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P10845

- BXA1_CLOBO

UniProt

P10845 - BXA1_CLOBO

Protein

Botulinum neurotoxin type A

Gene

botA

Organism
Clostridium botulinum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the 197-Gln-|-Arg-198 bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure.

    Catalytic activityi

    Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi223 – 2231Zinc; catalytic
    Active sitei224 – 2241
    Metal bindingi227 – 2271Zinc; catalytic
    Metal bindingi262 – 2621Zinc; catalytic

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: Reactome
    2. protein binding Source: IntAct
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. inhibition of neurotransmitter uptake Source: InterPro
    2. neurotransmitter secretion Source: Reactome
    3. pathogenesis Source: UniProtKB-KW
    4. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Neurotoxin, Protease, Toxin

    Keywords - Biological processi

    Virulence

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_200737. Toxicity of botulinum toxin type A (BoNT/A).

    Protein family/group databases

    TCDBi1.C.8.1.1. the botulinum and tetanus toxin (btt) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Botulinum neurotoxin type A (EC:3.4.24.69)
    Short name:
    BoNT/A
    Alternative name(s):
    Bontoxilysin-A
    Short name:
    BOTOX
    Cleaved into the following 2 chains:
    Gene namesi
    Name:botA
    Synonyms:atx, bna
    OrganismiClostridium botulinum
    Taxonomic identifieri1491 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

    Subcellular locationi

    GO - Cellular componenti

    1. host cell cytosol Source: UniProtKB-SubCell
    2. host cell junction Source: UniProtKB-KW
    3. host cell presynaptic membrane Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Pharmaceutical usei

    Available under the name BOTOX (Allergan) for the treatment of strabismus and blepharospasm associated with dystonia and cervical dystonia. Also used for the treatment of hemifacial spasm and a number of other neurological disorders characterized by abnormal muscle contraction.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi262 – 2621E → A: Drastic decrease in enzymatic activity. 1 Publication
    Mutagenesisi266 – 2661F → A: Decreases enzymatic activity. 1 Publication
    Mutagenesisi366 – 3661Y → A: Decreases enzymatic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 448447Botulinum neurotoxin A light chainPRO_0000029211Add
    BLAST
    Chaini449 – 1296848Botulinum neurotoxin A heavy chainPRO_0000029212Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi430 ↔ 454Interchain (between light and heavy chains)
    Disulfide bondi1235 ↔ 1280

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Disulfide-linked heterodimer of a light chain (L) and a heavy chain (H).

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Sv2aQ025632EBI-8178893,EBI-466194From a different organism.
    Sv2cQ9Z2I612EBI-8178893,EBI-8178859From a different organism.

    Protein-protein interaction databases

    DIPiDIP-42781N.
    IntActiP10845. 3 interactions.
    MINTiMINT-1795451.

