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Information on EC 7.2.2.3 - P-type Na+ transporter
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7.2.2.3 P-type Na+ transporterIUBMB Comments
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. Some forms can also export Li+ ions. cf. EC 7.2.2.1, Na+-transporting two-sector ATPase and EC 7.2.2.4, ABC-type Na+ transporter.
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Word Map
- 7.2.2.3
- cardiac
- erythrocyte
-
ouabain-sensitive
- atpases
- hypertension
- myosin
- sarcoplasmic
-
electrogenic
-
contractile
- ca2+-atpase
- nerve
- arterial
- gill
-
basolateral
- glycoside
-
sodium-potassium
- tubule
- na,k-atpase
-
depolarization
- migraine
- alpha-subunits
- digoxin
-
hyperpolarization
-
cotransporter
- myofibrillar
- vanadate
-
normotensive
-
inotropic
- h+-atpase
-
cytochemical
-
cardiotonic
- amiloride
-
sarcolemmal
-
mg2+-dependent
-
transepithelial
- digitalis
- aura
-
k+-dependent
- phosphoenzyme
- oligomycin
- rb+
- actomyosin
-
branchial
-
osmoregulatory
- dicyclohexylcarbodiimide
-
natriuresis
- hemiplegia
- menkes
-
proton-translocating
- serca
- medicine
- biotechnology
- pharmacology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
adenosine triphosphatase, na+,k+-atpase, sodium pump, na+/k+-atpase, p-type atpase, atp1a2, atp hydrolase, vacuolar-type atpase, adenosine 5'-triphosphatase, na+-stimulated atpase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine 5'-triphosphatase
-
-
-
-
adenosine triphosphatase
-
-
-
-
ATP hydrolase
-
-
-
-
ATP4
ATPase
-
-
-
-
complex V (mitochondrial electron transport)
-
-
-
-
EC 3.6.3.7
-
-
formerly
-
Ena1
KPA1
KPA2
Na+,K+-ATPase
Na+-ATPase
Na+-exporting ATPase
NtpK
P-type ATPase
P-type Na+-ATPase
P2-type ATPase
sodium ATPase
sodium pump
vacuolar-type ATPase
NtpK
-
V-type Na+-ATPase subunit, the NtpK subunit forms the rotor ring of the Vo moiety, which is responsible for ion translocation
NtpK
-
V-type Na+-ATPase subunit, the NtpK subunit forms the rotor ring of the Vo moiety, which is responsible for ion translocation
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + n Na+[side 1] = ADP + phosphate + n Na+[side 2]
-
-
-
-
ATP + H2O + n Na+[side 1] = ADP + phosphate + n Na+[side 2]
efflux in the absence of external Na+ follows first order kinetics
-
ATP + H2O + n Na+[side 1] = ADP + phosphate + n Na+[side 2]
Ena1 gene plays a fundamental role in the salt stress response
ATP + H2O + n Na+[side 1] = ADP + phosphate + n Na+[side 2]
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 + n Na+[side 1] = ADP + phosphate + n Na+[side 2]
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 + n Na+[side 1] = ADP + phosphate + n Na+[side 2]
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 + n Na+[side 1] = ADP + phosphate + n Na+[side 2]
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 + n Na+[side 1] = ADP + phosphate + n Na+[side 2]
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 + n Na+[side 1] = ADP + phosphate + n Na+[side 2]
the enzyme function is triggered when the cells are suffering K+ starvation
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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 (P-type, 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. Some forms can also export Li+ ions. cf. EC 7.2.2.1, Na+-transporting two-sector ATPase and EC 7.2.2.4, ABC-type Na+ transporter.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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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 + K+[side 1]
ADP + phosphate + K+[side 2]
-
-
-
-
?
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 + Li+[side 1]
ADP + phosphate + Li+[side 2]
-
-
-
-
?
ATP + H2O + Li+[side 1]
ADP + phosphate + Li+[side 2]
-
-
-
-
?
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
-
-
-
-
?
ATP + H2O + Na+[side 1]
ADP + phosphate + Na+[side 2]
-
-
-
-
?
