Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.6.4.6 - vesicle-fusing ATPase and Organism(s) Drosophila melanogaster and UniProt Accession P46461

for references in articles please use BRENDA:EC3.6.4.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (_A_TPase _a_ssociated with a variety of cell _a_ctivities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger's syndrome.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Drosophila melanogaster
UNIPROT: P46461
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
n-ethylmaleimide-sensitive factor, cdc48, aaa-atpase, n-ethylmaleimide-sensitive fusion protein, atp6v0d2, n-ethylmaleimide sensitive factor, sec18p, sec18, cdc48p, pex1p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-ethylmaleimide sensitive factor
-
dNSF1
-
isoform 1
N-ethylmaleimide sensitive factor
-
-
N-ethylmaleimide sensitive fusion protein
-
-
-
-
NEM-sensitive fusion protein
NSF protein
-
N-ethyl-maleimide-sensitive fusion protein
SKD2 protein
-
-
-
-
vacuolar protein sorting 4
-
Vesicular-fusion protein NSF
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
hydrolysis of phosphoric ester
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (vesicle-fusing)
A large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (_A_TPase _a_ssociated with a variety of cell _a_ctivities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger's syndrome.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
ir
ATP + H2O
ADP + phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
ir
ATP + H2O
ADP + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
activity is dependent upon hexamerisation
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
predominantly expressed in larval and adult nervous system, dNSF-1 is abundant in synaptic vesicle fraction and may have a function in synaptic vesicle release
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
NSF requires a peripheral membrane protein to bind Golgi membranes
Manually annotated by BRENDA team
NSF requires a peripheral membrane protein to bind Golgi membranes
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
enzyme vacuolar protein sorting 4, Vps4, belongs to the AAA ATPases. Vps4 forms a hexameric complex that disassembles ESCRT-III, allowing recycling of its components, and also plays an active role in scission of the vesicle neck. Vps4 is required for epidermal growth factor receptor signaling even in the absence of Shibire, the Dynamin that internalizes epidermal growth factor receptor from the plasma membrane. In ovarian follicle cells, in contrast, Vps4 does not affect epidermal growth factor receptor signaling, although it is still essential for receptor degradation, Vps4 is not required for EGFR or Notch signaling in follicle cells. Enzyme Vps4 can promote epidermal growth factor receptor activity through an endocytosis-independent mechanism, a non-endocytic and cell type-dependent mechanism. Protein Vps4 is the only energy-utilizing ESCRT component
malfunction
photoreceptors are largely absent from Vps4 mutant clones in the eye disc, the resulting mutant R8 photoreceptors fail to recruit surrounding cells to differentiate as R1-R7 photoreceptors. Loss of Vps4 disrupts the epidermal growth factor receptor, EGFR, pathway. In imaginal disc cells deficient for enzyme Vps4, EGFR and other receptors accumulate in endosomes, and EGFR target genes are not expressed
physiological function
enzyme vacuolar protein sorting 4, Vps4, interacts with the endosomal sorting complexes required for transport, ESCRT-III, complex to drive the final step of intra-lumenal vesicles formation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NSF1_DROME
745
0
82555
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E209K
site-directed mutagenesis
additional information
construction of Vps4 knockout mutants, loss of Vps4 affects multiple signaling pathways, phenotypes, detailed overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
dysfunction of p97 has serious pathological consequences and has been implicated in a variety of cancers and neurodegenerative deseases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Confalonieri, F.; Duguet, M.
A 200-amino acid ATPase module in search of a basic function
Bioessays
17
639-650
1995
Saccharomyces cerevisiae, Candida albicans, Cricetulus longicaudatus, Drosophila melanogaster, Homo sapiens, Mus musculus, Sulfolobus acidocaldarius, Xenopus laevis
Manually annotated by BRENDA team
Patel, S.; Latterich, M.
The AAA team: related ATPases with diverse functions
Trends Cell Biol.
8
65-71
1998
Saccharomyces cerevisiae, Mus musculus, Drosophila melanogaster (P54351)
Manually annotated by BRENDA team
Mohtashami, M.; Stewart, B.A.; Boulianne, G.L.; Trimble, W.S.
Analysis of the mutant Drosophila N-ethylmaleimide sensitive fusion-1 protein in comatose reveals molecular correlates of the behavioural paralysis
J. Neurochem.
77
1407-1417
2001
Drosophila melanogaster
Manually annotated by BRENDA team
Littleton, J.T.; Barnard, R.J.; Titus, S.A.; Slind, J.; Chapman, E.R.; Ganetzky, B.
SNARE-complex disassembly by NSF follows synaptic-vesicle fusion
Proc. Natl. Acad. Sci. USA
98
12233-12238
2001
Drosophila melanogaster
Manually annotated by BRENDA team
Zhao, C.; Slevin, J.T.; Whiteheart, S.W.
Cellular functions of NSF: not just SNAPs and SNAREs
FEBS Lett.
581
2140-2149
2007
Saccharomyces cerevisiae, Drosophila melanogaster, Drosophila melanogaster (P46461), Mammalia, Rattus norvegicus
Manually annotated by BRENDA team
Pye, V.E.; Dreveny, I.; Briggs, L.C.; Sands, C.; Beuron, F.; Zhang, X.; Freemont, P.S.
Going through the motions: The ATPase cycle of p97
J. Struct. Biol.
156
12-28
2006
Arabidopsis thaliana, Archaea, Saccharomyces cerevisiae, Drosophila melanogaster, protozoa
Manually annotated by BRENDA team
Legent, K.; Liu, H.H.; Treisman, J.E.
Drosophila Vps4 promotes epidermal growth factor receptor signaling independently of its role in receptor degradation
Development
142
1480-1491
2015
Drosophila melanogaster (Q9Y162)
Manually annotated by BRENDA team