    Structurei

    Secondary structure

    1
    1296
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64
    Beta strandi16 – 238
    Beta strandi26 – 283
    Beta strandi33 – 397
    Beta strandi42 – 487
    Beta strandi51 – 533
    Helixi54 – 563
    Turni64 – 663
    Turni68 – 703
    Turni75 – 784
    Helixi81 – 9919
    Helixi102 – 11312
    Beta strandi126 – 1283
    Helixi131 – 1333
    Beta strandi134 – 1385
    Beta strandi140 – 1423
    Beta strandi144 – 1485
    Beta strandi150 – 1556
    Beta strandi158 – 1614
    Beta strandi164 – 1663
    Turni175 – 1773
    Beta strandi178 – 1803
    Beta strandi184 – 1874
    Beta strandi192 – 1965
    Helixi200 – 2034
    Beta strandi210 – 2145
    Helixi217 – 23216
    Beta strandi242 – 2443
    Helixi249 – 2535
    Beta strandi257 – 2593
    Helixi260 – 2667
    Helixi268 – 2714
    Helixi276 – 29924
    Beta strandi302 – 3087
    Helixi310 – 32112
    Beta strandi323 – 3253
    Beta strandi327 – 3293
    Beta strandi331 – 3333
    Helixi335 – 34713
    Helixi351 – 3588
    Beta strandi366 – 3683
    Beta strandi372 – 3754
    Turni381 – 3833
    Turni386 – 3883
    Beta strandi393 – 3953
    Helixi396 – 3983
    Helixi399 – 4013
    Helixi402 – 4043
    Turni406 – 4094
    Helixi410 – 4123
    Beta strandi414 – 4185
    Turni421 – 4233
    Beta strandi424 – 4318
    Beta strandi454 – 4585
    Helixi459 – 4613
    Helixi468 – 4703
    Beta strandi479 – 4813
    Helixi496 – 5038
    Beta strandi542 – 5476
    Helixi550 – 5556
    Beta strandi563 – 5653
    Beta strandi570 – 5734
    Beta strandi576 – 5794
    Beta strandi581 – 5833
    Helixi589 – 5935
    Helixi600 – 6023
    Helixi603 – 61816
    Beta strandi625 – 6295
    Helixi637 – 6415
    Turni642 – 6454
    Beta strandi648 – 6503
    Helixi652 – 6598
    Helixi661 – 6633
    Beta strandi679 – 6813
    Helixi688 – 72033
    Helixi722 – 75231
    Turni758 – 7614
    Helixi766 – 79934
    Helixi801 – 82525
    Turni826 – 8338
    Helixi834 – 84512
    Helixi853 – 8553
    Helixi860 – 87112
    Helixi873 – 8764
    Beta strandi877 – 8848
    Beta strandi887 – 8904
    Beta strandi897 – 9004
    Beta strandi904 – 9063
    Beta strandi908 – 9103
    Beta strandi914 – 9196
    Beta strandi924 – 9274
    Helixi930 – 9323
    Beta strandi935 – 9384
    Beta strandi941 – 9488
    Helixi955 – 9573
    Beta strandi962 – 9698
    Beta strandi972 – 9798
    Beta strandi982 – 9887
    Beta strandi990 – 9923
    Beta strandi994 – 10007
    Beta strandi1003 – 10075
    Beta strandi1015 – 10217
    Beta strandi1025 – 10317
    Beta strandi1034 – 10407
    Beta strandi1051 – 10599
    Beta strandi1066 – 107712
    Helixi1081 – 109212
    Beta strandi1102 – 11043
    Beta strandi1106 – 11083
    Beta strandi1111 – 11177
    Beta strandi1122 – 11265
    Beta strandi1133 – 11375
    Beta strandi1142 – 11454
    Turni1146 – 11483
    Beta strandi1149 – 11524
    Beta strandi1160 – 11667
    Beta strandi1170 – 11734
    Beta strandi1179 – 118810
    Beta strandi1190 – 11956
    Beta strandi1199 – 12024
    Beta strandi1207 – 12093
    Helixi1211 – 12133
    Beta strandi1220 – 12256
    Beta strandi1229 – 12313
    Beta strandi1235 – 12406
    Beta strandi1246 – 125510
    Beta strandi1258 – 12647
    Helixi1267 – 12693
    Helixi1275 – 12773
    Turni1278 – 12803
    Beta strandi1282 – 12854
    Turni1289 – 12913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UEEmodel-A2-545[»]
    1XTFX-ray2.20A/B2-420[»]
    1XTGX-ray2.10A2-420[»]
    2ILPX-ray1.90A/B3-424[»]
    2IMAX-ray1.94A/B1-424[»]
    2IMBX-ray2.41A/B3-424[»]
    2IMCX-ray2.00A/B3-424[»]
    2ISEX-ray2.20A/B1-420[»]
    2ISGX-ray2.00A/B1-420[»]
    2ISHX-ray2.00A/B1-420[»]
    2NYYX-ray2.61A2-1296[»]
    2NZ9X-ray3.79A/B2-1296[»]
    2VU9X-ray1.60A876-1296[»]
    2VUAX-ray1.70A876-1296[»]
    2W2DX-ray2.59A/C3-442[»]
    B/D447-877[»]
    3BOKX-ray1.25A3-425[»]
    3BONX-ray1.20A3-425[»]
    3BOOX-ray1.40A3-425[»]
