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Enzyme Nomenclature
Information on EC 3.6.3.7 - Na+-exporting ATPase
for references in articles please use BRENDA:EC3.6.3.7
Word Map on EC 3.6.3.7
- 3.6.3.7
- potassium
- cardiac
-
ouabain-sensitive
- hypertension
- atpases
- erythrocyte
-
electrogenic
- na,k-atpase
-
basolateral
-
depolarization
- triphosphatase
-
contractile
-
hyperpolarization
-
normotensive
-
3houabain
-
inotropic
- vanadate
-
alpha1
- digoxin
- digitalis
-
digitalis-like
-
cotransporter
- mg2+-atpase
-
sarcolemmal
-
cardiotonic
- na+-k+-atpase
-
k+-free
- menkes
-
ouabain-induced
- rb+
-
k+-dependent
-
sodium-potassium
- amiloride
-
rubidium
-
phosphoenzyme
-
k+-activated
-
h+,k+-atpase
-
k-atpase
-
natriuresis
-
countertransport
-
alpha-isoforms
-
alpha1-subunit
-
3.6.1.3
-
copper-transporting
- p-nitrophenylphosphatase
-
ouabain-resistant
-
aminophospholipids
- flippase
- pharmacology
- biotechnology
-
sodium-calcium
- medicine
-
ca2+-atpases
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
3.6.3.7
-
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RECOMMENDED NAME
GeneOntology No.
Na+-exporting ATPase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Na+/in = ADP + phosphate + Na+/out
-
-
-
-
ATP + H2O + Na+/in = ADP + phosphate + Na+/out
the enzyme function is triggered when the cells are suffering K+ starvation
ATP + H2O + Na+/in = ADP + phosphate + Na+/out
Ena1 gene plays a fundamental role in the salt stress response
ATP + H2O + Na+/in = ADP + phosphate + Na+/out
membrane bound ATPase. It splits the energy-storing adenosine triphosphate, ATP, to yield adenosine diphosphate, ADP, releasing inorganic phosphate, and moves three sodium ions out of the cell in exchange for two potassium ions. The protein is composed of three chains, the larges possessing many hydrophobic sequences presumed to be transmembranal, the smallest, and the third, involved in the pump´s regulation
-
ATP + H2O + Na+/in = ADP + phosphate + Na+/out
membrane bound ATPase. It splits the energy-storing adenosine triphosphate, ATP, to yield adenosine diphosphate, ADP, releasing inorganic phosphate, and moves three sodium ions out of the cell in exchange for two potassium ions. The protein is composed of three chains, the larges possessing many hydrophobic sequences presumed to be transmembranal, the smallest, and the third, involved in the pump´s regulation
-
ATP + H2O + Na+/in = ADP + phosphate + Na+/out
membrane bound ATPase. It splits the energy-storing adenosine triphosphate, ATP, to yield adenosine diphosphate, ADP, releasing inorganic phosphate, and moves three sodium ions out of the cell in exchange for two potassium ions. The protein is composed of three chains, the larges possessing many hydrophobic sequences presumed to be transmembranal, the smallest, and the third, involved in the pump´s regulation
-
ATP + H2O + Na+/in = ADP + phosphate + Na+/out
membrane bound ATPase. It splits the energy-storing adenosine triphosphate, ATP, to yield adenosine diphosphate, ADP, releasing inorganic phosphate, and moves three sodium ions out of the cell in exchange for two potassium ions. The protein is composed of three chains, the larges possessing many hydrophobic sequences presumed to be transmembranal, the smallest, and the third, involved in the pump´s regulation
-
ATP + H2O + Na+/in = ADP + phosphate + Na+/out
membrane bound ATPase. It splits the energy-storing adenosine triphosphate, ATP, to yield adenosine diphosphate, ADP, releasing inorganic phosphate, and moves three sodium ions out of the cell in exchange for two potassium ions. The protein is composed of three chains, the larges possessing many hydrophobic sequences presumed to be transmembranal, the smallest, and the third, involved in the pump´s regulation
-
ATP + H2O + Na+/in = ADP + phosphate + Na+/out
efflux in the absence of external Na+ follows first order kinetics
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
transmembrane transport
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (Na+-exporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme from yeast is involved in the efflux of Na+, with one ion being exported per ATP hydrolysed.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
