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Protein

Botulinum neurotoxin type A

Gene

botA

Organism
Clostridium botulinum
Status
Reviewed-Annotation score: 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

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi223Zinc; catalytic1
Active sitei2241
Metal bindingi227Zinc; catalytic1
Metal bindingi262Zinc; catalytic1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Neurotoxin, Protease, Toxin

Keywords - Biological processi

Virulence

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.69. 1462.
ReactomeiR-HSA-5250968. 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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei627 – 647HelicalSequence analysisAdd BLAST21
Transmembranei656 – 676HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Mutagenesisi262E → A: Drastic decrease in enzymatic activity. 1 Publication1
Mutagenesisi266F → A: Decreases enzymatic activity. 1 Publication1
Mutagenesisi366Y → A: Decreases enzymatic activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5192.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00000292112 – 448Botulinum neurotoxin A light chainAdd BLAST447
ChainiPRO_0000029212449 – 1296Botulinum neurotoxin A heavy chainAdd BLAST848

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 interactors.
MINTiMINT-1795451.
STRINGi445335.CBN_0826.

Chemistry databases

BindingDBiP10845.

Structurei

Secondary structure

11296
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Beta strandi16 – 23Combined sources8
Beta strandi26 – 28Combined sources3
Beta strandi33 – 39Combined sources7
Beta strandi42 – 48Combined sources7
Beta strandi51 – 53Combined sources3
Helixi54 – 56Combined sources3
Turni64 – 66Combined sources3
Turni68 – 70Combined sources3
Turni75 – 78Combined sources4
Helixi81 – 99Combined sources19
Helixi102 – 113Combined sources12
Beta strandi126 – 128Combined sources3
Helixi131 – 133Combined sources3
Beta strandi134 – 138Combined sources5
Beta strandi140 – 142Combined sources3
Beta strandi144 – 148Combined sources5
Beta strandi150 – 155Combined sources6
Beta strandi158 – 161Combined sources4
Beta strandi164 – 166Combined sources3
Turni170 – 172Combined sources3
Turni175 – 177Combined sources3
Beta strandi178 – 180Combined sources3
Beta strandi184 – 187Combined sources4
Beta strandi192 – 196Combined sources5
Helixi200 – 203Combined sources4
Helixi206 – 208Combined sources3
Beta strandi210 – 214Combined sources5
Helixi217 – 232Combined sources16
Beta strandi242 – 244Combined sources3
Helixi249 – 253Combined sources5
Beta strandi257 – 259Combined sources3
Helixi260 – 266Combined sources7
Helixi268 – 271Combined sources4
Helixi276 – 299Combined sources24
Beta strandi302 – 308Combined sources7
Helixi310 – 321Combined sources12
Beta strandi323 – 325Combined sources3
Beta strandi327 – 329Combined sources3
Beta strandi331 – 333Combined sources3
Helixi335 – 347Combined sources13
Helixi351 – 358Combined sources8
Beta strandi366 – 368Combined sources3
Beta strandi372 – 375Combined sources4
Turni381 – 383Combined sources3
Turni386 – 388Combined sources3
Beta strandi393 – 395Combined sources3
Helixi396 – 398Combined sources3
Helixi399 – 401Combined sources3
Helixi402 – 404Combined sources3
Turni406 – 409Combined sources4
Helixi410 – 412Combined sources3
Beta strandi414 – 418Combined sources5
Turni420 – 422Combined sources3
Beta strandi424 – 431Combined sources8
Beta strandi454 – 458Combined sources5
Helixi459 – 461Combined sources3
Helixi468 – 470Combined sources3
Beta strandi479 – 481Combined sources3
Helixi496 – 503Combined sources8
Beta strandi542 – 547Combined sources6
Helixi550 – 555Combined sources6
Beta strandi563 – 565Combined sources3
Beta strandi570 – 573Combined sources4
Beta strandi576 – 579Combined sources4
Beta strandi581 – 583Combined sources3
Helixi589 – 593Combined sources5
Helixi600 – 602Combined sources3
Helixi603 – 618Combined sources16
Beta strandi625 – 629Combined sources5
Helixi637 – 641Combined sources5
Turni642 – 645Combined sources4
Beta strandi648 – 650Combined sources3
Helixi652 – 659Combined sources8
Helixi661 – 663Combined sources3
Beta strandi679 – 681Combined sources3
