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

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