CBCP:BXC

Species (Taxon ID)	Clostridium botulinum C phage (Clostridium botulinum C bacteriophage). (12336)
Gene Name(s)	No Information Provided.
Protein Name(s)	Botulinum neurotoxin type C BoNT/C Bontoxilysin-C1 BoNT/C1 (ECO:0000303 with PMID:2204031^[1]) Botulinum neurotoxin type C1 Botulinum neurotoxin C light chain LC Botulinum neurotoxin C heavy chain HC
External Links
UniProt	P18640
EMBL	X66433 X72793 X53751 D90210 X62389 AB200358
RefSeq	YP_398516.1
PDB	2QN0 3DEB 3N7K 3R4S 3R4U
PDBsum	2QN0 3DEB 3N7K 3R4S 3R4U
SMR	P18640
DrugBank	DB13898
UniLectin	P18640
PRIDE	P18640
GeneID	3772941
KEGG	vg:3772941
BRENDA	3.4.24.69
Reactome	R-HSA-5250971
EvolutionaryTrace	P18640
GO	GO:0005576 GO:0035594 GO:0004222 GO:0008320 GO:0090729 GO:0008270 GO:0033619 GO:0045955 GO:0046929
Gene3D	1.20.1120.10
InterPro	IPR000395 IPR036248 IPR013320 IPR011065 IPR013104 IPR012928 IPR012500
Pfam	PF01742 PF07951 PF07953 PF07952
PRINTS	PR00760
SUPFAM	SSF49899 SSF50386 SSF58091
PROSITE	PS00142

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes
enables	GO:0090729	toxin activity	PMID:7901002^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt
involved_in	GO:0046929	negative regulation of neurotransmitter secretion	PMID:7901002^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt
enables	GO:0008270	zinc ion binding	PMID:17718519^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt
enables	GO:0035594	ganglioside binding	PMID:16115873^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt
involved_in	GO:0071806	protein transmembrane transport	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0008320	P	Seeded From UniProt
enables	GO:0004222	metalloendopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000395	F	Seeded From UniProt
part_of	GO:0005576	extracellular region	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012928	C	Seeded From UniProt
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000395	P	Seeded From UniProt
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000395	F	Seeded From UniProt
enables	GO:0008320	protein transmembrane transporter activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012500	F	Seeded From UniProt
involved_in	GO:0009405	pathogenesis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012500 InterPro:IPR012928	P	Seeded From UniProt
involved_in	GO:0046929	negative regulation of neurotransmitter secretion	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000395 InterPro:IPR012500 InterPro:IPR012928 InterPro:IPR013104	P	Seeded From UniProt
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P	Seeded From UniProt
enables	GO:0008289	lipid binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0446	F	Seeded From UniProt
involved_in	GO:0009405	pathogenesis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0843	P	Seeded From UniProt
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C	Seeded From UniProt
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F	Seeded From UniProt
enables	GO:0008237	metallopeptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0482	F	Seeded From UniProt
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt
enables	GO:0090729	toxin activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0800	F	Seeded From UniProt
enables	GO:0090729	toxin activity	PMID:7901002^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt
involved_in	GO:0046929	negative regulation of neurotransmitter secretion	PMID:7901002^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt
enables	GO:0008270	zinc ion binding	PMID:17718519^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt
enables	GO:0035594	ganglioside binding	PMID:16115873^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt
involved_in	GO:0045955	negative regulation of calcium ion-dependent exocytosis	PMID:8611567^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt
involved_in	GO:0033619	membrane protein proteolysis	PMID:8611567^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt
involved_in	GO:0071806	protein transmembrane transport	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0008320	P	Seeded From UniProt
enables	GO:0004222	metalloendopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000395	F	Seeded From UniProt
part_of	GO:0005576	extracellular region	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012928	C	Seeded From UniProt
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000395	P	Seeded From UniProt
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000395	F	Seeded From UniProt
enables	GO:0008320	protein transmembrane transporter activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012500	F	Seeded From UniProt
involved_in	GO:0009405	pathogenesis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012500 InterPro:IPR012928	P	Seeded From UniProt
involved_in	GO:0046929	negative regulation of neurotransmitter secretion	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000395 InterPro:IPR012500 InterPro:IPR012928 InterPro:IPR013104	P	Seeded From UniProt
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P	Seeded From UniProt
enables	GO:0008289	lipid binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0446	F	Seeded From UniProt
involved_in	GO:0009405	pathogenesis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0843	P	Seeded From UniProt
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C	Seeded From UniProt
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F	Seeded From UniProt
enables	GO:0008237	metallopeptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0482	F	Seeded From UniProt
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt
enables	GO:0090729	toxin activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0800	F	Seeded From UniProt
part_of	GO:0005576	extracellular region	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0243	C	Seeded From UniProt
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Hauser, D et al. (1990) Nucleotide sequence of Clostridium botulinum C1 neurotoxin. Nucleic Acids Res. 18 4924 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Blasi, J et al. (1993) Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. EMBO J. 12 4821-8 PubMed GONUTS page
↑ ^3.0 ^3.1 Jin, R et al. (2007) Structural and biochemical studies of botulinum neurotoxin serotype C1 light chain protease: implications for dual substrate specificity. Biochemistry 46 10685-93 PubMed GONUTS page
↑ ^4.0 ^4.1 Tsukamoto, K et al. (2005) Binding of Clostridium botulinum type C and D neurotoxins to ganglioside and phospholipid. Novel insights into the receptor for clostridial neurotoxins. J. Biol. Chem. 280 35164-71 PubMed GONUTS page
↑ ^5.0 ^5.1 Foran, P et al. (1996) Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilized chromaffin cells: correlation with its blockade of catecholamine release. Biochemistry 35 2630-6 PubMed GONUTS page

[PMID:2204031-1] Hauser, D et al. (1990) Nucleotide sequence of Clostridium botulinum C1 neurotoxin. Nucleic Acids Res. 18 4924 PubMed GONUTS page

[PMID:7901002-2] 2.0 ^2.1 ^2.2 ^2.3 Blasi, J et al. (1993) Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. EMBO J. 12 4821-8 PubMed GONUTS page

[PMID:17718519-3] 3.0 ^3.1 Jin, R et al. (2007) Structural and biochemical studies of botulinum neurotoxin serotype C1 light chain protease: implications for dual substrate specificity. Biochemistry 46 10685-93 PubMed GONUTS page

[PMID:16115873-4] 4.0 ^4.1 Tsukamoto, K et al. (2005) Binding of Clostridium botulinum type C and D neurotoxins to ganglioside and phospholipid. Novel insights into the receptor for clostridial neurotoxins. J. Biol. Chem. 280 35164-71 PubMed GONUTS page

[PMID:8611567-5] 5.0 ^5.1 Foran, P et al. (1996) Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilized chromaffin cells: correlation with its blockade of catecholamine release. Biochemistry 35 2630-6 PubMed GONUTS page

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CBCP:BXC

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