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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{technical|date=August 2012}}
{{PBB_Controls
{{Infobox_gene}}
| update_page = yes
'''N'''-ethylmaleimide-sensitive factor '''A'''ttachment '''P'''rotein '''A'''lpha, 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.<ref>{{cite journal |pmid=2111733 | volume=61 | title=SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast | year=1990 | journal=Cell | pages=709–21 | doi=10.1016/0092-8674(90)90482-t | vauthors=Clary DO, Griff IC, Rothman JE}}</ref>
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = N-ethylmaleimide-sensitive factor attachment protein, alpha
| HGNCid = 7641
| Symbol = NAPA
| AltSymbols =; SNAPA
| OMIM = 603215
| ECnumber = 
| Homologene = 2839
| MGIid = 104563
| GeneAtlas_image1 = PBB_GE_NAPA_206491_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NAPA_208751_at_tn.png
| Function = {{GNF_GO|id=GO:0005478 |text = transporter activity}} {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0019905 |text = syntaxin binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}}
| Process = {{GNF_GO|id=GO:0006886 |text = intracellular protein transport}} {{GNF_GO|id=GO:0006888 |text = ER to Golgi vesicle-mediated transport}} {{GNF_GO|id=GO:0006891 |text = intra-Golgi vesicle-mediated transport}} {{GNF_GO|id=GO:0006944 |text = membrane fusion}} {{GNF_GO|id=GO:0007420 |text = brain development}} {{GNF_GO|id=GO:0030182 |text = neuron differentiation}} {{GNF_GO|id=GO:0045176 |text = apical protein localization}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8775
    | Hs_Ensembl = ENSG00000105402
    | Hs_RefseqProtein = NP_003818
    | Hs_RefseqmRNA = NM_003827
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 52682703
    | Hs_GenLoc_end = 52710309
    | Hs_Uniprot = P54920
    | Mm_EntrezGene = 108124
    | Mm_Ensembl = ENSMUSG00000006024
    | Mm_RefseqmRNA = NM_025898
    | Mm_RefseqProtein = NP_080174
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 15257165
    | Mm_GenLoc_end = 15276497
    | Mm_Uniprot = Q9CXX1
  }}
}}
'''N-ethylmaleimide-sensitive factor attachment protein, alpha''', also known as '''NAPA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NAPA N-ethylmaleimide-sensitive factor attachment protein, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8775| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The '[[SNARE]] hypothesis' is a model explaining the process of docking and fusion of [[vesicle (biology and chemistry)|vesicles]] to their target [[cell membrane|membranes]]. According to this model, membrane [[protein]]s 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 [[N-ethylmaleimide sensitive fusion protein|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, [[USO1|p115/TAP]], alpha-SNAP (this protein), [[gamma-SNAP]], and the t-SNAREs [[syntaxin-2]] and [[STX4|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|date=March 2015}}
{{PBB_Summary
| section_title =
| summary_text = 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, 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.<ref name="entrez">{{cite web | title = Entrez Gene: NAPA N-ethylmaleimide-sensitive factor attachment protein, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8775| accessdate = }}</ref>
}}