deletion of ENA1 has no effect on the tolerance to potassium and rubidium. Mutant cells are unable to grow on media containing higher concentrations of sodium and lithium cations
metabolism
-
important regulatory role of Ang-(1-7) in the action of angiotensin II on the Na+-ATPase activity of proximal tubule cells by activation of MAS receptor. The MAS receptor plays an important role as a regulator of the effects mediated by AT1 receptor on proximal tubule sodium reabsorption and renal sodium excretion, overview
physiological function
additional information
physiological function
-
the Na+-ATPase is involved in Na+ reabsorption in the kidney. Ouabain-insensitive Na+-ATPase is considered the fine tuner of cytosolic Na+, the selective key roles of ceramide under Na+-induced osmotic stress
physiological function
-
the enzyme functions as an electrogenic Na+ pump which transports only Na+ upon hydrolysis of ATP. Na+- and ATP-dependent H+ efflux from proteoliposomes, is driven by the electric potential generated by Na+-stimulated ATPase
physiological function
Na+ATPase is involved in Candida glabrata tolerance to high concentrations of Na+ and Li+
physiological function
isoform KPA1 plays an important role in alkali and cold stress tolerance; isoform KPA2 plays an important role in alkali and cold stress tolerance
physiological function
-
isoform KPA1 plays an important role in alkali and cold stress tolerance; isoform KPA2 plays an important role in alkali and cold stress tolerance
-
additional information
-
inosine-induced inhibition of Na+-ATPase activity could be involved in the increased renal sodium excretion during short periods of ischemia
additional information
-
Cer acts as a potent physiological modulator of the Na+-ATPase, participating in a regulatory network in kidney cells and counteracting the stimulatory effect of PKA via PKCzeta
additional information
-
increase in sodium reabsorption on the proximal tubule in essential hypertension. Na+-ATPase activity is enhanced in14-week-old but not in 6-week-old spontaneously hypertensive rats. correlation between AT1 receptor activation in spontaneously hypertensive rats and increased ouabaininsensitive Na+-ATPase activity. Ang II interacts with different receptors in spontaneously hypertensive rats and WKY wild-type rats. The AT1 receptor is responsible for activation in spontaneously hypertensive rats. Role of the AT2 receptor in counteracting the AT1 receptor to achieve hydroelectrolytic balance in normotensive rats
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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 + Rb+/in
ADP + phosphate + Rb+/out
is transported as efficiently as K+
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
as effective as for Na+
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
as effective as for Na+
-
-
?
ATP + H2O + K+/in
ADP + phosphate + K+/out
-
more effective than for Na+
-
-
?
ATP + H2O + Li+/in
ADP + phosphate + Li+/out
-
wild-type enzyme thus recognizes Na+ slightly better than Li+
-
-
?
ATP + H2O + Li+/in
ADP + phosphate + Li+/out
-
wild-type enzyme thus recognizes Na+ slightly better than Li+
-
-
?
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
the purified enzyme catalyzes the hydrolysis of ATP in the presence of Na+ but not K+, Li+ and Ca2+
-
-
?
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
-
-
?
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
wild-type enzyme thus recognizes Na+ slightly better than Li+
-
-
?
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
wild-type enzyme thus recognizes Na+ slightly better than Li+
-
-
?
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
-
-
r
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
-
-
r
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
more effective than for K+
-
-
?
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
more effective than for K+
-
-
?
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
-
-
-
?
additional information
?
-
the enzyme has broad substrate specificity for alkali metal cations and is able to transport both sodium and potassium when expressed in Saccharomyces cerevisiae
-
-
-
additional information
?
-
Li+ and NH4+ are not transported by the enzyme
-
-
-
additional information
?
