Trafficking protein particle complex subunit 3 (TRAPPC3)
The protein contains 180 amino acids for an estimated molecular weight of 20274 Da.
May play a role in vesicular transport from endoplasmic reticulum to Golgi. (updated: March 4, 2015)
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.
- 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.
| 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.
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Biological Process
COPII vesicle coating
Endoplasmic reticulum to Golgi vesicle-mediated transport
Intra-Golgi vesicle-mediated transport
Vesicle-mediated transport
Cellular Component
Cis-Golgi network membrane
Cytosol
Endoplasmic reticulum
Golgi apparatus
Golgi membrane
TRAPP complex
The reference OMIM entry for this protein is 610955
Trafficking protein particle complex, subunit 3; trappc3
Bet3, yeast, homolog of; bet3
DESCRIPTION
TRAPPC3 is a component of the TRAPP complex, which is involved in tethering of transport vesicles to the cis-Golgi membrane (Turnbull et al., 2005).CLONING
Loh et al. (2005) reported that the human TRAPPC3 protein, which they called BET3, contains 180 amino acids. Northern blot analysis detected Bet3 expression in all mouse tissues examined. Western blot analysis of fractionated rat liver showed that most Bet3 was present in the cytosolic fraction, with a lesser amount in the Golgi-enriched membrane fraction. By immunohistochemical analysis, Yu et al. (2006) found that endogenous BET3 showed perinuclear localization in several mammalian cell lines, including HeLa cells.GENE FUNCTION
Loh et al. (2005) found that antibodies against Bet3 inhibited in vitro transport of the envelope glycoprotein of vesicular stomatitis virus from the endoplasmic reticulum (ER) to the Golgi apparatus of semi-intact rat kidney cells in a dose-dependent manner. Cytosol depleted of Bet3 was also defective in this transport and could be rescued by recombinant Bet3. Bet3 acted after coat protein II (COPII; see 601924) but before Rab1 (179508), alpha-Snap (NAPA; 603215), and the EGTA-sensitive stage during ER-Golgi transport. Turnbull et al. (2005) found that both human and yeast BET3 were palmitoylated in recombinant yeast cells, but palmitoylation of BET3 was only partly responsible for the its membrane localization. Both wildtype yeast Bet3 and mutant yeast Bet3 lacking palmitoylation rescued cell viability in Bet3-deleted yeast, suggesting that palmitoylation is not required for cell viability. Despite high sequence conservation, human BET3 failed to rescue Bet3-deleted yeast. In mammalian cells, COPII vesicles derived from the transitional ER do not tether directly to the Golgi, but rather tether to each other to form vesicular tubular clusters (VTCs). Using various mammalian cell lines, including HeLa cells, Yu et al. (2006) showed that BET3 resided in the transitional ER and adjacent to VTCs. Inactivation of BET3 resulted in accumulation of cargo in membranes that colocalized with the COPII coat. Using an assay that reconstituted VTC biogenesis in vitro, Yu et al. (2006) demonstrated that BET3 was required for the tethering and fusion of COPII vesicles to each other. Depletion of BET3 by small interfering RNA disrupted a VTC marker and Golgi architecture. Yu et al. (2006) concluded that BET3 is essential for VTC biogenesis. Cai et al. (2007) reported that in yeast and mammalian cells the tethering complex TRAPP I binds to the coat subunit SEC23 (see 610511). This event requires the BET3 subunit. In vitro studies demonstrated that the interaction between SEC23 and BET3 targets TRAPP I to COPII vesicles to mediate vesicle tethering. Cai et al. (2007) proposed that the binding of TRAPP I to SEC23 marks a coated vesicle for fusion with another COPII vesicle or the Golgi apparatus. An implication of these findings is that the intracellular destination of a transport vesicle may be determined in part by its coat and its associated cargo.BIOCHEMICAL FEATURES
Turnbull et al. (2005) determined the crystal structure of human BET3 to 1.55-angstrom resolution. BET3 assumes an alpha/beta-plait topology constructed by a twisted, antiparallel, 4-stranded beta sheet on one side, with the 5 alpha helices forming the other side of the structural motif. BET3 forms a dimer around the crystallographic 2-fold axis. A hyd ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 610955 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed