| General information | | DisProt: | DP00069 | | Name: | Vesicle-associated membrane protein 2 | | Synonym(s): | VAMP2_HUMAN
VAMP-2
Synaptobrevin-2
| | First appeared in release: | Release 1.2 (01/14/2005) | | UniProt: | P63027 | | UniGene: | Hs.25348 | | SwissProt: | VAMP2_HUMAN | | TrEMBL: | | | NCBI (GI): | 51704192 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 116 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MSATAATAPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL - 60
SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFSS
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| Functional narrative |
Synaptobrevin 2, a member of the SNARE superfamily, is a small synaptic vesicle protein involved in intracellular membrane fusion. In complex with syntaxin and SNAP-25, the SNARE protein complex forms bridges between two membranes and thereby facilitates trafficking between eukaryotic compartments. Isolated in solution, synaptobrevin 2 has been shown to be unfolded by HSQC NMR, CD and 2D NOE NMR. Upon formation of the SNARE complex, an increase in alpha-helicity and induced structure can be detected. May be involved in familial infantile myasthenia (FIMG).
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered - Extended | | Name: | | | Location: | 1 - 116 | | Length: | 116 | | Region sequence: |
MSATAATAPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKL
SELDDRADALQAGASQFETSAAKLKRKYWWKNLKMMIILGVICAIILIIIIVYFSS | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 7.4; dithiothreitol 1 mM; NaCl (salt) 100 mM; Tris 20 mM)
| References:
- Fasshauer D, Otto H, Eliason WK, Jahn R, Brunger AT. "Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation." J Biol Chem. 1997; 272(44): 28036-41. PubMed: 9346956
| Comments:
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| Region 2 | | Type: | Disordered - Extended | | Name: | | | Location: | 1 - 96 | | Length: | 96 | | Region sequence: |
MSATAATAPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKL
SELDDRADALQAGASQFETSAAKLKRKYWWKNLKMM | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (278 K; pH: 6.1; phosphate (buffer) 60 mM; protein 0.45 mM; water/D2O (solvent (9:1)))
| References:
- Hazzard J, Sudhof TC, Rizo J. "NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin." J Biomol NMR. 1999; 14(3): 203-207. PubMed: 10481273
| Comments:
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| Region 3 | | Type: | Disordered - Extended | | Name: | | | Location: | 40 - 67 | | Length: | 28 | | Region sequence: |
DEVVDIMRVNVDKVLERDQKLSELDDRA | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 7.4; NaCl (salt) 100 mM; sodium phosphate 10 mM)
| References:
- Cánaves JM, Montal M. "Assembly of a ternary complex by the predicted minimal coiled-coil-forming domains of syntaxin, SNAP-25, and synaptobrevin. A circular dichroism study." J Biol Chem. 1998; 273(51): 34214-21. PubMed: 9852083
| Comments:
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