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CLOTE:TETX
Contents
| Species (Taxon ID) | Clostridium tetani (strain Massachusetts / E88). (212717) | |
| Gene Name(s) | tetX | |
| Protein Name(s) | Tetanus toxin
Tentoxylysin Tetanus toxin light chain Tetanus toxin chain L Tetanus toxin heavy chain Tetanus toxin chain H | |
| External Links | ||
| UniProt | P04958 | |
| EMBL | X04436 X06214 AF528097 M12739 | |
| PIR | A25689 | |
| RefSeq | NP_783831.1 WP_011100836.1 | |
| PDB | 1A8D 1AF9 1D0H 1DFQ 1DIW 1DLL 1FV2 1FV3 1YVG 1YXW 1YYN 1Z7H 3HMY 3HN1 4J1L | |
| PDBsum | 1A8D 1AF9 1D0H 1DFQ 1DIW 1DLL 1FV2 1FV3 1YVG 1YXW 1YYN 1Z7H 3HMY 3HN1 4J1L | |
| ProteinModelPortal | P04958 | |
| SMR | P04958 | |
| STRING | 212717.pE88_60 | |
| BindingDB | P04958 | |
| ChEMBL | CHEMBL2036 | |
| Allergome | 2757 | |
| MEROPS | M27.001 | |
| TCDB | 1.C.8.1.2 | |
| EnsemblBacteria | AAO37454 | |
| GeneID | 1061100 | |
| KEGG | ctc:pE88_60 | |
| PATRIC | 19513592 | |
| eggNOG | NOG12793 | |
| KO | K08644 | |
| OMA | DFWGNPL | |
| OrthoDB | EOG67T5DS | |
| BioCyc | CTET212717:GJAM-2513-MONOMER | |
| EvolutionaryTrace | P04958 | |
| PMAP-CutDB | P04958 | |
| Proteomes | UP000001412 | |
| GO | GO:0005576 GO:0004222 GO:0008270 GO:0051609 GO:0046929 GO:0009405 | |
| Gene3D | 2.60.120.200 3.90.1240.10 | |
| InterPro | IPR000395 IPR013320 IPR011065 IPR013104 IPR012928 IPR012500 | |
| Pfam | PF01742 PF07951 PF07953 PF07952 | |
| PRINTS | PR00760 | |
| SUPFAM | SSF49899 SSF50386 | |
| PROSITE | PS00142 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0046929 |
negative regulation of neurotransmitter secretion |
ECO:0000314 |
P |
Figure 1 shows that an increase in Tetanus toxin causes a decrease in noradrenaline release from rat brain cells. |
complete | |||||
| GO:0033619 |
membrane protein proteolysis |
ECO:0000314 |
P |
"Figure 8 demonstrated TeNT cleavage of VAMP2 (Vesicle-associated membrane protein 2) in rat cortical neurons." |
complete | |||||
| GO:0004222 |
metalloendopeptidase activity |
ECO:0000314 |
F |
Figure 7. Shows that the L chain of TeTx when bound to zinc is able to proteolytically cleave Synaptobrevin |
complete | |||||
|
enables |
GO:0004222 |
metalloendopeptidase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0046929 |
negative regulation of neurotransmitter secretion |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008320 |
protein transmembrane transporter activity |
ECO:0000269 |
experimental evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0071806 |
protein transmembrane transport |
ECO:0000366 |
evidence based on logical inference from automatic annotation used in automatic assertion |
GO:0008320 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0071806 |
protein transmembrane transport |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0008320 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004222 |
metalloendopeptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005576 |
extracellular region |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006508 |
proteolysis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008320 |
protein transmembrane transporter activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009405 |
pathogenesis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0046929 |
negative regulation of neurotransmitter secretion |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR000395 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0030669 |
clathrin-coated endocytic vesicle membrane |
Reactome:R-HSA-5228411 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
|
C |
Seeded From UniProt |
complete | |
|
part_of |
GO:0030666 |
endocytic vesicle membrane |
Reactome:R-HSA-5228408 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
|
C |
Seeded From UniProt |
complete | |
|
part_of |
GO:0005886 |
plasma membrane |
Reactome:R-HSA-5228411 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
|
C |
Seeded From UniProt |
complete | |
|
part_of |
GO:0005829 |
cytosol |
Reactome:R-HSA-5228578 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
|
C |
Seeded From UniProt |
complete | |
|
part_of |
GO:0005576 |
extracellular region |
Reactome:R-HSA-5228407 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0008233 |
peptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009405 |
pathogenesis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008237 |
metallopeptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0090729 |
toxin activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006508 |
proteolysis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Presek, P et al. (1992) Tetanus toxin inhibits depolarization-stimulated protein phosphorylation in rat cortical synaptosomes: effect on synapsin I phosphorylation and translocation. J. Neurochem. 59 1336-43 PubMed GONUTS page
- ↑ Blum, FC et al. (2012) Tetanus toxin and botulinum toxin a utilize unique mechanisms to enter neurons of the central nervous system. Infect. Immun. 80 1662-9 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 Schiavo, G et al. (1992) Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc. EMBO J. 11 3577-83 PubMed GONUTS page
- ↑ Montal, M (2010) Botulinum neurotoxin: a marvel of protein design. Annu. Rev. Biochem. 79 591-617 PubMed GONUTS page
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