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Information on EC 3.6.4.6 - vesicle-fusing ATPase and Organism(s) Rattus norvegicus and UniProt Accession P46462
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3.6.4.6 vesicle-fusing ATPaseIUBMB 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.
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Word Map
- 3.6.4.6
- snare
-
exocytosis
- syntaxins
- synaptic
- proteasome
-
disassembly
- snap-25
- endosomal
-
neurotransmitter
-
vesicle-associated
-
traffic
-
t-snares
- synaptobrevin
-
presynaptic
- atpases
-
neurotoxin
-
escrt-iii
-
exocytic
-
synaptosome-associated
-
multivesicular
- synapses
-
er-associated
- vamp
-
escrts
- synaptotagmins
-
snare-mediated
- botulinum
-
homotypic
-
cargo
-
dc-stamp
-
reticulum-associated
- nfatc1
- tetanus
-
valosin-containing
-
rankl-induced
-
ampars
-
retrotranslocation
-
four-helix
-
intra-golgi
-
fusogenic
-
neurosecretion
-
exocyst
-
3.6.1.3
-
autophagosome-lysosome
- peroxins
-
bonts
- medicine
- rab3a
-
tail-anchored
- oscar
-
ca2+-triggered
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
n-ethylmaleimide-sensitive factor, cdc48, aaa-atpase, n-ethylmaleimide-sensitive fusion protein, atp6v0d2, n-ethylmaleimide sensitive factor, sec18p, sec18, cdc48p, pex1p, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
peptide p97
essential chaperone in endoplasmic reticulum-associated degradation and organelle biogenesis, contains two ATPases associated with various cellular activities domains (D1 and D2)
N-ethylmaleimide sensitive fusion protein
NEM-sensitive fusion protein
-
-
-
-
SKD2 protein
-
-
-
-
Vesicular-fusion protein NSF
-
-
-
-
N-ethylmaleimide sensitive fusion protein
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
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 (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger 's syndrome.
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
9000-83-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
-
coordinated action of NSF and PKC regulates GABAB receptor signaling efficacy
-
-
?
ATP + H2O
ADP + phosphate
-
the enzyme plays a crucial role in the fusion of vesicles with target membranes. NSF-SNAP complexes may be involved in the disassembly of coiled-coil-mediated interactions underlying not only SNARE complexes but also other forms of stable oligomers, and the C-terminal membrane anchoring of NSF-SNAP targets may be mechanistically involved in the dissociation process
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
-
coordinated action of NSF and PKC regulates GABAB receptor signaling efficacy
-
-
?
ATP + H2O
ADP + phosphate
-
the enzyme plays a crucial role in the fusion of vesicles with target membranes. NSF-SNAP complexes may be involved in the disassembly of coiled-coil-mediated interactions underlying not only SNARE complexes but also other forms of stable oligomers, and the C-terminal membrane anchoring of NSF-SNAP targets may be mechanistically involved in the dissociation process
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the protein p47 forms a tight complex with p97, which is essential for the in vitro Golgi reassmbly
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
phosphorylation by Pctaire1 attenuates the hexamerization of NSF
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the protein VCIP135 is essential for p97/p47-mediated membrane fusion
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
NSF requires a peripheral membrane protein to bind Golgi membranes
-
NSF requires a peripheral membrane protein to bind membranes
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TERA_RAT
806
0
89349
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K251A
K524A
the p97 mutant carrying mutations in the D2 domain shows little ATPase activity when compared with wild type enzyme
R359A
the p97 mutant carrying mutations in the D2 domain shows little ATPase activity when compared with wild type enzyme
R635A
the p97 mutant carrying mutations in the D2 domain shows little ATPase activity when compared with wild type enzyme
S569A
-
mutation of serine 569 to alanine abolishs the phosphorylation of D2 domain by active Pctaire1
K251A
the p97 mutant carrying mutations in the D2 domain shows little ATPase activity when compared with wild type enzyme
K251A
the Walker A mutation to the D1 domain alone shows a moderate decrease in ATPase activity, has reduced affinity for nucleotide in the D1 domain and so contains little prebound ADP
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tamura, S.; Shimozawa, N.; Suzuki, Y.; Tsukamoto, T.; Osumi, T.; Fujiki, Y.
A cytoplasmic AAA family peroxin, Pex1p, interacts with Pex6p
Biochem. Biophys. Res. Commun.
245
883-886
1998
Homo sapiens, Rattus norvegicus
Meyer, H.H.; Kondo, H.; Warren, G.
The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97
FEBS Lett.
437
255-257
1998
Saccharomyces cerevisiae, Rattus norvegicus, Xenopus laevis
Yoshimori, T.; Yamagata, F.; Yamamoto, A.; Mizushima, N.; Kabeya, Y.; Nara, A.; Miwako, I.; Ohashi, M.; Ohsumi, M.; Ohsumi, Y.
The mouse SKD1, a homologue of yeast Vps4p, is required for normal endosomal trafficking and morphology in mammalian cells
Mol. Biol.
11
747-763
2000
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Rattus norvegicus
Uchiyama, K.; Jokitalo, E.; Kano, F.; Murata, M.; Zhang, X.; Canas, B.; Newman, R.; Rabouille, C.; Pappin, D.; Freemont, P.; Kondo, H.
VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo
J. Cell Biol.
159
855-866
2002
Rattus norvegicus
Liu, C.; Hu, B.
Alterations of N-ethylmaleimide-sensitive ATPase following transient cerebral ischemia
Neuroscience
128
767-774
2004
Rattus norvegicus
Pontier, S.M.; Lahaie, N.; Ginham, R.; St-Gelais, F.; Bonin, H.; Bell, D.J.; Flynn, H.; Trudeau, L.E.; McIlhinney, J.; White, J.H.; Bouvier, M.
Coordinated action of NSF and PKC regulates GABAB receptor signaling efficacy
EMBO J.
25
2698-2709
2006
Rattus norvegicus
Martin, H.G.; Henley, J.M.; Meyer, G.
Novel putative targets of N-ethylmaleimide sensitive fusion protein (NSF) and alpha/beta soluble NSF attachment proteins (SNAPs) include the Pak-binding nucleotide exchange factor betaPIX
J. Cell. Biochem.
99
1203-1215
2006
Rattus norvegicus
Beuron, F.; Dreveny, I.; Yuan, X.; Pye, V.E.; McKeown, C.; Briggs, L.C.; Cliff, M.J.; Kaneko, Y.; Wallis, R.; Isaacson, R.L.; Ladbury, J.E.; Matthews, S.J.; Kondo, H.; Zhang, X.; Freemont, P.S.
Conformational changes in the AAA ATPase p97-p47 adaptor complex
EMBO J.
25
1967-1976
2006
Rattus norvegicus
Jung, C.H.; Yang, Y.S.; Kim, J.S.; Shin, J.I.; Jin, Y.S.; Shin, J.Y.; Lee, J.H.; Chung, K.M.; Hwang, J.S.; Oh, J.M.; Shin, Y.K.; Kweon, D.H.
A search for synthetic peptides that inhibit soluble N-ethylmaleimide sensitive-factor attachment receptor-mediated membrane fusion
FEBS J.
275
3051-3063
2008
Rattus norvegicus
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
Liu, Y.; Cheng, K.; Gong, K.; Fu, A.K.; Ip, N.Y.
Pctaire1 phosphorylates N-ethylmaleimide-sensitive fusion protein: implications in the regulation of its hexamerization and exocytosis
J. Biol. Chem.
281
9852-9858
2006
Mus musculus, Rattus norvegicus
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