Information on EC 3.6.3.11 - Cl--transporting ATPase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.6.3.11
-
RECOMMENDED NAME
GeneOntology No.
Cl--transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + H2O + Cl-/out = ADP + phosphate + Cl-/in
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
hydrolysis of phosphoric ester
Q99ML5
-
hydrolysis of phosphoric ester
-
-
transmembrane transport
-
-
-
-
transmembrane transport
Q99ML5
-
transmembrane transport
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (Cl--importing)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. An animal and plant enzyme involved in the import of chloride anions.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ATP-dependent GABAA receptor-coupled Cl- channel
-
-
Cl ATPase pump
Q99ML5
-
Cl-,HCO3--ATPase
-
-
Cl-,HCO3--Mg2+-ATPase
-
-
Cl--motive ATPase
-
-
-
-
Cl--translocating ATPase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to the P-type transport ATPases
physiological function
-
the enzyme plays a role as Cl- channel and coupled to GABAA receptors. It might also play a role in anion transport across the neuronal membrane is required to evaluate the pathogenesis of some diseases, e.g. epilepsy
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Cl-/out
ADP + phosphate + Cl-/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Cl-/out
ADP + phosphate + Cl-/in
show the reaction diagram
-
the direction of Cl- transport depends strongly on the intracellular concentration of Cl- ions and extracellular concentrations of HCO3- ions. Cl- transport is reversed (ion efflux from the cell) at high concentrations of Cl- and HCO3- in the cell and incubation medium, respectively
-
-
r
Br-/out + ATP + H2O
Br-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
r
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
?
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
?
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
?
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
r
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
?
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
r
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
?
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
Q99ML5
-
-
-
r
F-/out + ATP + H2O
F-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
the enzyme acts as an ethacrynic acid-sensitive ATPase chloride pump in the central nervous system involved in regultion of postsynaptic membrane potentials, the raft protein NAP-22 might be involved in the regulation of ion transport through the membrane
-
-
-
additional information
?
-
-
the anion-activated Mg2+-ATPase exhibits the properties of Cl--ATPase and HCO3--ATPase
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Cl-/out
ADP + phosphate + Cl-/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Cl-/out
ADP + phosphate + Cl-/in
show the reaction diagram
-
the direction of Cl- transport depends strongly on the intracellular concentration of Cl- ions and extracellular concentrations of HCO3- ions. Cl- transport is reversed (ion efflux from the cell) at high concentrations of Cl- and HCO3- in the cell and incubation medium, respectively
-
-
r
Br-/out + ATP + H2O
Br-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
r
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
?
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
?
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
?
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
?
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
r
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
?
Cl-/out + ATP + H2O
Cl-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
ir
F-/out + ATP + H2O
F-/in + ADP + phosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
the enzyme acts as an ethacrynic acid-sensitive ATPase chloride pump in the central nervous system involved in regultion of postsynaptic membrane potentials, the raft protein NAP-22 might be involved in the regulation of ion transport through the membrane
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
can substitute for Mg2+
Cl-
-
stimulates the dephosphorylation step
HCO3-
-
maximal activity in the presence of both anions at a Cl-/HCO3- in a ratio of 5:1 for Cl-,HCO3--ATPase
Mg2+
-
absolute requirement, optimal concentration 3 mM
Mg2+
-
stimulates the phosphorylation step, optimal concentration at 3 mM
Mg2+
-
required
Mn2+
-
can substitute for Mg2+
Zn2+
-
can substitute for Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetazolamide
-
-
adenosine triphosphopyridoxal
-
activity inhibited in a concentration-dependent fashion, IC 50 at 0.017 mM
azide
-
complete inhibition within 10 min at 20 mM
bicuculline
-
-
-
Ethacrynic acid
-
complete inhibition at 0.3 mM
Ethacrynic acid
-
-
Ethacrynic acid
-
Ki: 0.057 mM
Ethacrynic acid
-
i.e. EAA
N-ethylmaleimide
-
complete inhibition
N-ethylmaleimide
-
88% inhibition at 0.01 mM
N-ethylmaleimide
-
-
orthovanadate
-
inhibitor of the transient-state phosphate bond
p-chloromercuribenzene sulfonate
-
-
p-chloromercuribenzoate
-
52% inhibition at 0.1 mM
vanadate
-
partial inhibition
vanadate
-
95% inhibition at 1 mM
additional information
-
no inhibition by oubain
-
additional information
-
-
-
additional information
-
no inhibition by furosemide; no inhibition by oubain, 0.5 mM
-
additional information
-
no inhibition by oubain, 0.5 mM
-
additional information
-
bafilomycin, N,N'-dicyclohexylcarbodiimide and efrapeptin have no inhibitory effect, suggesting that this Cl- pump is a P-type ATPase
-
additional information
-
the enzyme is ouabain-insensitive
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.017
-
adenosine triphosphopyridoxal
-
activity inhibited in a concentration-dependent fashion, IC 50 at 0.017 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.46
-
-
Cl-ATPase activity with 5 mM ATP
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.6
7.8
-
activity reduced at values below or above
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
42
-
activity reduced or not detectable at values below or above
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
proteoliposomes
Manually annotated by BRENDA team
-
hippocampal neurons
Manually annotated by BRENDA team
Q99ML5
hippocampal pyramidal neurones and cerebellar Purkinje cell
Manually annotated by BRENDA team
-
foregut epithelial cells
Manually annotated by BRENDA team
-
basolateral membranes of type A intercalated cells of cortical and medullar collecting ducts, detected by immunohistochemical analysis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
co-localization with raft protein NAP-22, NAP-22-enriched membrane microdomain of brain
Manually annotated by BRENDA team
additional information
-
subcellular localization analysis, overview
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
56290
-
Q99ML5
CIP55 subunit, calculated from amino acid sequence, confirmed by SDS-PAGE
110000
-
-
SDS-PAGE
300000
-
-
SDS-PAGE
520000
-
-
SDS-PAGE
580000
-
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
trimer
-
a,b,c subunit, 1 * 54000 + 1 * 50000 + 1 * 40000
additional information
-
subunit of 51000, SDS-PAGE
additional information
-
subunit of 50000
additional information
-
a subunit of 54000, b subunit of 50000, faint band around 40000
additional information
-
catalytic subunit of 51000; subunits of 62000, 60000, 55000, 51000
additional information
-
subunit a 54000, subunit b 50000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
transient phosphorylation is the first step in the catalytic cycle, dephosphorylation occurs after Cl- transport
glycoprotein
Q99ML5
subunit CIP55
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
at 4°C ATPase is released from liposomes it was incorporated in and loses the activity
-
in the presence of liposomes: 80% loss of activity after 2 h at 4°C with freeze-thaw method, in the absence of liposomes: stable in Mono Q-III fraction, loss of activity after 24 h for all samples
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of the subunit CIP55 in Escherichia coli
Q99ML5