|-Lys' sites in VAMP2 and VAMP3 (PubMed:8175689, PubMed:8505288). Cleaves the '48-Gln-|-Lys-49' bond of A.californica synaptobrevin (AC P35589) (PubMed:8197120)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin F light chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A7GBG3"}],"value":"Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into 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 cell surface. It simultaneously recognizes 2 coreceptors; polysialated gangliosides and the receptor protein SV2A, SV2B and SV2C in close proximity on host synaptic vesicles; although not all evidence indicates these are the receptors (By similarity). The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) 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 (By similarity)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin F heavy chain"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.","ecNumber":"3.4.24.69","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8197120"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8505288"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16128577"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8505288"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16128577"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8505288"}],"value":"Binds 1 zinc ion per subunit (PubMed:16128577, PubMed:8505288)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8505288"}],"value":"Proteolysis inhibited by 1,10-phenanthroline, captopril and EDTA (PubMed:8505288)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A7GBG3"}],"value":"Heterodimer; disulfide-linked heterodimer of a light chain (LC) and a heavy chain (HC). The LC has the proteolytic/pharmacological activity, while the N- and C-terminal of the HC mediate channel formation and toxin binding, respectively. Interacts with host synaptic vesicle glycoproteins SV2A, SV2B and SV2C (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin type F","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}],"value":"Secreted","id":"SL-0243"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin F light chain","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8175689"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8505288"}],"value":"Host cytoplasm, host cytosol","id":"SL-0384"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin F heavy chain","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Host synapse, host presynaptic cell membrane","id":"SL-0434"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}],"value":"Host cytoplasmic vesicle, host secretory vesicle, host synaptic vesicle membrane","id":"SL-0503"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8175689"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8197120"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8505288"}],"value":"Has protease activity (PubMed:8175689, PubMed:8197120, PubMed:8505288)"}],"commentType":"DOMAIN","molecule":"Botulinum neurotoxin F light chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A7GBG3"}],"value":"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) (By similarity). The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) 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 (By similarity). The RBD binds transiently exposed coreceptors on the host presynaptic cell membrane (By similarity)"}],"commentType":"DOMAIN","molecule":"Botulinum neurotoxin F heavy chain"},{"texts":[{"value":"There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C, D, E, F, and G; new subtypes are quite frequent"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}],"value":"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"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the peptidase M27 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1274,"modifier":"EXACT"}},"description":"Botulinum neurotoxin type F","featureId":"PRO_0000444921"},{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":436,"modifier":"EXACT"}},"description":"Botulinum neurotoxin F light chain","featureId":"PRO_0000029225"},{"type":"Chain","location":{"start":{"value":437,"modifier":"EXACT"},"end":{"value":1274,"modifier":"EXACT"}},"description":"Botulinum neurotoxin F heavy chain","featureId":"PRO_0000029226"},{"type":"Region","location":{"start":{"value":440,"modifier":"EXACT"},"end":{"value":862,"modifier":"EXACT"}},"description":"Translocation domain 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domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50386","properties":[{"key":"EntryName","value":"STI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00142","properties":[{"key":"EntryName","value":"ZINC_PROTEASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPVAINSFNYNDPVNDDTILYMQIPYEEKSKKYYKAFEIMRNVWIIPERNTIGTNPSDFDPPASLKNGSSAYYDPNYLTTDAEKDRYLKTTIKLFKRINSNPAGKVLLQEISYAKPYLGNDHTPIDEFSPVTRTTSVNIKLSTNVESSMLLNLLVLGAGPDIFESCCYPVRKLIDPDVVYDPSNYGFGSINIVTFSPEYEYTFNDISGGHNSSTESFIADPAISLAHELIHALHGLYGARGVTYEETIEVKQAPLMIAEKPIRLEEFLTFGGQDLNIITSAMKEKIYNNLLANYEKIATRLSEVNSAPPEYDINEYKDYFQWKYGLDKNADGSYTVNENKFNEIYKKLYSFTESDLANKFKVKCRNTYFIKYEFLKVPNLLDDDIYTVSEGFNIGNLAVNNRGQSIKLNPKIIDSIPDKGLVEKIVKFCKSVIPRKGTKAPPRLCIRVNNSELFFVASESSYNENDINTPKEIDDTTNLNNNYRNNLDEVILDYNSQTIPQISNRTLNTLVQDNSYVPRYDSNGTSEIEEYDVVDFNVFFYLHAQKVPEGETNISLTSSIDTALLEESKDIFFSSEFIDTINKPVNAALFIDWISKVIRDFTTEATQKSTVDKIADISLIVPYVGLALNIIIEAEKGNFEEAFELLGVGILLEFVPELTIPVILVFTIKSYIDSYENKNKAIKAINNSLIEREAKWKEIYSWIVSNWLTRINTQFNKRKEQMYQALQNQVDAIKTAIEYKYNNYTSDEKNRLESEYNINNIEEELNKKVSLAMKNIERFMTESSISYLMKLINEAKVGKLKKYDNHVKSDLLNYILDHRSILGEQTNELSDLVTSTLNSSIPFELSSYTNDKILIIYFNRLYKKIKDSSILDMRYENNKFIDISGYGSNISINGNVYIYSTNRNQFGIYNSRLSEVNIAQNNDIIYNSRYQNFSISFWVRIPKHYKPMNHNREYTIINCMGNNNSGWKISLRTVRDCEIIWTLQDTSGNKENLIFRYEELNRISNYINKWIFVTITNNRLGNSRIYINGNLIVEKSISNLGDIHVSDNILFKIVGCDDETYVGIRYFKVFNTELDKTEIETLYSNEPDPSILKNYWGNYLLYNKKYYLFNLLRKDKYITLNSGILNINQQRGVTEGSVFLNYKLYEGVEVIIRKNGPIDISNTDNFVRKNDLAYINVVDRGVEYRLYADTKSEKEKIIRTSNLNDSLGQIIVMDSIGNNCTMNFQNNNGSNIGLLGFHSNNLVASSWYYNNIRRNTSSNGCFWSSISKENGWKE","length":1274,"molWeight":146710,"crc64":"5B99756A7438B921","md5":"7C51675857BBFCF84017CF82ACBA4EAB"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":3,"DOMAIN":2,"MISCELLANEOUS":2,"SIMILARITY":1},"countByFeatureType":{"Chain":3,"Region":4,"Motif":1,"Active