==References==
== Clinical significance ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Wilson DW, Whiteheart SW, Wiedmann M, ''et al.'' |title=A multisubunit particle implicated in membrane fusion. |journal=J. Cell Biol. |volume=117 |issue= 3 |pages= 531-8 |year= 1992 |pmid= 1315316 |doi=  }}
*{{cite journal  | author=Whiteheart SW, Brunner M, Wilson DW, ''et al.'' |title=Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) bind to a multi-SNAP receptor complex in Golgi membranes. |journal=J. Biol. Chem. |volume=267 |issue= 17 |pages= 12239-43 |year= 1992 |pmid= 1601890 |doi=  }}
*{{cite journal  | author=Hanson PI, Otto H, Barton N, Jahn R |title=The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin. |journal=J. Biol. Chem. |volume=270 |issue= 28 |pages= 16955-61 |year= 1995 |pmid= 7622514 |doi=  }}
*{{cite journal  | author=Whiteheart SW, Griff IC, Brunner M, ''et al.'' |title=SNAP family of NSF attachment proteins includes a brain-specific isoform. |journal=Nature |volume=362 |issue= 6418 |pages= 353-5 |year= 1993 |pmid= 8455721 |doi= 10.1038/362353a0 }}
*{{cite journal  | author=Timmers KI, Clark AE, Omatsu-Kanbe M, ''et al.'' |title=Identification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion protein. |journal=Biochem. J. |volume=320 ( Pt 2) |issue=  |pages= 429-36 |year= 1997 |pmid= 8973549 |doi=  }}
*{{cite journal  | author=Lemons PP, Chen D, Bernstein AM, ''et al.'' |title=Regulated secretion in platelets: identification of elements of the platelet exocytosis machinery. |journal=Blood |volume=90 |issue= 4 |pages= 1490-500 |year= 1997 |pmid= 9269766 |doi=  }}
*{{cite journal  | author=Subramaniam VN, Loh E, Hong W |title=N-Ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment proteins (SNAP) mediate dissociation of GS28-syntaxin 5 Golgi SNAP receptors (SNARE) complex. |journal=J. Biol. Chem. |volume=272 |issue= 41 |pages= 25441-4 |year= 1997 |pmid= 9325254 |doi=  }}
*{{cite journal  | author=Lowe SL, Peter F, Subramaniam VN, ''et al.'' |title=A SNARE involved in protein transport through the Golgi apparatus. |journal=Nature |volume=389 |issue= 6653 |pages= 881-4 |year= 1997 |pmid= 9349823 |doi= 10.1038/39923 }}
*{{cite journal  | author=Barnard RJ, Morgan A, Burgoyne RD |title=Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis. |journal=J. Cell Biol. |volume=139 |issue= 4 |pages= 875-83 |year= 1997 |pmid= 9362506 |doi=  }}
*{{cite journal  | author=Wong SH, Xu Y, Zhang T, Hong W |title=Syntaxin 7, a novel syntaxin member associated with the early endosomal compartment. |journal=J. Biol. Chem. |volume=273 |issue= 1 |pages= 375-80 |year= 1998 |pmid= 9417091 |doi=  }}
*{{cite journal  | author=Tang BL, Tan AE, Lim LK, ''et al.'' |title=Syntaxin 12, a member of the syntaxin family localized to the endosome. |journal=J. Biol. Chem. |volume=273 |issue= 12 |pages= 6944-50 |year= 1998 |pmid= 9507000 |doi=  }}
*{{cite journal  | author=Wong SH, Zhang T, Xu Y, ''et al.'' |title=Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with the early endosome. |journal=Mol. Biol. Cell |volume=9 |issue= 6 |pages= 1549-63 |year= 1998 |pmid= 9614193 |doi=  }}
*{{cite journal  | author=Osten P, Srivastava S, Inman GJ, ''et al.'' |title=The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs. |journal=Neuron |volume=21 |issue= 1 |pages= 99-110 |year= 1998 |pmid= 9697855 |doi=  }}
*{{cite journal  | author=Prekeris R, Klumperman J, Chen YA, Scheller RH |title=Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes. |journal=J. Cell Biol. |volume=143 |issue= 4 |pages= 957-71 |year= 1998 |pmid= 9817754 |doi=  }}
*{{cite journal  | author=Nagamatsu S, Watanabe T, Nakamichi Y, ''et al.'' |title=alpha-soluble N-ethylmaleimide-sensitive factor attachment protein is expressed in pancreatic beta cells and functions in insulin but not gamma-aminobutyric acid secretion. |journal=J. Biol. Chem. |volume=274 |issue= 12 |pages= 8053-60 |year= 1999 |pmid= 10075705 |doi=  }}
*{{cite journal  | author=Subramaniam VN, Loh E, Horstmann H, ''et al.'' |title=Preferential association of syntaxin 8 with the early endosome. |journal=J. Cell. Sci. |volume=113 ( Pt 6) |issue=  |pages= 997-1008 |year= 2000 |pmid= 10683148 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Hirose H, Arasaki K, Dohmae N, ''et al.'' |title=Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi. |journal=EMBO J. |volume=23 |issue= 6 |pages= 1267-78 |year= 2005 |pmid= 15029241 |doi= 10.1038/sj.emboj.7600135 }}
*{{cite journal  | author=Singh BB, Lockwich TP, Bandyopadhyay BC, ''et al.'' |title=VAMP2-dependent exocytosis regulates plasma membrane insertion of TRPC3 channels and contributes to agonist-stimulated Ca2+ influx. |journal=Mol. Cell |volume=15 |issue= 4 |pages= 635-46 |year= 2004 |pmid= 15327778 |doi= 10.1016/j.molcel.2004.07.010 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
}}
{{refend}}


