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P10845

- BXA1_CLOBO

UniProt

P10845 - BXA1_CLOBO

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Protein

Botulinum neurotoxin type A

Gene

botA

Organism
Clostridium botulinum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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 cytoplasm Source: UniProtKB-KW
  2. host cell junction Source: UniProtKB-KW
  3. host cell synapse Source: UniProtKB-KW
  4. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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.
InterProiIPR013320. ConA-like_dom.
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

        10         20         30         40         50
MPFVNKQFNY KDPVNGVDIA YIKIPNVGQM 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):149,454
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.
RefSeqiWP_003356619.1. NZ_JFGM01000026.1.

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.
RefSeqi WP_003356619.1. NZ_JFGM01000026.1.

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.

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 IPR013320. ConA-like_dom.
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 29, 2014
This is version 166 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

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