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Entry version 101 (11 Dec 2019)
Sequence version 1 (11 Sep 2007)
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Protein

Botulinum neurotoxin type F

Gene

F

Organism
Clostridium botulinum (strain Langeland / NCTC 10281 / Type F)
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:14423425). 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 (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. 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). Requires complex gangliosides for full neurotoxicity (PubMed:19650874, PubMed:21483489). Electrical stimulation increases uptake of toxin, presumably by transiently exposing a receptor usually found in eukaryotic target synaptic vesicles (PubMed:19476346, PubMed:19650874). Blocks neurotransitter release by cleaving synaptobrevin-2/VAMP2 (PubMed:19476346). It is not clear whether a synaptic vesicle protein acts as its receptor; there is evidence for and against SV2 fulfilling this function (PubMed:19650874, PubMed:21483489, PubMed:19476346).By similarity4 Publications
Has protease activity (PubMed:19476346, PubMed:19543288). After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '58-Gln-|-Lys-59' bond of synaptobrevin-2/VAMP2 and probably also the equivalent 'Gln-|-Lys' sites in VAMP1 and VAMP3 (PubMed:19476346, PubMed:19543288). Substrate specificity is conferred by multiple interactions of LC with substrate (PubMed:19543288).By similarity1 Publication1 Publication
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 (PubMed:19476346, PubMed:19650874). 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). Isolated HC binds to host synaptosomes and neurons, significantly decreases uptake and toxicity of whole BoNT/F (PubMed:19476346, PubMed:19650874). Interferes with uptake of BoNT/E and to a lesser extent BoNT/C (PubMed:19650874). in vitro binds gangliosides GT1b, GD1b and GD1a (PubMed:19650874, PubMed:19476346, PubMed:21849494). Binds to synaptic vesicle glycoproteins SV2A, SV2B and SV2C which may serve as coreceptors with gangliosides (PubMed:19650874, PubMed:19476346). Interaction with SV2 proteins requires SV2 glycosylation (PubMed:19476346). However knockout SV2A/SV2B mice still cleave synaptobrevin, leaving the identification of its receptor unclear (PubMed:21483489).By similarity3 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.
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
Strain Langeland / NCTC 10281 / Type F was isolated from home-made liver paste associated with human botulism in Denmark in 1958 (PubMed:14423425). It is type F1 (PubMed:20511432).2 Publications

Caution

It is not clear whether a synaptic vesicle protein acts as its receptor; there is evidence for and against SV2 fulfilling this function (PubMed:19650874, PubMed:21483489, PubMed:19476346).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

  • Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.1 Publication EC:3.4.24.69

<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+1 PublicationNote: Binds 1 zinc ion per subunit (PubMed:19543288).1 Publication

<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 16.12, 34.37 and 28.57 s(-1) for over-expressed human VAMP1, VAMP2 and VAMP3 respectively.1 Publication
  1. KM=19.0 µM for over-expressed human VAMP11 Publication
  2. KM=24.5 µM for over-expressed human VAMP21 Publication
  3. KM=15.0 µM for over-expressed human VAMP31 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi227Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei228PROSITE-ProRule annotation1
    Metal bindingi231Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationCombined sources1 Publication1
    Metal bindingi266Zinc; catalyticCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei1111Host ganglioside GD1a binding1 Publication1
    Binding sitei1195Host ganglioside GD1a bindingCombined sources1 Publication1
    Binding sitei1256Host ganglioside GD1a bindingCombined sources1 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

    GO - Biological processi

    <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

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    CBOT441772:G1G98-834-MONOMER

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    M27.002

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Botulinum neurotoxin type F
    Short name:
    BoNT/F1 Publication
    Alternative name(s):
    Bontoxilysin-F
    Cleaved into the following 2 chains:
    Botulinum neurotoxin F light chain (EC:3.4.24.69)
    Short name:
    LC
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:FImported
    Synonyms:bontImported, boNT/FImported
    Ordered Locus Names:CLI_0851Imported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiClostridium botulinum (strain Langeland / NCTC 10281 / Type F)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri441772 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002410 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    <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

    GO - Cellular componenti

    Keywords - Cellular componenti

    Host cell junction, Host cell membrane, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host synapse, Membrane, Secreted

