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Entry version 10 (16 Oct 2019)
Sequence version 1 (18 Jul 2018)
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Protein

Botulinum neurotoxin type A

Gene

botA

Organism
Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
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 neurotoxin type A: 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:8103915). Precursor of botulinum neurotoxin A which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins of synaptic vesicles (By similarity). Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them (PubMed:19476346). Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway (By similarity). 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 (By similarity). Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release (By similarity).By similarity2 Publications
Botulinum neurotoxin A light chain: Has proteolytic activity (PubMed:8103915, PubMed:8294407). In vitro the whole toxin is reduced to release LC (PubMed:8103915, PubMed:8294407). After translocation into the eukaryotic host cytosol, LC hydrolyzes the 197-Gln-|-Arg-198 bond in SNAP25, blocking neurotransmitter release (PubMed:8103915, PubMed:8294407).1 Publication2 Publications
Botulinum neurotoxin A heavy chain: 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) (PubMed:9783750, PubMed:17173035). The RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously recognizes 2 coreceptors; polysialated gangliosides and synaptic vesicle glycoproteins SV2A, SV2B and SV2C in close proximity on host synaptic vesicles (By similarity). The RBD specifically recognizes the N-linked glycan on 'Asn-559' of SV2A, SV2B and SV2C (By similarity). Isolated HC binds to host synaptosomes, significantly decreases uptake and toxicity of whole BoNT/A (PubMed:19476346). Binds ganglioside GD1a in vitro (PubMed:21849494). 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 to protect toxin prior to translocation (PubMed:9783750). The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol (By similarity).By similarity4 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
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).1 Publication
Neurotoxin type A is released from bacteria in the two-chain form (PubMed:4030755).1 Publication
Neutralizing antibodies are used to treat botulism; in at least 2 cases they bind to HC.1 Publication

<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

<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+3 PublicationsNote: Binds 1 zinc ion per subunit (PubMed:9783750, PubMed:17173035, PubMed:21434688).3 Publications

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

SNAP25 proteolysis is inhibited by 1,10-phenanthroline and 2,2'-dipyridyl but not EDTA (PubMed:8103915). Inhibited by hydroxamate compounds with halogenated benzene-containing arms which directly bind the zinc ion (PubMed:21434688).2 Publications

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 bindingi223Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationCombined sources1 Publication1 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 sitei224PROSITE-ProRule annotation1
Metal bindingi227Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationCombined sources1 Publication1 Publication1
Metal bindingi262Zinc; catalyticPROSITE-ProRule annotationCombined 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
LigandMetal-binding, Zinc

Protein family/group databases

UniLectin database of carbohydrate-binding proteins

More...
UniLectini
P0DPI1

<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 A
Short name:
BoNT/A
Alternative name(s):
Bontoxilysin-A
Short name:
BOTOX
Cleaved into the following 2 chains:
Botulinum neurotoxin A light chain (EC:3.4.24.691 Publication)
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:botA1 Publication
Synonyms:bna1 Publication
Ordered Locus Names:CBO0806, CLC_0862
<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 Hall / ATCC 3502 / NCTC 13319 / Type A)
<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 identifieri441771 [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
  • UP000001986 <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

Chain Botulinum neurotoxin A light chain :
Chain Botulinum neurotoxin A heavy chain :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei627 – 647HelicalSequence analysisAdd BLAST21
Transmembranei656 – 676HelicalSequence analysisAdd BLAST21

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

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

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. 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.1 Publication

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>Mutagenesisi224E → K or Q: Light chain no longer cleaves SNAP25. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5344

<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_processing_section">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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004449032 – 1296Botulinum neurotoxin type AAdd BLAST1295
ChainiPRO_00003089062 – 448Botulinum neurotoxin A light chainAdd BLAST447
ChainiPRO_0000308907449 – 1296Botulinum neurotoxin A heavy chainAdd BLAST848

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 bondi430 ↔ 454Interchain (between light and heavy chains)Combined sources2 Publications
Disulfide bondi1235 ↔ 1280Combined sources2 Publications

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) (PubMed:9783750, PubMed:17173035).