-
NH4+ is not transported by the enzyme
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + Na+/in
ADP + phosphate + Na+/out
-
-
-
r
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
-
-
r
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Li+
Mg2+
Na+
NH4+
additional information
Na+
-
the enzyme is stimulated about 9fold at pH 7.6 and about 11fold at both pH 9.0 and 11.0 with 10 mM NaCl
additional information
-
K+, Li+, and Ca2+ have no stimulatory effect on enzyme activity
additional information
-
changes in Ca2+ concentration do not alter expression of the enzyme
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3beta,22alpha,25R)-26-(beta-D-glucopyranosyloxy)-2-methoxyfurost-5-en-3-yl O-D-apio-beta-D-furanosyl-(1-2)-O-[6-deoxy-alpha-L-mannopyranosyl-(1-4)]-beta-D-glucopyranoside
-
-
(3beta,22alpha,25R)-spirostan-3-yl O-D-apio-beta-D-furanosyl-(1-2)-O-[6-deoxy-alpha-L-mannopyranosyl-(1-4)]-beta-D-glucopyranoside
-
-
angiotensin II
-
angiotensin II has an activating and regulatory role for Na+-ATPase activity in healthy rats, and angiotensin II links the enzyme activity to hypertension in spontaneously hypertensive rats, where it has an inhibitory effect on Na+-ATPase activity. The Ang II inhibitory effect is completely reversed by a specific antagonist of AT2 receptor, PD123319. Ang II interacts with different receptors in spontaneously hypertensive rats and WKY wild-type rats
atrial natriuretic peptide
-
selectively inhibits the enzyme in basolateral membranes of kidney proximal tubules by activation of guanylyl cyclase activity, which is inhibited by LY83583
-
ceramide
-
mediates enzyme inhibition to about 60% by activating protein kinase A and protein kinase Czeta, that regulate ion transporter activities. Inhibition of the kinase reverses the inhibitory effect of ceramide on Na+-ATPase
losartan
-
prevents the increase in Na+-ATPase activity observed in 14-weekold spontaneously hypertensive rats
N,N’-dicyclohexylcarbodiimide
-
78% residual activity at 1 mM in the presence of 10 mM NaCl. Inhibition in the absence of NaCl occurs after 20 min yielding 80 and 70% inhibition at pH 7.6 and pH 9.0, respectively
prostaglandin E2
-
dose-dependent inhibition with maximal effect at 1 nM. The addition of 0.001 mM prostaglandin E2 decreases Na+-ATPase activity by 41%. The inhibitory effect of prostaglandin E2 on proximal tubule Na+-ATPase activity involves G protein and the activation of protein kinase A. The protein A-mediated inhibitory effect of prostaglandin E2 on Na+-ATPase activity requires previous activation of protein kinase C
urodilatin
-
selectively inhibits the enzyme transiently in basolateral membranes of kidney proximal tubules by activation of guanylyl cyclase activity, which is inhibited by LY83583
-
Carbonyl cyanide m-chlorophenylhydrazone
0.1 mM, only partial inhibition
Ouabain
-
binding of inhibitor to enzyme results in activation of the proliferation and survival pathways involving PI3K, Akt activation, stimulation of eNOS, and production of NO in human umbilical cord endothelial cells
additional information
-
not inhibited by 0.2 mM amiloride, 0.01 mM orthovanadate, 0.5 mM NEM, 50 mM KNO3, 20 mM KSCN, 1 mM CCP, and 1 mM ouabain
-
additional information
high affinity Na+ uptake is not inhibited by Ba2+
-
additional information
-
ouabain-insensitive Na+-ATPase. A system leading to activation of the enzyme in spontaneously hypertensive rats is inhibited by AT2-mediated Ang II
-
additional information
-
guanylyl cyclase inhibitor LY83583 alone does not change the enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
ATPase activity increases as ATP increased and the activity is saturated at about 6 mM ATP
bile salt
-
induction of enzyme expression and increase in enzymic activity with concomitant decrease in intracellular ATP levels. In a bile salt-resistant mtant strain, tolerance of acidic pH-value is better than in parent strain. Expression and activity of enzyme are increased in the mutant
lysophosphatidic acid
-
