Vesicle-associated membrane protein 3 (VAMP3)

The protein contains 100 amino acids for an estimated molecular weight of 11309 Da.

 

SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. (updated: April 1, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. 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.
  4. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  7. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

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.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

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.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

This protein is annotated as membranous in Gene Ontology, is predicted to be membranous by TOPCONS.

Topcons

Interpro domains
Total structural coverage: 99%
Model score: 81
MODL_MODELLER-9.18

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The reference OMIM entry for this protein is 603657

Vesicle-associated membrane protein 3; vamp3
Cellubrevin; ceb

CLONING

To understand more about the membrane trafficking events in platelets that have been activated, Bernstein and Whiteheart (1999) searched for proteins that could mediate platelet exocytosis or endocytosis. They identified a novel member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. See VAMP8 (603177). Originally cloned from a human megakaryocyte library, the VAMP3 gene was found by Northern blot analysis to be expressed in many human tissues. Because of its high homology to other known VAMPs, its broad tissue distribution, and its subcellular localization, this protein appeared to be the human equivalent of the rodent cellubrevin (CEB). Bernstein and Whiteheart (1999) showed that in platelets CEB resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.

GENE FUNCTION

Membrane traffic in activated macrophages is required for 2 critical events in innate immunity: proinflammatory cytokine secretion and phagocytosis of pathogens. Murray et al. (2005) found a joint trafficking pathway linking both actions, which may economize membrane transport and augment the immune response. Tumor necrosis factor-alpha (TNFA; 191160) is trafficked from the Golgi to the recycling endosome, where VAMP3 mediates its delivery to the cell surface at the site of phagocytic cup formation. Fusion of the recycling endosome at the cup simultaneously allows rapid release of TNF-alpha and expands the membrane for phagocytosis.

MAPPING

In the study of a form of autosomal recessive early-onset parkinsonism, PARK7 (606324), and search for candidate genes in the region of mapping on 1p36, van Duijn et al. (2001) found that the VAMP3 gene is in this region by scanning a working draft of the Human Genome Project's sequence. ... More on the omim web site

Subscribe to this protein entry history

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 VAMP3

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 603657 was added.