NAPA (gene)

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N-ethylmaleimide-sensitive factor attachment protein, alpha
Identifiers
Symbols NAPA ; SNAPA
External IDs OMIM603215 MGI104563 HomoloGene2839 GeneCards: NAPA Gene
RNA expression pattern
PBB GE NAPA 206491 s at tn.png
PBB GE NAPA 208751 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 8775 108124
Ensembl ENSG00000105402 ENSMUSG00000006024
UniProt P54920 Q9DB05
RefSeq (mRNA) NM_003827 NM_025898
RefSeq (protein) NP_003818 NP_080174
Location (UCSC) Chr 19:
47.99 – 48.02 Mb
Chr 7:
16.1 – 16.12 Mb
PubMed search [1] [2]

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.[1]

Function[edit]

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 increase risk of birth defects in these ART.[2]

Interactions[edit]

NAPA has been shown to interact with:


References[edit]

  1. ^ http://www.ncbi.nlm.nih.gov/pubmed/2111733
  2. ^ Zhang Y, Zhang YL, Feng C, Wu YT, Liu AX, Sheng JZ et al. (September 2008). "Comparative proteomic analysis of human placenta derived from assisted reproductive technology". Proteomics 8 (20): 4344–56. doi:10.1002/pmic.200800294. PMID 18792929. 
  3. ^ 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. doi:10.1074/jbc.270.28.16955. PMID 7622514. 
  4. ^ 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. doi:10.1083/jcb.139.4.875. PMC 2139964. PMID 9362506. 
  5. ^ a b c Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N et al. (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  6. ^ McMahon HT, Missler M, Li C, Südhof TC (Oct 1995). "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell 83 (1): 111–9. doi:10.1016/0092-8674(95)90239-2. PMID 7553862. 
  7. ^ 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. doi:10.1016/s0092-8674(00)81128-9. PMID 9506515. 

Further reading[edit]