Detail Information for IndEnz0002009143
IED ID IndEnz0002009143
Enzyme Type ID protease009143
Protein Name Vesicle-associated membrane protein 1
VAMP-1
Synaptobrevin-1
Gene Name VAMP1 SYB1
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MSAPAQPPAEGTEGTAPGGGPPGPPPNMTSNRRLQQTQAQVEEVVDIIRVNVDKVLERDQKLSELDDRADALQAGASQFESSAAKLKRKYWWKNCKMMIMLGAICAIIVVVIVIYFFT
Enzyme Length 118
Uniprot Accession Number P23763
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (2); Chain (1); Domain (1); Modified residue (1); Mutagenesis (3); Natural variant (1); Region (1); Sequence conflict (1); Site (4); Topological domain (2); Transmembrane (1)
Keywords Alternative splicing;Cell junction;Coiled coil;Congenital myasthenic syndrome;Cytoplasmic vesicle;Disease variant;Membrane;Mitochondrion;Mitochondrion outer membrane;Neurodegeneration;Phosphoprotein;Reference proteome;Synapse;Synaptosome;Transmembrane;Transmembrane helix
Interact With Q8N6L0; O95721; Q12846; Q13520; Q3SXY8; Q9BUF7-2; Q96BA8; P00387; Q15125; Q9GZR5; A1L3X0; Q9Y282; Q96KR6; Q8TDT2; Q13571; Q9H6H4; Q86VR2; Q9Y225-2; Q9NY72; Q9BY50; Q8NHU3; Q8IWU4; Q16623; P61266; Q12846; Q96IK0; Q9NUH8; Q53FP2; Q9Y320; Q12888
Induction
Subcellular Location SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cell junction, synapse, synaptosome {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion outer membrane; Single-pass type IV membrane protein {ECO:0000269|PubMed:9658161}.
Modified Residue MOD_RES 63; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q62442
Post Translational Modification PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type B (BoNT/B, botB) which probably hydrolyzes the 78-Gln-|-Phe-79 bond and inhibits neurotransmitter release (PubMed:22289120). {ECO:0000269|PubMed:22289120, ECO:0000305|PubMed:22289120}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type D (BoNT/D, botD) which probably hydrolyzes the 61-Arg-|-Leu-62 bond and inhibits neurotransmitter release (PubMed:22289120). BoNT/D has low catalytic activity on this protein due to its sequence (PubMed:22289120). Note that humans are not known to be infected by C.botulinum type D. {ECO:0000269|PubMed:22289120, ECO:0000305, ECO:0000305|PubMed:22289120}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type F (BoNT/F, botF) which probably hydrolyzes the 60-Gln-|-Lys-61 bond and inhibits neurotransmitter release (PubMed:22289120). {ECO:0000269|PubMed:22289120, ECO:0000305|PubMed:22289120}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type X (BoNT/X) which probably hydrolyzes the 68-Arg-|-Ala-69 bond and inhibits neurotransmitter release (PubMed:29540745). It remains unknown whether BoNT/X is ever produced, or what organisms it targets. {ECO:0000269|PubMed:29540745, ECO:0000305|PubMed:29540745}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 15217342; 16519520; 17903296; 18457912; 20877624; 21330375; 25010769; 25416956; 25881291; 33631708; 7527117; 7910017; 8051110; 8175689; 8226912; 8402889;
Motif
Gene Encoded By
Mass 12,902
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda