Vesicle-associated membrane protein 2 (VAMP2)
The protein contains 116 amino acids for an estimated molecular weight of 12663 Da.
Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). Major SNARE protein of synaptic vesicles which mediates fusion of synaptic vesicles to release neurotransmitters. Essential for fast vesicular exocytosis and activity-dependent neurotransmitter release as well as fast endocytosis that mediates rapid reuse of synaptic vesicles (By similarity) (PubMed:30929742). Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. (updated: Aug. 12, 2020)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| NEDHAHM | |
| NEDHAHM | |
| NEDHAHM; no effect on vesicle fusion |
Biological Process
Calcium-ion regulated exocytosis
Cellular protein metabolic process
Cellular response to insulin stimulus
Chemical synaptic transmission
Energy reserve metabolic process
Eosinophil degranulation
Exocytosis
Glutamate secretion
Golgi to plasma membrane protein transport
Long-term synaptic potentiation
Membrane fusion
Membrane organization
Neurotransmitter secretion
Neurotransmitter transport
Pathogenesis
Positive regulation of intracellular protein transport
Post-Golgi vesicle-mediated transport
Protein complex assembly
Protein insertion into ER membrane
Protein transport
Protein-containing complex assembly
Regulation of delayed rectifier potassium channel activity
Regulation of exocytosis
Regulation of insulin secretion
Regulation of vesicle-mediated transport
Response to glucose
Small molecule metabolic process
SNARE complex assembly
Synaptic vesicle endocytosis
Synaptic vesicle exocytosis
Vesicle fusion
Vesicle-mediated transport
Cellular Component
Cell junction
Clathrin-coated endocytic vesicle membrane
Clathrin-coated vesicle
Clathrin-coated vesicle membrane
Clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane
Clathrin-sculpted glutamate transport vesicle membrane
Clathrin-sculpted monoamine transport vesicle membrane
Cytoplasmic vesicle
Cytosol
Extracellular exosome
Integral component of plasma membrane
Intracellular membrane-bounded organelle
Membrane
Neuron projection
Neuron projection terminus
Perinuclear region of cytoplasm
Plasma membrane
Secretory granule
Secretory granule membrane
SNARE complex
Synapse
Synaptic vesicle
Synaptic vesicle membrane
Synaptobrevin 2-SNAP-25-syntaxin-1a complex
Synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex
Synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex
Trans-Golgi network
Vesicle
Zymogen granule membrane
The reference OMIM entry for this protein is 185881
Vesicle-associated membrane protein 2; vamp2
Synaptobrevin 2; syb2
DESCRIPTION
Intracellular vesicles travel among cellular compartments and deliver their specific cargo to target membranes by membrane fusion. The specificity of cargo delivery and membrane fusion is controlled, in part, by the pairing of vesicle v-SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors), such as VAMP2, with target membrane t-SNAREs (summary by McNew et al., 2000).CLONING
Archer et al. (1990) isolated and characterized cosmid clones containing the human genes encoding synaptobrevins 1 and 2. Their coding regions are highly homologous, being interrupted at identical positions by introns of different size and sequence. The deduced synaptobrevin-2 protein contains 116 amino acids.GENE FUNCTION
Hunt et al. (1994) presented evidence that synaptobrevin participates in neurotransmitter release at a step between docking and fusion. Using yeast 2-hybrid analysis and in vitro binding assays, Martincic et al. (1997) showed that rat Pra1 (RABAC1; 604925) bound prenylated Rab GTPases, including Rab3a (179490) and Rab1 (179508), but not other small Ras-like GTPases. Pra1 also interacted with Vamp2, but not Vamp1 (185880) or cellubrevin (VAMP3; 603657). Interaction with Vamp2 involved the N-terminal proline-rich domain of Vamp2 and required the C-terminal transmembrane domain of Vamp2. Deletion analysis showed that both an N-terminal region spanning amino acids 30 to 54 and the extreme C-terminal domain of Pra1 were required for binding both Rab GTPases and Vamp1. Martincic et al. (1997) suggested that PRA1 may link Rab proteins and VAMP2 in the control of vesicle docking and fusion. McNew et al. (2000) tested all of the potential v-SNAREs encoded in the yeast genome for their capacity to trigger fusion by partnering with t-SNAREs that mark the Golgi, the vacuole, and the plasma membrane. McNew et al. (2000) found that, to a marked degree, the pattern of membrane flow in the cell is encoded and recapitulated by its isolated SNARE proteins, as predicted by the SNARE hypothesis. The heterodimer of syntaxin Sso1, which is homologous to syntaxin-1A, and Sec9, which is homologous to SNAP25, is a t-SNARE of the yeast plasma membrane, with Snc2, which is homologous to VAMP2, as its cognate v-SNARE. Thus, the yeast plasma membrane t-SNARE complex closely resembles its neuronal counterpart (Weber et al., 1998). SNARE proteins normally face the cytoplasm, within which their helical domains can pair to link membranes for fusion. To ascertain whether SNAREs can fuse cells, Hu et al. (2003) flipped their orientation and engineered cognate cells to express either the v- or t-SNAREs. Hu et al. (2003) found that cells expressing the interacting domains of v- (VAMP2) and t-SNAREs (syntaxin 1A and SNAP25) on the cell surface fused spontaneously, demonstrating that SNAREs are sufficient to fuse biological membranes. To investigate the role of astrocytes in regulating synaptic transmission, Pascual et al. (2005) generated inducible transgenic mice that expressed a dominant-negative SNARE domain selectively in astrocytes to block the release of transmitters from these glial cells. By releasing ATP, which accumulates as adenosine, astrocytes tonically suppressed synaptic transmission, thereby enhancing the dynamic range for long-term potentiation and mediated activity-dependent, heterosynaptic depression. Pascual et al. (2005) concluded that their results indicated that astrocytes are intricately li ... More on the omim web site
Aug. 24, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for VAMP2
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 185881 was added.