Interacts with host synaptic vesicle glycoproteins SV2A, SV2B and SV2C which serve as coreceptors (By similarity). Glycosylation of 'Asn-559' in SV2C probably contributes a 12-fold increase in affinity to this interaction (By similarity). Depolarization of target tissue with high levels of K+ leads to greater levels of receptor exposure (PubMed:19476346).

By similarity3 Publications

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P0DPI1

<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

11296
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
P0DPI1

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>Regioni449 – 872Translocation domain (TD)2 PublicationsAdd BLAST424
Regioni492 – 545BeltBy similarityAdd BLAST54
Regioni873 – 1092N-terminus of receptor binding domain (N-RBD)2 PublicationsAdd BLAST220
Regioni1093 – 1296C-terminus of receptor binding domain (C-RBD)2 PublicationsAdd BLAST204

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>Motifi1264 – 1267Host ganglioside-binding motifBy similarity4

<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

Botulinum neurotoxin A light chain: Has protease activity (PubMed:8103915, PubMed:8294407).2 Publications
Botulinum neurotoxin A heavy chain: 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:17173035, 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 (PubMed:9783750). The RBD binds transiently exposed coreceptors on the host presynaptic cell membrane (PubMed:19476346).3 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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

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

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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_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.

P0DPI1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPFVNKQFNY KDPVNGVDIA YIKIPNAGQM QPVKAFKIHN KIWVIPERDT
60 70 80 90 100
FTNPEEGDLN PPPEAKQVPV SYYDSTYLST DNEKDNYLKG VTKLFERIYS
110 120 130 140 150
TDLGRMLLTS IVRGIPFWGG STIDTELKVI DTNCINVIQP DGSYRSEELN
160 170 180 190 200
LVIIGPSADI IQFECKSFGH EVLNLTRNGY GSTQYIRFSP DFTFGFEESL
210 220 230 240 250
EVDTNPLLGA GKFATDPAVT LAHELIHAGH RLYGIAINPN RVFKVNTNAY
260 270 280 290 300
YEMSGLEVSF EELRTFGGHD AKFIDSLQEN EFRLYYYNKF KDIASTLNKA
310 320 330 340 350
KSIVGTTASL QYMKNVFKEK YLLSEDTSGK FSVDKLKFDK LYKMLTEIYT
360 370 380 390 400
EDNFVKFFKV LNRKTYLNFD KAVFKINIVP KVNYTIYDGF NLRNTNLAAN
410 420 430 440 450
FNGQNTEINN MNFTKLKNFT GLFEFYKLLC VRGIITSKTK SLDKGYNKAL
460 470 480 490 500
NDLCIKVNNW DLFFSPSEDN FTNDLNKGEE ITSDTNIEAA EENISLDLIQ
510 520 530 540 550
QYYLTFNFDN EPENISIENL SSDIIGQLEL MPNIERFPNG KKYELDKYTM
560 570 580 590 600
FHYLRAQEFE HGKSRIALTN SVNEALLNPS RVYTFFSSDY VKKVNKATEA
610 620 630 640 650
AMFLGWVEQL VYDFTDETSE VSTTDKIADI TIIIPYIGPA LNIGNMLYKD
660 670 680 690 700
DFVGALIFSG AVILLEFIPE IAIPVLGTFA LVSYIANKVL TVQTIDNALS
710 720 730 740 750
KRNEKWDEVY KYIVTNWLAK VNTQIDLIRK KMKEALENQA EATKAIINYQ
760 770 780 790 800
YNQYTEEEKN NINFNIDDLS SKLNESINKA MININKFLNQ CSVSYLMNSM
810 820 830 840 850
IPYGVKRLED FDASLKDALL KYIYDNRGTL IGQVDRLKDK VNNTLSTDIP
860 870 880 890 900
FQLSKYVDNQ RLLSTFTEYI KNIINTSILN LRYESNHLID LSRYASKINI
910 920 930 940 950
GSKVNFDPID KNQIQLFNLE SSKIEVILKN AIVYNSMYEN FSTSFWIRIP
960 970 980 990 1000
KYFNSISLNN EYTIINCMEN NSGWKVSLNY GEIIWTLQDT QEIKQRVVFK
1010 1020 1030 1040 1050
YSQMINISDY INRWIFVTIT NNRLNNSKIY INGRLIDQKP ISNLGNIHAS
1060 1070 1080 1090 1100
NNIMFKLDGC RDTHRYIWIK YFNLFDKELN EKEIKDLYDN QSNSGILKDF
1110 1120 1130 1140 1150
WGDYLQYDKP YYMLNLYDPN KYVDVNNVGI RGYMYLKGPR GSVMTTNIYL
1160 1170 1180 1190 1200
NSSLYRGTKF IIKKYASGNK DNIVRNNDRV YINVVVKNKE YRLATNASQA
1210 1220 1230 1240 1250
GVEKILSALE IPDVGNLSQV VVMKSKNDQG ITNKCKMNLQ DNNGNDIGFI
1260 1270 1280 1290
GFHQFNNIAK LVASNWYNRQ IERSSRTLGC SWEFIPVDDG WGERPL
Length:1,296
Mass (Da):149,426
Last modified:July 18, 2018 - 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:iDEA8CF2754AE43E6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti876T → L AA sequence (PubMed:3178218).Curated1
Sequence conflicti892S → K AA sequence (PubMed:3178218).Curated1
Sequence conflicti1218S → Y AA sequence (PubMed:8397793).Curated1

