P18708
Gene name |
NSF |
Protein name |
Vesicle-fusing ATPase |
Names |
N-ethylmaleimide-sensitive fusion protein, NEM-sensitive fusion protein, Vesicular-fusion protein NSF |
Species |
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
KEGG Pathway |
cge:100770898 |
EC number |
3.6.4.6: Acting on ATP; involved in cellular and subcellular movement |
Protein Class |
VESICULAR-FUSION PROTEIN NSF (PTHR23078) |

Descriptions
NSF is a member of the type II AAA+ (ATPase associated with various cellular activities) family. It plays a critical role in intracellular membrane trafficking by disassembling soluble NSF attachment protein receptor (SNARE) complexes. NSF is a ring-shaped homohexameric protein, with each protomer consisting of three domains: an N-terminal domain (N domain) and two highly conserved AAA+ domains (D1 and D2 domains). Mutations within the N-D1 linker region (203-222) cause significant defects in the disassembly of the SNARE complex and the SNARE/α-SNAP complex binding activity. The middle and C-terminal region mutants of the NSF N-D1 linker have also increased basal ATPase activity.
Autoinhibitory domains (AIDs)
Target domain |
252-399 (D1 domain or ATPase domain) |
Relief mechanism |
Partner binding |
Assay |
Mutagenesis experiment |
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

16 structures for P18708
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
1D2N | X-ray | 175 A | A | 487-740 | PDB |
1NSF | X-ray | 190 A | A | 478-744 | PDB |
1QCS | X-ray | 190 A | A | 1-205 | PDB |
1QDN | X-ray | 230 A | A/B/C | 1-203 | PDB |
3J94 | EM | 420 A | A/B/C/D/E/F | 1-744 | PDB |
3J95 | EM | 760 A | A/B/C/D/E/F | 1-744 | PDB |
3J96 | EM | 760 A | A/B/C/D/E/F | 1-744 | PDB |
3J97 | EM | 780 A | A/B/C/D/E/F | 1-744 | PDB |
3J98 | EM | 840 A | A/B/C/D/E/F | 1-744 | PDB |
3J99 | EM | 820 A | A/B/C/D/E/F | 1-744 | PDB |
6IP2 | EM | 370 A | A/B/C/D/E/F | 1-744 | PDB |
6MDM | EM | 440 A | A/B/C/D/E/F | 1-744 | PDB |
6MDN | EM | 440 A | A/B/C/D/E/F | 1-723 | PDB |
6MDO | EM | 390 A | A/B/C/D/E/F | 1-723 | PDB |
6MDP | EM | 380 A | A/B/C/D/E/F | 1-723 | PDB |
AF-P18708-F1 | Predicted | AlphaFoldDB |
No variants for P18708
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for P18708 |
No associated diseases with P18708
8 regional properties for P18708
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | CDC48, N-terminal subdomain | 5 - 86 | IPR003338 |
domain | AAA+ ATPase domain | 252 - 399 | IPR003593-1 |
domain | AAA+ ATPase domain | 535 - 671 | IPR003593-2 |
domain | ATPase, AAA-type, core | 256 - 396 | IPR003959-1 |
domain | ATPase, AAA-type, core | 539 - 668 | IPR003959-2 |
conserved_site | ATPase, AAA-type, conserved site | 367 - 385 | IPR003960 |
domain | CDC48, domain 2 | 111 - 183 | IPR004201 |
domain | AAA ATPase, AAA+ lid domain | 423 - 461 | IPR041569 |
Functions
Description | ||
---|---|---|
EC Number | 3.6.4.6 | Acting on ATP; involved in cellular and subcellular movement |
Subcellular Localization |
|
|
PANTHER Family | PTHR23078 | VESICULAR-FUSION PROTEIN NSF |
PANTHER Subfamily | PTHR23078:SF3 | VESICLE-FUSING ATPASE |
PANTHER Protein Class | membrane traffic protein | |
PANTHER Pathway Category |
Ionotropic glutamate receptor pathway NSF Synaptic vesicle trafficking NSF |
4 GO annotations of cellular component
Name | Definition |
---|---|
cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
