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Entry version 133 (11 Dec 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Botulinum neurotoxin type G

Gene

botG

Organism
Clostridium botulinum
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: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).By similarity1 Publication
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).1 Publication
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 Zn2+ in the active site; it may also prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation (By similarity). The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol (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).By similarity5 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
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).1 Publication2 Publications
Trypsinization of purified toxin increases its toxicity, suggesting it is released as a single chain (PubMed:4922309, PubMed:74236).2 Publications

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

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

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit (PubMed:16008342).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi230Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei231PROSITE-ProRule annotation1
Metal bindingi234Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi268Zinc; catalyticCombined sources1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1268Ganglioside-binding site1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.69 1462

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-5250989 Toxicity of botulinum toxin type G (BoNT/G)

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M27.002

UniLectin database of carbohydrate-binding proteins

More...
UniLectini
Q60393

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Botulinum neurotoxin type G
Short name:
BoNT/G1 Publication
Alternative name(s):
Bontoxilysin-G
Cleaved into the following 2 chains:
Botulinum neurotoxin G light chain (EC:3.4.24.691 Publication)
Short name:
LC
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:botG
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiClostridium botulinum
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1491 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

<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

  • Secreted 1 Publication1 Publication

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%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1080 – 1084SSLYW → EERYK: Improves solubility of isolated heavy chain (HC), used for crystallization. 1 Publication5
Mutagenesisi1126M → D: Significantly decreased binding of HC to host SYT1 and SYT2 independent of gangliosides. 1 Publication1
Mutagenesisi1191L → R: Significantly decreased binding of HC to host SYT1 and SYT2 independent of gangliosides. 1 Publication1
Mutagenesisi1200Q → E: Significantly decreased binding of HC to host SYT1 and SYT2 independent of gangliosides. 1 Publication1
Mutagenesisi1200Q → K: Decreased binding of HC to host SYT1 and SYT2 independent of gangliosides; whole toxin is less toxic. Dramatically decreased toxicity; when associated with L-1268. HC no longer inhibits whole-toxin uptake and toxicity. 2 Publications1
Mutagenesisi1262Y → F: Slightly increased binding of HC to host SYT1 and SYT2 in presence of gangliosides. 1 Publication1
Mutagenesisi1268W → L: Gangliosides no longer increase HC affinity for SYT1 or SYT2; whole toxin about significantly less toxic. Dramatically decreased toxicity; when associated with K-1200. In mice without complex gangliosides no change compared to wild-type protein. HC no longer inhibits whole-toxin uptake and toxicity. 2 Publications1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB13899 Equine Botulinum Neurotoxin G Immune FAB2

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004449222 – 1297Botulinum neurotoxin type GAdd BLAST1296
ChainiPRO_00000292272 – 442Botulinum neurotoxin G light chainAdd BLAST441
ChainiPRO_0000029228443 – 1297Botulinum neurotoxin G heavy chainAdd BLAST855

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 bondi436 ↔ 450Interchain (between light and heavy chains)By similarityCurated

Keywords - PTMi

Disulfide bond

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterodimer; disulfide-linked heterodimer of a light chain (LC) and a heavy chain (HC). 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).

3 Publications

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-60790N

Protein interaction database and analysis system

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IntActi
Q60393, 3 interactors

Molecular INTeraction database

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MINTi
Q60393

<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

11297
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

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SMRi
Q60393

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q60393

<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>Regioni446 – 862Translocation domain (TD)By similarityAdd BLAST417
Regioni488 – 537BeltBy similarityAdd BLAST50
Regioni868 – 1073N-terminus of receptor binding domain (N-RBD)2 PublicationsAdd BLAST206
Regioni1089 – 1297C-terminus of receptor binding domain (C-RBD)2 PublicationsAdd BLAST209

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>Motifi1266 – 1269Host ganglioside-binding motif1 Publication4

<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:7910017).1 Publication
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:20507178, PubMed:20219474). 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 (Probable).By similarity1 Publication3 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M27 family.Curated

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.1120.10, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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PRINTSi
PR00760 BONTOXILYSIN