Helixi688 – 720Combined sources33
Helixi722 – 752Combined sources31
Turni758 – 761Combined sources4
Helixi766 – 799Combined sources34
Helixi801 – 825Combined sources25
Turni826 – 833Combined sources8
Helixi834 – 845Combined sources12
Helixi853 – 855Combined sources3
Helixi860 – 871Combined sources12
Helixi872 – 875Combined sources4
Beta strandi877 – 884Combined sources8
Beta strandi887 – 890Combined sources4
Beta strandi897 – 900Combined sources4
Beta strandi904 – 906Combined sources3
Beta strandi908 – 910Combined sources3
Beta strandi914 – 919Combined sources6
Beta strandi924 – 927Combined sources4
Helixi930 – 932Combined sources3
Beta strandi935 – 938Combined sources4
Beta strandi941 – 948Combined sources8
Helixi955 – 957Combined sources3
Beta strandi962 – 969Combined sources8
Beta strandi972 – 979Combined sources8
Beta strandi982 – 988Combined sources7
Beta strandi990 – 992Combined sources3
Beta strandi994 – 1000Combined sources7
Beta strandi1003 – 1007Combined sources5
Beta strandi1015 – 1021Combined sources7
Beta strandi1025 – 1031Combined sources7
Beta strandi1034 – 1040Combined sources7
Beta strandi1051 – 1059Combined sources9
Beta strandi1066 – 1077Combined sources12
Helixi1081 – 1092Combined sources12
Beta strandi1102 – 1104Combined sources3
Beta strandi1106 – 1108Combined sources3
Beta strandi1111 – 1117Combined sources7
Beta strandi1122 – 1126Combined sources5
Beta strandi1133 – 1137Combined sources5
Beta strandi1142 – 1145Combined sources4
Turni1146 – 1148Combined sources3
Beta strandi1149 – 1152Combined sources4
Beta strandi1160 – 1166Combined sources7
Beta strandi1170 – 1173Combined sources4
Beta strandi1179 – 1188Combined sources10
Beta strandi1190 – 1195Combined sources6
Beta strandi1199 – 1202Combined sources4
Beta strandi1207 – 1209Combined sources3
Helixi1211 – 1213Combined sources3
Beta strandi1220 – 1225Combined sources6
Beta strandi1229 – 1231Combined sources3
Beta strandi1235 – 1240Combined sources6
Beta strandi1242 – 1244Combined sources3
Beta strandi1246 – 1255Combined sources10
Beta strandi1258 – 1264Combined sources7
Helixi1267 – 1269Combined sources3
Helixi1275 – 1277Combined sources3
Turni1278 – 1280Combined sources3
Beta strandi1282 – 1285Combined sources4
Turni1289 – 1291Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4ZJXX-ray1.94A1-424[»]
5JLVX-ray2.00A/B872-1296[»]
5JMCX-ray2.64A/C/E/G872-1296[»]
ProteinModelPortaliP10845.
SMRiP10845.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10845.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M27 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProiIPR000395. Bot/tetX.
IPR013320. ConA-like_dom.
IPR011065. Kunitz_inhibitor_ST1-like.
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)DescriptionActionsGraphical viewLength
Sequence conflicti2P → Q in CAA36289 (PubMed:2185020).Curated1
Sequence conflicti480E → P AA sequence (PubMed:3896784).Curated1
Sequence conflicti876T → L AA sequence (PubMed:3178218).Curated1
Sequence conflicti892S → K AA sequence (PubMed:3178218).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti27V → A.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_LFOS01000037.1.
WP_011948511.1. NZ_LHUL01000004.1.

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:
EMBLi
GenBanki
DDBJi
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_LFOS01000037.1.
WP_011948511.1. NZ_LHUL01000004.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4ZJXX-ray1.94A1-424[»]
5JLVX-ray2.00A/B872-1296[»]
5JMCX-ray2.64A/C/E/G872-1296[»]
ProteinModelPortaliP10845.
SMRiP10845.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42781N.
IntActiP10845. 3 interactors.
MINTiMINT-1795451.
STRINGi445335.CBN_0826.

Chemistry databases

BindingDBiP10845.
ChEMBLiCHEMBL5192.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.24.69. 1462.
ReactomeiR-HSA-5250968. Toxicity of botulinum toxin type A (BoNT/A).

Miscellaneous databases

EvolutionaryTraceiP10845.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProiIPR000395. Bot/tetX.
IPR013320. ConA-like_dom.
IPR011065. Kunitz_inhibitor_ST1-like.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 184 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.