site":1,"Binding site":3,"Disulfide bond":1,"Beta strand":17,"Helix":14,"Turn":7},"uniParcId":"UPI0000126B8A"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P10844","secondaryAccessions":["P10843"],"uniProtkbId":"BXB_CLOBO","entryAudit":{"firstPublicDate":"1989-07-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-01-23","entryVersion":199,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Clostridium botulinum","taxonId":1491,"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Eubacteriales","Clostridiaceae","Clostridium","Clostridium botulinum group"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Botulinum neurotoxin type B"},"shortNames":[{"value":"BoNT/B"}]},"alternativeNames":[{"fullName":{"value":"Bontoxilysin-B"}}],"contains":[{"recommendedName":{"fullName":{"value":"Botulinum neurotoxin B light chain"},"shortNames":[{"value":"LC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1331807"}],"value":"3.4.24.69"}]}},{"recommendedName":{"fullName":{"value":"Botulinum neurotoxin B heavy chain"},"shortNames":[{"value":"HC"}]}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1514783"}],"value":"botB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1331807"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14504267"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15123599"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17167418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17167421"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17185412"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21925111"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22720883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23807078"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3856850"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7803399"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8144634"}],"value":"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. Precursor of botulinum neurotoxin B which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles (PubMed:17167418, PubMed:17167421, PubMed:17185412, PubMed:23807078). Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them (PubMed:14504267). Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway (PubMed:14504267). When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the HC forms pores that allows the light chain (LC) to translocate into the cytosol (PubMed:3856850). 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. Binds to host peripheral neuronal presynaptic membranes via synaptotagmins 1 and 2 (SYT1 and SYT2) (PubMed:14504267, PubMed:8144634). Toxin binds to the membrane proximal extra-cytoplasmic region of host SYT1 and SYT2 that is transiently exposed outside of cells during exocytosis; exogenous gangliosides enhance binding and subsequent uptake of toxin into host cells (PubMed:14504267, PubMed:15123599). Toxin uptake into neural cells requires stimulation (incubation with K(+) to stimulate SYT protein receptor exposure); subsequently the toxin colocalizes with its receptor in host cells with a concomitant decrease in target protein (synaptobrevin-2/VAMP2) immunoreactivity (PubMed:14504267). Toxin uptake can be blocked by the appropriate synaptotagmin protein fragments and gangliosides in cell culture and in mice (PubMed:14504267, PubMed:15123599). BoNT/B is a 'coincidence detector'; it requires simultaneous binding to coreceptor GT1b and low pH to transform into a membrane-bound, oligomeric channel (PubMed:21925111, PubMed:22720883). Whole toxin only has protease activity after reduction which releases LC (PubMed:1331807, PubMed:7803399)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin type B"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1331807"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7803399"}],"value":"Has proteolytic activity (PubMed:1331807). After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that cleaves the '76-Gln-|-Phe-77' bond of synaptobrevin-2/VAMP2, blocking neurotransmitter release (PubMed:1331807, PubMed:7803399). In vitro the LC only has protease activity after reduction (PubMed:1331807, PubMed:7803399)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin B light chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10413679"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10932256"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14504267"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14731268"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15123599"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17167418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17167421"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17185412"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19650874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23807078"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8144634"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21925111"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3856850"}],"value":"Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The