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P63045 (VAMP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vesicle-associated membrane protein 2

Short name=VAMP-2
Alternative name(s):
Synaptobrevin-2
Gene names
Name:Vamp2
Synonyms:Syb2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length116 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the targeting and/or fusion of transport vesicles to their target membrane By similarity.

Subunit structure

Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A. This complex binds to CPLX1. Interacts with BVES and STX4. Interacts with VAPA and VAPB By similarity.

Subcellular location

Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Single-pass type IV membrane protein. Cell junctionsynapsesynaptosome. Note: Neuronal synaptic vesicles.

Tissue specificity

Nervous system specific. A higher level expression is seen in the brain as compared to the spinal cord. Ref.1

Sequence similarities

Belongs to the synaptobrevin family.

Contains 1 v-SNARE coiled-coil homology domain.

Ontologies

Keywords
   Cellular componentCell junction
Cytoplasmic vesicle
Membrane
Synapse
Synaptosome
   DomainCoiled coil
Transmembrane
Transmembrane helix
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processprotein complex assembly

Inferred from direct assay. Source: RGD

protein transport

Inferred from mutant phenotype. Source: RGD

regulation of exocytosis

Traceable author statement. Source: UniProtKB

response to glucose stimulus

Inferred from direct assay. Source: UniProtKB

vesicle-mediated transport

Inferred from mutant phenotype. Source: RGD

   Cellular componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

microsome

Inferred from direct assay. Source: RGD

plasma membrane

Inferred from direct assay. Source: UniProtKB

secretory granule

Inferred from direct assay. Source: UniProtKB

synaptic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

synaptobrevin 2-SNAP-25-syntaxin-1a complex

Inferred from direct assay. Source: MGI

synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex

Inferred from direct assay. Source: MGI

synaptosome

Inferred from direct assay. Source: RGD

   Molecular functionmyosin binding

Inferred from physical interaction. Source: RGD

protein C-terminus binding

Inferred from physical interaction. Source: RGD

syntaxin-1 binding

Inferred from direct assay. Source: MGI

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 116115Vesicle-associated membrane protein 2
PRO_0000206726

Regions

Topological domain2 – 9493Cytoplasmic Potential
Transmembrane95 – 11420Helical; Anchor for type IV membrane protein; Potential
Topological domain115 – 1162Vesicular Potential
Domain31 – 9161v-SNARE coiled-coil homology

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue751Phosphoserine By similarity

Secondary structure

... 116
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63045 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4A0D0D56B5409D0A

FASTA11612,691
        10         20         30         40         50         60 
MSATAATVPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL 

        70         80         90        100        110 
SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFST 

« Hide

References

« Hide 'large scale' references
[1]"Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system."
Elferink L.A., Trimble W.S., Scheller R.H.
J. Biol. Chem. 264:11061-11064(1989) [PubMed: 2472388] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[3]Lubec G., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 32-47 AND 60-83, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
[4]"Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution."
Sutton R.B., Fasshauer D., Jahn R., Brunger A.T.
Nature 395:347-353(1998) [PubMed: 9759724] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-97 IN COMPLEX WITH STX1A AND SNAP25.
[5]"Three-dimensional structure of the complexin/SNARE complex."
Chen X., Tomchick D.R., Kovrigin E., Arac D., Machius M., Suedhof T.C., Rizo J.
Neuron 33:397-409(2002) [PubMed: 11832227] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 30-94 IN COMPLEX WITH STX1A; CPLX1 AND SNAP25, STRUCTURE BY NMR.
[6]"High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex."
Ernst J.A., Brunger A.T.
J. Biol. Chem. 278:8630-8636(2003) [PubMed: 12496247] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 29-90 IN COMPLEX WITH STX1A AND SNAP25.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24105 mRNA. Translation: AAA42321.1.
BC074003 mRNA. Translation: AAH74003.1.
IPIIPI00781701.
PIRB34288.
RefSeqNP_036795.1. NM_012663.2.
UniGeneRn.12939.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KILX-ray2.30A28-92[»]
1N7SX-ray1.45A28-89[»]
1SFCX-ray2.40A/E/I1-96[»]
2BU0model-A25-88[»]
2KOGNMR-A1-116[»]
3HD7X-ray3.40A/E30-116[»]
3IPDX-ray4.80A/E30-116[»]
ProteinModelPortalP63045.
SMRP63045. Positions 30-116.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-35503N.
IntActP63045. 12 interactions.
MINTMINT-1487471.
STRINGP63045.

PTM databases

PhosphoSiteP63045.

Proteomic databases

PRIDEP63045.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000057295; ENSRNOP00000054114; ENSRNOG00000006989.
GeneID24803.
KEGGrno:24803.
UCSCNM_012663. rat.

Organism-specific databases

CTD6844.
RGD3949. Vamp2.

Phylogenomic databases

eggNOGveNOG21495.
HOVERGENHBG006675.
InParanoidP63045.
OrthoDBEOG43JC6B.

Gene expression databases

ArrayExpressP63045.
GenevestigatorP63045.
GermOnlineENSRNOG00000006989. Rattus norvegicus.

Family and domain databases

InterProIPR001388. Synaptobrevin.
IPR016444. Synaptobrevin_met/fun.
[Graphical view]
KOK13504.
PfamPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PIRSFPIRSF005409. Synaptobrevin_euk. 1 hit.
PRINTSPR00219. SYNAPTOBREVN.
PROSITEPS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604468.
PMAP-CutDBP63045.

Entry information

Entry nameVAMP2_RAT
AccessionPrimary (citable) accession number: P63045
Secondary accession number(s): Q64357
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families