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi133R → A: Dramatically decreased cleavage of host synaptobrevin-2 (VAMP2). 1 Publication1
    Mutagenesisi133R → K: Dramatically decreased cleavage of VAMP2. 1 Publication1
    Mutagenesisi164E → A: Significantly decreased cleavage of VAMP2. 1 Publication1
    Mutagenesisi171R → K: Dramatically decreased cleavage of VAMP2. 1 Publication1
    Mutagenesisi316Y → A: Slightly decreased cleavage of VAMP2. 1 Publication1
    Mutagenesisi1111R → A: Decreased heavy chain (HC) binding to ganglioside GD1a. Dramatically decreased HC binding to GD1a; when associated with A-1256. Significantly decreased; when associated with K-1241 and A-1256, which partially restores binding. 1 Publication1
    Mutagenesisi1195E → A: Significantly decreased binding of heavy chain to synaptosomes, significantly decreased binding to ganglioside GT1b. 2 Publications1
    Mutagenesisi1241H → K: Dramatically decreased heavy chain (HC) binding to ganglioside GD1a. Significantly decreased HC binding to GD1a; when associated with A-1111 and A-1256, partially restores binding. 1 Publication1
    Mutagenesisi1248S → A: Significantly decreased heavy chain binding to ganglioside GT1b. 1 Publication1
    Mutagenesisi1250W → L: Significantly decreased binding of heavy chain (HC) to synaptosomes, significantly decreased binding to ganglioside GT1b. HC no longer inhibits BoNT/F whole-toxin uptake and toxicity. Loss of HC binding to synaptic vesicles, greatly decreased binding to neurons. 2 Publications1
    Mutagenesisi1251Y → F: Decreased heavy chain binding to ganglioside GT1b. 1 Publication1
    Mutagenesisi1254N → A: Wild-type heavy chain binding to ganglioside GT1b. 1 Publication1
    Mutagenesisi1256R → A: Decreased heavy chain (HC) binding to ganglioside GD1a. Dramatically decreased HC binding to GD1a; when associated with A-1111. Significantly decreased; when associated with A-1111 and K-1241, which partially restores binding. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004449081 – 1278Botulinum neurotoxin type FAdd BLAST1278
    ChainiPRO_00004449091 – 436Botulinum neurotoxin F light chainAdd BLAST436
    ChainiPRO_0000444910437 – 1278Botulinum neurotoxin F 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 bondi429 ↔ 445Interchain (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_section">'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_section">'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). 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 (PubMed:19650874). HC interacts with a complex including at least host SV2 and synaptotagmin-1 (SYT1); copurification depends on glycosylation of SV2 (PubMed:19476346).

    2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    P630272EBI-7604673,EBI-520113From Homo sapiens.

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    A7GBG3, 1 interactor

    Molecular INTeraction database

    More...
    MINTi
    A7GBG3

    <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

    11278
    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
    A7GBG3

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    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>Regioni440 – 862Translocation domain (TD)By similarityAdd BLAST423
    Regioni485 – 534BeltBy similarityAdd BLAST50
    Regioni864 – 1085N-terminus of receptor binding domain (N-RBD)1 PublicationAdd BLAST222
    Regioni1086 – 1278C-terminus of receptor binding domain (C-RBD)1 PublicationAdd BLAST193
    Regioni1240 – 1241Host ganglioside GD1a bindingCombined sources1 Publication2
    Regioni1248 – 1250Host ganglioside GD1a bindingCombined sources1 Publication3

    Coiled coil

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili717 – 783Sequence analysisAdd BLAST67

    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>Motifi1245 – 1248Host ganglioside-binding motifBy similarity2 Publications4

    <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 protease activity (PubMed:19476346, PubMed:19543288).1 Publication1 Publication
    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:19476346). 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 (By similarity). The RBD binds transiently exposed coreceptors on the host presynaptic cell membrane (PubMed:19476346, PubMed:19650874).By similarity1 Publication1 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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000234384

    KEGG Orthology (KO)

    More...
    KOi
    K06011

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    DEGYNKA

    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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    A7GBG3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPVVINSFNY NDPVNDDTIL YMQIPYEEKS KKYYKAFEIM RNVWIIPERN
    60 70 80 90 100
    TIGTDPSDFD PPASLENGSS AYYDPNYLTT DAEKDRYLKT TIKLFKRINS
    110 120 130 140 150
    NPAGEVLLQE ISYAKPYLGN EHTPINEFHP VTRTTSVNIK SSTNVKSSII
    160 170 180 190 200
    LNLLVLGAGP DIFENSSYPV RKLMDSGGVY DPSNDGFGSI NIVTFSPEYE
    210 220 230 240 250
    YTFNDISGGY NSSTESFIAD PAISLAHELI HALHGLYGAR GVTYKETIKV
    260 270 280 290 300
    KQAPLMIAEK PIRLEEFLTF GGQDLNIITS AMKEKIYNNL LANYEKIATR
    310 320 330 340 350
    LSRVNSAPPE YDINEYKDYF QWKYGLDKNA DGSYTVNENK FNEIYKKLYS
    360 370 380 390 400
    FTEIDLANKF KVKCRNTYFI KYGFLKVPNL LDDDIYTVSE GFNIGNLAVN
    410 420 430 440 450
    NRGQNIKLNP KIIDSIPDKG LVEKIVKFCK SVIPRKGTKA PPRLCIRVNN
    460 470 480 490 500
    RELFFVASES SYNENDINTP KEIDDTTNLN NNYRNNLDEV ILDYNSETIP
    510 520 530 540 550
    QISNQTLNTL VQDDSYVPRY DSNGTSEIEE HNVVDLNVFF YLHAQKVPEG
    560 570 580 590 600
    ETNISLTSSI DTALSEESQV YTFFSSEFIN TINKPVHAAL FISWINQVIR
    610 620 630 640 650
    DFTTEATQKS TFDKIADISL VVPYVGLALN IGNEVQKENF KEAFELLGAG
    660 670 680 690 700
    ILLEFVPELL IPTILVFTIK SFIGSSENKN KIIKAINNSL MERETKWKEI
    710 720 730 740 750
    YSWIVSNWLT RINTQFNKRK EQMYQALQNQ VDAIKTVIEY KYNNYTSDER
    760 770 780 790 800
    NRLESEYNIN NIREELNKKV SLAMENIERF ITESSIFYLM KLINEAKVSK
    810 820 830 840 850
    LREYDEGVKE YLLDYISEHR SILGNSVQEL NDLVTSTLNN SIPFELSSYT
    860 870 880 890 900
    NDKILILYFN KLYKKIKDNS ILDMRYENNK FIDISGYGSN ISINGDVYIY
    910 920 930 940 950
    STNRNQFGIY SSKPSEVNIA QNNDIIYNGR YQNFSISFWV RIPKYFNKVN
    960 970 980 990 1000
    LNNEYTIIDC IRNNNSGWKI SLNYNKIIWT LQDTAGNNQK LVFNYTQMIS
    1010 1020 1030 1040 1050
    ISDYINKWIF VTITNNRLGN SRIYINGNLI DEKSISNLGD IHVSDNILFK
    1060 1070 1080 1090 1100
    IVGCNDTRYV GIRYFKVFDT ELGKTEIETL YSDEPDPSIL KDFWGNYLLY
    1110 1120 1130 1140 1150
    NKRYYLLNLL RTDKSITQNS NFLNINQQRG VYQKPNIFSN TRLYTGVEVI
    1160 1170 1180 1190 1200
    IRKNGSTDIS NTDNFVRKND LAYINVVDRD VEYRLYADIS IAKPEKIIKL
    1210 1220 1230 1240 1250
    IRTSNSNNSL GQIIVMDSIG NNCTMNFQNN NGGNIGLLGF HSNNLVASSW
    1260 1270
    YYNNIRKNTS SNGCFWSFIS KEHGWQEN
    Length:1,278
    Mass (Da):147,075
    Last modified:September 11, 2007 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA1BE1318431D6918
    GO

    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
    X81714 Genomic DNA Translation: CAA57358.1
    GU213203 Genomic DNA Translation: ADA79551.1
    X70821 Genomic DNA Translation: CAA50152.1
    CP000728 Genomic DNA Translation: ABS41202.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S48110

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_011987710.1, NC_009699.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    ABS41202; ABS41202; CLI_0851

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    cbf:CLI_0851

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    BotDB - A Database Resource for Clostridial Neurotoxins

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X81714 Genomic DNA Translation: CAA57358.1
    GU213203 Genomic DNA Translation: ADA79551.1
    X70821 Genomic DNA Translation: CAA50152.1
    CP000728 Genomic DNA Translation: ABS41202.1
    PIRiS48110
    RefSeqiWP_011987710.1, NC_009699.1

    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
    3FIEX-ray2.10A/B1-419[»]
    3FIIX-ray2.17A1-419[»]
    3FUQX-ray2.10A862-1278[»]
    3RSJX-ray2.00A/B/C/D866-1278[»]
    SMRiA7GBG3
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    IntActiA7GBG3, 1 interactor
    MINTiA7GBG3

    Protein family/group databases

    MEROPSiM27.002

    Protocols and materials databases

    ABCD curated depository of sequenced antibodies

    More...
    ABCDi
    A7GBG3

    Genome annotation databases

    EnsemblBacteriaiABS41202; ABS41202; CLI_0851
    KEGGicbf:CLI_0851

    Phylogenomic databases

    HOGENOMiHOG000234384
    KOiK06011
    OMAiDEGYNKA

    Enzyme and pathway databases

    BioCyciCBOT441772:G1G98-834-MONOMER

    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    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 nameiBXF_CLOBL
    <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: A7GBG3
    Secondary accession number(s): Q79AH9
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 18, 2018
    Last sequence update: September 11, 2007
    Last modified: December 11, 2019
    This is version 101 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Peptidase families
      Classification of peptidase families and list of entries
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