ATP + H2O + Na+[side 1]
ADP + phosphate + Na+[side 2]
-
-
-
-
?
additional information
?
-
Li+ and NH4+ are not transported by the enzyme
-
-
?
additional information
?
-
NH4+ is not transported by the enzyme
-
-
?
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
-
-
?
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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 + Na+/in
ADP + phosphate + Na+/out
-
-
-
r
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
-
-
r
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
-
-
-
?
ATP + H2O + Na+[side 1]
ADP + phosphate + Na+[side 2]
-
-
-
-
?
ATP + H2O + Na+[side 1]
ADP + phosphate + Na+[side 2]
-
-
-
-
?
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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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INHIBITOR
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
cipargamin
-
previously known as KAE609 and NITD609, complete inhibition at 500 nM
Fe2+
-
dithiothreitol exerts considerable protective effect on the activity of the Fe2+-inhibited enzyme
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
Ouabain
shows moderate selectivity (approximately 2.5fold) for alpha1 over alpha2 subunits of the enzyme
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 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
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
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
16.1
Na+[side 1]
-
at pH 7.2, 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
0.00001
(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
0.000001
(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
12.3
cipargamin
Plasmodium falciparum
-
wild type enzyme, at pH 7.2, temperature not specified in the publication
21.1
cipargamin
Plasmodium falciparum
-
mutant enzyme T418N, at pH 7.2, temperature not specified in the publication
32.5
cipargamin
Plasmodium falciparum
-
mutant enzyme T418N/P990R, at pH 7.2, temperature not specified in the publication
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
+AHw-LDCA1, present as a single copy gene+AHwAfA-
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
isoform KPA2 is expressed specifically in gametophytes
brenda
-
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
brenda
-
basolateral membranes of kidney proximal tubule cells
brenda
-
basolateral membranes of kidney proximal tubule cells
brenda
isoform KPA1 is expressed preferentially in sporophytes
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
sequence contains ten membrane-spanning segments
brenda
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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
isoform KPA1 plays an important role in alkali and cold stress tolerance
physiological function
isoform KPA2 plays an important role in alkali and cold stress tolerance
physiological function
Na+ATPase is involved in Candida glabrata tolerance to high concentrations of Na+ and Li+
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
cardiomyocyte ATP1A2 is a target of anoxia-reoxygenation injury
physiological function
the sodium pump alpha1 subunit potentially mediates various antiglioblastoma signaling pathways and affects the sensitivity of glioblastoma cells to drugs
physiological function
Neopyropia yezoensis TU-1
-
isoform KPA2 plays an important role in alkali and cold stress tolerance
-
physiological function
Neopyropia yezoensis TU-1
-
isoform KPA1 plays an important role in alkali and cold stress tolerance
-
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
additional information
-
inosine-induced inhibition of Na+-ATPase activity could be involved in the increased renal sodium excretion during short periods of ischemia
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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). ATN1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
1091
10
120357
Swiss-Prot
other Location (Reliability: 1)
ATN2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
1091
10
120317
Swiss-Prot
other Location (Reliability: 1)
ATN5_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
1091
10
120296
Swiss-Prot
other Location (Reliability: 1)
Q4WIM5_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
1079
9
116266
TrEMBL
other Location (Reliability: 1)
A0A0F8CUI4_CERFI
1104
9
119439
TrEMBL
other Location (Reliability: 3)
Q4WD68_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
1060
10
116447
TrEMBL
other Location (Reliability: 3)
B8LXI0_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
1079
9
117782
TrEMBL
other Location (Reliability: 5)
A0A084FVG3_PSEDA
1073
10
118203
TrEMBL
other Location (Reliability: 3)
M5BTS3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
165
0
17185
TrEMBL
other Location (Reliability: 2)
A0A084FUW6_PSEDA
1107
8
121721
TrEMBL
other Location (Reliability: 3)
A0A084G766_PSEDA
1062
8
116728
TrEMBL
other Location (Reliability: 5)
