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Information on EC 7.2.2.10 - P-type Ca2+ transporter
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7.2.2.10 P-type Ca2+ transporterIUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria. The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolysed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolysed. In muscle cells Ca2+ is transported from the cytosol (side 1) into the sarcoplasmic reticulum (side 2).
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Word Map
- 7.2.2.10
- cardiac
- thapsigargin
-
contractile
- ventricular
- phospholamban
- myocardial
- cardiomyocytes
- calmodulin
-
ryanodine
- myocytes
- na+
- myosin
-
pmcas
- atpases
- hypertrophy
-
blocker
-
cyclopiazonic
- inositol
-
diastolic
- caffeine
-
ca2+-free
-
fura-2
-
l-type
- vanadate
-
extrusion
- plb
- overload
- phosphoenzyme
-
systolic
- nifedipine
- cpa
-
excitation-contraction
- ouabain
-
store-operated
-
1,4,5-trisphosphate
-
ca2+-binding
-
calmodulin-dependent
-
twitch
- na+-k+-atpase
-
slow-twitch
-
ca2+-sensitive
- na,k-atpase
-
refilling
-
inotropic
- myofibrillar
-
k+-atpase
-
fast-twitch
-
ca2+-induced
- medicine
- insp3
-
actin-activated
- biotechnology
- pharmacology
- agriculture
The enzyme appears in viruses and cellular organisms
Synonyms
serca, ca2+-atpase, serca2a, ca2+ pump, serca2, ca-atpase, calcium pump, ca2+ atpase, serca1, serca2b, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACA8
ATP-consuming plasma membrane calcium pump
ATP-dependent Ca2+ pump PMR1
-
-
-
-
Atp2b
ATP6
ATPase 2C1
Ca2+ ATPase
Ca2+-ATPase
Ca2+-ATPase, isoform 10
-
-
-
-
Ca2+-ATPase, isoform 11
-
-
-
-
Ca2+-ATPase, isoform 12
-
-
-
-
Ca2+-ATPase, isoform 13
-
-
-
-
Ca2+-pumping ATPase
Ca2+-transporting ATPase
Ca2+/Mn2+ P-type ATPase
calcium pump
-
-
-
-
Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform
-
-
-
-
Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
-
-
-
-
ChkSERCA3
-
-
-
-
EC 3.6.1.3
-
-
related
-
EC 3.6.1.38
-
-
formerly
-
EC 3.6.3.8
-
-
formerly
-
endoplasmic reticulum class 1/2 Ca(2+) ATPase
-
-
-
-
Golgi Ca2+-ATPase
-
-
-
-
HUSSY-28
-
-
-
-
Mn2+-transporting P-type ATPase
P-type ATPase
P-type Ca2+-ATPase
P-type Ca2+/Mn2+-ATPase
P-type calcium ATPase
PCA1
-
PCA1 represents a PIIB-type Ca2+-ATPase containing a N-terminal autoinhibitory domain
PfATP6
phosphatase, adenosine tri
-
-
-
-
plasma membrane ATPase related 1
plasma membrane Ca-ATPase
-
-
-
-
plasma membrane Ca2+ ATPase
plasma membrane Ca2+-ATPase
plasma membrane Ca2+-ATPase 4
plasma membrane calcium ATPase
plasma membrane calcium pump
plasma-membrane Ca2+-ATPase
PMCA
PMCA pump
PMCA1
PMCA2
PMCA3
PMCA4
PMCA4b
PMR1
Pmr1p
sarco(endo)plasmic reticulum Ca2+ ATPase
sarco(endo)plasmic reticulum Ca2+-ATPase
sarco-endoplasmic reticulum Ca2+ ATPase
sarco/endoplasmic reticulum Ca2+-ATPase
sarcoendoplasmic reticulum Ca2+ ATPase6
sarcoendoplasmic reticulum Ca2+-ATPase
sarcoplasmic reticulum ATPase
-
-
-
-
sarcoplasmic reticulum Ca2+-ATPase
sarcoplasmic reticulum calcium ATPase
sarcoplasmic reticulum calcium pump
sarcoplasmic reticulum calcium-dependent adenosine triphosphatase
-
sarcoplasmic/endoplasmic reticulum Ca2+-ATPase
secretory pathway Ca-ATPase
Secretory pathway Ca2+ transporting ATPase
-
-
-
-
SERCA
SERCA 1
SERCA pump
SERCA1
SERCA1a
SERCA2
SERCA2a
SERCA2b
SERCA3
SPCA1
SPCA2
SR Ca2+-ATPase
Vacuolar Ca2+-ATPase
-
-
-
-
additional information
ATPase 2C1
-
-
-
-
Ca2+ ATPase
-
-
-
-
Ca2+-pumping ATPase
-
-
-
-
Ca2+-transporting ATPase
-
-
-
-
P-type calcium ATPase
-
-
-
-
PMCA
-
-
PMCA1
-
-
-
-
PMCA2
-
-
-
-
PMCA3
-
-
-
-
PMCA4
-
-
-
-
sarco(endo)plasmic reticulum Ca2+-ATPase
-
-
-
-
SERCA
-
-
-
-
SERCA1
-
-
-
-
SERCA2
-
-
-
-
SERCA3
-
-
-
-
additional information
-
the enzyme belongs to the P2B subfamily of P-type ATPases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
phosphoenzyme intermediate formation
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
formation of a phosphorylated intermediate
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
formation of a phosphorylated intermediate
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
formation of a phosphorylated intermediate
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
Ca2+ and ATP bind to the enzyme by a random mechanism, study of relationship between the various conformations of the enzyme. The calcium binding increases the spatial separation between the P and N domains.
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
the enzyme is a Ca2+-dependent phosphoprotein intermediate
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
Ca2+ binding site structure and mechanism
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
isozyme SPCA2 shows Ca2+- and Mn2+-dependent phosphoprotein intermediate formation
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
kinetic mechanism of isozymes SPCA1 and SPCA2, phosphorylated intermediate, overview
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
reaction and kinetic mechanism, phosphorylated intermediate, detailed overview
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
transmembrane transport
hydrolysis of phosphoric ester
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, Ca2+-transporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria. The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolysed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolysed. In muscle cells Ca2+ is transported from the cytosol (side 1) into the sarcoplasmic reticulum (side 2).
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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 + Ca2+[side 1] + H+[side 2]
ADP + phosphate + Ca2+[side 2] + H+[side 1]
-
-
-
-
?
ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
the enzyme has a much lower affinity for Mn2+ than for Ca2+
-
-
?
CTP + H2O + Ca2+[side 1]
CDP + phosphate + Ca2+[side 2]
-
best substrate
-
-
?
GTP + H2O + Ca2+[side 1]
GDP + phosphate + Ca2+[side 2]
-
best substrate
-
-
?
ITP + H2O + Ca2+[side 1]
IDP + phosphate + Ca2+[side 2]
-
best substrate
-
-
?
UTP + H2O + Ca2+[side 1]
UDP + phosphate + Ca2+[side 2]
-
best substrate
-
-
?
ATP + H2O + 2 Ca2+[cytoplasm side]
ADP + phosphate + 2 Ca2+[lumen side]
-
-
-
?
ATP + H2O + 2 Ca2+[cytoplasm side]
ADP + phosphate + 2 Ca2+[lumen side]
-
-
-
-
?
ATP + H2O + 2 Ca2+[side 1]
ADP + phosphate + 2 Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
recombinant enzyme
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
Ca2+-dependent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
Homarus sp.
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
ATPase activity and Ca2+ transport activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
the enzyme is a plasma membrane calcium pump performing Ca2+-dependent ATPase and ATP-dependent Ca2+ transport reactions
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
the PMCA pump uses a molecule of ATP to transport one molecule of Ca2+ from the cytosol to the external environment
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
SERCA1 is responsible for ATPase activity and intermediate reactions, as well as ATP-dependent Ca2+ transport
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
analysis of Ca2+ binding at the two specific transmembrane sites using detergent- and ATP-free enzyme, yielding cooperative isotherms. Calcium occupancy of site I is required to trigger cooperative binding to site II and catalytic activation. Charge transfer and current transients measurements, overview
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
the PMCA pump uses a molecule of ATP to transport one molecule of Ca2+ from the cytosol to the external environment
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
the enzyme is the Ca2+ pump in sarcoplasmic reticulum membranes
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
the enzyme is the Ca2+ pump in sarcoplasmic reticulum membranes, the ATP hydrolysis energy is used for uphill transport and accumulation of Ca2+
-
-
r
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
assay with labeled ATP substrate
-
-
r
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
Ca2+ transport
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
the enzyme performs ATP-dependent Ca2+/H+ antiport and Ca2+-dependent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
sarcoplasmic reticulum Ca-ATPase transports calcium ions from the myoplasm to the reticulum lumen at the expense of ATP hydrolysis
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
the enzyme has one high affinity ATP binding site (catalytic site) and two calcium-binding sites
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
ATPase activity and Ca2+ uptake into artificial proteoliposomes activity
-
-
?
ATP + H2O + Ca2+/in
ADP + phosphate + Ca2+/out
-
plasma-membrane Ca2+-ATPase is a calcium pump that exports Ca2+ from the cytosol to the extracellular environment of eukaryotic cells and thus maintain overall Ca2+ homoeostasis and provide local control of intracellular Ca2+ signalling
-
-
?
ATP + H2O + Ca2+/out
?
-
responsible for Ca2+ uptake into the alveolar sac
-
-
?
ATP + H2O + Ca2+/out
?
-
responsible for Ca2+ uptake into the alveolar sac
-
-
?
ATP + H2O + Ca2+/out
?
-
high affinity (Ca2+-Mg2+)-ATPase is responsible for Ca2+ transport
-
-
?
ATP + H2O + Ca2+/out
?
-
filling of the Ca2+ pool in the endoplasmic reticulum
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
-
existence of two different conformations of chemically equivalent Ca2+-ATPase: E1, the high affinity state for Ca2+ and E2, the low affinity state for Ca2+
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
Plasmodium falciparum isolate K1
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
best substrate
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
-
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
-
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
-
ER-type Ca2+-ATPases show a strong preference for ATP as substrate. Conversely, auto-inhibited Ca2+-ATPases are able to use ITP or GTP as an alternative to ATP
-
-
?
additional information
?
-
the Arabidopsis thaliana endoplasmic reticulum-localized Ca2+-ATPase, ECA1, with homology to PMR1, can also transport Mn2+. Molecular determinants of the Mn2+ specificity of transport proteins
-
-
-
additional information
?
-
-
the enzyme is involved in calcium and maganese homeostasis
-
-
?
additional information
?
-
-
the P-type calcium ATPase is important for calcium/manganese homeostasis and oxidative stress response
-
-
?
additional information
?
-
the enzyme is a P-type Ca2+/Mn2+-ATPase involved in the secretory pathway
-
-
?
additional information
?
-
-
the enzyme is a P-type Ca2+/Mn2+-ATPase involved in the secretory pathway
-
-
?
additional information
?
-
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity, functional regulation by phospholamban
-
-
?
additional information
?
-
Homarus sp.
-
the enzyme is involved in the transepithelial Ca2+ flow in hepatopancreas of lobster acting as an ATP-driven Ca2+ pump in conjunction with a Na+/Ca2+ antiporter in the basolateral cell region, Ca2+ transport mechanism by endoplasmic reticular vesicles, overview
-
-
?
additional information
?
-
-
the Ca2+,Mn2+-ATPase SPCA2 is involved in the secretory pathway
-
-
?
additional information
?
-
-
the enzyme is important in the secretory pathway
-
-
?
additional information
?
-
the enzyme is important in the secretory pathway
-
-
?
additional information
?
-
-
dissection of the functional differences between secretory pathway Ca2+/Mn2+-ATPase isoenzymes SPCA 1 and 2
-
-
?
additional information
?
-
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
-
the activity of the plasma membrane Ca2+-pump decreases steeply throughout the 120 days lifespan of normal human red blood cells, the Ca2+ pump is a major regulator of Ca2+ homeostasis in all cells
-
-
?
additional information
?
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
-
the ATP-binding cleft is mainly located within the p29/30 domain with the phosphorylation site strategically located at the N-terminal border of this domain
-
-
?
additional information
?
-
interaction of Ca2+-ATPase with phospholamban is involved in regulation of heart contractility, overview
-
-
?
additional information
?
-
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
additional information
?
-
interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals, overview
-
-
?
additional information
?
-
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity, the detergent-solubilized enzyme shows monomeric catalytic function as deduced from kinetic modelling, while the native enzyme shows features of oligomeric protein conformational interactions that constrain the subunits to a staggered or out-of-phase mode of action
-
-
?
additional information
?
-
-
SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
-
-
?
additional information
?
-
SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
-
-
?
additional information
?
-
SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
-
-
?
additional information
?
-
-
the SERCA 1 Ca2+-ATPase in white muscle is able to work as ion pumps, but clearly also as heat pumps because of their large ATPase activity. This may explain why SERCA 1 type Ca2+-ATPases dominate in tissues where thermal regulation is important.
-
-
?
additional information
?
-
the SERCA 1 Ca2+-ATPase in white muscle is able to work as ion pumps, but clearly also as heat pumps because of their large ATPase activity. This may explain why SERCA 1 type Ca2+-ATPases dominate in tissues where thermal regulation is important.
-
-
?
additional information
?
-
the SERCA 1 Ca2+-ATPase in white muscle is able to work as ion pumps, but clearly also as heat pumps because of their large ATPase activity. This may explain why SERCA 1 type Ca2+-ATPases dominate in tissues where thermal regulation is important.
