Search by BoMiProt ID - Bomi10478


Primary Information

BoMiProt ID Bomi10478
Protein Name Vesicle-associated membrane protein 1/Synaptobrevin-1
Organism Bos taurus
Uniprot IdQ0V7N0
Milk FractionWhey
Ref Sequence Id NP_001069098.2
Aminoacid Length 118
Molecular Weight 12860
Fasta Sequence https://www.uniprot.org/uniprot/Q0V7N0.fasta
Gene Name VAMP1/SYB1
Gene Id 513621
Protein Existence Status reviewed

Secondary Information

Protein Function involved in the synaptic vesicle cycle, exocytosis, at the presynaptic nerve terminal. Neuronal VAMPs are anchored in the vesicle membrane by their C-terminal domain.
Biochemical Properties 118-aa long.a cytoplasmic N-terminal domain rich in prolines and glycines, followed by a highly conserved hydrophilic region, a transmembrane domain, and a C-terminal intravesicular domain.
PTMs phosphorylation
Linking IDs Bomi10478
Bibliography Hu K, Carroll J, Fedorovich S, Rickman C, Sukhodub A, Davletov B. Vesicular restriction of synaptobrevin suggests a role for calcium in membrane fusion. Nature. 2002 Feb 7;415(6872):646-50. doi: 10.1038/415646a. PMID: 11832947.
Protein Function involved in the synaptic vesicle cycle, exocytosis, at the presynaptic nerve terminal. Neuronal VAMPs are anchored in the vesicle membrane by their C-terminal domain.
Biochemical Properties 118-aa long.a cytoplasmic N-terminal domain rich in prolines and glycines, followed by a highly conserved hydrophilic region, a transmembrane domain, and a C-terminal intravesicular domain.
PTMs phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q0V7N0|VAMP1_BOVIN Vesicle-associated membrane protein 1 OS=Bos taurus OX=9913 GN=VAMP1 PE=3 SV=2 MSAPAQPPTEGAEGAAPGGGPPGPPPNMTSNRRLQQTQAQVEEVVDIMRVNVDKVLERDQ KLS*63ELDDRADALQAGASQFESSAAKLKRKYWWKNCKMMIMLGAICAIIVVVIVIYFFA
Predicted Disorder Regions 2 disordered segments; (1-42), (69-83)
DisProt Annotation
TM Helix Prediction 1TMH; (99-117)
Linking IDs
Bibliography Hu K, Carroll J, Fedorovich S, Rickman C, Sukhodub A, Davletov B. Vesicular restriction of synaptobrevin suggests a role for calcium in membrane fusion. Nature. 2002 Feb 7;415(6872):646-50. doi: 10.1038/415646a. PMID: 11832947.