Q4WPJ1_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
1048
8
114383
TrEMBL
other Location (Reliability: 2)
B9W6J0_CANDC
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841)
1067
8
116799
TrEMBL
other Location (Reliability: 2)
A0A072V2S7_MEDTR
1191
10
131804
TrEMBL
other Location (Reliability: 2)
A0A084G6D5_PSEDA
1032
10
111558
TrEMBL
other Location (Reliability: 3)
K0KJC4_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
1054
10
116081
TrEMBL
other Location (Reliability: 2)
A0A084GCP0_PSEDA
1060
12
115417
TrEMBL
other Location (Reliability: 2)
K7WVI3_GANLU
930
8
99895
TrEMBL
Mitochondrion (Reliability: 4)
A0A0F4YMJ4_TALEM
1150
10
125409
TrEMBL
Mitochondrion (Reliability: 4)
A0A1S8A692_ROSNE
842
6
93094
TrEMBL
other Location (Reliability: 2)
AT1A1_HUMAN
1023
10
112896
Swiss-Prot
other Location (Reliability: 4)
Q4LB57_NEOYE
1169
0
128429
TrEMBL
Secretory Pathway (Reliability: 1)
Q5A9B2_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
355
0
38870
TrEMBL
-
Q6VAH6_FUSOX
1087
0
119632
TrEMBL
-
Q703F7_MAGGR
960
0
104579
TrEMBL
Mitochondrion (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
115500
+AHw-predicted from cDNA sequence, 1047 amino acids+AHwAfA-
120000
calculated molecular mass, determined by SDS-PAGE and Western-blotting
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
400000
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
6500
66000
-
1 * 66000 + 1 * 61000 + 1 * 51000 + 1 * 37000 + 1 * 26000 + 1 * 17000, SDS-PAGE
69000
8000
-
1 * 69000 + 1 * 52000 + 1 * 38000 + 1 * 27000 + 1 * 24000 + 1 * 15000 + 1 * 14000 + 1 * 8000, SDS-PAGE
additional information
open reading frame of 3261 nucleotides encoding a predicted protein of 1087 amino acids
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 * 56000 + 1 * 52000 + 1 * 35000 + 1 * 16500 + 1 * 6500, SDS-PAGE
35000
-
1 * 57000 + 1 * 52000 + 1 * 35000 + 1 * 19000 + 1 * 15000 + 1 * 4800, SDS-PAGE
35000
-
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE
52000
-
1 * 56000 + 1 * 52000 + 1 * 35000 + 1 * 16500 + 1 * 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
-
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
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
69000
-
1 * 69000 + 1 * 52000 + 1 * 38000 + 1 * 27000 + 1 * 24000 + 1 * 15000 + 1 * 14000 + 1 * 8000, SDS-PAGE
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SUBUNIT
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
-
phosphorylation of the enzyme increases from pH 5.0 up to 8.5
phosphoprotein
Saccharomyces cerevisiae DBY746
-
phosphorylation of the enzyme increases from pH 5.0 up to 8.5
-
phosphoprotein
-
Na+-ATPase is inhibited by reversible phosphorylation through protein kinase A and protein kinase Czeta
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E139D
T418N
-
the mutant shows a lower level of inhibition by cipargamin compared to the wild type enzyme
T418N/P990R
-
the mutant shows a lower level of inhibition by cipargamin compared to the wild type enzyme
T418N
-
the mutant shows a lower level of inhibition by cipargamin compared to the wild type enzyme
-
T418N/P990R
-
the mutant shows a lower level of inhibition by cipargamin compared to 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
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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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
-
enzyme expression is induced as response to salt stress in the rim101 mutant which is sensitive to both alkaline pH and salt stress
expression of the sodium pump alpha1 subunit in glioblastoma tissues is generally higher than that in normal tissues
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 (15C, 3.3fold 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
-
subunit ATP1A2 expression is downregulated upon anoxia-reoxygenation injury
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))
transcription of isoform KPA2 in gametophytes is also induced by cold stress (15C, 3.6fold increase of expression)
enzyme expression is induced as response to salt stress in the rim101 mutant which is sensitive to both alkaline pH and salt stress
-
enzyme expression is induced as response to salt stress in the rim101 mutant which is sensitive to both alkaline pH and salt stress
-
-
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)
Neopyropia yezoensis TU-1
-
-
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 (15C, 3.3fold 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 (15C, 3.3fold increase of expression)
Neopyropia yezoensis TU-1
-
-
transcription of isoform KPA2 in gametophytes is also induced by cold stress (15C, 3.6fold increase of expression)
transcription of isoform KPA2 in gametophytes is also induced by cold stress (15C, 3.6fold increase of expression)
Neopyropia yezoensis TU-1
-
-
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Murata, T.; Igarashi, K.; Kakinuma, Y.; Yamato, I.