-
-
?
additional information
?
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
additional information
?
-
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
additional information
?
-
-
the enzyme plays a significant role in cellular Ca2+ homeostasis
-
-
?
additional information
?
-
-
the enzyme is responsible for the Ca2+ sequestering
-
-
?
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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 + Ca2+/in
ADP + phosphate + Ca2+/out
-
plasma-membrane Ca2+-ATPase is a calcium pump that exports Ca2+ from the cytosol to the extracellular environment of eukaryotic cells and thus maintain overall Ca2+ homoeostasis and provide local control of intracellular Ca2+ signalling
-
-
?
ATP + H2O + Ca2+[side 1] + H+[side 2]
ADP + phosphate + Ca2+[side 2] + H+[side 1]
-
-
-
-
?
ATP + H2O + 2 Ca2+[cytoplasm side]
ADP + phosphate + 2 Ca2+[lumen side]
-
-
-
?
ATP + H2O + 2 Ca2+[cytoplasm side]
ADP + phosphate + 2 Ca2+[lumen side]
-
-
-
-
?
ATP + H2O + 2 Ca2+[side 1]
ADP + phosphate + 2 Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
ATPase activity and Ca2+ transport activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
the enzyme is a plasma membrane calcium pump performing Ca2+-dependent ATPase and ATP-dependent Ca2+ transport reactions
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
SERCA1 is responsible for ATPase activity and intermediate reactions, as well as ATP-dependent Ca2+ transport
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
the enzyme is the Ca2+ pump in sarcoplasmic reticulum membranes
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
the enzyme is the Ca2+ pump in sarcoplasmic reticulum membranes, the ATP hydrolysis energy is used for uphill transport and accumulation of Ca2+
-
-
r
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
sarcoplasmic reticulum Ca-ATPase transports calcium ions from the myoplasm to the reticulum lumen at the expense of ATP hydrolysis
-
-
?
ATP + H2O + Ca2+/out
?
-
responsible for Ca2+ uptake into the alveolar sac
-
-
?
ATP + H2O + Ca2+/out
?
-
responsible for Ca2+ uptake into the alveolar sac
-
-
?
ATP + H2O + Ca2+/out
?
-
high affinity (Ca2+-Mg2+)-ATPase is responsible for Ca2+ transport
-
-
?
ATP + H2O + Ca2+/out
?
-
filling of the Ca2+ pool in the endoplasmic reticulum
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
Plasmodium falciparum isolate K1
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
best substrate
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
-
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
-
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
-
the enzyme is involved in calcium and maganese homeostasis
-
-
?
additional information
?
-
-
the P-type calcium ATPase is important for calcium/manganese homeostasis and oxidative stress response
-
-
?
additional information
?
-
the enzyme is a P-type Ca2+/Mn2+-ATPase involved in the secretory pathway
-
-
?
additional information
?
-
-
the enzyme is a P-type Ca2+/Mn2+-ATPase involved in the secretory pathway
-
-
?
additional information
?
-
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity, functional regulation by phospholamban
-
-
?
additional information
?
-
Homarus sp.
-
the enzyme is involved in the transepithelial Ca2+ flow in hepatopancreas of lobster acting as an ATP-driven Ca2+ pump in conjunction with a Na+/Ca2+ antiporter in the basolateral cell region, Ca2+ transport mechanism by endoplasmic reticular vesicles, overview
-
-
?
additional information
?
-
-
the Ca2+,Mn2+-ATPase SPCA2 is involved in the secretory pathway
-
-
?
additional information
?
-
-
the enzyme is important in the secretory pathway
-
-
?
additional information
?
-
the enzyme is important in the secretory pathway
-
-
?
additional information
?
-
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
-
the activity of the plasma membrane Ca2+-pump decreases steeply throughout the 120 days lifespan of normal human red blood cells, the Ca2+ pump is a major regulator of Ca2+ homeostasis in all cells
-
-
?
additional information
?
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
interaction of Ca2+-ATPase with phospholamban is involved in regulation of heart contractility, overview
-
-
?
additional information
?
-
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
additional information
?
-
-
SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
-
-
?
additional information
?
-
SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
-
-
?
additional information
?
-
SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
-
-
?
additional information
?
-
-
the SERCA 1 Ca2+-ATPase in white muscle is able to work as ion pumps, but clearly also as heat pumps because of their large ATPase activity. This may explain why SERCA 1 type Ca2+-ATPases dominate in tissues where thermal regulation is important.
-
-
?
additional information
?
-
the SERCA 1 Ca2+-ATPase in white muscle is able to work as ion pumps, but clearly also as heat pumps because of their large ATPase activity. This may explain why SERCA 1 type Ca2+-ATPases dominate in tissues where thermal regulation is important.
-
-
?
additional information
?
-
the SERCA 1 Ca2+-ATPase in white muscle is able to work as ion pumps, but clearly also as heat pumps because of their large ATPase activity. This may explain why SERCA 1 type Ca2+-ATPases dominate in tissues where thermal regulation is important.
-
-
?
additional information
?
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
additional information
?
-
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
additional information
?
-
-
the enzyme plays a significant role in cellular Ca2+ homeostasis
-
-
?
additional information
?
-
-
the enzyme is responsible for the Ca2+ sequestering
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
PMCA of neurons is electroneutral and exchanges 2 H+ for each Ca2+ or Ba2+ ion extruded
Ca2+
K+
Mg2+
Mn2+
Na+
-
when an outwardly directed Na+ gradient is imposed on the plasma membrane vesicles from the optic nerve, they accumulate Ca2+ in the absence of Mg2+ and/or ATP. Km for Na+ is 74 mM
Zn2+
-
ER-type Ca2+-ATPases can transport, beside Ca2+, also Mn2+ and Zn2+ ions
Ca2+
-
in the resting state, the plant plasma-membrane Ca2+-ATPase is autoinhibited by binding of its N-terminal tail to two major intracellular loops. Activation requires the binding of calcium-bound calmodulin to this tail and a conformational change that displaces the autoinhibitory tail from the catalytic domain
Ca2+
-
the enzyme is a P-type PMR1-like calcium ATPase, Ca2+ interacts with residues E386, N871, D875, and Q880, the latter alters ion selectivity of the enzyme
Ca2+
-
PMCA of neurons is electroneutral and exchanges 2 H+ for each Ca2+ or Ba2+ ion extruded
Ca2+
quantitative Ca2+ flux analysis of recombinant isozymes in COS-1 cells permeabilized by saponin
Ca2+
dependent on, at very low Ca2+ concentrations the PMCA is nearly inactive, unstimulated PMCA pumps have poor affinity for Ca2+
Ca2+
-
SERCA2a transfers Ca2+ from the cytosol of the cardiomyocyte to the lumen of the sarcoplasmic reticulum during muscle relaxation
Ca2+
-
calcium occupancy of site I is required to trigger cooperative binding to site II and catalytic activation
Ca2+
-
required, one calcium ion becomes occluded in the E1P-phosphorylated intermediate of the enzyme
Ca2+
-
dependent on, but at high Ca2+ concentrations no significant increase in enzyme activity is observed
Ca2+
dependent on, at very low Ca2+ concentrations the PMCA is nearly inactive, unstimulated PMCA pumps have poor affinity for Ca2+
Ca2+
-
PMCA extrudes Ca2+ but has little effect on excitation-contraction coupling, Pmca4b likely reduces the local Ca2+ signals involved in reactive cardiomyocyte hypertrophy via calcineurin regulation
Ca2+
-
SPCA1 mediates the accumulation of Ca2+ with high affinity into Golgi reservoirs
Ca2+
binding involves Glu309 which acts as a gating residue for cytoplasmic Ca2+ to reach the binding cavity, Ca2+ binding site structure and mechanism
Ca2+
binding structure and kinetics in the crystallized enzyme-phospholamban complex, overview
Ca2+
-
optimal at 0.008-0.01 mM, the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
Ca2+
SERCA1 has two high affinity transmembrane Ca2+-binding sites
Mg2+
-
competitive Mg2+ binding can occur at Ca2+ binding site I but not at site II
Mg2+
binding structure in the crystallized enzyme-phospholamban complex, overview
Mg2+
-
required, best at 0.09 mM in all muscle tissue, higher concentration are inhibitory
Mg2+
-
1 mM Mg2+ (a concentration equivalent to that of ATP) is an absolute requirement for ATPase activity
Mg2+
-
plasma membrane vesicles from the optic nerve accumulate Ca2+ in the presence of Mg2+
Mn2+
-
ER-type Ca2+-ATPases can transport, beside Ca2+, also Mn2+ and Zn2+ ions
Mn2+
-
SPCA1 mediates the accumulation Mn2+ with high affinity into Golgi reservoirs
Mn2+
Mn2+ induces accumulation of Pmr1 and Pmc1 mRNAs in a calcineurin/Prz1-dependent manner
Mn2+
LCA1 may also act as a Mn2+ pump, consistent with a possible role in secretory pathway divalent cation homeostasis
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(12S,12aR)-3-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(1R,9aR)-9-[2-[(4-fluorobenzyl)oxy]ethyl]-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepine
-
(1S,6R,9aS)-3,6-dimethyloctahydro-3,9a-epidioxy-2-benzoxepin-1(1H)-yl phenylacetate
-
(1S,9aR)-1-methoxy-3-methyl-9-[2-(phenylperoxy)ethyl]octahydro-3,9a-epidioxy-2-benzoxepine
-
(1S,9aR)-1-methoxy-3-methyl-9-[2-(prop-2-en-1-yloxy)ethyl]octahydro-3,9a-epidioxy-2-benzoxepine
-
(1S,9aR)-9-[2-(benzyloxy)ethyl]-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepine
-
(1S,9aS)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepine
-
(1S,9aS)-1-[2-(benzyloxy)ethyl]-1,3,9-trimethyloctahydro-3,9a-epidioxy-2-benzoxepine
-
(3R,5aS,6R,8aS,12aS)-11-benzyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3,6-dimethyl-11-(2-methylbutyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3,6-dimethyl-11-(2-phenylethyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3,6-dimethyl-11-(3-phenylpropyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3,6-dimethyl-11-(4-methylbenzyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3,6-dimethyl-11-pentyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3-butyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3-ethyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3-[3-(4-chlorophenyl)propyl]-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-6-methyl-3-(3-phenylpropyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-6-methyl-3-propyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,9R,12aR)-3,9-dibutyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,9R,12aR)-9-butyl-3-ethyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,9R,12aR)-9-butyl-3-[3-(4-chlorophenyl)propyl]-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,9R,12aR)-9-butyl-6-methyl-3-(4-phenylbutyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-ol
-
(3R,5aS,6R,8aS,9R,12S,12aR)-3,6,9-trimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,6R,9R,12R,12aR)-6,9-dimethyl-10-(2,2,2-trifluoroethyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-9-ol
-
(3R,6R,9S,12R,12aR)-10-ethoxy-6,9-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-9-ol
-
(3R,6R,9S,12R,12aR)-6,9-dimethyl-10-(2,2,2-trifluoroethyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-9-ol
-
(3R,6R,9S,12R,12aR)-6,9-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,10-diol
-
(3S,5aR,6S,8aR,9R,12S,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl N-[(2-methylpropoxy)carbonyl]-b-alaninate
-
(3S,5aS,6R,8aS,12aS)-6-methyl-3-(2-methylpropyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3S,5aS,6R,8aS,12aS)-6-methyl-3-(2-phenylethyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3S,5aS,6R,8aS,9R,12aR)-9-butyl-6-methyl-3-(2-phenylethyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3S,6R,12R,12aS)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(4-chlorophenyl)(pyridin-2-yl)[4-(pyrrolidin-1-ylmethyl)phenyl]methanol
-
(4-chlorophenyl)[4-([[3-(4-[3-[(7-chloroquinolin-4-yl)amino]propyl]piperazin-1-yl)propyl]amino]methyl)phenyl]methanone
-
(4aS)-3,3-diethylhexahydro-6H-[1,2,4]trioxino[6,5-j]isochromen-6-one
-
(4aS)-3,3-dimethylhexahydro-6H-[1,2,4]trioxino[6,5-j]isochromen-6-one
-
(5S,6R,9R,10S,12R,12aS)-10-ethoxy-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-5-ol
-
(6'R,12'S,12a'R)-3',6'-dimethyl-3',4',5',5a',6',7',8',8a'-octahydrospiro[cyclopent-3-ene-1,9'-[1,2,11,13]tetraoxa[3,12]epoxy[1,2]dioxepino[4,3-i]isochromen]-10'-one
-
(6'R,12'S,12a'R)-3',6'-dimethyloctahydrospiro[1,3-dioxolane-2,9'-[3,12]epoxy[1,2]dioxepino[4,3-i]isochromen]-10'-one
-
(6R,10R,12R,12aR)-3,6-dimethyl-9-methylidenedecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl hydroperoxide
-
(6R,10R,12R,12aR)-3,6-dimethyloctahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,2'-oxiran]-10-ol
-
(6R,10R,12R,12aR)-3,6-dimethyloctahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,2'-oxiran]-10-yl hydroperoxide
-
(6R,10S,12R,12aR)-3,6-dimethyl-9-methylidenedecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-ol
-
