NAPA (gene)

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Aliases NAPA, SNSF attachment protein alpha
External IDs MGI: 104563 HomoloGene: 2839 GeneCards: NAPA
Gene location (Human)
Chromosome 19 (human)
Chr. Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for NAPA
Genomic location for NAPA
Band 19q13.32-q13.33 Start 47,487,637 bp[1]
End 47,515,240 bp[1]
RNA expression pattern
PBB GE NAPA 208751 at fs.png

PBB GE NAPA 206491 s at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 19: 47.49 – 47.52 Mb Chr 19: 16.1 – 16.12 Mb
PubMed search [3] [4]
View/Edit Human View/Edit Mouse

N-ethylmaleimide-sensitive factor Attachment Protein Alpha, also known as SNAP-α, is a protein that is involved in the intra-cellular trafficking and fusing of vesicles to target membranes in cells.[5]


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) and SNAPs (soluble NSF-attachment proteins), to the site of membrane fusion, thereby forming the 20S fusion complex. Alpha- and gamma-SNAP are found in a wide range of tissues and act synergistically in intra-Golgi transport. The sequence of the predicted 295-amino acid human protein encoded by NAPA shares 37%, 60%, and 67% identity with the sequences of yeast, Drosophila, and squid alpha-SNAP, respectively. Platelets contain some of the same proteins, including NSF, p115/TAP, alpha-SNAP (this protein), gamma-SNAP, and the t-SNAREs syntaxin-2 and syntaxin-4, that are used in many vesicular transport processes in other cell types. 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.[citation needed]

Clinical significance[edit]

NAPA is abnormally expressed in fetuses of both IVF and ICSI, which may contribute to the increased risk of birth defects in these methods of assisted reproductive technology, ART.[6]


NAPA has been shown to interact with:


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000105402 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000006024 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Clary DO, Griff IC, Rothman JE (1990). "SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast". Cell. 61: 709–21. PMID 2111733. doi:10.1016/0092-8674(90)90482-t. 
  6. ^ Zhang Y, Zhang YL, Feng C, Wu YT, Liu AX, Sheng JZ, Cai J, Huang HF (September 2008). "Comparative proteomic analysis of human placenta derived from assisted reproductive technology". Proteomics. 8 (20): 4344–56. PMID 18792929. doi:10.1002/pmic.200800294. 
  7. ^ a b Hanson PI, Otto H, Barton N, Jahn R (Jul 1995). "The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin". J. Biol. Chem. 270 (28): 16955–61. PMID 7622514. doi:10.1074/jbc.270.28.16955. 
  8. ^ Barnard RJ, Morgan A, Burgoyne RD (Nov 1997). "Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis". J. Cell Biol. 139 (4): 875–83. PMC 2139964Freely accessible. PMID 9362506. doi:10.1083/jcb.139.4.875. 
  9. ^ a b c 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 (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. PMID 16189514. doi:10.1038/nature04209. 
  10. ^ McMahon HT, Missler M, Li C, Südhof TC (Oct 1995). "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell. 83 (1): 111–9. PMID 7553862. doi:10.1016/0092-8674(95)90239-2. 
  11. ^ Rabouille C, Kondo H, Newman R, Hui N, Freemont P, Warren G (Mar 1998). "Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro". Cell. 92 (5): 603–10. PMID 9506515. doi:10.1016/s0092-8674(00)81128-9. 
  12. ^ Miao Y, Miner C, Zhang L, Hanson PI, Dani A, Vig M (July 2013). "An essential and NSF independent role for α-SNAP in store-operated calcium entry". eLIFE. 2: e00802. PMC 3713520Freely accessible. PMID 23878724. doi:10.7554/eLife.00802. 

Further reading[edit]