Na+ binding of V-type Na+-ATPase in Enterococcus hirae
J. Biol. Chem.
275
13415-13419
2000
Enterococcus hirae
brenda
Murata, T.; Takase, K.; Yamato, I.; Igarashi, K.; Kakinuma, Y.
Purification and reconstitution of Na+-translocating vacuolar ATPase from Enterococcus hirae
J. Biol. Chem.
272
24885-24890
1997
Enterococcus hirae
brenda
Kluge, C.; Dimroth, P.
Studies on Na+ and H+ translocation through the F0 part of the Na+-translocating F1F0 ATPase from Propionibacterium modestum: discovery of a membrane potential dependent step
Biochemistry
31
12665-12672
1992
Propionigenium modestum
brenda
Kakinuma, Y.; Yamato, I.; Murata, T.
Structure and function of vacuolar Na+-translocating ATPase in Enterococcus hirae
J. Bioenerg. Biomembr.
31
7-14
1999
Enterococcus hirae
brenda
Kakinuma, Y.; Igarashi, K.
Purification and characterization of the catalytic moiety of vacuolar-type Na+-ATPase from Enterococcus hirae
J. Biochem.
116
1302-1308
1994
Enterococcus hirae
brenda
Reidlinger, J.; Muller, V.
Purification of ATP synthase from Acetobacterium woodii and identification as a Na+-translocating F1F0-type enzyme
Eur. J. Biochem.
223
275-283
1994
Acetobacterium woodii
brenda
Dmitriev, O.; Deckers-Hebestreit, G.; Altendorf, K.
ATP synthesis energized by deltapNa und deltaphi in proteoliposomes containing the F0F1-ATPase from Propionigenium modestum
J. Biol. Chem.
268
14776-14780
1993
Propionigenium modestum
brenda
Kholodenko, B.N.
Kinetic models of coupling between H+ and Na+-translocation and ATP synthesis/hydrolysis by F0F1-ATPases: Can a cell utilize both delta mu H+ and delta mu Na+ for ATP synthesis under in vivo conditions using the same enzyme?
J. Bioenerg. Biomembr.
25
285-295
1993
Propionigenium modestum
brenda
Becher, B.; Muller, V.
delta mu Na+ drives the synthesis of ATP via an delta mu Na+-translocating F1F0-ATP synthase in membrane vesicles of the archaeon Methanosarcina mazei G1
J. Bacteriol.
176
2543-2550
1994
Methanosarcina mazei G1
brenda
Wieland, J.; Nitsche, A.M.; Strayle, J.; Steiner, H.; Rudolph, H.K.
The PMR2 gene cluster encodes functionally distinct isoforms of a putative Na+ pump in the yeast plasma membrane
EMBO J.
14
3870-3882
1995
Saccharomyces cerevisiae, Saccharomyces pastorianus, Saccharomyces chevalieri, Saccharomyces norbensis, Saccharomyces uvarum
brenda
Smigan, P.; Majernik, A.; Polak, P.; Hapala, I.; Greksak, M.
The presence of H+ and Na+-translocating ATPases in Methanobacterium thermoautotrophicum and their possible function under alkaline conditions
FEBS Lett.
371
119-122
1995
Methanothermobacter thermautotrophicus
brenda
Hner zu Bentrup, K.; Ubbink-Kok, T.; Lolkema, J.S.; Konings, W.N.