(6R,12aS)-11-(4-chlorobenzyl)-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12aS)-11-acetyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12aS)-11-benzyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12aS)-3,6-dimethyl-11-(2-phenylethyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12aS)-3,6-dimethyl-11-(3-phenylpropyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12aS)-3,6-dimethyl-11-(pyridin-2-ylmethyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12aS)-3,6-dimethyl-11-(thiophen-2-yl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12aS)-3,6-dimethyl-11-pentyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12R,12aR)-3,6-dimethyl-9-methylidenedecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl hydroperoxide
-
(6R,12R,12aS)-3-butyl-6-methyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,12R,12aS)-3-ethyl-6-methyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,12R,12aS)-3-[3-(4-chlorophenyl)propyl]-6-methyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,12R,12aS)-6-methyl-3-(2-methylpropyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,12R,12aS)-6-methyl-3-(4-phenylbutyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,12R,12aS)-6-methyl-3-propyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,12S,12aS)-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,12S,12aS)-3-ethyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,12S,12aS)-6-methyl-3-(4-phenylbutyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,12S,12aS)-6-methyl-3-propyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,8aR,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,8aR,9R,12aR)-3,6,9-trimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,8aR,9R,12S,12aR)-9-bromo-9-(bromomethyl)-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,8aS,9S,10R,12R,12aR)-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,10-diol
-
(6R,8aS,9Z,12S,12aR)-9-ethylidene-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12R,12aR)-10-(tert-butylperoxy)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-10-ethoxy-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-10-ethoxy-3,6-dimethyl-9-propyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-10-ethoxy-9-ethyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-10-methoxy-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-ol
-
(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-3,6-dimethyl-9-(3-phenylpropyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-3,6-dimethyl-9-pentyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-3,6-dimethyl-9-propyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-3,6-dimethyloctahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,2'-oxiran]-10-yl hydroperoxide
-
(6R,9R,12R,12aR)-9-butyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-9-ethyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12S,12aR)-3,6,9-trimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-3,4,4',5,5',5a,6,7,8,8a-decahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,3'-pyrazol]-10-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(2-methylpropyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(2-phenylethyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(3-phenylpropyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(4-phenylbutyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(prop-2-en-1-yl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(propan-2-yl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-pentyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-9-butyl-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-9-butyl-6-methyl-3-(4-phenylbutyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-9-ethyl-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-9-hexyl-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-9-[3-(4-chlorophenyl)propyl]-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9S,10R,12R,12aR)-3,6-dimethyloctahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,2'-oxiran]-10-yl hydroperoxide
-
(6R,9S,11aR)-3,6,9-trimethyloctahydro-3H-3,11-epoxyfuro[3,4-j][1,2]benzodioxepine
-
(6R,9S,12R,12aR)-9-bromo-3,6,9-trimethyl-N-phenyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-amine
-
(6R,9S,12R,12aR)-9-bromo-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9S,12S,12aR)-9-[(1E)-but-1-en-1-yl]-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9S,12S,12aR)-9-[(2E)-but-2-en-1-yl]-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6S,7S,10S,12aS)-10-ethoxy-7-fluoro-3,6,7-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6S,7S,10S,12R,12aS)-10-ethoxy-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-7-ol
-
(6S,9R,10S,12aS)-10-ethoxy-3,6,9-trimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-7(3H)-one
-
(6S,9R,10S,12aS)-10-ethoxy-7,7-difluoro-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(7R,12aR)-7,10-dimethyldodecahydro-2H-10,13-epoxy[1,2]dioxepino[4,3-i]pyrano[2,3-c]isochromene
-
(N-((3-chlorophenyl)(4-(pyrrolidin-1-yl)methyl)phenyl)methyl)-7-chloro-4-aminoquinoline
NF1058, inhibits the enzyme SERCA1 stabilizing an E2 state that can still be phosphorylated with phosphate
1,2-dichlorobenzene
-
at concentrations of 0.25-0.75 mM, 1,2-dichlorobenzene inhibits the ATP hydrolysis to about 80%. Starting at 0.05 mM, 1,2-dichlorobenzene is able to uncouple the ratio of hydrolysis/Ca2+transporte
1,3-dibromo-2,4,6-tri(methylisothiouronium)benzene
micromolar inhibitor of SERCA
1-[(4-chlorophenyl)(phenyl)[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-1H-1,2,4-triazole
-
1-[(4-chlorophenyl)(phenyl)[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-1H-imidazole
-
1-[(6R)-3,3,6-trimethyloctahydro-9aH-1,2-benzodioxepin-9a-yl]ethanone
-
2,5-di(tert-butyl)hydroquinone
micromolar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation
2-(dimethylamino)ethyl 4-(2-oxo-2-[[(3S,5aR,6S,8aR,9R,12S,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]ethyl)benzoate
-
2-(dimethylamino)ethyl 4-[([2-[(1S,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethyl]peroxy)methyl]benzoate
-
2-[(1R,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethyl diethylcarbamate
-
2-[(1R,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethyl diphenylcarbamate
-
2-[(1S,9aS)-1,3,9-trimethyloctahydro-3,9a-epidioxy-2-benzoxepin-1(1H)-yl]ethanol
-
2-[(1S,9aS)-1,3-dimethyloctahydro-3,9a-epidioxy-2-benzoxepin-1(1H)-yl]ethanol
-
2-[(1S,9aS)-3,9-dimethyloctahydro-3,9a-epidioxy-2-benzoxepin-1(1H)-yl]ethanol
-
3-[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]propan-1-ol
-
4,5-dimethyl-2-([[5-methyl-2-(propan-2-yl)phenoxy]acetyl]amino)thiophene-3-carboxamide
-
-
4-(2-[2-[(1S,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethoxy]ethyl)pyridine
-
4-([2-[(1R,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethoxy]methyl)pyrimidine
-
4-([[(3R,5aS,6R,8aS,9R,10S,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]methyl)benzoic acid
-
5-chloro-N-(3,5-dimethoxyphenyl)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-2-methoxybenzamide
-
-
6-amino-2-(hex-1-yn-1-yl)-9H-purin-9-yl-beta-D-N-ethylribofuranoic amide
-
-
6-[(3R,5aS,6R,8aS,12aS)-3,6-dimethyl-10-oxodecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-11(12H)-yl]hexanoic acid
-
aluminium fluoride
-
the inhibition by aluminium fluoride is dependend on Mg2+ concentration
amyloid beta-peptide
-
the addition of amyloid beta-peptide to normal brain decreases the PMCA activity resulting in the same Ca2+ dependency as that seen in Alzheimer's disease brain, whereas the addition of amyloid beta-peptide to Alzheimer's disease brain has no effect on PMCA activity, in the absence of cholesterol, the level of inhibition of cerebrum PMCA is 60%, but levels of inhibition decreases with increasing concentrations of cholesterol
-
beryllium fluoride
-
the inhibition by beryllium fluoride is dependend on Mg2+ concentration
bupivacaine
-
inhibition by bupivacaine is not competitive with respect to the specific transport and catalytic sites of the enzyme
eosin Y
-
auto-inhibited Ca2+-ATPases are particularly sensitive to inhibition by eosin Y
ethyl 3-[(3S,5aS,6R,8aS,12aS)-6-methyl-10-oxooctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propanoate
-
ethyl 3-[(3S,5aS,6R,8aS,9R,12aR)-9-butyl-6-methyl-10-oxooctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propanoate
-
ethyl 3-[(6R,12R,12aS)-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propanoate
-
ethyl 3-[(6R,12S,12aS)-6-methyl-10-oxooctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propanoate
-
ethyl 3-[(6R,9R,12S,12aR)-9-butyl-6-methyl-10-oxooctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propanoate
-
ethyl [[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]acetate
-
fluoroglycofen
-
i.e. O-[5-(2-chloro-alpha,alpha,alpha-trifluoro-of-toluene-oxy)-2-nitro-benzoyl]-hydroxyethyl, a high concentration of fluoroglycofen (37.5 g ai ha-1) decreases the enzyme activity in grape leaves
lidocaine
-
inhibition by lidocaine is not competitive with respect to the specific transport and catalytic sites of the enzyme
magnesium fluoride
-
the inhibition by magnesium fluoride is dependend on Mg2+ concentration
methyl 2-methyl-3-[[(3R,5aS,6R,8aS,9R,10R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]propanoate
-
methyl 2-methyl-3-[[(6R,9R,10R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]propanoate
-
methyl 2-methyl-3-[[(6R,9R,10S,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]propanoate
-
methyl 2-[[(6R,9R,10R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]propanoate
-
methyl 2-[[(6R,9R,10S,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]propanoate
-
methyl 3-[[(3R,5aS,6R,8aS,9R,10R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]butanoate
-
methyl 3-[[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]propanoate
-
methyl 4-(2-oxo-2-[[(3S,5aR,6S,8aR,9R,12S,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]ethyl)benzoate
-
methyl 4-([[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]methyl)benzoate
-
methyl 4-[[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]butanoate
-
N,N-dimethylalkylamine N-oxide
-
slight stimulation at low concentrations, inhibition at higher concentrations, maximal inhibition for the homologue with the alkyl chain length n=16
N-((3-chlorophenyl)(4-((4-(7-chloroquinolin-4-yl)piperazin-1-yl)methyl)phenyl)methyl)-7-chloro-4-aminoquinoline
NF1442
N-alkyl-N,N-dimethylamine-N-oxide
-
CnNO with n = 10-20, stimulate at low concentrations and inhibit at high concentrations dependent on the compound alkyl chain length, overview, inhibition occurs due to compound-induced lipid bilayer structure perturbation in the ATPase annular region
N-[(6R,9R,12R,12aR)-9-bromo-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]pyridin-2-amine
-
N-[(6R,9S,12R,12aR)-9-bromo-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]-1,3-thiazol-2-amine
-
N-[(6R,9S,12R,12aR)-9-bromo-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]pyridin-2-amine
-
palytoxin
-
the inhibition process exhibits the following characteristics: the degree of inhibition is dependent on membrane protein concentration, no protection is observed when the ATP concentration is raised, dependence on Ca2+ concentration with a decreased maximum catalytic rate, and it occurrs in the absence of Ca2+ ionophoric activity
peptide C28
-
peptide C28 is a peptide that prevents activation of PMCA by calmodulin
-
phosphatidylcholine
-
native PMCA from erythrocytes in mixed micelles of phosphatidylcholine-detergent has 30% of its maximal activity, while the recombinant PMCA enzyme is nearly inactive, increasing the phosphatidylcholine content of the micelles does not increase the activity of recombinant PMCA but the activity in the presence of phosphatidylcholine improves by partially removing the detergent
polysubstituted fullerene C60-II
-
noncompetitive and reversible inhibition, complete inhibition at 0.05 mM
-
polysubstituted fullerene C60-IV
-
76% inhibition of Ca2+ transport and 91% inhibition of ATP hydrolysis at 0.05 mM
-
polysubstituted fullerene C60-VI
-
63% inhibition of Ca2+ transport and 38% inhibition of ATP hydrolysis at 0.05 mM
-
polysubstituted fullerene C60-VII
-
60% inhibition of Ca2+ transport and 38% inhibition of ATP hydrolysis at 0.05 mM
-
polysubstituted fullerene C60-VIII
-
82% inhibition of Ca2+ transport and 67% inhibition of ATP hydrolysis at 0.05 mM
-
Sodium fluoride
-
the inhibition by magnesium fluoride is dependend on Mg2+ concentration. The enzyme is totally inhibited by NaF at total Mg2+ concentrations higher than 3.5 mM
tert-butyl [(1E)-1-([2-[(1S,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethyl]peroxy)ethylidene]carbamate
-
tetrabromobisphenol A
-
can inhibit SERCA at low concentrations (IC50, 0.0004-0.0012 mM)
[3-[(6R,9R,12S,12aR)-9-butyl-6-methyl-10-oxooctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propyl]phenylphosphinous chloride
-
2,5-di-tert-butyl-1,4-dihydroxybenzene
-
inhibitory effects on wild-type and mutant enzymes, overview
2,5-di-tert-butyl-1,4-dihydroxybenzene
stabilizes the enzyme structure in absence of Ca2+, binding site structure and binding mode involving Asp59 and Pro308, overview
amyloid beta-peptide 25-35
-
a maximum inhibition of 75% is observed with 0.0025 mM amyloid beta-peptide 25-35 for PMCA reconstituted in phosphatidylcholine.
