VAMP3

VAMP3
Identifiers
AliasesVAMP3, CEB, vesicle associated membrane protein 3
External IDsMGI: 1321389 HomoloGene: 3511 GeneCards: VAMP3
Gene location (Human)
Chr.Chromosome 1 (human)[1]
BandNo data availableStart7,771,269 bp[1]
End7,781,432 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

9341

22319

Ensembl

ENSG00000049245

ENSMUSG00000028955

UniProt

Q15836
Q6FGG2

P63024

RefSeq (mRNA)

NM_004781

NM_009498

RefSeq (protein)

NP_004772
NP_004772.1

NP_033524

Location (UCSC)Chr 1: 7.77 – 7.78 MbChr 1: 151.05 – 151.06 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Vesicle-associated membrane protein 3 is a protein that in humans is encoded by the VAMP3 gene.[5][6]

Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. This gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Because of its high homology to other known VAMPs, its broad tissue distribution, and its subcellular localization, the protein encoded by this gene was shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.[6]

Interactions

VAMP3 has been shown to interact with

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000049245 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028955 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Bernstein AM, Whiteheart SW (Apr 1999). "Identification of a cellubrevin/vesicle associated membrane protein 3 homologue in human platelets". Blood. 93 (2): 571–9. PMID 9885218.
  6. 1 2 "Entrez Gene: VAMP3 vesicle-associated membrane protein 3 (cellubrevin)".
  7. ↑ Annaert WG, Becker B, Kistner U, Reth M, Jahn R (December 1997). "Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31". J. Cell Biol. 139 (6): 1397–410. PMC 2132629 Freely accessible. PMID 9396746. doi:10.1083/jcb.139.6.1397.
  8. ↑ Hager HA, Roberts RJ, Cross EE, Proux-Gillardeaux V, Bader DM (February 2010). "Identification of a novel Bves function: regulation of vesicular transport". EMBO J. 29 (3): 532–45. PMC 2830705 Freely accessible. PMID 20057356. doi:10.1038/emboj.2009.379.
  9. 1 2 Imai A, Nashida T, Yoshie S, Shimomura H (August 2003). "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Arch. Oral Biol. 48 (8): 597–604. PMID 12828989. doi:10.1016/S0003-9969(03)00116-X.
  10. 1 2 Paumet F, Le Mao J, Martin S, Galli T, David B, Blank U, Roa M (June 2000). "Soluble NSF attachment protein receptors (SNAREs) in RBL-2H3 mast cells: functional role of syntaxin 4 in exocytosis and identification of a vesicle-associated membrane protein 8-containing secretory compartment". J. Immunol. 164 (11): 5850–7. PMID 10820264. doi:10.4049/jimmunol.164.11.5850.
  11. ↑ Freedman SJ, Song HK, Xu Y, Sun ZY, Eck MJ (April 2003). "Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain". J. Biol. Chem. 278 (15): 13462–7. PMID 12556468. doi:10.1074/jbc.M210483200.
  12. ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. PMID 16189514. doi:10.1038/nature04209.
  13. ↑ Polgár J, Chung SH, Reed GL (August 2002). "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion". Blood. 100 (3): 1081–3. PMID 12130530. doi:10.1182/blood.V100.3.1081.
  14. ↑ Mallard F, Tang BL, Galli T, Tenza D, Saint-Pol A, Yue X, Antony C, Hong W, Goud B, Johannes L (February 2002). "Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform". J. Cell Biol. 156 (4): 653–64. PMC 2174079 Freely accessible. PMID 11839770. doi:10.1083/jcb.200110081.

Further reading

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