An Na+-pumping V1V0-ATPase complex in the thermophilic bacterium Clostridium fervidus
J. Bacteriol.
179
1274-1279
1997
Caloramator fervidus
brenda
Cheng, J.; Guffanti, A.A.; Krulwich, T.A.
A two-gene ABC-type transport system that extrudes Na+ in Bacillus subtilis is induced by ethanol or protonophore
Mol. Microbiol.
23
1107-1120
1997
Bacillus subtilis
brenda
Catty, P.; de Kerchove d'Exaerde, A.; Goffeau, A.
The complete inventory of the yeast Saccharomyces cerevisiae P-type transport ATPases
FEBS Lett.
409
325-332
1997
Saccharomyces cerevisiae
brenda
Popova, L.; Balnokin, Y.; Dietz, K.J.; Gimmler, H.
Na+-ATPase from the plasma membrane of the marine alga Tetraselmis (Platymonas) viridis forms a phosphorylated intermediate
FEBS Lett.
426
161-164
1998
Tetraselmis viridis
brenda
Neumann, S.; Matthey, U.; Kaim, G.; Dimroth, P.
Purification and properties of the F1F0 ATPase of Ilyobacter tartaricus, a sodium ion pump
J. Bacteriol.
180
3312-3316
1998
Ilyobacter tartaricus
brenda
Stiles, J.K.; Kucerova, Z.; Sarfo, B.; Meade, C.A.; Thompson, W.; Shah, P.; Xue, L.; Meade, J.C.
Identification of surface-membrane P-type ATPases resembling fungal K+- and Na+-ATPases, in Trypanosoma brucei, Trypanosoma cruzi and Leishmania donovani
Ann. Trop. Med. Parasitol.
97
351-366
2003
Leishmania donovani (O61136), Leishmania donovani, Trypanosoma cruzi (Q86QH8), Trypanosoma cruzi, Trypanosoma brucei (Q9XZJ9), Trypanosoma brucei
brenda
Benito, B.; Garciadeblas, B.; Schreier, P.; Rodriguez-Navarro, A.
Novel P-type ATPases mediate high-affinity potassium or sodium uptake in fungi
Eukaryot. Cell
3
359-368
2004
Candida albicans (Q5A9B2), Pyricularia grisea (Q703F6), Pyricularia grisea (Q703F7), Millerozyma farinosa (Q703G3), Ustilago maydis (Q703G5)
brenda
Caracuel, Z.; Casanova, C.; Roncero, M.I.G.; Di Pietro, A.; Ramos, J.
pH response transcription factor PacC controls salt stress tolerance and expression of the P-Type Na+-ATPase Ena1 in Fusarium oxysporum
Eukaryot. Cell
2
1246-1252
2003
Fusarium oxysporum (Q6VAH6)
brenda
Becker, S.; Schneider, H.; Schneider-Bovis, G.
The highly conserved extracellular peptide, DSYG(893-896), is a critical structure for sodium pump function
Eur. J. Biochem.
271
3821-3831
2004
Ovis aries
brenda
Stein, W.D.
Cell volume homeostasis: ionic and nonionic mechanisms. The sodium pump in the emergence of animal cells
Int. Rev. Cytol.
215
231-258
2002
Drosophila melanogaster, Homo sapiens, Mus musculus, Lithobates catesbeianus, Hydra sp.
brenda
Benito, B.; Garciadeblas, B.; Rodriguez-Navarro, A.
Potassium- or sodium-efflux ATPase, a key enzyme in the evolution of fungi
Microbiology
148
933-941
2002
Saccharomyces cerevisiae, Debaryomyces hansenii, Neurospora crassa, Schizosaccharomyces pombe, Pleurotus ostreatus (Q8WZN5), Phycomyces blakesleeanus (Q8WZP1), Phycomyces blakesleeanus (Q8WZP2), Blakeslea trispora (Q8X0Z9), Blakeslea trispora (Q8X100), Blakeslea trispora (Q8X101), Neurospora crassa NcENA1
brenda
Benito, B.; Rodriguez-Navarro, A.
Molecular cloning and characterization of a sodium-pump ATPase of the moss Physcomitrella patens
Plant J.