-
amyloid beta-peptide 25-35
the activity of overexpressed PMCA4 in a microsomal fraction of the HEK-293 cells is inhibited by amyloid beta-peptide 25-35, a slight inhibition of the activity of PMCA3 is observed
-
artemisinin
Ca2+-ATPase and Golgi localized Pmr1p appears to be targets for artemisinin
Cd2+
-
enzyme activity shows a gradual decrease in post larvae on exposure to 0.12 and 0.24 ppm cadmium
cyclopiazonic acid
nanomalar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation
cyclopiazonic acid
highly sensitive to the specific inhibitor cyclopiazonic acid
erythrosin B
-
auto-inhibited Ca2+-ATPases are particularly sensitive to inhibition by erythrosin B
La3+
-
prevents the Mg2+-dependent transition E1P->E2P, acting noncompetitively with respect to Ca2+ and ATP
Mg2+
-
competitive Mg2+ binding can occur at Ca2+ binding site I but not at site II
Mg2+
-
required, best at 0.09 mM in all muscle tissue, higher concentration are inhibitory
Mg2+
-
Mg2+ at high concentration (10 mM) and high pH inhibits the ATPase by binding to low affinity sites made available by the high pH in the medium
orthovanadate
-
the Ca2+ pump is inhibited by orthovanadate (0.1 mM) once sufficient Ca2+ accumulation has occurred
phospholamban
-
complex formation with the recombinant SERCA2a in transfected insect cells, regulatory function, overiew
-
phospholamban
-
phospholamban inhibits SERCA2a activity in its dephosphorylated state
-
phospholamban
phospholamban inhibits the enzyme by reducing the Ca2+ affinity, phospholamban mutant I40A is highly inhibitory, increases the dissociation constant of the enzyme for Ca2+
-
thapsigargin
nanomalar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation
thapsigargin
only mildly sensitive to the ER-type pump inhibitor thapsigargin
vanadate
inhibits the phosphorylation reaction; inhibits the phosphorylation reaction
additional information
-
in the resting state, the plant plasma-membrane Ca2+-ATPase is autoinhibited by binding of its N-terminal tail to two major intracellular loops. Activation requires the binding of calcium-bound calmodulin to this tail and a conformational change that displaces the autoinhibitory tail from the catalytic domain
-
additional information
-
PMCA is insensitive to increases in membrane potential
-
additional information
-
the Na+/Ca2+ exchanger plays a minimal role in the cell Ca2+-fluxes
-
additional information
-
the enzyme has an autoinhibitory domain which is coupled to the ATP binding domain, oxidative modification alters the interaction and inhibits the enzyme, proteolysis pattern of inactive PMCAox by chymotrypsin, overview
-
additional information
the Ca2+ and Mn2+ transport of SPCA2 is insensitive to thapsigargin inhibition
-
additional information
-
the Ca2+ and Mn2+ transport of SPCA2 is insensitive to thapsigargin inhibition
-
additional information
-
SERCA protein expression is decreased by inhibition of cystic fibrosis transmembrane regulator function with the specific cystic fibrosis transmembrane regulator inhibitor CFTRinh172
-
additional information
-
the function of recombinant PMCA is highly sensitive to delipidation
-
additional information
-
glycation of a lysine residue near the catalytic site of the pump ATPase has a powerful inhibitory effect, in intact cells the Ca2+ pump is protected from glycation-induced inactivation
-
additional information
-
no inhibition of isoforms PMCA4 and PMCA2 is observed with the amyloid beta-peptide 25-35. The addition of 0.0025 mM amyloid beta-peptide 25-35 to Alzheimer's disease brain has no effect on PMCA activity. No effect of amyloid beta-peptides is seen on SERCA or SPCA activity in either control or Alzheimer's disease brains
-
additional information
-
PCA1 contains a N-terminal autoinhibitory domain
-
additional information
artemisinins have been widely used to treat both Plasmodium falciparum and Plasmodium vivax infections due to their high clinical efficacy (immediate onset and rapid parasite clearance) and minimal side effects. Moreover, artemisinins remain highly effective against malaria parasites that show resistance to other classes of antimalarial medicine. Combinations of artemisinin and other antimalarial drugs are utilized clinically to enhance effectiveness and minimize the development of artemisinin resistance in Plasmodium species. Despite this strategy, artemisinin-resistant Plasmodium isolates have emerged
-
additional information
-
artemisinins have been widely used to treat both Plasmodium falciparum and Plasmodium vivax infections due to their high clinical efficacy (immediate onset and rapid parasite clearance) and minimal side effects. Moreover, artemisinins remain highly effective against malaria parasites that show resistance to other classes of antimalarial medicine. Combinations of artemisinin and other antimalarial drugs are utilized clinically to enhance effectiveness and minimize the development of artemisinin resistance in Plasmodium species. Despite this strategy, artemisinin-resistant Plasmodium isolates have emerged
-
additional information
-
the Ca2+ transporting function of SERCA2a is decreased by about 18% 1 week, 1 month, and 3 months after myocardial infarction, while PMCA1, 2, and 4 mRNAs are unchanged in the ventricular muscle 3 months after myocardial infarction
-
additional information
-
PMCA is inhibited by acutely lowering extracellular proton concentration (pH raised to 9.0)
-
additional information
artemisinin resistance in pmr1DELTA cells is not caused by alteration in the localization or accumulation of the multidrug transporter Pdr5p as well as not by association between defects in calcium homeostasis or protein glycosylation and sensitivity to artemisinin
-
additional information
-
artemisinin resistance in pmr1DELTA cells is not caused by alteration in the localization or accumulation of the multidrug transporter Pdr5p as well as not by association between defects in calcium homeostasis or protein glycosylation and sensitivity to artemisinin
-
additional information
no inhibition of isoforms PMCA4 and PMCA2 is observed with the amyloid beta-peptide 25-35, 0.0025 mM amyloid beta-peptide 25-35 has no effect on the activity of PMCA purified from cerebellum
-
additional information
-
no inhibition of isoforms PMCA4 and PMCA2 is observed with the amyloid beta-peptide 25-35, 0.0025 mM amyloid beta-peptide 25-35 has no effect on the activity of PMCA purified from cerebellum
-
additional information
the enzyme is not significantly inhibited by oligomycin
-
additional information
the enzyme possesses an autoinhibitory domain at its C-terminal tail
-
additional information
-
the enzyme possesses an autoinhibitory domain at its C-terminal tail
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-dichlorobenzene
-
concentrations of 0.05-0.2 mM of 1,2-dichlorobenzene stimulate the hydrolytic activity of the enzyme in a medium-containing Ca2+-ionophore
Calcineurin
-
Pmr1p is positively controlled by the calmodulin and calcineurin complex in the presence of an elevated Ca2+ level
-
calcium-bound calmodulin
-
in the resting state, the plant plasma-membrane Ca2+-ATPase is autoinhibited by binding of its N-terminal tail to two major intracellular loops. Activation requires the binding of calcium-bound calmodulin to this tail and a conformational change that displaces the autoinhibitory tail from the catalytic domain
-
calmodulin-like 36
CML36 interacts directly with the regulative N terminus of the Arabidopsis plasma membrane Ca2+-ATPase isoform 8 which stimulates the enzyme activity
-
G-actin
-
when purified enzyme is incubated with increasing concentrations of G-actin, an increase in the rate of ATP hydrolysis is observed
-
HSP70
-
chaperone system can bind to enzyme and, depending on the severity of heat stress, protect the enzyme's function by stabilizing the nucleotide binding domain
-
N,N-dimethylalkylamine N-oxide
-
slight stimulation at low concentrations, inhibition at higher concentrations
N-alkyl-N,N-dimethylamine-N-oxide
-
CnNO with n = 10-20, stimulate at low concentrations and inhibit at high concentrations dependent on the compound alkyl chain length, overview
phosphatidylinositol 4-monophosphate
-
433% stimulation of activity at 1 mM
valinomycin
-
the rate of Ca2+ uptake is stimulated by a inside-negative potential induced in the presence of valinomycin
Calmodulin
0.001 mM calmodulin stimulates the activity of wild type enzyme by about 300%
Calmodulin
the fully auto-inhibited enzyme has a very low basal Ca2+-ATPase activity which is stimulated more than 5fold by calmodulin
Calmodulin
-
calmodulin depletion results in the transition of the Ca2+-pumping ATPase to a low Ca2+-affinity form
Calmodulin
-
activates, single-molecule characterization of the dynamics of calmodulin bound to oxidatively modified PMCA, overview
Calmodulin
-
the amino acid sequence of the calmodulin binding site is L1086RRGQILWFRGLNRIQTQIKVVKAFHSS1113, i.e. peptide 28, determination of essential residues for binding, overview, complex structure modelling, calmodulin binding mechanism, overview
Calmodulin
-
calmodulin stimulates Ca2+ pumping in the plasma-membrane Ca2+-ATPase by binding to an autoinhibitory domain, which then dissociates from the catalytic domain of PMCA to allow full activation of the enzyme. Although the purified PMCA exhibits a significant basal Ca2+-dependent ATPase activity, the addition of calmodulin fluorescently labeled with tetramethylrhodamine (120 nM) at a saturating Ca2+ concentration (0.1 mM) results in significant activation of PMCA. The enzyme is fully activated at 0.025 mM calmodulin.
Calmodulin
-
Pmr1p is positively controlled by the calmodulin and calcineurin complex in the presence of an elevated Ca2+ level
Calmodulin
2fold increase of activity in the presence of 200 nM calmodulin
calpain
cleavage of PMCA by calpain activates it irreversibly
-
phosphatidylinositol bisphosphate
the most active in stimulating PMCA activity
phosphatidylinositol bisphosphate
the most active in stimulating PMCA activity
phosphatidylserine
-
can replace calmodulin in shifting the enzyme to the high-affinity form
additional information
-
PMCA isoform ACA8 activity is hardly affected by phosphatidylcholine or phosphatidylethanolamine
-
additional information
-
2-chloro-(epsilon-amino-Lys75)-[6-(4-[N,N-diethylamino]phenyl)-1,3,5-triazin]-4-yl-calmodulin-labeled calmodulin is used for determination of enzyme amino acids essential for binding, peptide mapping with full-length bindng site peptide 28 and truncated versions, overview, complex structure modelling, calmodulin binding mechanism, overview
-
additional information
-
isoform SERCA3f mRNA is up-regulated in failing hearts
-
additional information
-
native and recombinant enzymes achieve maximal activity when supplemented with acidic phospholipids
-
additional information
-
calcium occupancy of site I is required to trigger cooperative binding to site II and catalytic activation
-
additional information
cold acclimation induces an increase in the expression and activity of SERCA1, cold tolerance is probably related to increased muscle oxidative metabolism and heat production by SERCA1
-
additional information
-
cold acclimation induces an increase in the expression and activity of SERCA1, cold tolerance is probably related to increased muscle oxidative metabolism and heat production by SERCA1
-
additional information
-
PCA1 mRNA levels are up-regulated by dehydration, NaCl, and abscisic acid
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0005
Ca2+
-
phosphatidylserine environment with or without calmodulin, enzyme from erythrocytes
0.02
Ca2+
-
phosphatidylcholine environment with or without calmodulin, enzyme from erythrocytes
0.0013
Ca2+/cis
-
SERCA from undifferentiated or differentiated PC-12 cells
0.00018
Ca2+[side 1]
in the presence of 0.008 mg/ml calmodulin, at pH 7.2 and 37°C
0.00035
Ca2+[side 1]
in the absence of calmodulin, at pH 7.2 and 37°C
additional information
additional information
-
ATPase and phosphorylation kinetics, kinetics of activation by Ca2+, and binding and transport of Ca2+
-
additional information
additional information
ATPase and phosphorylation kinetics, kinetics of activation by Ca2+, and binding and transport of Ca2+
-
additional information
additional information
-
ATPase and phosphorylation kinetics, kinetics of isozymes of activation by Ca2+, and binding and transport of Ca2+
-
additional information
additional information
ATPase and phosphorylation kinetics, kinetics of isozymes of activation by Ca2+, and binding and transport of Ca2+
-
additional information
additional information
-
binding kinetics of calmodulin and labeled calmodulin to enzyme binding site-derived peptides, overview
-
additional information
additional information
-
detailed de-/phosphorylation reaction kinetics, kinetic modelling
-
additional information
additional information
-
isoenzymes SPCA 1 and 2, steady-state and transient kinetic analyses of Ca2+ transport and of phosphorylation and dephosphorylation reactions, overview
-
additional information
additional information
-
kinetics of Ca2+ uptake and efflux, overview
-
additional information
additional information
-
charge transfer and current transients measurements, kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
90
Ca2+
-
isoform 3c in presence of a saturing Ca2+ at pH 7.0, in presence of ionophore
95
Ca2+
-
in presence of 0.1 mM Ca2+ at pH optimum 7.23, in presence of ionophore
98
Ca2+
-
isoform 3a in presence of a saturing Ca2+ concentration at pH 7.0, in presence of ionophore
100
Ca2+
-
isoform 3b in presence of a saturing Ca2+ at pH 7.0, in presence of ionophore
128
Ca2+
-
in presence of a saturing Ca2+ at pH 7.0, in presence of ionophore
132
Ca2+
-
isoform 3a in presence of 0.1 mM Ca2+ at pH optimum 7.72, in presence of ionophore
134
Ca2+
-
isoform 3c in presence of 0.1 mM Ca2+ at pH optimum 7.78, in presence of ionophore
149
Ca2+
-
isoform 3b in presence of 0.1 mM Ca2+ at pH optimum 7.74, in presence of ionophore
additional information
additional information
Ca2+ binding transition rate
-
additional information
additional information
-
Ca2+ binding transition rates of isozymes, overview
-
additional information
additional information
Ca2+ binding transition rates of isozymes, overview
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0023
polysubstituted fullerene C60-II
-
pH and temperature not specified in the publication
-
0.000023
thapsigargin
-
pH 7.2, 37°C, enzyme from medial pterygoid muscles
additional information
additional information
-
Ki of thapsigargin in inhibition of Ca2+ uptake, overview
-
additional information
additional information
-
inhibitory potencies of narcotic substances on Ca2+-ATPase activity in masticatory muscles, masseter and medial pterygoid, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
(2Z)-2-cyano-3-(3,4-dihydroxyphenyl)prop-2-enethioamide
Plasmodium falciparum
-
at pH 7.5 and 25°C
0.152
(4-chlorophenyl)(pyridin-2-yl)[4-(pyrrolidin-1-ylmethyl)phenyl]methanol
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.022 - 0.029
(4-chlorophenyl)[4-([[3-(4-[3-[(7-chloroquinolin-4-yl)amino]propyl]piperazin-1-yl)propyl]amino]methyl)phenyl]methanone
0.0013
(N-((3-chlorophenyl)(4-(pyrrolidin-1-yl)methyl)phenyl)methyl)-7-chloro-4-aminoquinoline