    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[»]
    3FUOX-ray1.80A871-1296[»]
    3V0AX-ray2.70A1-1296[»]
    3V0BX-ray3.90A1-1296[»]
    3V0CX-ray4.30A1-1296[»]
    3ZURX-ray2.71A/B3-430[»]
    A/B454-865[»]
    3ZUSX-ray2.95A/B/C/D3-431[»]
    A/B/C/D454-865[»]
    4EJ5X-ray1.87A1-425[»]
    4EL4X-ray1.20A1-425[»]
    4ELCX-ray1.80A1-425[»]
    4HEVX-ray2.50A/B1-425[»]
    4IQPX-ray2.30A871-1296[»]
    4JRAX-ray2.30A/B871-1296[»]
    ProteinModelPortaliP10845.
    SMRiP10845. Positions 1-423.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10845.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei627 – 64721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei656 – 67621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M27 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG119715.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    3.90.1240.10. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR011065. Kunitz_inhibitor_ST1-like.
    IPR000395. Neurotox_Zn_protease.
    IPR013104. Toxin_rcpt-bd_C.
    IPR012928. Toxin_rcpt-bd_N.
    IPR012500. Toxin_trans.
    [Graphical view]
    PfamiPF01742. Peptidase_M27. 1 hit.
    PF07951. Toxin_R_bind_C. 1 hit.
    PF07953. Toxin_R_bind_N. 1 hit.
    PF07952. Toxin_trans. 1 hit.
    [Graphical view]
    PRINTSiPR00760. BONTOXILYSIN.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF50386. SSF50386. 1 hit.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P10845-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFVNKQFNY KDPVNGVDIA YIKIPNVGQM QPVKAFKIHN KIWVIPERDT     50
    FTNPEEGDLN PPPEAKQVPV SYYDSTYLST DNEKDNYLKG VTKLFERIYS 100
    TDLGRMLLTS IVRGIPFWGG STIDTELKVI DTNCINVIQP DGSYRSEELN 150
    LVIIGPSADI IQFECKSFGH EVLNLTRNGY GSTQYIRFSP DFTFGFEESL 200
    EVDTNPLLGA GKFATDPAVT LAHELIHAGH RLYGIAINPN RVFKVNTNAY 250
    YEMSGLEVSF EELRTFGGHD AKFIDSLQEN EFRLYYYNKF KDIASTLNKA 300
    KSIVGTTASL QYMKNVFKEK YLLSEDTSGK FSVDKLKFDK LYKMLTEIYT 350
    EDNFVKFFKV LNRKTYLNFD KAVFKINIVP KVNYTIYDGF NLRNTNLAAN 400
    FNGQNTEINN MNFTKLKNFT GLFEFYKLLC VRGIITSKTK SLDKGYNKAL 450
    NDLCIKVNNW DLFFSPSEDN FTNDLNKGEE ITSDTNIEAA EENISLDLIQ 500
    QYYLTFNFDN EPENISIENL SSDIIGQLEL MPNIERFPNG KKYELDKYTM 550
    FHYLRAQEFE HGKSRIALTN SVNEALLNPS RVYTFFSSDY VKKVNKATEA 600
    AMFLGWVEQL VYDFTDETSE VSTTDKIADI TIIIPYIGPA LNIGNMLYKD 650
    DFVGALIFSG AVILLEFIPE IAIPVLGTFA LVSYIANKVL TVQTIDNALS 700
    KRNEKWDEVY KYIVTNWLAK VNTQIDLIRK KMKEALENQA EATKAIINYQ 750
    YNQYTEEEKN NINFNIDDLS SKLNESINKA MININKFLNQ CSVSYLMNSM 800
    IPYGVKRLED FDASLKDALL KYIYDNRGTL IGQVDRLKDK VNNTLSTDIP 850
    FQLSKYVDNQ RLLSTFTEYI KNIINTSILN LRYESNHLID LSRYASKINI 900
    GSKVNFDPID KNQIQLFNLE SSKIEVILKN AIVYNSMYEN FSTSFWIRIP 950
    KYFNSISLNN EYTIINCMEN NSGWKVSLNY GEIIWTLQDT QEIKQRVVFK 1000
    YSQMINISDY INRWIFVTIT NNRLNNSKIY INGRLIDQKP ISNLGNIHAS 1050
    NNIMFKLDGC RDTHRYIWIK YFNLFDKELN EKEIKDLYDN QSNSGILKDF 1100
    WGDYLQYDKP YYMLNLYDPN KYVDVNNVGI RGYMYLKGPR GSVMTTNIYL 1150
    NSSLYRGTKF IIKKYASGNK DNIVRNNDRV YINVVVKNKE YRLATNASQA 1200
    GVEKILSALE IPDVGNLSQV VVMKSKNDQG ITNKCKMNLQ DNNGNDIGFI 1250
    GFHQFNNIAK LVASNWYNRQ IERSSRTLGC SWEFIPVDDG WGERPL 1296
    Length:1,296
    Mass (Da):149,454
    Last modified:January 23, 2007 - v4
    Checksum:iB731EF5BA5E62FDA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21P → Q in CAA36289. (PubMed:2185020)Curated
    Sequence conflicti480 – 4801E → P AA sequence (PubMed:3896784)Curated
    Sequence conflicti876 – 8761T → L AA sequence (PubMed:3178218)Curated
    Sequence conflicti892 – 8921S → K AA sequence (PubMed:3178218)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti27 – 271V → A.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52066 Genomic DNA. Translation: CAA36289.1.
    M30196 Genomic DNA. Translation: AAA23262.1.
    X92973 Genomic DNA. Translation: CAA63551.1.
    D67030 Genomic DNA. Translation: BAA11051.1.
    M27892 Genomic DNA. Translation: AAA23269.1.
    PIRiA35294. BTCLAB.