36
382-389
2003
Physcomitrium patens
brenda
Suzuki, Y.; Ueno, S.; Ohnuma, R.; Koyama, N.
Cloning, sequencing and functional expression in Escherichia coli of the gene for a P-type Na(+)-ATPase of a facultatively anaerobic alkaliphile, Exiguobacterium aurantiacum
Biochim. Biophys. Acta
1727
162-168
2005
Exiguobacterium aurantiacum
brenda
Eva, A.; Kirch, U.; Scheiner-Bobis, G.
Signaling pathways involving the sodium pump stimulate NO production in endothelial cells
Biochim. Biophys. Acta
1758
1809-1814
2006
Homo sapiens
brenda
Nakayama, H.; Yoshida, K.; Shinmyo, A.
Yeast plasma membrane Ena1p ATPase alters alkali-cation homeostasis and confers increased salt tolerance in tobacco cultured cells
Biotechnol. Bioeng.
85
776-789
2004
Saccharomyces cerevisiae
brenda
Sanchez, B.; de los Reyes-Gavilan, C.G.; Margolles, A.
The F1F0-ATPase of Bifidobacterium animalis is involved in bile tolerance
Environ. Microbiol.
8
1825-1833
2006
Bifidobacterium animalis
brenda
Iizumi, K.; Mikami, Y.; Hashimoto, M.; Nara, T.; Hara, Y.; Aoki, T.
Molecular cloning and characterization of ouabain-insensitive Na+-ATPase in the parasitic protist, Trypanosoma cruzi
Biochim. Biophys. Acta
1758
738-746
2006
Trypanosoma cruzi (Q76DT8), Trypanosoma cruzi
brenda
Fujii, T.; Ohira, Y.; Itomi, Y.; Takahashi, Y.; Asano, S.; Morii, M.; Takeguchi, N.; Sakai, H.
Inhibition of P-type ATPases by [(dihydroindenyl)oxy]acetic acid (DIOA), a K+ -Cl- cotransporter inhibitor
Eur. J. Pharmacol.
560
123-126
2007
Canis lupus familiaris, Sus scrofa
brenda
de Almeida-Amaral, E.E.; Caruso-Neves, C.; Pires, V.M.; Meyer-Fernandes, J.R.
Leishmania amazonensis: characterization of an ouabain-insensitive Na+-ATPase activity
Exp. Parasitol.
118
165-171
2008
Leishmania amazonensis, Leishmania amazonensis MHOM/BR/75/Josefa
brenda
Wiangnon, K.; Raksajit, W.; Incharoensakdi, A.
Presence of a Na+-stimulated P-type ATPase in the plasma membrane of the alkaliphilic halotolerant cyanobacterium Aphanothece halophytica
FEMS Microbiol. Lett.
270
139-145
2007
Aphanothece halophytica
brenda
Saraiva, V.B.; Wengert, M.; Gomes-Quintana, E.; Heise, N.; Caruso-Neves, C.
Na(+)-ATPase and protein kinase C are targets to 1-O-hexadecylphosphocoline (miltefosine) in Trypanosoma cruzi
Arch. Biochem. Biophys.
481
65-71
2009
Trypanosoma cruzi, Trypanosoma cruzi Y-
brenda
Logg, K.; Warringer, J.; Hashemi, S.H.; Kaell, M.; Blomberg, A.
The sodium pump Ena1p provides mechanistic insight into the salt sensitivity of vacuolar protein sorting mutants
Biochim. Biophys. Acta
1783
974-984
2008
Saccharomyces cerevisiae
brenda
Gomes, C.P.; Leao-Ferreira, L.R.; Pinheiro, A.A.; Gomes-Quintana, E.; Wengert, M.; Lopes, A.G.; Caruso-Neves, C.
Crosstalk between the signaling pathways triggered by angiotensin II and adenosine in the renal proximal tubules: implications for modulation of Na(+)-ATPase activity
Peptides
29
2033-2038
2008
Sus scrofa
brenda
de Souza, A.M.; Lara, L.d.a..S.; Previato, J.O.; Lopes, A.G.; Caruso-Neves, C.; da Silva, B.P.; Parente, J.P.