N-terminus of the TD wraps an extended belt around the perimeter of the LC; it does not seem to protect the active site, but might prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation (PubMed:10932256, PubMed:17167418). Has 2 coreceptors; complex gangliosides found primarily on neural tissue and host synaptotagmin-1 and -2 (SYT1 and SYT2) which bind simultaneously to adjacent but separate sites at the tip of the HC (PubMed:17167418, PubMed:17167421, PubMed:17185412, PubMed:23807078, PubMed:8144634). HC alone partially prevents uptake of whole toxin by neural cells, and delays paralysis onset by 160% (PubMed:10413679). Binding probably positions the TD for integration into the synaptic vesicle membrane (PubMed:17167418, PubMed:23807078). The HC forms channels at low pH that mediate transport of the light chain (LC) from the endocytic vesicle to the cytosol (PubMed:3856850). Binds gangliosides GD1b and GT1b (PubMed:10413679, PubMed:14731268). Gangliosides are not only a coreceptor, but also required for uptake into nerve cells (PubMed:17167418, PubMed:21925111). HC alone binds to host receptor proteins SYT1 and SYT2 (PubMed:14504267, PubMed:15123599, PubMed:17185412, PubMed:19650874). Interaction with SYT1 protein does not require SYT1 glycosylation (PubMed:19476346). The HC C-terminus (approximately residues 1079-1291) interacts with host SYT2 (PubMed:15123599, PubMed:17167418, PubMed:17167421, PubMed:23807078). Has higher affinity for SYT2 than SYT1 (PubMed:17167421, PubMed:17185412). Significantly decreases uptake and toxicity of whole BoNT/B and BoNT/G (PubMed:19650874)"}],"commentType":"FUNCTION","molecule":"Botulinum neurotoxin B heavy chain"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.","ecNumber":"3.4.24.69","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1331807"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10932256"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1429690"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17167418"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10932256"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1429690"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17167418"}],"value":"Binds 1 zinc ion per subunit, to the LC (PubMed:10932256, PubMed:1429690, PubMed:17167418)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1331807"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21925111"}],"value":"Proteolysis inhibited by EDTA and captopril, and by peptides that encompass the VAMP2 cleavage site (Ala-Ser-Gln-Phe-Glu-Thr-Ser and Gln-Phe-Glu-Thr) (PubMed:1331807). Translocation of whole toxin into neurons is inhibited by toosendanin (PubMed:21925111)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":19.2,"unit":"uM","substrate":"over-expressed human VAMP1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22289120"}]},{"constant":29.9,"unit":"uM","substrate":"over-expressed human VAMP2","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22289120"}]},{"constant":11.6,"unit":"uM","substrate":"over-expressed human VAMP3","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22289120"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22289120"}],"value":"kcat is 3.96, 4.68 and 3.50 sec(-1) for over-expressed human VAMP1, VAMP2 and VAMP3 respectively."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1331807"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14504267"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15123599"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17167418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17167421"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19476346"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19650874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21925111"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22720883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23807078"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3139097"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8144634"}],"value":"Heterodimer; disulfide-linked heterodimer of a light chain (LC) and a heavy chain (HC) (PubMed:1331807, PubMed:3139097). At pH 4.4 in the presence of ganglioside GT1b may form trimers (PubMed:21925111, PubMed:22720883). Interacts with host receptor synaptotagmin-1 (SYT1); interaction is improved in the presence of gangliosides (PubMed:14504267, PubMed:19650874, PubMed:8144634). Interacts with host receptor synaptotagmin-2 (SYT2) (PubMed:14504267, PubMed:15123599, PubMed:17167418, PubMed:17167421, PubMed:19650874, PubMed:23807078). SYT2 interaction and toxin uptake do not require gangliosides but are improved in their presence (PubMed:14504267, PubMed:15123599). HC interacts with a complex including at least host synaptic vesicle glycoprotein 2 (SV2) and synaptotagmin-1 (SYT1); copurification does not depend on glycosylation of either protein (PubMed:19476346)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P10844","intActId":"EBI-7661991"},"interactantTwo":{"uniProtKBAccession":"P29101","geneName":"Syt2","intActId":"EBI-458017"},"numberOfExperiments":6,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P10844","intActId":"EBI-7661991"},"interactantTwo":{"uniProtKBAccession":"P46097","geneName":"Syt2","intActId":"EBI-457969"},"numberOfExperiments":3,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin type B","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14504267"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21925111"}],"value":"Colocalizes with its SYT1 