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.015
1,1'-methanediyldinaphthalen-2-ol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0273
1-(naphthalen-1-ylmethyl)naphthalen-2-ol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.032
1-[(4-chlorophenyl)(phenyl)[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-1H-1,2,4-triazole
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.057
1-[(4-chlorophenyl)(phenyl)[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-1H-imidazole
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.0213
2,2',2''-methanetriyltris(4-tert-butylphenol)
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0118
2,2'-methanediylbis(4-tert-butylphenol)
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.001
2,3-bis[(2-hydroxyethyl)sulfanyl]naphthalene-1,4-dione
Plasmodium falciparum
-
at pH 7.5 and 25°C
0.0338
2,4-di-tert-butyl-6-(1-phenylethyl)phenol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0353
2,4-di-tert-butyl-6-[1-(4-methoxyphenyl)ethyl]phenol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0188
2,5-bis(2-methylpropyl)phenol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0094
2,5-bis(cyclopenta-2,4-dien-1-ylmethyl)benzene-1,4-diol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0454
2,6-di-tert-butyl-4-[1-(4-methoxyphenyl)ethyl]phenol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0202
2-(cyclopenta-2,4-dien-1-ylmethyl)benzene-1,4-diol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0115
2-cyclooctylbenzene-1,4-diol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0031
2-[(cyclopropylcarbonyl)amino]-4,5-dimethylthiophene-3-carboxamide
Plasmodium falciparum
-
at pH 7.5 and 25°C
0.0497
3-(1,1-diphenylethyl)cyclopentanol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0393
4,4'-butane-2,2-diylbis(2-methylphenol)
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0283
4,4'-butane-2,3-diyldiphenol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0195
4,4'-propane-2,2-diylbis(2,6-dimethylphenol)
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0238
4,5-dibenzylbenzene-1,2-diol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0011
4,5-dimethyl-2-([[5-methyl-2-(propan-2-yl)phenoxy]acetyl]amino)thiophene-3-carboxamide
Plasmodium falciparum
-
at pH 7.5 and 25°C
0.0172
4-(7-methyloctyl)phenol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.003
5-chloro-N-(3,5-dimethoxyphenyl)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-2-methoxybenzamide
Plasmodium falciparum
-
at pH 7.5 and 25°C
0.0085
6-amino-2-(hex-1-yn-1-yl)-9H-purin-9-yl-beta-D-N-ethylribofuranoic amide
Plasmodium falciparum
-
at pH 7.5 and 25°C
0.0281
6-tert-butyl-2,3-dihydro-1H-inden-5-ol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.00229
biphenyl-2,5-diol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.04
bis(maltolato)oxovanadium(IV)
Oryctolagus cuniculus
-
in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25°C
0.325
bis(N-hydroxylamidoiminodiacetato)vanadium(IV)
Oryctolagus cuniculus
-
in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25°C
35
clotrimazole
Oryctolagus cuniculus
IC50 about 0.035 mM, in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.0008
N-((3-chlorophenyl)(4-((4-(7-chloroquinolin-4-yl)piperazin-1-yl)methyl)phenyl)methyl)-7-chloro-4-aminoquinoline
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.0004
palytoxin
Oryctolagus cuniculus
-
in 20 mM MOPS, pH 7.0, 80 mM KC1, 5 mM MgCl2, 0.5 mM EGTA, 0.55 mM CaC12, at 25°C
0.025
pyridine-2,6-dicarboxylatodioxovanadium
Oryctolagus cuniculus
-
in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25°C
0.022
(4-chlorophenyl)[4-([[3-(4-[3-[(7-chloroquinolin-4-yl)amino]propyl]piperazin-1-yl)propyl]amino]methyl)phenyl]methanone
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.029
(4-chlorophenyl)[4-([[3-(4-[3-[(7-chloroquinolin-4-yl)amino]propyl]piperazin-1-yl)propyl]amino]methyl)phenyl]methanone
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.15
chlorpromazine
Homo sapiens
-
native enzyme in the presence of 0.002 mg/ml calmodulin, at pH 7.2 and 25°C
0.00016
cyclopiazonic acid
Solanum lycopersicum
in 1 mM EGTA, 130 mM NaCl, 3 mM MgCl2, at 37°C
0.000635
thapsigargin
Solanum lycopersicum
recombinant enzyme expressed in Saccharomyces cerevisiae strain HI227, in 1 mM EGTA, 130 mM NaCl, 3 mM MgCl2, at 37°C
0.00095
thapsigargin
Solanum lycopersicum
recombinant enzyme expressed in Saccharomyces cerevisiae strain K616, in 1 mM EGTA, 130 mM NaCl, 3 mM MgCl2, at 37°C
0.08
vanadate
Oryctolagus cuniculus
-
in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0241
recombinant wild type enzyme, in the presence of Ca2+, pH not specified in the publication, at 25°C
0.1181
recombinant wild type enzyme, in the presence of Ca2+ and 0.001 mM calmodulin, pH not specified in the publication, at 25°C
additional information
additional information
-
activity during purification and after solubilization/reconstitution with different detergents, overview
additional information
-
Ca2+ uptake and efflux activity of recombinant enzyme in membrane vesicles of transfected insect cells
additional information
-
Ca2+ ionophore A23187 effect, Ca2+ transport rate isozymes, overview
additional information
Ca2+ ionophore A23187 effect, Ca2+ transport rate isozymes, overview
additional information
-
Ca2+ ionophore A23187 effect, Ca2+ transport rate, overview
additional information
Ca2+ ionophore A23187 effect, Ca2+ transport rate, overview
additional information
-
determination of enzyme activity distribution in different muscle types, overview
additional information
-
determination of enzyme activity in a coupled assay method using linked pyruvate kinase/lactate dehydrogenase
additional information
-
Ca2+ uptake activity into artificial proteoliposomes, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
the effect of pH on enzyme activity is determined using 50 mM Tris-HCl buffer in the range of pH 5-10, a peak is is found between pH 7.5 to 8.0
6 - 8
-
pH 6.0: 43% of maximal activity, pH 8.0: 20% of maximal activity
6 - 8.5
-
isozyme SPCA2, about 20% of maximal activity at pH 6.0, and about 60% at pH 8.5, isozyme SPCA1d, about 35% of maximal activity at pH 6.0, and about 60% at pH 8.5
additional information
additional information
-
different types of proton participation in E1 to E2 transition and in calcium binding
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
Pigeon
-
30°C: about 20% of maximal activity, 55°C: about 55% of maximal activity, 60°C: about 5% of maximal activity
additional information
-
temperature dependence of the Ca2+ transport at different pH values, overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
696391, 697160, 697167, 697168, 697858, 698973, 700358, 701104, 719962, 733067, 733277, 733466, 734224, 734517, 735113, 748570, 749980, 750486, 750998, 751534, 751700, 752192
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression and activity during molting cycle, overview
brenda
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primary, isozyme SPCA2 shows a highly punctate distribution
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isoform PMCA 4 is more abundant in the cerebrum than in the cerebellum
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additional information
PMCA1 is ubiquitous, but is expressed most abundantly in brain, lung and intestine
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PMCA1 is ubiquitous, but is expressed most abundantly in brain, lung and intestine. The PMCA3 and PMCA4 pumps are expressed in brain, the PMCA2 pump is a brain isoform.
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expression and activity during molting cycle, overview
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PMCA2 is highly expressed in cerebellar Purkinje cells
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PMCA2 is highly expressed in cerebellar Purkinje cells
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isoform PMCA 2 is more abundant in the cerebellum than in the cerebrum
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expression and activity during molting cycle, overview
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PMCA2 is expressed at a lower level in the heart
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methods to employ tissue homogenates to study sarcoplasmatic reticulum Ca2+ transport function in individual mouse hearts
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the PMCA4 pump is expressed in heart, PMCA2 is expressed at a lower level in the heart
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PMCA2 is highly expressed in the hair cells of the inner ear
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PMCA2 is highly expressed in the hair cells of the inner ear
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PMCA1 is ubiquitous, but is expressed most abundantly in brain, lung and intestine
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PMCA1 is ubiquitous, but is expressed most abundantly in brain, lung and intestine. The PMCA4 pump is expressed in intestine.
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expression and activity during molting cycle, overview
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PMCA1 is ubiquitous, but is expressed most abundantly in brain, lung and intestine
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PMCA1 is ubiquitous, but is expressed most abundantly in brain, lung and intestine
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the brain isoform PMCA2 pump is also expressed in the lactating mammary glands
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SPCA2 is expressed predominately in luminal epithelial cells of the mouse mammary gland during lactation with noexpression in cells outside the acini, SPCA1 is found in all cell types of the tissue section including myoepithelial and stromal cells, PMCA2 expression appears confined to the alveolus, whereas non-acinar cells do not express PMCA2, PMCA1 is ubiquitously expressed in the mammary gland sections with expression outside the acini
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the brain isoform PMCA2 pump is also expressed in the lactating mammary glands
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strongest expression of isoform PMCA1 in the prelactating mammary gland
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isoform SERCA1b is only expressed in prematured infant leg and arm muscles. It is replaced by isoform SERCA1a in more matured neonatal muscles and is completely absent in human foetal and neonatal diaphragm. Only isoform SERCA1a and not SERCA1is detected in muscles of 7-12 years old boys with Duchenne. In adult patients with myotonic dystrophy type 2 the SERCA1b isoform dominates over SERCA1a
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masticatory, fast, masseter, and pterygoid muscles, determination of enzyme activity distribution in different muscle types, overview
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axial abdominal muscle, expression and activity during molting cycle, overview
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SPCA1 localizes in the initial part of primary dendritic trunk in main cortical, hippocampal and cerebellar neurons from the earliest postnatal stages
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the PMCA3 and PMCA4 pumps are expressed in skeletal muscles
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the PMCA3 pump is expressed in skeletal muscles
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the PMCA3 and PMCA4 pumps are expressed in skeletal muscles
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210474, 210475, 210478, 210484, 210490, 210493, 210496, 670493, 695859, 695863, 698270, 698857, 698885, 733861, 750181
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PMCA4 is the most abundant isoform in smooth muscles
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PMCA4 is the most abundant isoform in smooth muscles
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PMCA4 is expressed at particularly high levels in the testis (more than 90% of PMCA protein expressed there is isoform 4)
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PMCA4 is expressed at particularly high levels in the testis (more than 90% of PMCA protein expressed there is isoform 4)
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additional information
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isozyme SPCA1 is ubiquitously expressed, while SPCA2 is limited to some tissues
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additional information
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isozyme SPCA1 shows a less limited tissue distribution than isozyme SPCA2
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additional information
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PMCA1 and PMCA4 isoforms are distributed ubiquitously, PMCA2 and 3 are found mainly in excitable cell types
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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SERCA2a transfers Ca2+ from the cytosol of the cardiomyocyte to the lumen of the sarcoplasmic reticulum during muscle relaxation
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the main part of activity of total membrane vesicles results from the enzyme of the Golgi
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the enzyme is intracellular in epidermal keratinocytes
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the enzyme is intracellular in epidermal keratinocytes
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in membranes isolated from sporulating bacteria but not from vegetative cells, the expression of enzyme is dependent on the sporulating time
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methods using bile salt detergents to reconstitute the purified Ca-ATPase into a variety of phospholipid bilayers and compare their ATP hydrolytic and Ca2+ pumping properties in these phospholipid membranes
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a microsomal fraction enriched in the transverse tubular system (T-tubule)/sarcoplasmic reticulum, SR, complex is prepared
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696391, 697160, 697168, 697858, 698973, 701104, 719962, 733067, 733277, 733466, 734224, 735113, 748570, 749980, 750998, 752192
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isoform SERCA3f is observed in close vicinity of plasma membrane
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P2B type pumps are expressed at the plasma membrane
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the enzyme is enriched in plasma membranes of the intestinal epithelium
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the enzyme is enriched in plasma membranes of the intestinal epithelium
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SERCA2a transfers Ca2+ from the cytosol of the cardiomyocyte to the lumen of the sarcoplasmic reticulum during muscle relaxation
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210474, 210475, 210490, 210496, 210498, 654747, 656229, 667604, 667995, 669646, 670493, 670793, 695859, 697684
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