Modulation of sodium pumps by steroidal saponins
Z. Naturforsch. C
59
432-436
2008
Sus scrofa
brenda
Assaife-Lopes, N.; Wengert, M.; de Sa Pinheiro, A.A.; Leao-Ferreira, L.R.; Caruso-Neves, C.
Inhibition of renal Na+-ATPase activity by inosine is mediated by A1 receptor-induced inhibition of the cAMP signaling pathway
Arch. Biochem. Biophys.
489
76-81
2009
Sus scrofa
brenda
Lara, L.S.; Vives, D.; Correa, J.S.; Cardozo, F.P.; Marques-Fernades, M.F.; Lopes, A.G.; Caruso-Neves, C.
PKA-mediated effect of MAS receptor in counteracting angiotensin II-stimulated renal Na+-ATPase
Arch. Biochem. Biophys.
496
117-122
2010
Sus scrofa
brenda
Cabral, L.M.; Wengert, M.; Almeida, F.G.; Caruso-Neves, C.; Vieyra, A.; Einicker-Lamas, M.
Ceramide-activated protein kinases A and C zeta inhibit kidney proximal tubule cell Na+-ATPase
Arch. Biochem. Biophys.
498
57-61
2010
Sus scrofa
brenda
De Souza, A.M.; de Carvalho, T.L.; Lara, L.d.a..S.; Gomes-Quintana, E.; Lopes, A.G.; Caruso-Neves, C.
The stimulatory effect of angiotensin II on Na+-ATPase activity involves sequential activation of phospholipases and sustained PKC activity
Biochim. Biophys. Acta
1798
354-359
2010
Sus scrofa
brenda
Queiroz-Madeira, E.P.; Lara, L.S.; Wengert, M.; Landgraf, S.S.; Libano-Soares, J.D.; Zapata-Sudo, G.; Sudo, R.T.; Takiya, C.M.; Gomes-Quintana, E.; Lopes, A.G.; Caruso-Neves, C.
Na+-ATPase in spontaneous hypertensive rats: possible AT1 receptor target in the development of hypertension
Biochim. Biophys. Acta
1798
360-366
2010
Rattus norvegicus
brenda
Vives, D.; Farage, S.; Motta, R.; Lopes, A.G.; Caruso-Neves, C.
Atrial natriuretic peptides and urodilatin modulate proximal tubule Na+-ATPase activity through activation of the NPR-A/cGMP/PKG pathway
Peptides
31
903-908
2010
Sus scrofa
brenda
Libano-Soares, J.D.; Landgraf, S.S.; Gomes-Quintana, E.; Lopes, A.G.; Caruso-Neves, C.
Prostaglandin E2 modulates proximal tubule Na+-ATPase activity: cooperative effect between protein kinase A and protein kinase C
Arch. Biochem. Biophys.
507
281-286
2011
Sus scrofa
brenda
Rocafull, M.A.; Romero, F.J.; Thomas, L.E.; del Castillo, J.R.
Isolation and cloning of the K+-independent, ouabain-insensitive Na+-ATPase
Biochim. Biophys. Acta
1808
1684-1700
2011
Cavia porcellus (B3SI05), Cavia porcellus
brenda
Soontharapirakkul, K.; Incharoensakdi, A.
Na+-stimulated ATPase of alkaliphilic halotolerant cyanobacterium Aphanothece halophytica translocates Na+ into proteoliposomes via Na+ uniport mechanism
BMC Biochem.
11
30
2010
Aphanothece halophytica
brenda
Diniz, L.R.; Portella, V.G.; Cardoso, F.M.; Sousa, A.M.; Caruso-Neves, C.; Cassali, G.D.; Reis, A.M.; Brandao, M.G.; Vieira, M.A.
The effect of saponins from Ampelozizyphus amazonicus Ducke on the renal Na+ pumps activities and urinary excretion of natriuretic peptides
BMC Complement. Altern. Med.
12
40
2012
Rattus norvegicus
brenda
Krauke, Y.; Sychrova, H.