    Cross-referencesi

    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52066 Genomic DNA. Translation: CAA36289.1 .
    M30196 Genomic DNA. Translation: AAA23262.1 .
    X92973 Genomic DNA. Translation: CAA63551.1 .
    D67030 Genomic DNA. Translation: BAA11051.1 .
    M27892 Genomic DNA. Translation: AAA23269.1 .
    PIRi A35294. BTCLAB.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UEE model - A 2-545 [» ]
    1XTF X-ray 2.20 A/B 2-420 [» ]
    1XTG X-ray 2.10 A 2-420 [» ]
    2ILP X-ray 1.90 A/B 3-424 [» ]
    2IMA X-ray 1.94 A/B 1-424 [» ]
    2IMB X-ray 2.41 A/B 3-424 [» ]
    2IMC X-ray 2.00 A/B 3-424 [» ]
    2ISE X-ray 2.20 A/B 1-420 [» ]
    2ISG X-ray 2.00 A/B 1-420 [» ]
    2ISH X-ray 2.00 A/B 1-420 [» ]
    2NYY X-ray 2.61 A 2-1296 [» ]
    2NZ9 X-ray 3.79 A/B 2-1296 [» ]
    2VU9 X-ray 1.60 A 876-1296 [» ]
    2VUA X-ray 1.70 A 876-1296 [» ]
    2W2D X-ray 2.59 A/C 3-442 [» ]
    B/D 447-877 [» ]
    3BOK X-ray 1.25 A 3-425 [» ]
    3BON X-ray 1.20 A 3-425 [» ]
    3BOO X-ray 1.40 A 3-425 [» ]
    3BTA X-ray 3.20 A 2-1296 [» ]
    3BWI X-ray 1.70 A 1-424 [» ]
    3C88 X-ray 1.60 A 1-424 [» ]
    3C89 X-ray 1.58 A 1-424 [» ]
    3C8A X-ray 1.52 A 1-424 [» ]
    3C8B X-ray 1.47 A 1-424 [» ]
    3DDA X-ray 1.50 A 1-424 [» ]
    3DDB X-ray 1.60 A 1-424 [» ]
    3DS9 X-ray 1.76 A 1-417 [» ]
    3FUO X-ray 1.80 A 871-1296 [» ]
    3V0A X-ray 2.70 A 1-1296 [» ]
    3V0B X-ray 3.90 A 1-1296 [» ]
    3V0C X-ray 4.30 A 1-1296 [» ]
    3ZUR X-ray 2.71 A/B 3-430 [» ]
    A/B 454-865 [» ]
    3ZUS X-ray 2.95 A/B/C/D 3-431 [» ]
    A/B/C/D 454-865 [» ]
    4EJ5 X-ray 1.87 A 1-425 [» ]
    4EL4 X-ray 1.20 A 1-425 [» ]
    4ELC X-ray 1.80 A 1-425 [» ]
    4HEV X-ray 2.50 A/B 1-425 [» ]
    4IQP X-ray 2.30 A 871-1296 [» ]
    4JRA X-ray 2.30 A/B 871-1296 [» ]
    ProteinModelPortali P10845.
    SMRi P10845. Positions 1-423.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-42781N.
    IntActi P10845. 3 interactions.
    MINTi MINT-1795451.

    Chemistry

    BindingDBi P10845.
    ChEMBLi CHEMBL5192.
    DrugBanki DB00083. Botulinum Toxin Type A.

    Protein family/group databases

    TCDBi 1.C.8.1.1. the botulinum and tetanus toxin (btt) family.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG119715.

    Enzyme and pathway databases

    Reactomei REACT_200737. Toxicity of botulinum toxin type A (BoNT/A).