stimulates the enzyme to 120% at 0.01 nM. Protein kinase C mediates the modulation of Na+-ATPase activity by lysophosphatidic acid
PacC transcription factor
required for efficient cation efflux at alkaline ambient pH
-
angiotensin II
-
angiotensin II has an activating and regulatory role for Na+-ATPase activity in healthy rats, and angiotensin II links the enzyme activity to hypertension in spontaneously hypertensive rats, where it has an inhibitory effect on Na+-ATPase activity. Ang II interacts with different receptors in spontaneously hypertensive rats and WKY wild-type rats
angiotensin II
-
physiological activation at femtomolar concentration. The activation by angiotensin II is completely abolished in the adult progeny of rats that are undernourished during lactation
angiotensin II
-
stimulates the renal Na+-ATPase, reversed by Ang-(1-7) via MAS and the A779-sensitive MAS receptor in a Gs/PKA pathway, molecular mechanism, overview
angiotensin II
-
stimulates the proximal tubule Na+-ATPase through the AT1 receptor/phosphoinositide phospholipase Cbeta/protein kinase C pathway, molecular mechanisms, overview. Ang II induces fast and correlated activation of Na+-ATPase and PKC activities with the maximal effect of 115% activation observed at 1 min and sustained for 30 min. Involvement of phospholipase A2, PLA2, on the modulation of Na+-ATPase activity by Ang II, and modulation of the effect of Ang II on Na+-ATPase activity by PLA2 inhibitors, e.g. quinacrine, PACOCF3 and a specific inhibitor, BEL, overview
additional information
-
a system leading to activation of the enzyme in spontaneously hypertensive rats is inhibited by AT2-mediated Ang II
-
additional information
-
a saponin mixture isolated from the roots of Ampelozizyphus amazonicus (50 mg/kg) significantly increases the activity of renal Na+-ATPase
-
additional information
-
phopshatidic acid stimulates the enzyme via activation of phospholipase A2, PLA2, which is inhibited by specific PLA2 inhibitors, overview
-
additional information
-
the addition of 0.001 mM guanosine 5’-O-(2-thiodiphosphate) does not change the enzyme activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06
Li+/in
-
wild type enzyme, pH and temperature not specified in the publication
0.029
ATP
-
wild type enzyme, in the presence of Na+, pH and temperature not specified in the publication
0.04
ATP
-
wild type enzyme, in the presence of Li+, pH and temperature not specified in the publication
0.067
ATP
-
mutant enzyme E139D, in the presence of Li+, pH and temperature not specified in the publication
0.1
ATP
-
mutant enzyme E139D, in the presence of Na+, pH and temperature not specified in the publication
1.2
ATP
-
apparent value, at pH 7.6, temperature not specified in the publication
3 - 3.2
Na+
-
in the presence of 0.00001 mM (3beta,22alpha,25R)-spirostan-3-yl O-D-apio-beta-D-furanosyl-(1-2)-O-[6-deoxy-alpha-L-mannopyranosyl-(1-4)]-beta-D-glucopyranoside
56.7
Na+
-
in the presence of 0.00001 mM (3beta,22alpha,25R)-26-(beta-D-glucopyranosyloxy)-2-methoxyfurost-5-en-3-yl O-D-apio-beta-D-furanosyl-(1-2)-O-[6-deoxy-alpha-L-mannopyranosyl-(1-4)]-beta-D-glucopyranoside
0.02
Na+/in
-
wild type enzyme, pH and temperature not specified in the publication
2
Na+/in
-
apparent value, at pH 7.6, temperature not specified in the publication
additional information
additional information
-
EC50 of 0.00072 mM, 0.00107 mM and 0.0008 mM for Y895C, Y895F and Y895W mutants, respectively, with ATP as substrate. EC50 of 1.44 mM, 1.36 mM and 1.87 mM for Y895C, Y895F and Y895W mutants, respectively, with Na+ as substrate. EC50 of 3.74 mM, 1.75 mM and 2.78 mM for Y895C, Y895F and Y895W mutants, respectively, with K+ as substrate
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0
(3beta,22alpha,25R)-26-(beta-D-glucopyranosyloxy)-2-methoxyfurost-5-en-3-yl O-D-apio-beta-D-furanosyl-(1-2)-O-[6-deoxy-alpha-L-mannopyranosyl-(1-4)]-beta-D-glucopyranoside
Sus scrofa
-
obtained by extrapolation of half maximal inhibition
0
(3beta,22alpha,25R)-spirostan-3-yl O-D-apio-beta-D-furanosyl-(1-2)-O-[6-deoxy-alpha-L-mannopyranosyl-(1-4)]-beta-D-glucopyranoside