Saccharomyces cerevisiae enzyme Pmr1p is a functional homologue of Plasmodium falciparum enzyme PfATP6
evolution
Saccharomyces cerevisiae enzyme Pmr1p is a functional homologue of Plasmodium falciparum enzyme PfATP6. Pmr1p is a key transporter for uptake of Ca2+ into the Golgi, which is important for maintaining the Ca2+ homeostasis of yeast cells
evolution
Plasmodium falciparum Thailand
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Saccharomyces cerevisiae enzyme Pmr1p is a functional homologue of Plasmodium falciparum enzyme PfATP6
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evolution
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Saccharomyces cerevisiae enzyme Pmr1p is a functional homologue of Plasmodium falciparum enzyme PfATP6. Pmr1p is a key transporter for uptake of Ca2+ into the Golgi, which is important for maintaining the Ca2+ homeostasis of yeast cells
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evolution
Plasmodium falciparum isolate K1
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Saccharomyces cerevisiae enzyme Pmr1p is a functional homologue of Plasmodium falciparum enzyme PfATP6
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malfunction
-
knock-out mutants of isoform ACA9 displays reduced growth of pollen tubes, with high frequency of aborted fertilization leading to a 3fold reduction in seed set. Knock-out mutants of isoforms ACA8 or ACA10 do not have an altered phenotype, with a noticeable exception: knock-out of ACA10 in a genotype containing a naturally occurring dominant allele of an unlinked gene causes altered adult vegetative development and the formation of floral clusters. Isoform ECA1 knock-out mutant is indistinguishable from the wild type, but it clearly shows reduced root growth and toxicity symptoms when exposed to 0.5 mM Mn2+. An ECA3 knock-out mutant is not more sensitive than the wild type to Mn2+ toxicity, but rather requires higher Mn2+ concentrations for growth. Both isoform ECA1 and ECA3 knock-out mutants have slightly altered Ca2+ sensitivity
malfunction
-
after injection of thapsigargin to block enzyme activity, silkworms show a silk-spinning deficiency (30% of silkworms cannot spin normally and another 25% constructes abnormal cocoons) and their cocoons have higher calcium content compared to that of controls
malfunction
-
age-associated loss in PMCA activity results in part from changes in the lipid environment of this Ca2+ transporter
malfunction
-
gene disruption causes severe defects in glycosylation of the endoplasmic reticulum (ER)-localized protein Cdc101 and secretory acid phosphatase, and a decrease in expression of SEC61 which encodes an important ER protein. Moreover, the enzyme deletion mutant shows increased sensitivity to cell wall stresses, abnormal cell wall composition, delayed cell wall reconstruction and decreased flocculation and adherence
malfunction
-
isoform PMCA2 or PMCA3 knock-down delays Ca2+ clearance and partially attenuates cellular acidification during KCl-stimulated Ca2+ influx
malfunction
-
plasma membrane Ca2+-ATPase 1 deficiency increases susceptibility to atrial tachyarrhythmia in Langendorff-perfused hearts under stress conditions. Enzyme deficiency produces instabilities in membrane potentials and Ca2+ handling in atrial myocytes
malfunction
-
enzyme function is not altered in muscle of patients with myotonic dystrophy and with hypothyroid myopathy
malfunction
-
silencing of isoform PMCA2 reduces MDA-MB-231 breast cancer cell proliferation, whereas silencing of the related isoforms PMCA1 and PMCA4 has no effect. PMCA2 silencing also sensitizes MDA-MB-231 cells to doxorubicin
malfunction
a T-DNA knockout of ECA1, grown on high-Mn media, displays a strong stress phenotype when compared to wild-type plants. This phenotype includes a significant reduction in fresh weight, dramatic leaf chlorosis, a significant inhibition of leaf expansion and root elongation, and a loss of root hair tip growth. The Arabidopsis IAA-leucine resistant 2 (ilr2) mutant has a slight tolerance to Mn stress. Transport characterization of microsomal membrane vesicles from ilr2 plants demonstrated a significant increase in ATP-dependent Mn2+ transport compared to wild-type plants. ILR2 might act as a regulator of Mn2+ transport, possibly acting on Mn2+ efflux from the cell mediated by either an ATPase or an ABC transporter
malfunction
cells lacking Pmr1p are less susceptible to growth inhibition from artemisinin and its derivatives. No association between sensitivity to artemisinin and altered trafficking of the drug efflux pump Pdr5p, calcium homeostasis, or protein glycosylation is found in pmr1DELTA yeast mutant. Basal ROS levels are elevated in pmr1D yeast and artemisinin exposure does not enhance ROS accumulation. Yeast deleted for PMR1 are known to accumulate excess manganese ions that can function as ROS-scavenging molecules. Loss-of-function mutations in Pmr1p in yeast cells are protective against artemisinin toxicity due to reduced intracellular oxidative damage, artemisinin resistance in pmr1DELTA cells. The loss of function in Pmr1p results in reduced artemisinin sensitivity due to insufficient ROS being generated to cause significant cellular damage
malfunction
loss-of-function mutations in PfATP6 in Plasmodium falciparum cells are protective against artemisinin toxicity due to reduced intracellular oxidative damage. The loss of function in PfATP6 results in reduced artemisinin sensitivity due to insufficient ROS being generated to cause significant cellular damage
malfunction
the pmr1 knockout (DELTApmr1) cells exhibit hypersensitivity to EGTA. The EGTA-hypersensitive phenotype of DELTApmr1 leads to the identification of pdt1+ gene, which encodes an Nramp-related metal transporter. The DELTApmr1 cells show round cell morphology. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
malfunction
Plasmodium falciparum Thailand
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loss-of-function mutations in PfATP6 in Plasmodium falciparum cells are protective against artemisinin toxicity due to reduced intracellular oxidative damage. The loss of function in PfATP6 results in reduced artemisinin sensitivity due to insufficient ROS being generated to cause significant cellular damage
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malfunction
-
the pmr1 knockout (DELTApmr1) cells exhibit hypersensitivity to EGTA. The EGTA-hypersensitive phenotype of DELTApmr1 leads to the identification of pdt1+ gene, which encodes an Nramp-related metal transporter. The DELTApmr1 cells show round cell morphology. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
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malfunction
-
cells lacking Pmr1p are less susceptible to growth inhibition from artemisinin and its derivatives. No association between sensitivity to artemisinin and altered trafficking of the drug efflux pump Pdr5p, calcium homeostasis, or protein glycosylation is found in pmr1DELTA yeast mutant. Basal ROS levels are elevated in pmr1D yeast and artemisinin exposure does not enhance ROS accumulation. Yeast deleted for PMR1 are known to accumulate excess manganese ions that can function as ROS-scavenging molecules. Loss-of-function mutations in Pmr1p in yeast cells are protective against artemisinin toxicity due to reduced intracellular oxidative damage, artemisinin resistance in pmr1DELTA cells. The loss of function in Pmr1p results in reduced artemisinin sensitivity due to insufficient ROS being generated to cause significant cellular damage
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malfunction
Plasmodium falciparum isolate K1
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loss-of-function mutations in PfATP6 in Plasmodium falciparum cells are protective against artemisinin toxicity due to reduced intracellular oxidative damage. The loss of function in PfATP6 results in reduced artemisinin sensitivity due to insufficient ROS being generated to cause significant cellular damage
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metabolism
-
Ca2+ removal by the enzyme influences the propensity for stimulus-evoked Ca2+-induced Ca2+ release by adjusting the amount of Ca2+ available for mitochondrial Ca2+ uptake
metabolism
several transporter gene families have been implicated in Mn2+ transport, including cation/H+ antiporters, natural resistance-associated macrophage protein (Nramp) transporters, zinc-regulated transporter/iron-regulated transporter (ZRT/IRT1)-related protein (ZIP) transporters, the cation diffusion facilitator (CDF) transporter family, and P-type ATPases
metabolism
several transporter gene families have been implicated in Mn2+ transport, including cation/H+ antiporters, natural resistance-associated macrophage protein (Nramp) transporters, zinc-regulated transporter/iron-regulated transporter (ZRT/IRT1)-related protein (ZIP) transporters, the cation diffusion facilitator (CDF) transporter family, and P-type ATPases
metabolism
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several transporter gene families have been implicated in Mn2+ transport, including cation/H+ antiporters, natural resistance-associated macrophage protein (Nramp) transporters, zinc-regulated transporter/iron-regulated transporter (ZRT/IRT1)-related protein (ZIP) transporters, the cation diffusion facilitator (CDF) transporter family, and P-type ATPases
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physiological function
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plasma-membrane Ca2+-ATPases, PMCAs, are high-affinity calcium pumps that expel Ca2+ from eukaryotic cells to maintain overall Ca2+ homoeostasis and to provide local control of intracellular Ca2+ signalling. They are of major physiological importance, with different isoforms being essential, for example, for presynaptic and postsynaptic Ca2+ regulation in neurons, feedback signalling in the heart and sperm motility
physiological function
-
sarcoplasmic reticulum Ca-ATPase is a membrane-bound protein which transports calcium ions from the myoplasm to the reticulum lumen at the expense of ATP hydrolysis, leading to muscle relaxation
physiological function
-
both endomembrane P2A and P2B Ca2+-ATPases play significant roles in adaptive responses to oxidative stress by removing excessive Ca2+ from the cytosol. Plasma membrane P2B type pumps play no major role in removing excess Ca2+ from the cytosol under oxidative stress conditions
physiological function
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Ca2+-ATPases use the energy of ATP hydrolysis to pump Ca2+ from the cytoplasm into intracellular compartments or into the apoplast. Ca2+-ATPases play an important role in maintenance of cytoplasmic Ca2+ homeostasis. Isoform ECA3 may also play an essential role in Mn2+ nutrition. Plasma membrane-localized auto-inhibited Ca2+-ATPases are also involved in the response to pathogens, hormonal regulation, salt stress, and cold stress
physiological function
enzyme overexpression decreases [Ca2+] in the cytosol, the endoplasmic reticulum (ER), and the mitochondria and activates the inositol-requiring transmembrane kinase and endonuclease 1alpha-spliced X-box binding protein 1 but inhibits the PRKR-like ER kinase-eIF2alpha and the activation of transcription factor 6-immunoglobulin heavy chain binding protein pathways of the ER-unfolded protein response. Isoform PMCA2 overexpression depletes cytosolic, ER and mitochondrial Ca2+ stores and induces apoptosis via the mitochondrial pathway. PMCA2-overexpressing cells also display increased levels of caspase-3 cleavage
physiological function
isoform SERCA2b plays an important role in dysregulated glucose and lipid homeostasis in the liver of obese mice. Overexpression of isoform SERCA2b in the liver of obese mice significantly reduces the lipogenic gene expression and the triglyceride content in the liver and reduces steatohepatitis. Increasing the levels of isoform SERCA2b greatly reduces endoplasmic reticulum stress in the liver, increases glucose tolerance, and establishes euglycemia in severely obese and diabetic mice. Isoform SERCA2b can increase endoplasmic reticulum folding capacity
physiological function
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isoforms PMCA2 and PMCA3 are mainly responsible for transport of protons to the intracellular milieu and the regulation of cellular pH
physiological function
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sarcoplasmic reticulum Ca2+ ATPase pump is a major regulator of glucose transport in the healthy and diabetic heart. Cardiac-specific enzyme expression increases active cell-surface GLUT4 and glucose uptake in the myocardium, as well as whole body glucose tolerance. The enzyme regulates cardiac GLUT4 translocation
physiological function
the combination of the functional attributes of both PMCA4 variants leads to heightened efficiency of the pump in the maintenance of Ca2+ homeostasis, which is crucial for normal motility and male fertility
physiological function
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the enzyme has a key function in calcium transportation in anterior silk gland that is related to maintaining a suitable ionic environment. This ionic environment with a proper Ca2+ concentration is crucial for the formation of silk fibers with favorable mechanical performances
physiological function
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the enzyme is responsible for intracellular Ca2+ homeostasis. Enzyme uncoupling of Ca2+ transport from ATP hydrolysis by sarcolipin increases heat production implicating sarcolipin-enzyme interaction in muscle thermogenesis
physiological function
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the enzyme plays key roles in maintenance of cellular Ca2+ homeostasis, morphogenesis and virulence and is essential for endoplasmic reticulum (ER) functions and consequent cell wall integrity implicating a role of ER Ca2+ homeostasis in Candida albicans physiology
physiological function
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the limited ability of isoform PMCA2 to extrude the Ca2+ load through mechanotransducer channels may constitute a major cause of cochlear outer hair cell vulnerability and high-frequency hearing loss
physiological function
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luteolin enhances sarcoplasmic reticulum Ca2+-ATPase activity to improve systolic/diastolic function during ischemia/reperfusion in rat hearts and cardiomyocytes by attenuating the inhibitive effects of the p38 pathway on phospholamban
physiological function
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plasma membrane Ca2+-ATPase 1 is required for maintaining atrial Ca2+ homeostasis and electrophysiological stability in mouse atria under stress conditions
physiological function
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plasma membrane Ca2+-ATPase 2 regulates breast cancer cell proliferation and sensitivity to doxorubicin
physiological function
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the enzyme contributes to the migration of lymphoid chemokine CCL21-activated dendritic cells as an important feature of the adaptive immune response
physiological function
the enzyme maintains Ca2+ homeostasis in molting glands/Y-organs of Callinectes sapidus
physiological function
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the enzyme mediates sperm chemotaxis towards sperm-activating and attracting factor
physiological function
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the enzyme removes excess Ca2+ from the cytosol and maintains intracellular Ca homeostasis essential for the living cell
physiological function
artemisinins are widely used to treat Plasmodium infections due to their high clinical efficacy. Possible role of the Ca2+/Mn2+ P-type ATPase Pmr1p on artemisinin toxicity through an induction of intracellular oxidative stress
physiological function
artemisinins are widely used to treat Plasmodium infections due to their high clinical efficacy. Possible role of the Ca2+/Mn2+ P-type ATPase Pmr1p on artemisinin toxicity through an induction of intracellular oxidative stress. Wild-type cells exhibit a significant increase in ROS production following treatment with artemisinin. Enzyme Pmr1p may play a role in ROS generation or accumulation from artemisinin
physiological function
ECA1 is originally identified as Ca2+ transporter, but has subsequently been shown to also transport Mn2+. AtECA1 is an endoplasmic reticulum (ER) Ca2+- and Mn2+-transporting P-type ATPase (see also EC 7.2.2.22). Manganese (Mn) is an essential nutrient in plants. It is of particular importance in photosynthetic organisms where a cluster of Mn atoms is required as the catalytic centre for light-induced water oxidation in photosystem II, and is required as a cofactor for a variety of enzymes, such as the Mn2+-dependent superoxide dismutase (MnSOD). Mn can be particularly toxic to plant growth and a variety of mechanisms exist to overcome such toxicity, including the conversion of the metal to a metabolically inactive compound, such as a Mn2+-chelate complex, or sequestration of the Mn2+ ion or a Mn2+-chelate complex into an internal compartment such as the vacuole. At the cellular level, Mn2+ accumulates predominantly in the vacuole and to some extent in chloroplasts, and can be associated with the cell wall fraction. Mn2+ has a critical role in the water oxidation step of photosynthesis, and the chloroplast is the second-largest sink for Mn2+ in the cell
physiological function
enzymes Pmr1 and Pdt1 cooperatively regulate cell morphogenesis through the control of Mn2+ homeostasis, and calcineurin functions as a Mn2+ sensor as well as a Mn2+ homeostasis regulator. The pmr1+ gene has strong genetic interactions with pdt1+ gene that encodes the Nramp-related divalent metal transporte. Pmr1 is regulated by the Ca2+/calcineurin/Prz1 pathway
physiological function
PMR1 is a Golgi Ca2+- and Mn2+-transporting P-type ATPase (see also EC 7.2.2.22). Manganese (Mn) is an essential nutrient in plants. It is of particular importance in photosynthetic organisms where a cluster of Mn atoms is required as the catalytic centre for light-induced water oxidation in photosystem II, and is required as a cofactor for a variety of enzymes, such as the Mn2+-dependent superoxide dismutase (MnSOD). Mn can be particularly toxic to plant growth and a variety of mechanisms exist to overcome such toxicity, including the conversion of the metal to a metabolically inactive compound, such as a Mn2+-chelate complex, or sequestration of the Mn2+ ion or a Mn2+-chelate complex into an internal compartment such as the vacuole. At the cellular level, Mn2+ accumulates predominantly in the vacuole and to some extent in chloroplasts, and can be associated with the cell wall fraction
physiological function
Plasmodium falciparum Thailand
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artemisinins are widely used to treat Plasmodium infections due to their high clinical efficacy. Possible role of the Ca2+/Mn2+ P-type ATPase Pmr1p on artemisinin toxicity through an induction of intracellular oxidative stress
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physiological function
Ciona intestinalis KH.C8.156
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the enzyme mediates sperm chemotaxis towards sperm-activating and attracting factor
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physiological function
-
enzymes Pmr1 and Pdt1 cooperatively regulate cell morphogenesis through the control of Mn2+ homeostasis, and calcineurin functions as a Mn2+ sensor as well as a Mn2+ homeostasis regulator. The pmr1+ gene has strong genetic interactions with pdt1+ gene that encodes the Nramp-related divalent metal transporte. Pmr1 is regulated by the Ca2+/calcineurin/Prz1 pathway
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physiological function
-
artemisinins are widely used to treat Plasmodium infections due to their high clinical efficacy. Possible role of the Ca2+/Mn2+ P-type ATPase Pmr1p on artemisinin toxicity through an induction of intracellular oxidative stress. Wild-type cells exhibit a significant increase in ROS production following treatment with artemisinin. Enzyme Pmr1p may play a role in ROS generation or accumulation from artemisinin
-
physiological function
-
PMR1 is a Golgi Ca2+- and Mn2+-transporting P-type ATPase (see also EC 7.2.2.22). Manganese (Mn) is an essential nutrient in plants. It is of particular importance in photosynthetic organisms where a cluster of Mn atoms is required as the catalytic centre for light-induced water oxidation in photosystem II, and is required as a cofactor for a variety of enzymes, such as the Mn2+-dependent superoxide dismutase (MnSOD). Mn can be particularly toxic to plant growth and a variety of mechanisms exist to overcome such toxicity, including the conversion of the metal to a metabolically inactive compound, such as a Mn2+-chelate complex, or sequestration of the Mn2+ ion or a Mn2+-chelate complex into an internal compartment such as the vacuole. At the cellular level, Mn2+ accumulates predominantly in the vacuole and to some extent in chloroplasts, and can be associated with the cell wall fraction
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physiological function
Plasmodium falciparum isolate K1
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artemisinins are widely used to treat Plasmodium infections due to their high clinical efficacy. Possible role of the Ca2+/Mn2+ P-type ATPase Pmr1p on artemisinin toxicity through an induction of intracellular oxidative stress
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additional information
a subfamily of P-type ATPases, the P1B-ATPases, catalyse transition metal efflux in many organisms including plants, and are predicted to transport either Zn2+/Cd2+/Pb2+/Co2+ or Cu2+/Ag2+, but there is no evidence that Mn2+ is a substrate for P1B-ATPases from any organism
additional information
a subfamily of P-type ATPases, the P1B-ATPases, catalyse transition metal efflux in many organisms including plants, and are predicted to transport either Zn2+/Cd2+/Pb2+/Co2+ or Cu2+/Ag2+, but there is no evidence that Mn2+ is a substrate for P1B-ATPases from any organism
additional information
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a subfamily of P-type ATPases, the P1B-ATPases, catalyse transition metal efflux in many organisms including plants, and are predicted to transport either Zn2+/Cd2+/Pb2+/Co2+ or Cu2+/Ag2+, but there is no evidence that Mn2+ is a substrate for P1B-ATPases from any organism
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Show AA Sequence and Transmembrane Helices (32778 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
103000
110000
115000
138000
72000
138000
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x * 138000, enzyme may exist in both the monomeric and dimeric enzyme form, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
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x * 138000, enzyme may exist in both the monomeric and dimeric enzyme form, SDS-PAGE
additional information
-
the enzyme contains P-type ATPase subdomains such as the phosphatase region, the phosphorylation site, the FITC labeling site, and the ATP binding site
additional information
-
enzyme structure and conformational transition upon Ca2+ binding or release
additional information
interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals, overview
additional information
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the detergent-solubilized enzyme shows monomeric catalytic function as deduced from kinetic modelling, while the native enzyme shows features of oligomeric protein conformational interactions that constrain the subunits to a staggered or out-of-phase mode of action
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nitrosylation
phosphoprotein
proteolytic modification
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chymotrypsin has a cleavage site in the autoinhibitory domain of the native 138 kDa enzyme resultng in a 125 kDa protein, proteolysis pattern of inactive PMCAox by chymotrypsin
phosphoprotein
PMCA can be phosphorylated both at serine/threonine and at tyrosine residues, the phosphorylation increases both the Vmax and the Ca2+ affinity of the pump
phosphoprotein
PMCA can be phosphorylated both at serine/threonine and at tyrosine residues, the phosphorylation increases both the Vmax and the Ca2+ affinity of the pump
phosphoprotein
upon binding to the Ca2E1 state, ATP phosphorylates the enzyme, and by binding to other conformational states in a non-phosphorylating modulatory mode ATP stimulates the dephosphorylation and other partial reaction steps of the cycle, thereby ensuring a high rate of Ca2+ transport under physiological conditions
phosphoprotein
-
enzyme activity is blunted by protein phosphorylation and enhanced by dephosphorylation. In muscle, incubations promoting protein kinase A or protein kinase G activity reduces enzyme activity in extracts from normoxic turtles by 65% and 83%, respectively, to levels more typical of anoxia-treated animals
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant complex between calmodulin and the regulatory domain of the plasma-membrane Ca2+-ATPase ACA8, mixing of 0.0006 ml of protein solution, containing 16 mg/ml protein in 25 mM Tris, pH 7.0, 50 mM NaCl, 10 mM 2-mercaptoethanol, 5 mM CaCl2, with 0.001 ml reservoir solution, containing 2.0 M ammonium sulfate, 0.1 M CAPS, pH 10.5, 0.2 M lithium sulfate, at final pH 8.2, ar 20°C, X-ray diffraction structure determination and analysis at 3.0 A resolution
-
hanging drop vapor diffusion method, using 220 mM sodium acetate, 4% (v/v) tert-butanol, 5 mM 2-mercaptoethanol, 15% (v/v) glycerol, and 6-7% (w/v) PEG 6000
hanging drop vapor diffusion method, using 220 mM sodium acetate, 4% (v/v) tert-butanol, 5 mM 2-mercaptoethanol, 15% (v/v) glycerol, and 6-7% (w/v) PEG 6000
-
purified enzyme in 0.02 mM octaethyleneglycol mono-N-dodecylether and 1 mM Ca2+, mixed with 0.03 mM thapsigargin, 0.12 mM 2,5-di-tert-butyl-1,4-dihydroxybenzene, and 3 mM EGTA, dialysis against a buffer consisting of 2.75 M glycerol, 4% PEG 400, 3 mM MgCl2, 0.04 mM 2,5-di-tert-butyl-1,4-dihydroxybenzene, 2.5 mM NaN3, 0.002 mg/ml butylhydroxytoluene, 0.2 mM DTT, 1 mM EGTA, and 20 mM MES, pH 6.1, 1 month, X-ray diffraction structure determination and analysis at 2.4-2.5 A resolution, molecular replacement and structure modelling
purified enzyme in complex with purified recombinant phospholamban, from 20 mM imidazole, pH 7.4, 100 mM KCl, 35 mM MgCl2, 0.5 mM EGTA, 0.25 mM Na3VO4, 0.03 mM thapsigargin, three freeze-thaw cycles using liquid nitrogen and thawing in hand, reconstitution at 4°C for several days to 1 week, analysis of interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals, overview
purified enzyme is crystallized preserving natural and essential lipids, high resolution crystal structure determination and analysis, crystallization method optimization
purified recombinant enzyme, hanging drop vapour diffusion method, 12 mg/ml protein in a solution containing 10 mM Ca2+, 1 mm beta,gamma-methyleneadenosine 5'-triphosphate, and 1,2-dioleoyl-sn-glycero-3-phosphocholine, 0.002 ml is mixed with 0.002 ml well solution containing 0.2 M sodium acetate, 10-14% w/v PEG 6000, 10% glycerol, and 4% tert-butanol, crystals grow within 1 to 14 days at 19°C, X-ray diffraction structure determination and analysis at 3.3 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A56S
-
the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
R123I
site-directed mutagenesis, when Arg123 of ShMTP1 is mutated to Ile, the ability to confer Mn tolerance to either yeast or Arabidopsis is completely lost
R59A
-
the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
S19D
the mutant with 163% of wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus
S22D
the mutant with wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus
S27D
the mutant with 89% of wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus
S57D
the mutant with 120% of wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus. The mutant shows 10fold higher affinity towards calmodulin compared to the wild type enzyme
S99D
the mutant with 77% of wild type activity shows half of the wild type affinity towards calmodulin
Y62A
-
the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
E309Q
-
the mutation of Ca2+-binding site II leads to non-cooperative binding of only one Ca2+, and loss of ATPase activation, catalytically inactive mutant
E771Q
-
the mutation of Ca2+-binding site I leads to no Ca2+ binding to either site, catalytically inactive mutant
F1110A
-
2-chloro-(epsilon-amino-Lys75)-[6-(4-[N,N-diethylamino]phenyl)-1,3,5-triazin]-4-yl-calmodulin-labeled calmodulin is used for determination of enzyme amino acids essential for binding, peptide mapping with full-length binding site peptide 28 and truncated and mutated versions, overview
L321F
-
Darier disease causing mutant, the mutant has the dramatically reduced sensitivity to the feedback inhibition by the accumulated lumenal Ca2+, the insensitivity to luminal Ca2+ raises this ion to an abnormally elevated level, 100% activity in comparison to wild-type enzyme
R268Q
-
the mutation in isoform PMCA4 is likely causative for autosomal dominant familial spastic paraplegia
V1107A
-
2-chloro-(epsilon-amino-Lys75)-[6-(4-[N,N-diethylamino]phenyl)-1,3,5-triazin]-4-yl-calmodulin-labeled calmodulin is used for determination of enzyme amino acids essential for binding, peptide mapping with full-length binding site peptide 28 and truncated and mutated versions, overview
D203R
the mutant shows an about 5fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
D203R/R678D
the mutant shows an about 3.5fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
D813A/D818A
-
the mutant displays a very low activity in presence of detergent, but the same maximal velocity and apparent affinity for Ca2+ as the wild-type enzyme in absence of detergent, the mutation affects pronotation-dependent winding and unwinding events in the nearby M6 transmembrane segment
E439A
the mutant shows an about 15fold basal dephosphorylation rate constant compared to the wild type enzyme
E439S
the mutant shows an about 10fold basal dephosphorylation rate constant compared to the wild type enzyme
E90A
the mutant shows a reduction of the apparent affinity for luminal Ca2+ and exhibits 19% of wild type activity