    Miscellaneous databases

    EvolutionaryTracei P10845.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    3.90.1240.10. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR011065. Kunitz_inhibitor_ST1-like.
    IPR000395. Neurotox_Zn_protease.
    IPR013104. Toxin_rcpt-bd_C.
    IPR012928. Toxin_rcpt-bd_N.
    IPR012500. Toxin_trans.
    [Graphical view ]
    Pfami PF01742. Peptidase_M27. 1 hit.
    PF07951. Toxin_R_bind_C. 1 hit.
    PF07953. Toxin_R_bind_N. 1 hit.
    PF07952. Toxin_trans. 1 hit.
    [Graphical view ]
    PRINTSi PR00760. BONTOXILYSIN.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF50386. SSF50386. 1 hit.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete amino acid sequence of the Clostridium botulinum type A neurotoxin, deduced by nucleotide sequence analysis of the encoding gene."
      Thompson D.E., Brehm J.K., Oultram J.D., Swinfield T.-J., Shone C.C., Atkinson T., Melling J., Minton N.P.
      Eur. J. Biochem. 189:73-81(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Type A / NCTC 2916.
    2. "The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins."
      Binz T., Kurazono H., Wille M., Frevert J., Wernars K., Niemann H.
      J. Biol. Chem. 265:9153-9158(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Type A / 62A.
    3. "Organization and phylogenetic interrelationships of genes encoding components of the botulinum toxin complex in proteolytic Clostridium botulinum types A, B, and F: evidence of chimeric sequences in the gene encoding the nontoxic nonhemagglutinin component."
      East A.K., Bhandari M., Stacey J.M., Campbell K.D., Collins M.D.
      Int. J. Syst. Bacteriol. 46:1105-1112(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
      Strain: Type A / 62A.
    4. "Molecular characterization of two forms of nontoxic-nonhemagglutinin components of Clostridium botulinum type A progenitor toxins."
      Fujita R., Fujinaga Y., Inoue K., Nakajima H., Kumon H., Oguma K.
      FEBS Lett. 376:41-44(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
      Strain: Type A / NIH.
    5. "Partial amino acid sequence of the heavy and light chains of botulinum neurotoxin type A."
      Schmidt J.J., Sartymoorthy V., Dasgupta B.R.
      Biochem. Biophys. Res. Commun. 119:900-904(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-17.
    6. "Partial sequence of the light chain of botulinum neurotoxin type A."
      Dasgupta B.R., Foley J., Niece R.
      Biochemistry 26:4162-4162(1987)
      Cited for: PROTEIN SEQUENCE OF 2-47.
    7. "Botulinum neurotoxin type A: sequence of amino acids at the N-terminus and around the nicking site."
      Dasgupta B.R., Dekleva M.L.
      Biochimie 72:661-664(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-6 AND 445-457.
    8. "Botulinum neurotoxin type A: cleavage of the heavy chain into two halves and their partial sequences."
      Sathymoorthy V., Dasgupta B.R., Foley J., Niece R.L.
      Arch. Biochem. Biophys. 266:142-151(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 449-475 AND 873-896.
    9. "Inactivation of Clostridium botulinum type A neurotoxin by trypsin and purification of two tryptic fragments. Proteolytic action near the COOH-terminus of the heavy subunit destroys toxin-binding activity."
      Shone C.C., Hambleton P., Melling J.
      Eur. J. Biochem. 151:75-82(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 449-483.
    10. "Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds."
      Schiavo G., Santtuci A., Dasgupta B.R., Mehta P.P., Jontes J., Benfenati F., Wilson M.C., Montecucco C.
      FEBS Lett. 335:99-103(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF SUBSTRATE.
    11. "Site-directed mutagenesis identifies active-site residues of the light chain of botulinum neurotoxin type a."
      Rigoni M., Caccin P., Johnson E.A., Montecucco C., Rossetto O.
      Biochem. Biophys. Res. Commun. 288:1231-1237(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-262; PHE-266 AND TYR-366.
    12. "SV2 is the protein receptor for botulinum neurotoxin A."
      Dong M., Yeh F., Tepp W.H., Dean C., Johnson E.A., Janz R., Chapman E.R.
      Science 312:592-596(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SV2.
    13. "Crystal structure of botulinum neurotoxin type A and implications for toxicity."
      Lacy D.B., Tepp W., Cohen A.C., Dasgupta B.R., Stevens R.C.
      Nat. Struct. Biol. 5:898-902(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).

    Entry informationi

    Entry nameiBXA1_CLOBO
    AccessioniPrimary (citable) accession number: P10845
    Secondary accession number(s): P01561, P18639
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 165 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C1, D, E, F, and G.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Pharmaceutical

    Documents

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

    External Data

    Dasty 3