Sus scrofa
-
obtained by extrapolation of half maximal inhibition
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000046
-
enzyme in isolated basolateral membranes of kidney proximal tubules, in presence of urodilatin or atrial natriuretic peptide, pH 7.0, temperature not specified in the publication
0.0000084
-
enzyme in isolated basolateral membranes of kidney proximal tubules, pH 7.0, temperature not specified in the publication
0.00325
-
ATPase activity in homogenate, hydrolysis of ATP, without ouabain, control
0.00336
-
ATPase activity in homogenate, hydrolysis of ATP, with 1 mM ouabain, control
0.00734
-
ATPase activity in homogenate, hydrolysis of ATP, with 1 mM ouabain, control, 10 mM MgCl2
0.00741
-
ATPase activity in homogenate, hydrolysis of ATP, without ouabain, control, 10 mM MgCl2
0.00808
-
ATPase activity in homogenate, hydrolysis of ATP, with 1 mM ouabain, control, 10 mM MgCl2, 120 mM NaCl
0.00813
-
ATPase activity in homogenate, hydrolysis of ATP, without ouabain, control, 10 mM MgCl2, 120 mM NaCl
0.00818
-
ATPase activity in homogenate, hydrolysis of ATP, with 1 mM ouabain, control, 10 mM MgCl2, 120 mM NaCl, 30 mM KCl
0.00907
-
ATPase activity in homogenate, hydrolysis of ATP, without ouabain, control, 10 mM MgCl2, 120 mM NaCl, 30 mM KCl
0.0103
-
ATPase activity in plasma membranes in the presence of 1 mM ouabain, hydrolysis of ATP, control
0.0266
-
crude enzyme from membrane vesicles, at pH 7.6, temperature not specified in the publication
0.0272
-
ATPase activity in plasma membranes in the presence of 1 mM ouabain, hydrolysis of ATP, 10 mM MgCl2
0.0286
-
ATPase activity in plasma membranes in the presence of 1 mM ouabain, hydrolysis of ATP, 10 mM MgCl2, 120 mM NaCl, 30 mM KCl
0.0294
-
ATPase activity in plasma membranes in the presence of 1 mM ouabain, hydrolysis of ATP, 10 mM MgCl2, 120 mM NaCl
0.4667
-
after 17.5fold purification, at pH 7.6, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.6
8
the enzyme is strongly induced in the presence of Na+ at alkaline pH
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
high external pH enhances expression of the enzyme
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
; isoform KPA2 is expressed specifically in gametophytes
-
in the membrane of porcine LLC-PK1 cells stably expressing rabbit gastric H+,K+-ATPase, [(dihydroindenyl)oxy]acetic acid inhibits activities of endogenous Na+,K+-ATPase
-
basolateral membranes of kidney proximal tubule cells
; isoform KPA1 is expressed preferentially in sporophytes
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
sequence contains ten membrane-spanning segments
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6500
8000
-
1 * 69000 + 1 * 52000 + 1 * 38000 + 1 * 27000 + 1 * 24000 + 1 * 15000 + 1 * 14000 + 1 * 8000, SDS-PAGE
14000
-
1 * 69000 + 1 * 52000 + 1 * 38000 + 1 * 27000 + 1 * 24000 + 1 * 15000 + 1 * 14000 + 1 * 8000, SDS-PAGE
15000
16500
17000
-
1 * 66000 + 1 * 61000 + 1 * 51000 + 1 * 37000 + 1 * 26000 + 1 * 17000, SDS-PAGE
19000
-
1 * 57000 + 1 * 52000 + 1 * 35000 + 1 * 19000 + 1 * 15000 + 1 * 4800, SDS-PAGE
22000
-
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE
24000
-
1 * 69000 + 1 * 52000 + 1 * 38000 + 1 * 27000 + 1 * 24000 + 1 * 15000 + 1 * 14000 + 1 * 8000, SDS-PAGE
25000
-
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE
26000
-
1 * 66000 + 1 * 61000 + 1 * 51000 + 1 * 37000 + 1 * 26000 + 1 * 17000, SDS-PAGE
27000
-
1 * 69000 + 1 * 52000 + 1 * 38000 + 1 * 27000 + 1 * 24000 + 1 * 15000 + 1 * 14000 + 1 * 8000, SDS-PAGE
29000
35000
37000
-
1 * 66000 + 1 * 61000 + 1 * 51000 + 1 * 37000 + 1 * 26000 + 1 * 17000, SDS-PAGE
38000
-
1 * 69000 + 1 * 52000 + 1 * 38000 + 1 * 27000 + 1 * 24000 + 1 * 15000 + 1 * 14000 + 1 * 8000, SDS-PAGE
51000
-
1 * 66000 + 1 * 61000 + 1 * 51000 + 1 * 37000 + 1 * 26000 + 1 * 17000, SDS-PAGE
52000
56000
57000
-
1 * 57000 + 1 * 52000 + 1 * 35000 + 1 * 19000 + 1 * 15000 + 1 * 4800, SDS-PAGE
61000
-
1 * 66000 + 1 * 61000 + 1 * 51000 + 1 * 37000 + 1 * 26000 + 1 * 17000, SDS-PAGE