{{protein-stub}}
NAPA is abnormally expressed in fetuses of both [[in vitro fertilization|IVF]] and [[intracytoplasmic sperm injection|ICSI]], which may contribute to the increased risk of birth defects in these methods of [[assisted reproductive technology]], [[assisted reproductive technology|ART]].<ref name=zhang>{{cite journal | vauthors = Zhang Y, Zhang YL, Feng C, Wu YT, Liu AX, Sheng JZ, Cai J, Huang HF | title = Comparative proteomic analysis of human placenta derived from assisted reproductive technology | journal = Proteomics | volume = 8 | issue = 20 | pages = 4344–56 | date = September 2008 | pmid = 18792929 | doi = 10.1002/pmic.200800294 | url =  }}</ref>
{{WikiDoc Sources}}
 
== Interactions ==
 
NAPA has been shown to [[Protein-protein interaction|interact]] with:
* [[N-ethylmaleimide sensitive fusion protein|NSF]],<ref name = pmid7622514/><ref name = pmid9362506>{{cite journal | vauthors = Barnard RJ, Morgan A, Burgoyne RD | title = Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis | journal = J. Cell Biol. | volume = 139 | issue = 4 | pages = 875–83 | date = Nov 1997 | pmid = 9362506 | pmc = 2139964 | doi =  10.1083/jcb.139.4.875}}</ref>
* [[SNAP23]],<ref name = pmid16189514/>
* [[STX1A]],<ref name = pmid7622514>{{cite journal | vauthors = Hanson PI, Otto H, Barton N, Jahn R | title = The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin | journal = J. Biol. Chem. | volume = 270 | issue = 28 | pages = 16955–61 | date = Jul 1995 | pmid = 7622514 | doi =  10.1074/jbc.270.28.16955}}</ref><ref name = pmid7553862>{{cite journal | vauthors = McMahon HT, Missler M, Li C, Südhof TC | title = Complexins: cytosolic proteins that regulate SNAP receptor function | journal = Cell | volume = 83 | issue = 1 | pages = 111–9 | date = Oct 1995 | pmid = 7553862 | doi =  10.1016/0092-8674(95)90239-2}}</ref>
* [[STX4]],<ref name = pmid16189514>{{cite journal | vauthors = 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 | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 }}</ref>
* [[STX5]].<ref name = pmid16189514/><ref name = pmid9506515>{{cite journal | vauthors = Rabouille C, Kondo H, Newman R, Hui N, Freemont P, Warren G | title = Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro | journal = Cell | volume = 92 | issue = 5 | pages = 603–10 | date = Mar 1998 | pmid = 9506515 | doi =  10.1016/s0092-8674(00)81128-9}}</ref>
*  [[ORAI1]], [[STIM1]].<ref name = pmid23878724>{{cite journal | vauthors = Miao Y, Miner C, Zhang L, Hanson PI, Dani A, Vig M | title = An essential and NSF independent role for α-SNAP in store-operated calcium entry | journal =eLife | date = July 2013 | pmid = 23878724 | doi =  10.7554/eLife.00802 | volume=2 | pmc=3713520 | pages=e00802}}</ref>
 
== References ==
{{Reflist|30em}}
 
== Further reading ==
{{Refbegin|30em}}
* {{cite journal | vauthors = Wilson DW, Whiteheart SW, Wiedmann M, Brunner M, Rothman JE | title = A multisubunit particle implicated in membrane fusion | journal = J. Cell Biol. | volume = 117 | issue = 3 | pages = 531–8 | year = 1992 | pmid = 1315316 | pmc = 2289450 | doi = 10.1083/jcb.117.3.531 }}
* {{cite journal | vauthors = Whiteheart SW, Brunner M, Wilson DW, Wiedmann M, Rothman JE | title = Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) bind to a multi-SNAP receptor complex in Golgi membranes | journal = J. Biol. Chem. | volume = 267 | issue = 17 | pages = 12239–43 | year = 1992 | pmid = 1601890 | doi =  }}
* {{cite journal | vauthors = Hanson PI, Otto H, Barton N, Jahn R | title = The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin | journal = J. Biol. Chem. | volume = 270 | issue = 28 | pages = 16955–61 | year = 1995 | pmid = 7622514 | doi = 10.1074/jbc.270.28.16955 }}
* {{cite journal | vauthors = Whiteheart SW, Griff IC, Brunner M, Clary DO, Mayer T, Buhrow SA, Rothman JE | title = SNAP family of NSF attachment proteins includes a brain-specific isoform | journal = Nature | volume = 362 | issue = 6418 | pages = 353–5 | year = 1993 | pmid = 8455721 | doi = 10.1038/362353a0 }}
* {{cite journal | vauthors = Timmers KI, Clark AE, Omatsu-Kanbe M, Whiteheart SW, Bennett MK, Holman GD, Cushman SW | title = Identification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion protein | journal = Biochem. J. | volume = 320 | issue = Pt 2 | pages = 429–36 | year = 1997 | pmid = 8973549 | pmc = 1217948 | doi =  10.1042/bj3200429}}
* {{cite journal | vauthors = Lemons PP, Chen D, Bernstein AM, Bennett MK, Whiteheart SW | title = Regulated secretion in platelets: identification of elements of the platelet exocytosis machinery | journal = Blood | volume = 90 | issue = 4 | pages = 1490–500 | year = 1997 | pmid = 9269766 | doi =  }}
* {{cite journal | vauthors = Subramaniam VN, Loh E, Hong W | title = N-Ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment proteins (SNAP) mediate dissociation of GS28-syntaxin 5 Golgi SNAP receptors (SNARE) complex | journal = J. Biol. Chem. | volume = 272 | issue = 41 | pages = 25441–4 | year = 1997 | pmid = 9325254 | doi = 10.1074/jbc.272.41.25441 }}
* {{cite journal | vauthors = Lowe SL, Peter F, Subramaniam VN, Wong SH, Hong W | title = A SNARE involved in protein transport through the Golgi apparatus | journal = Nature | volume = 389 | issue = 6653 | pages = 881–4 | year = 1997 | pmid = 9349823 | doi = 10.1038/39923 }}
* {{cite journal | vauthors = Barnard RJ, Morgan A, Burgoyne RD | title = Stimulation of NSF ATPase Activity by α-SNAP Is Required for SNARE Complex Disassembly and Exocytosis | journal = J. Cell Biol. | volume = 139 | issue = 4 | pages = 875–83 | year = 1997 | pmid = 9362506 | pmc = 2139964 | doi = 10.1083/jcb.139.4.875 }}
* {{cite journal | vauthors = Wong SH, Xu Y, Zhang T, Hong W | title = Syntaxin 7, a novel syntaxin member associated with the early endosomal compartment | journal = J. Biol. Chem. | volume = 273 | issue = 1 | pages = 375–80 | year = 1998 | pmid = 9417091 | doi = 10.1074/jbc.273.1.375 }}
* {{cite journal | vauthors = Tang BL, Tan AE, Lim LK, Lee SS, Low DY, Hong W | title = Syntaxin 12, a member of the syntaxin family localized to the endosome | journal = J. Biol. Chem. | volume = 273 | issue = 12 | pages = 6944–50 | year = 1998 | pmid = 9507000 | doi = 10.1074/jbc.273.12.6944 }}
* {{cite journal | vauthors = Wong SH, Zhang T, Xu Y, Subramaniam VN, Griffiths G, Hong W | title = Endobrevin, a Novel Synaptobrevin/VAMP-Like Protein Preferentially Associated with the Early Endosome | journal = Mol. Biol. Cell | volume = 9 | issue = 6 | pages = 1549–63 | year = 1998 | pmid = 9614193 | pmc = 25382 | doi = 10.1091/mbc.9.6.1549 }}
* {{cite journal | vauthors = Osten P, Srivastava S, Inman GJ, Vilim FS, Khatri L, Lee LM, States BA, Einheber S, Milner TA, Hanson PI, Ziff EB | title = The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs | journal = Neuron | volume = 21 | issue = 1 | pages = 99–110 | year = 1998 | pmid = 9697855 | doi = 10.1016/S0896-6273(00)80518-8 }}
* {{cite journal | vauthors = Prekeris R, Klumperman J, Chen YA, Scheller RH | title = Syntaxin 13 Mediates Cycling of Plasma Membrane Proteins via Tubulovesicular Recycling Endosomes | journal = J. Cell Biol. | volume = 143 | issue = 4 | pages = 957–71 | year = 1998 | pmid = 9817754 | pmc = 2132958 | doi = 10.1083/jcb.143.4.957 }}
* {{cite journal | vauthors = Nagamatsu S, Watanabe T, Nakamichi Y, Yamamura C, Tsuzuki K, Matsushima S | title = alpha-soluble N-ethylmaleimide-sensitive factor attachment protein is expressed in pancreatic beta cells and functions in insulin but not gamma-aminobutyric acid secretion | journal = J. Biol. Chem. | volume = 274 | issue = 12 | pages = 8053–60 | year = 1999 | pmid = 10075705 | doi = 10.1074/jbc.274.12.8053 }}
* {{cite journal | vauthors = Subramaniam VN, Loh E, Horstmann H, Habermann A, Xu Y, Coe J, Griffiths G, Hong W | title = Preferential association of syntaxin 8 with the early endosome | journal = J. Cell Sci. | volume = 113 | issue = 6 | pages = 997–1008 | year = 2000 | pmid = 10683148 | doi =  }}
* {{cite journal | vauthors = Hirose H, Arasaki K, Dohmae N, Takio K, Hatsuzawa K, Nagahama M, Tani K, Yamamoto A, Tohyama M, Tagaya M | title = Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi | journal = EMBO J. | volume = 23 | issue = 6 | pages = 1267–78 | year = 2005 | pmid = 15029241 | pmc = 381410 | doi = 10.1038/sj.emboj.7600135 }}
* {{cite journal | vauthors = Singh BB, Lockwich TP, Bandyopadhyay BC, Liu X, Bollimuntha S, Brazer SC, Combs C, Das S, Leenders AG, Sheng ZH, Knepper MA, Ambudkar SV, Ambudkar IS | title = VAMP2-dependent exocytosis regulates plasma membrane insertion of TRPC3 channels and contributes to agonist-stimulated Ca2+ influx | journal = Mol. Cell | volume = 15 | issue = 4 | pages = 635–46 | year = 2004 | pmid = 15327778 | doi = 10.1016/j.molcel.2004.07.010 }}
{{Refend}}
 
[[Category:Human proteins]]

Latest revision as of 16:20, 29 November 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

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

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.[2]

Interactions

NAPA has been shown to interact with:

References

  1. ↑ 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. doi:10.1016/0092-8674(90)90482-t. PMID 2111733.
  2. ↑ 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. doi:10.1002/pmic.200800294. PMID 18792929.
  3. ↑ 3.0 3.1 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. ↑ 5.0 5.1 5.2 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. 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.
  8. ↑ 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. doi:10.7554/eLife.00802. PMC 3713520. PMID 23878724.

Further reading

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