Gamma-soluble NSF attachment protein (NAPG)
The protein contains 312 amino acids for an estimated molecular weight of 34746 Da.
Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. (updated: April 1, 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.
- 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.
- 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.
- 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.
- 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.
(right-click above to access to more options from the contextual menu)
| Variant | Description |
|---|---|
| dbSNP:rs2228300 | |
| dbSNP:rs2305370 |
Biological Process
Intra-Golgi vesicle-mediated transport
Intracellular protein transport
Membrane fusion
Protein complex assembly
Protein stabilization
Protein-containing complex assembly
The reference OMIM entry for this protein is 603216
N-ethylmaleimide-sensitive factor attachment protein, gamma; napg
Soluble nsf-attachment protein, gamma
Snap, gamma
CLONING
Whiteheart et al. (1993) cloned bovine cDNAs encoding alpha- (603215), beta- (611270), and gamma-SNAP. By searching a human EST database for homologs of bovine gamma-SNAP, Lemons et al. (1997) identified a melanocyte cell cDNA encoding human gamma-SNAP. The sequence of the predicted 312-amino acid human protein is 95% identical to that of bovine gamma-SNAP. These authors characterized gamma-SNAP and some of the other proteins that mediate platelet exocytosis and proposed a mechanism for controlling the membrane fusion events of this process.GENE FUNCTION
The 'SNARE hypothesis' is a model explaining the process of docking and fusion of vesicles to their target membranes. According to this model, membrane proteins from the vesicle (v-SNAREs) and proteins from the target membrane (t-SNAREs) govern the specificity of vesicle targeting and docking through mutual recognition. Once the 2 classes of SNAREs bind to each other, they form a complex that recruits the general elements of the fusion apparatus, namely NSF (N-ethylmaleimide-sensitive factor; 601633) and SNAPs (soluble NSF-attachment proteins), to the site of membrane fusion, thereby forming the 20S fusion complex. Lemons et al. (1997) found that platelets contain some of the same proteins, including NSF, p115/TAP (603344), alpha-SNAP, gamma-SNAP, and the t-SNAREs syntaxin-2 and syntaxin-4 (186591), that are used in many vesicular transport processes in other cell types. They concluded that platelet exocytosis uses a molecular mechanism similar to that used by other secretory cells, such as neurons, although the proteins used by the platelet and their modes of regulation may be quite different.MAPPING
Gross (2014) mapped the NAPG gene to chromosome 18p11.22 based on an alignment of the NAPG sequence (GenBank GENBANK BC001889) with the genomic sequence (GRCh37). ... 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
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 603216 was added.