66000
-
1 * 66000 + 1 * 61000 + 1 * 51000 + 1 * 37000 + 1 * 26000 + 1 * 17000, SDS-PAGE
69000
115500
+AHw-predicted from cDNA sequence, 1047 amino acids+AHwAfA-
120000
calculated molecular mass, determined by SDS-PAGE and Western-blotting
400000
additional information
open reading frame of 3261 nucleotides encoding a predicted protein of 1087 amino acids
6500
-
1 * 56000 + 1 * 52000 + 1 * 35000 + 1 * 16500 + 1 * 6500, SDS-PAGE
6500
-
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE
15000
-
1 * 69000 + 1 * 52000 + 1 * 38000 + 1 * 27000 + 1 * 24000 + 1 * 15000 + 1 * 14000 + 1 * 8000, SDS-PAGE
15000
-
1 * 57000 + 1 * 52000 + 1 * 35000 + 1 * 19000 + 1 * 15000 + 1 * 4800, SDS-PAGE
16500
-
1 * 56000 + 1 * 52000 + 1 * 35000 + 1 * 16500 + 1 * 6500, SDS-PAGE
16500
-
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE
35000
-
1 * 57000 + 1 * 52000 + 1 * 35000 + 1 * 19000 + 1 * 15000 + 1 * 4800, SDS-PAGE
35000
-
1 * 56000 + 1 * 52000 + 1 * 35000 + 1 * 16500 + 1 * 6500, SDS-PAGE
35000
-
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE
52000
-
1 * 69000 + 1 * 52000 + 1 * 38000 + 1 * 27000 + 1 * 24000 + 1 * 15000 + 1 * 14000 + 1 * 8000, SDS-PAGE
52000
-
1 * 57000 + 1 * 52000 + 1 * 35000 + 1 * 19000 + 1 * 15000 + 1 * 4800, SDS-PAGE
52000
-
1 * 56000 + 1 * 52000 + 1 * 35000 + 1 * 16500 + 1 * 6500, SDS-PAGE
52000
-
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE
56000
-
1 * 56000 + 1 * 52000 + 1 * 35000 + 1 * 16500 + 1 * 6500, SDS-PAGE
56000
-
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE
69000
-
1 * 69000 + 1 * 52000 + 1 * 38000 + 1 * 27000 + 1 * 24000 + 1 * 15000 + 1 * 14000 + 1 * 8000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
oligomer
?
-
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE
hexamer
-
1 * 57000 + 1 * 52000 + 1 * 35000 + 1 * 19000 + 1 * 15000 + 1 * 4800, SDS-PAGE
hexamer
-
1 * 66000 + 1 * 61000 + 1 * 51000 + 1 * 37000 + 1 * 26000 + 1 * 17000, SDS-PAGE
oligomer
-
1 * 69000 + 1 * 52000 + 1 * 38000 + 1 * 27000 + 1 * 24000 + 1 * 15000 + 1 * 14000 + 1 * 8000, SDS-PAGE
oligomer
-
1 * 56000 + 1 * 52000 + 1 * 35000 + 1 * 16500 + 1 * 6500, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
Na+-ATPase is inhibited by reversible phosphorylation through protein kinase A and protein kinase Czeta
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 11
-
when the pH is increased from pH 6.0 to pH 9.0, the enzyme activity is increased progressively. Increasing the pH further to pH 11.0 results in a slightly declined enzyme activity
719166
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
62%, 67.6% and 51.4% residual activity for wild-type, Y895F and YY895W mutant enzymes. Only 36.5% residual activity for Y895C mutant. The aromatic group contributes to thermal stability
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
concanavalin A affinity column chromatography and Q-Sepharose column chromatography
native enzyme from kidney cortex and basolateral membranes from renal outer cortex
-
native enzyme from kidney cortex and basolateral membranes of proximal renal tubule cells
-
partially through preparation of basolateral membranes of kidney proximal tubules
-
plasma membranes are isolated from the promastigotes of Leishmania amazonensis
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
+AHw-PCR products for the cytoplasmic-loop regions of the ATPase cloned into plasmid vectors and sequenced+AHwAfA-
expression in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae ena1-4 nha1 mutant, sensitive to high K+ and Na+ concentrations
expression in Sacharomyces cerevisiae
into tht pCR II-TOPO vector, into the mammalian expression vector pEGFP-N1 for transfection of FreeStyle 293-F cells, and into the trypanosomatid shuttle vector pTREX for transformation of Trypanosoma cruzi epimastigotes
PCR products for the cytoplasmic-loop regions of the ATPase cloned into plasmid vectors and sequenced
+AHw-PCR products for the cytoplasmic-loop regions of the ATPase cloned into plasmid vectors and sequenced+AHwAfA-