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49899 SSF49899, 1 hit
SSF50386 SSF50386, 1 hit
SSF58091 SSF58091, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q60393-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPVNIKXFNY NDPINNDDII MMEPFNDPGP GTYYKAFRII DRIWIVPERF
60 70 80 90 100
TYGFQPDQFN ASTGVFSKDV YEYYDPTYLK TDAEKDKFLK TMIKLFNRIN
110 120 130 140 150
SKPSGQRLLD MIVDAIPYLG NASTPPDKFA ANVANVSINK KIIQPGAEDQ
160 170 180 190 200
IKGLMTNLII FGPGPVLSDN FTDSMIMNGH SPISEGFGAR MMIRFCPSCL
210 220 230 240 250
NVFNNVQENK DTSIFSRRAY FADPALTLMH ELIHVLHGLY GIKISNLPIT
260 270 280 290 300
PNTKEFFMQH SDPVQAEELY TFGGHDPSVI SPSTDMNIYN KALQNFQDIA
310 320 330 340 350
NRLNIVSSAQ GSGIDISLYK QIYKNKYDFV EDPNGKYSVD KDKFDKLYKA
360 370 380 390 400
LMFGFTETNL AGEYGIKTRY SYFSEYLPPI KTEKLLDNTI YTQNEGFNIA
410 420 430 440 450
SKNLKTEFNG QNKAVNKEAY EEISLEHLVI YRIAMCKPVM YKNTGKSEQC
460 470 480 490 500
IIVNNEDLFF IANKDSFSKD LAKAETIAYN TQNNTIENNF SIDQLILDND
510 520 530 540 550
LSSGIDLPNE NTEPFTNFDD IDIPVYIKQS ALKKIFVDGD SLFEYLHAQT
560 570 580 590 600
FPSNIENLQL TNSLNDALRN NNKVYTFFST NLVEKANTVV GASLFVNWVK
610 620 630 640 650
GVIDDFTSES TQKSTIDKVS DVSIIIPYIG PALNVGNETA KENFKNAFEI
660 670 680 690 700
GGAAILMEFI PELIVPIVGF FTLESYVGNK GHIIMTISNA LKKRDQKWTD
710 720 730 740 750
MYGLIVSQWL STVNTQFYTI KERMYNALNN QSQAIEKIIE DQYNRYSEED
760 770 780 790 800
KMNINIDFND IDFKLNQSIN LAINNIDDFI NQCSISYLMN RMIPLAVKKL
810 820 830 840 850
KDFDDNLKRD LLEYIDTNEL YLLDEVNILK SKVNRHLKDS IPFDLSLYTK
860 870 880 890 900
DTILIQVFNN YISNISSNAI LSLSYRGGRL IDSSGYGATM NVGSDVIFND
910 920 930 940 950
IGNGQFKLNN SENSNITAHQ SKFVVYDSMF DNFSINFWVR TPKYNNNDIQ
960 970 980 990 1000
TYLQNEYTII SCIKNDSGWK VSIKGNRIIW TLIDVNAKSK SIFFEYSIKD
1010 1020 1030 1040 1050
NISDYINKWF SITITNDRLG NANIYINGSL KKSEKILNLD RINSSNDIDF
1060 1070 1080 1090 1100
KLINCTDTTK FVWIKDFNIF GRELNATEVS SLYWIQSSTN TLKDFWGNPL
1110 1120 1130 1140 1150
RYDTQYYLFN QGMQNIYIKY FSKASMGETA PRTNFNNAAI NYQNLYLGLR
1160 1170 1180 1190 1200
FIIKKASNSR NINNDNIVRE GDYIYLNIDN ISDESYRVYV LVNSKEIQTQ
1210 1220 1230 1240 1250
LFLAPINDDP TFYDVLQIKK YYEKTTYNCQ ILCEKDTKTF GLFGIGKFVK
1260 1270 1280 1290
DYGYVWDTYD NYFCISQWYL RRISENINKL RLGCNWQFIP VDEGWTE
Length:1,297
Mass (Da):149,146
Last modified:January 23, 2007 - v2
<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:i306CF54CF3973C3B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X74162 Genomic DNA Translation: CAA52275.1

Protein sequence database of the Protein Information Resource

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PIRi
S39791

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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

BotDB - A Database Resource for Clostridial Neurotoxins

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74162 Genomic DNA Translation: CAA52275.1
PIRiS39791

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZB7X-ray2.35A1-443[»]
2VXRX-ray1.90A863-1297[»]
3MPPX-ray1.98G867-1297[»]
SMRiQ60393
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-60790N
IntActiQ60393, 3 interactors
MINTiQ60393

Chemistry databases

DrugBankiDB13899 Equine Botulinum Neurotoxin G Immune FAB2

Protein family/group databases

MEROPSiM27.002
UniLectiniQ60393

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
Q60393

Enzyme and pathway databases

BRENDAi3.4.24.69 1462
ReactomeiR-HSA-5250989 Toxicity of botulinum toxin type G (BoNT/G)

Miscellaneous databases

EvolutionaryTraceiQ60393

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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiBXG_CLOBO
<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: Q60393
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: December 11, 2019
This is version 133 of the entry and version 2 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. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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