receptor, probably in synaptic vesicles (PubMed:14504267). At pH 4.4 in the presence of ganglioside GT1b becomes a membrane-associated hydrophobic protein (PubMed:21925111)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3139097"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14504267"}],"value":"Host synapse, host presynaptic cell membrane","id":"SL-0434"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin B light chain","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3139097"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"1331807"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8144634"}],"value":"Host cytoplasm, host cytosol","id":"SL-0384"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Botulinum neurotoxin B heavy chain","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3139097"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14504267"}],"value":"Host synapse, host presynaptic cell membrane","id":"SL-0434"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21925111"}],"value":"Host cytoplasmic vesicle, host secretory vesicle, host synaptic vesicle membrane","id":"SL-0503"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1331807"}],"value":"Has protease activity (PubMed:1331807)"}],"commentType":"DOMAIN","molecule":"Botulinum neurotoxin B light chain"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10932256"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3856850"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17907800"}],"value":"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) (PubMed:10932256). HC forms channels in bilayers at low pH (PubMed:3856850). The N-terminal belt of the TD wraps an extended belt around the perimeter of the LC; it is shorter than in BoNT/A and does not block the active site (PubMed:10932256). The belt may be a pseudosubstrate inhibitor which serves as an intramolecular chaperone for the LC prior to its translocation into the host cytosol (PubMed:17907800)"}],"commentType":"DOMAIN","molecule":"Botulinum neurotoxin B heavy chain"},{"texts":[{"value":"Available under the name MYOBLOC (rimabotulinumtoxinB, US WorldMeds, LLC) for the treatment of adults with cervical dystonia"}],"commentType":"PHARMACEUTICAL"},{"texts":[{"value":"There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C, D, E, F, and G; new subtypes are quite frequent"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}],"value":"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"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1431246"}],"value":"Types A, B and E are the most frequent cause of adult human foodborne botulism; type A is the most severe, while type E has the shortest incubation period (PubMed:1431246)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4030755"}],"value":"Neurotoxin type B is released from bacteria mostly as a single chain and cleaved by host proteases into the active dichain (PubMed:4030755)"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the peptidase M27 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10932255"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19578378"}],"value":"A structure of a fragment of this protein in complex with the catalytic domain of C.botulinum neurotoxin type B (BoNT/B, botB) was reported; because of the lack of clear and continuous electron density for the VAMP2 peptide in the complex structure, the paper was retracted. One of its associated structures remains valid (PDB:1F82, light chain alone) (PubMed:10932255, PubMed:19578378)"}],"commentType":"CAUTION"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3139097"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":1291,"modifier":"EXACT"}},"description":"Botulinum neurotoxin type B","featureId":"PRO_0000444904"},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":441,"modifier":"EXACT"}},"description":"Botulinum neurotoxin B light chain","featureId":"PRO_0000029215"},{"type":"Chain","location":{"start":{"value":442,"modifier":"EXACT"},"end":{"value":1291,"modifier":"EXACT"}},"description":"Botulinum neurotoxin B heavy chain","featureId":"PRO_0000029216"},{"type":"Transmembrane","location":{"start":{"value":614,"modifier":"EXACT"},"end":{"value":634,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":643,"modifier":"EXACT"},"end":{"value":663,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":442,"modifier":"EXACT"},"end":{"value":857,"modifier":"EXACT"}},"description":"Translocation domain (TD)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}]},{"type":"Region","location":{"start":{"value":481,"modifier":"EXACT"},"end":{"value":532,"modifier":"EXACT"}},"description":"Belt; not required for channel formation","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10932256"}]},{"type":"Region","location":{"start":{"value":858,"modifier":"EXACT"},"end":{"value":1079,"modifier":"EXACT"}},"description":"N-terminus of receptor binding domain (N-RBD)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}]},{"type":"Region","location":{"start":{"value":1080,"modifier":"EXACT"},"end":{"value":1291,"modifier":"EXACT"}},"description":"C-terminus of receptor binding domain (C-RBD)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DPI0"}]},{"type":"Motif","location":{"start":{"value":1260,"modifier":"EXACT"},"end":{"value":1263,"modifier":"EXACT"}},"description":"Host ganglioside-binding motif","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10932256"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"14731268"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"17185412"}]},{"type":"Active 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