Cnh1 Na+ /H+ antiporter and Ena1 Na+-ATPase play different roles in cation homeostasis and cell physiology of Candida glabrata
FEMS Yeast Res.
11
29-41
2011
[Candida] glabrata (P13587)
brenda
Kawano-Kawada, M.; Takahashi, H.; Igarashi, K.; Murata, T.; Yamato, I.; Homma, M.; Kakinuma, Y.
Significance of the glutamate-139 residue of the V-type Na+-ATPase NtpK subunit in catalytic turnover linked with salt tolerance of Enterococcus hirae
J. Bacteriol.
193
3657-3661
2011
Enterococcus hirae, Enterococcus hirae ATCC 9790
brenda
Uji, T.; Hirata, R.; Mikami, K.; Mizuta, H.; Saga, N.
Molecular characterization and expression analysis of sodium pump genes in the marine red alga Porphyra yezoensis
Mol. Biol. Rep.
39
7973-7980
2012
Neopyropia yezoensis (I4DSP4), Neopyropia yezoensis (Q4LB57), Neopyropia yezoensis, Neopyropia yezoensis TU-1 (I4DSP4), Neopyropia yezoensis TU-1 (Q4LB57)
brenda
Luzardo, R.; Silva, P.A.; Einicker-Lamas, M.; Ortiz-Costa, S.; do Carmo, M.d.a..G.; Vieira-Filho, L.D.; Paixao, A.D.; Lara, L.S.; Vieyra, A.
Metabolic programming during lactation stimulates renal Na+ transport in the adult offspring due to an early impact on local angiotensin II pathways
PLoS ONE
6
e21232
2011
Rattus norvegicus
brenda
Benito, B.; Quintero, F.; Rodriguez-Navarro, A.
Overexpression of the sodium ATPase of Saccharomyces cerevisiae Conditions for phosphorylation from ATP and Pi
Biochim. Biophys. Acta
1328
214-226
1997
Saccharomyces cerevisiae, Saccharomyces cerevisiae DBY746
brenda
Hu, Y.; Wang, Z.; Ge, N.; Huang, T.; Zhang, M.; Wang, H.
Sodium pump alpha-2 subunit (ATP1A2) alleviates cardiomyocyte anoxia-reoxygenation injury via inhibition of endoplasmic reticulum stress-related apoptosis
Can. J. Physiol. Pharmacol.
96
515-520
2018
Rattus norvegicus (P06686)
brenda
Lan, Y.L.; Yu, Z.L.; Lou, J.C.; Ma, X.C.; Zhang, B.
Update on the effects of the sodium pump alpha1 subunit on human glioblastoma from the laboratory to the clinic
Expert Opin. Investig. Drugs
27
753-763
2018
Homo sapiens (P05023), Homo sapiens
brenda
Marques, M.C.; Zamarbide-Fores, S.; Pedelini, L.; Llopis-Torregrosa, V.; Yenush, L.
A functional Rim101 complex is required for proper accumulation of the Ena1 Na+-ATPase protein in response to salt stress in Saccharomyces cerevisiae
FEMS Yeast Res.
15
fov017
2015
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Rosling, J.E.O.; Ridgway, M.C.; Summers, R.L.; Kirk, K.; Lehane, A.M.
Biochemical characterization and chemical inhibition of PfATP4-associated Na+-ATPase activity in Plasmodium falciparum membranes
J. Biol. Chem.
293
13327-13337
2018
Plasmodium falciparum, Plasmodium falciparum Dd2
brenda
Omotayo, T.I; Akinyemi, G.S.; Omololu, P.A.; Ajayi, B.O.; Akindahunsi, A.A.; Rocha, J.B.; Kade, I.J.
Possible involvement of membrane lipids peroxidation and oxidation of catalytically essential thiols of the cerebral transmembrane sodium pump as component mechanisms of iron-mediated oxidative stress-linked dysfunction of the pump's activity
Redox Biol.
4
234-241
2014
Rattus norvegicus
brenda
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EXTERNAL LINKS (specific for EC-Number 7.2.2.3)
Transporter Classification Database (TCDB): 3.A.3.9.1
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