Golgi apparatus | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. |
midbody | A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis. |
plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
11 GO annotations of molecular function
Name | Definition |
---|---|
ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
identical protein binding | Binding to an identical protein or proteins. |
ionotropic glutamate receptor binding | Binding to an ionotropic glutamate receptor. Ionotropic glutamate receptors bind glutamate and exert an effect through the regulation of ion channels. |
metal ion binding | Binding to a metal ion. |
PDZ domain binding | Binding to a PDZ domain of a protein, a domain found in diverse signaling proteins. |
protein disaggregase activity | An ATP-dependent molecular chaperone activity that mediates the solubilization of ordered protein aggregates. |
protein kinase binding | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. |
protein-containing complex binding | Binding to a macromolecular complex. |
SNARE binding | Binding to a SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) protein. |
syntaxin-1 binding | Binding to a syntaxin-1 SNAP receptor. |
5 GO annotations of biological process
Name | Definition |
---|---|
intracellular protein transport | The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell. |
positive regulation of protein catabolic process | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
positive regulation of receptor recycling | Any process that activates or increases the frequency, rate or extent of receptor recycling. |
potassium ion transport | The directed movement of potassium ions (K+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
SNARE complex disassembly | The disaggregation of the SNARE protein complex into its constituent components. The SNARE complex is a protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers. |
No homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
No homologous proteins |
10 | 20 | 30 | 40 | 50 | 60 |
MAGRSMQAAR | CPTDELSLSN | CAVVSEKDYQ | SGQHVIVRTS | PNHKYIFTLR | THPSVVPGSV |
70 | 80 | 90 | 100 | 110 | 120 |
AFSLPQRKWA | GLSIGQEIEV | ALYSFDKAKQ | CIGTMTIEID | FLQKKNIDSN | PYDTDKMAAE |
130 | 140 | 150 | 160 | 170 | 180 |
FIQQFNNQAF | SVGQQLVFSF | NDKLFGLLVK | DIEAMDPSIL | KGEPASGKRQ | KIEVGLVVGN |
190 | 200 | 210 | 220 | 230 | 240 |
SQVAFEKAEN | SSLNLIGKAK | TKENRQSIIN | PDWNFEKMGI | GGLDKEFSDI | FRRAFASRVF |
250 | 260 | 270 | 280 | 290 | 300 |
PPEIVEQMGC | KHVKGILLYG | PPGCGKTLLA | RQIGKMLNAR | EPKVVNGPEI | LNKYVGESEA |
310 | 320 | 330 | 340 | 350 | 360 |
NIRKLFADAE | EEQRRLGANS | GLHIIIFDEI | DAICKQRGSM | AGSTGVHDTV | VNQLLSKIDG |
370 | 380 | 390 | 400 | 410 | 420 |
VEQLNNILVI | GMTNRPDLID | EALLRPGRLE | VKMEIGLPDE | KGRLQILHIH | TARMRGHQLL |
430 | 440 | 450 | 460 | 470 | 480 |
SADVDIKELA | VETKNFSGAE | LEGLVRAAQS | TAMNRHIKAS | TKVEVDMEKA | ESLQVTRGDF |
490 | 500 | 510 | 520 | 530 | 540 |
LASLENDIKP | AFGTNQEDYA | SYIMNGIIKW | GDPVTRVLDD | GELLVQQTKN | SDRTPLVSVL |
550 | 560 | 570 | 580 | 590 | 600 |
LEGPPHSGKT | ALAAKIAEES | NFPFIKICSP | DKMIGFSETA | KCQAMKKIFD | DAYKSQLSCV |
610 | 620 | 630 | 640 | 650 | 660 |
VVDDIERLLD | YVPIGPRFSN | LVLQALLVLL | KKAPPQGRKL | LIIGTTSRKD | VLQEMEMLNA |
670 | 680 | 690 | 700 | 710 | 720 |
FSTTIHVPNI | ATGEQLLEAL | ELLGNFKDKE | RTTIAQQVKG | KKVWIGIKKL | LMLIEMSLQM |
730 | 740 | ||||
DPEYRVRKFL | ALLREEGASP | LDFD |