+AHw-PCR products for the cytoplasmic-loop regions of the ATPase cloned into plasmid vectors and sequenced+AHwAfA-
expression in Saccharomyces cerevisiae ena1-4 nha1 mutant, sensitive to high K+ and Na+ concentrations
-
expression in Saccharomyces cerevisiae ena1-4 nha1 mutant, sensitive to high K+ and Na+ concentrations
-
expression in Saccharomyces cerevisiae ena1-4 nha1 mutant, sensitive to high K+ and Na+ concentrations
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cells grown at 2 M NaCl show higher enzyme activity than those grown at 0.5 M NaCl. ATPase activity in is slightly increased upon increasing the pH from 5.0 to 7.6
-
isoform KPA2 transcript is down-regulated (0.2fold) in gametophytes during exposure to alkali stress (pH 9.5)
isoforms KPA1 transcript is up-regulated 2.3fold in gametophytes during exposure to alkali stress (pH 9.5). Transcription of isoform KPA1 in gametophytes is also induced by cold stress (15°C, 3.3fold increase of expression); transcription of isoform KPA2 in gametophytes is also induced by cold stress (15°C, 3.6fold increase of expression)
Na+-ATPase activity increases more than 2fold in the adult progeny of rats that are undernourished during lactation. Its physiological activation by angiotensin II is completely abolished
-
the Ena1 Na+-ATPase gene is highly upregulated by an increased osmotic pressure or sodium concentration (25fold increase of expression during the first 60 min of exposure to 1000 mM NaCl and then expression partly drops (12fold higher expression after 90 min))
isoform KPA2 transcript is down-regulated (0.2fold) in gametophytes during exposure to alkali stress (pH 9.5)
isoform KPA2 transcript is down-regulated (0.2fold) in gametophytes during exposure to alkali stress (pH 9.5)
-
-
isoforms KPA1 transcript is up-regulated 2.3fold in gametophytes during exposure to alkali stress (pH 9.5). Transcription of isoform KPA1 in gametophytes is also induced by cold stress (15°C, 3.3fold increase of expression); transcription of isoform KPA2 in gametophytes is also induced by cold stress (15°C, 3.6fold increase of expression)
isoforms KPA1 transcript is up-regulated 2.3fold in gametophytes during exposure to alkali stress (pH 9.5). Transcription of isoform KPA1 in gametophytes is also induced by cold stress (15°C, 3.3fold increase of expression); transcription of isoform KPA2 in gametophytes is also induced by cold stress (15°C, 3.6fold increase of expression)
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E139D
E139D
-
the E139D mutant of the NtpK subunit loses tolerance to sodium but not to lithium at pH 10. The mutant enzyme retains relatively high specific activity and affinity for the lithium ion compared to the sodium ion. Vmax values of the mutant enzyme are reduced to approximately 34% of that of the wild type enzyme
E139D
-
the E139D mutant of the NtpK subunit loses tolerance to sodium but not to lithium at pH 10. The mutant enzyme retains relatively high specific activity and affinity for the lithium ion compared to the sodium ion. Vmax values of the mutant enzyme are reduced to approximately 34% of that of the wild type enzyme
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
expression of triple hemagglutinin-tagged enzyme in Nicotiana tabacum confers increased NaCl and LiCl tolerance to cells. Under moderate slat stress, enzyme expression results in accumulation of less Na+, Li+ and K+ than in wild-type
medicine
pharmacology
pharmacology
-
lower concentration of [(dihydroindenyl)oxy]acetic acid should be used for evaluation of the activity of K+-Cl- cotranporter without affecting the activities of coexisting Na+,K+-ATPase and H+,K+-ATPase in cells
pharmacology
-
lower concentration of [(dihydroindenyl)oxy]acetic acid should be used for evaluation of the activity of K+-Cl- cotranporter without affecting the activities of coexisting Na+,K+-ATPase and H+,K+-ATPase in cells
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LINKS TO OTHER DATABASES (specific for EC-Number 3.6.3.7)
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