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
AM412317 Genomic DNA Translation: CAL82360.1
CP000727 Genomic DNA Translation: ABS38337.1
M27892 Genomic DNA Translation: AAA23269.1

Protein sequence database of the Protein Information Resource

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PIRi
A35294 BTCLAB

NCBI Reference Sequences

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RefSeqi
WP_011948511.1, NC_009698.1
YP_001253342.1, NC_009495.1
YP_001386738.1, NC_009698.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
5185061
5398487

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cbh:CLC_0862
cbo:CBO0806

<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

BOTOX product information Web site
Protein Spotlight

From sausages to wrinkles - Issue 19 of February 2002

BotDB - A Database Resource for Clostridial Neurotoxins

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM412317 Genomic DNA Translation: CAL82360.1
CP000727 Genomic DNA Translation: ABS38337.1
M27892 Genomic DNA Translation: AAA23269.1
PIRiA35294 BTCLAB
RefSeqiWP_011948511.1, NC_009698.1
YP_001253342.1, NC_009495.1
YP_001386738.1, NC_009698.1

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
2NYYX-ray2.61A2-1296[»]
2NZ9X-ray3.79A/B2-1296[»]
3BTAX-ray3.20A2-1296[»]
3BWIX-ray1.70A1-424[»]
3C88X-ray1.60A1-424[»]
3C89X-ray1.58A1-424[»]
3C8AX-ray1.52A1-424[»]
3C8BX-ray1.47A1-424[»]
3DDAX-ray1.50A1-424[»]
3DDBX-ray1.60A1-424[»]
3DS9X-ray1.76A1-417[»]
3DSEX-ray1.90A1-417[»]
3FUOX-ray1.80A871-1296[»]
3K3QX-ray2.60B3-250[»]
C251-425[»]
3QIXX-ray2.41A/B3-424[»]
3QIYX-ray2.30A3-424[»]
3QIZX-ray2.00A3-424[»]
3QJ0X-ray2.30A3-424[»]
3QW5X-ray1.60A1-424[»]
3QW6X-ray1.60A1-424[»]
3QW7X-ray1.50A1-424[»]
3QW8X-ray1.60A1-424[»]
4EJ5X-ray1.87A1-425[»]
4EL4X-ray1.20A1-425[»]
4ELCX-ray1.80A1-425[»]
4KS6X-ray1.93A1-425[»]
4KTXX-ray2.59A1-425[»]
4KUFX-ray1.70A1-425[»]
4ZJXX-ray1.94A1-424[»]
5L21X-ray1.68A872-1296[»]
SMRiP0DPI1
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

BindingDBiP0DPI1
ChEMBLiCHEMBL5344

Protein family/group databases

UniLectiniP0DPI1

Genome annotation databases

GeneIDi5185061
5398487
KEGGicbh:CLC_0862
cbo:CBO0806

Phylogenomic databases

KOiK06011
OMAiDEGYNKA

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
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiBXA1_CLOBH
<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: P0DPI1
Secondary accession number(s): A5HZZ9
, A7G1U9, P01561, P10845, P18639
<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: July 18, 2018
Last modified: October 16, 2019
This is version 10 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, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. Peptidase families
    Classification of peptidase families and list of entries
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