E90L
the mutant shows a reduction of the apparent affinity for luminal Ca2+ and exhibits less than 10% of wild type activity
E90R
the mutation allows E2P formation from phosphate even at luminal Ca2+ concentrations much too small to support phosphorylation in wild type. The mutant with less than 10% of wild type activity further displays a blocked dephosphorylation of E2P and an increased rate of conversion of the ADP-sensitive E1P phosphoenzyme intermediate to ADP-insensitive E2P as well as insensitivity of the E2-BeF3-complex to luminal Ca2+
I188A
-
displays about 30% reduced ATP turnover rate relative to wild type, whereas the ATP turnover rate is reduced by about 80%
I188F
-
the molecular rate of Ca2+-activated ATP hydrolysis at 37°C with 5 mM MgATP is slightly lower (by less than 15%) than that of wild type enzyme, the mutant displays reduced MgATP affinity
K204A
-
the mutant displays around 40% Ca2+ transport, compared with its about 70% rate of ATP turnover relative to the wild type enzyme
K205A
-
the molecular rate of Ca2+-activated ATP hydrolysis at 37°C with 5 mM MgATP slightly lower than that of wild type enzyme
K205E
-
the molecular rate of Ca2+-activated ATP hydrolysis at 37°C with 5 mM MgATP is slightly lower (by less than 15%) than that of wild type enzyme, the mutant displays reduced MgATP affinity
K234A
-
the mutant shows reduced relative Ca2+ ATPase activiy compared to the wild type enzyme
K234G
-
the mutant shows reduced relative Ca2+ ATPase activiy compared to the wild type enzyme
Q202A
th mutation causes reduced Ca2+ transport and ATPase activity
Q202A/D203A
the mutant shows an about 4fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
R174A
-
the molecular rate of Ca2+-activated ATP hydrolysis at 37°C with 5 mM MgATP is similar to, or slightly lower than (by less than 15%) that of wild type enzyme, the mutant displays wild type-like MgATP affinity
R678A
the mutant shows a reduced basal dephosphorylation rate constant compared to the wild type enzyme
R678D
the mutant shows an about 6fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
R678Q
the mutant shows an about 1.4fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
S186A
the mutant shows an about 6fold increased basal dephosphorylation rate constant compared to the wild type enzyme
S186E
the mutant shows an about 1,2fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
S186E/E439S
the mutant restores the basal dephosphorylation rate to a level about 2fold faster than that of the wild type. Little stimulation of the dephosphorylation by ATPis seen in this mutant
S186P
the mutant shows an about 18fold increased basal dephosphorylation rate constant compared to the wild type enzyme
S72R
the mutation allows E2P formation from phosphate even at luminal Ca2+ concentrations much too small to support phosphorylation in wild type. The mutant with less than 10% of wild type activity further displays a blocked dephosphorylation of E2P and an increased rate of conversion of the ADP-sensitive E1P phosphoenzyme intermediate to ADP-insensitive E2P as well as insensitivity of the E2-BeF3-complex to luminal Ca2+
S766C
the mutation of isoform SERCA1a strongly reduces the apparent Ca2+ affinity and ATPase activity of the enzyme
S766L
the mutation of isoform SERCA1a strongly reduces the apparent Ca2+ affinity and ATPase activity of the enzyme
S766V
the mutation of isoform SERCA1a strongly reduces the apparent Ca2+ affinity and ATPase activity of the enzyme
D100A
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
D136A
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
D100A
-
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
-
D136A
-
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
-
additional information
additional information
-
the N-deleted mutant DELTA74-ACA8 is also activated by acidic phospholipids
additional information
recombinant ECA1 shows ability to confer tolerance to toxic concentrations of Mn when heterologously expressed in a Mn-sensitive mutant yeast strain. The Arabidopsis IAA-leucine resistant 2 (ilr2) mutant has a slight tolerance to Mn stress. Transport characterization of microsomal membrane vesicles from ilr2 plants demonstrates a significant increase in ATP-dependent Mn2+ transport compared to wild-type plants
additional information
-
construction of a pmr1 knockout mutant, which shows high sensitivity to Mn2+ and EGTA, but also resistance to oxidative stress and suppression of highly reactive oxygen species sensitivity od smf3 RNA-mediated interference and daf16 worms, overview
additional information
disruption of gene PMR1 homologue CaPMR1 leads to inhibition of many Golgi-located, Mn2+-dependent mannosyltransferases, the Capmr1DELTA null mutant is viable in vitro and without phenotype on media supplemented with Ca2+ and Mn2+, but loose viability on minimal medium with low Ca2+/Mn2+ concentrations and enter in stationary phase, growth and glycosylation defects, overview
additional information
-
disruption of gene PMR1 homologue CaPMR1 leads to inhibition of many Golgi-located, Mn2+-dependent mannosyltransferases, the Capmr1DELTA null mutant is viable in vitro and without phenotype on media supplemented with Ca2+ and Mn2+, but loose viability on minimal medium with low Ca2+/Mn2+ concentrations and enter in stationary phase, growth and glycosylation defects, overview
additional information
-
2-chloro-(epsilon-amino-Lys75)-[6-(4-[N,N-diethylamino]phenyl)-1,3,5-triazin]-4-yl-calmodulin-labeled calmodulin is used for determination of enzyme amino acids essential for binding, peptide mapping with full-length binding site peptide 28 and truncated and mutated versions, overview
additional information
-
construction of a pmr1 null mutant, the mutant strain exhibits growth defects in media with added EGTA, the defect is reversible by addition of Ca2+ or Mn2+, the latter with less effect
additional information
a splice variant PMCA4b-Asp mutant exhibits 10% of the Ca2+ efflux activity of wild type isoform PMCA4
additional information
-
the deletion of either Glu243 or Gln244 results in a decrease in the relative Ca2+-ATPase activity, 1G and 3G inserts at site 2 have severe consequences consistent with the lack of measurable Ca2+ transport
additional information
-
DELTAPCA1 mutants fail to restore resting Ca2+ levels after salt stress treatments
additional information
Plasmodium falciparum mutant PfATP6DELTA phenotype, overview
additional information
-
Plasmodium falciparum mutant PfATP6DELTA phenotype, overview
additional information
Plasmodium falciparum isolate K1
-
Plasmodium falciparum mutant PfATP6DELTA phenotype, overview
-
additional information
Plasmodium falciparum Thailand
-
Plasmodium falciparum mutant PfATP6DELTA phenotype, overview
-
additional information
-
the yeast strain K610, which has the pmr1DELTA mutation, has the highest sensitivity to CdCl2 at a final concentration of 0.02 mM
additional information
construction of a pmr1 knockout (DELTApmr1) cells exhibiting hypersensitivity to EGTA. Overexpression of pdt1+ gene suppresses the EGTA-sensitive growth defects of DELTApmr1 cells. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
additional information
-
construction of a pmr1 knockout (DELTApmr1) cells exhibiting hypersensitivity to EGTA. Overexpression of pdt1+ gene suppresses the EGTA-sensitive growth defects of DELTApmr1 cells. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
additional information
Saccharomyces cerevisiae strain BY4742 cells lacking Pmr1p are less susceptible to growth inhibition from artemisinin and its derivatives. No association between sensitivity to artemisinin and altered trafficking of the drug efflux pump Pdr5p, calcium homeostasis, or protein glycosylation is found in pmr1DELTA yeast mutant. Basal ROS levels are elevated in pmr1DELTA yeast and artemisinin exposure does not enhance ROS accumulation. Yeast mutant pmr1DELTA phenotype, overview
additional information
-
Saccharomyces cerevisiae strain BY4742 cells lacking Pmr1p are less susceptible to growth inhibition from artemisinin and its derivatives. No association between sensitivity to artemisinin and altered trafficking of the drug efflux pump Pdr5p, calcium homeostasis, or protein glycosylation is found in pmr1DELTA yeast mutant. Basal ROS levels are elevated in pmr1DELTA yeast and artemisinin exposure does not enhance ROS accumulation. Yeast mutant pmr1DELTA phenotype, overview
additional information
-
construction of a pmr1 knockout (DELTApmr1) cells exhibiting hypersensitivity to EGTA. Overexpression of pdt1+ gene suppresses the EGTA-sensitive growth defects of DELTApmr1 cells. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
-
additional information
-
Saccharomyces cerevisiae strain BY4742 cells lacking Pmr1p are less susceptible to growth inhibition from artemisinin and its derivatives. No association between sensitivity to artemisinin and altered trafficking of the drug efflux pump Pdr5p, calcium homeostasis, or protein glycosylation is found in pmr1DELTA yeast mutant. Basal ROS levels are elevated in pmr1DELTA yeast and artemisinin exposure does not enhance ROS accumulation. Yeast mutant pmr1DELTA phenotype, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
the enzyme is almost inactivated (about 25% residual activity) by pH 5.5 acid treatment for 2 h at 0°C. The activity is reduced to about 80% at pH 6.0-6.5 for 2 h at 0°C
750573
6.6 - 8
-
anoxic muscle SERCA is relatively stable between pH 6.6 and pH 8.0
720121
7 - 7.4
-
normoxic enzyme shows broad peak of activity greater than anoxic muscle enzyme activity between pH 7.0 and 7.4, but normoxic enzyme activity sharply declines on either side of that range, and is less than that of anoxic muscle enzyme at low pH (6.6-6.8)
720121
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
the enzyme is half inactivated when heated at 45°C for 4 min and completely inactivated when heated at 45°C for 15 min
additional information
-
the maximal activity is reduced progressively with increasing temperature and time of incubation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
denaturation by acid treatment is strongly suppressed by the addition of 2 mM ATP. ATP also shows a strong suppressive effect against denaturation of the enzyme by freezing and heating
-
the less active enzyme in anoxic turtles features greater stability than the enzyme from normoxic animals. SERCA in liver from anoxic animals is more stable after urea treatment/thermolysin-mediated proteolysis than the normoxic counterpart
-
treatment with a variety of proteases, including elastase, proteinase K, and endoproteinase Asp-N and Hlu-C, results in accumulation of soluble fragments starting close to the ATPase phosphorylation site Asp351 and ending in the Lys605-Arg615 region. These fragments retain the ability to bind nucleoties, although with reduced affinity compared with the intact enzyme
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxidative moculation of the enzyme leads to loss of activity due to alterations of the coupling between the ATP binding domain and the autoinhibitory domain, proteolysis pattern of PMCAox by chymotrypsin, overview
-
667623
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, the activity of LCA1 prepared from yeast cells stored at -80°C is dramatically reduced when compared to LCA1 prepared from freshly harvested cells
4°C, purified enzyme in the detergent-solubilized form, several days, rapid loss of activity
-
4°C, purified enzyme in the reconstituted form, several days, little loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
calmodulin-Sepharose column chromatography
glutathione affinity column chromatography
native enzyme from pulmonary artery smooth muscle microsomes using different detergents, best is 1,2-diheptanoyl-sn-phosphatidylcholine in a ratio of protein to detergent of 1,5:1, which preserves the native structure, conformational transition, and function of the enzyme, mechanism, overview, solubilization is followed by adsorption chromatography and gel filtration
-
native enzyme from sekeletal muscle sarcoplasmic reticulum membranes by adsorption chromatography
nickel-NTA-agarose column chromatography and glutathione-Sepharose column chromatography
partially recombinant isozymes SPCA1 and SPCA2 in HEK293 cell microsomal membranes by differential centrifugation
-
partially, preparation of sarcoplasmic reticulum membrane vesicles
-
recombinant biotinylated SERCA1a 92fold from Saccharomyces cerevisiae light membrane fraction by avidin affinity chromatography, cleavage of the biotin tag by thrombin, and gel filtration
-
recombinant biotinylated SERCA1a from Saccharomyces cerevisiae cells by solubilization with dodecylmaltoside, avidin affinity chromatography and gel filtration, to homogeneity, the biotin tag is cleaved off by thrombin
recombinant His6-tagged ACA8 residues 40-95, comprising the calmodulin binding site of the enzyme, from Escherichia coli by nickel affinity chromatography and gel filtration to homogeneity
-
the protein is purified from healthy mussels by homogenization, centrifugation and passing through sterile gauzes
-
transport-specific fractionation for purification
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of PMR1, string and inducible heat shock promoter to direct high level expression of PMR1 from a multicopy plasmid
-
ECA3 mutant defective in its endogenous Ca21 pumps is expressed in Saccharomyces cerevisiae strain K616
expressed in a Saccharomyces cerevisiae triple mutant defective in both a Golgi and vacuolar Ca2+ pump, strain K616 and strain HI227
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21-DE3 pLysS cells
expressed in HEK-293 cells
expressed in Saccharomyces cerevisiae mutant strain K616 devoid of endogenous Ca2+-ATPases
expressed in Saccharomyces cerevisiae strain K616
expression of ACA8 residues 40-95, comprising the calmodulin binding site of the enzyme, in Escherichia coli as protein with an N-terminal fusion consisting of a His6 tag, a lipoyl domain and a TEV protease cleavage site
-
expression of C-terminally biotinylated SERCA1a in Saccharomyces cerevisiae strain W3031.b/Gal4, a thrombin cleavage site is inserted
-
expression of wild type and mutant D813A/D818A of L6-7 loop of enzyme in yeast
-
expression of wild-type SERCA2a in insect cell membranes using the baculovirus transfection system, process optimization, co-expression of phospholamban, overview
-
gene Afpmr1, DNA and amino acid sequence determination and analysis, functional expression in Saccharomyces cerevisiae strain K616, functional complementation of deficient growth in EGTA- and MnCl2-containing medium
-
gene ATP2C2, expression pattern, chromosomal localization 16q24.1, the genes ATP2C1 and ATP2C2 present an identical exon/intron layout, overview, functional expression of SPCA2 in COS-1 cell microsomes
gene ATP2C2, isozyme SPCA2, DNA and amino acid sequence determination and analysis, expression in Mn2+-sensitive pmr1 null mutant strain K616 of Saccharomyces cerevisiae, isozyme SPCA2 complements better than isozyme SPCA1
-
gene PM1 homologue, DNA and amino acid sequence determination and analysis
gene pmr1, expression pattern, overexpression of truncated pmr1 in transgenic worms
-
genes ATP2C genes encoding isozymes 1a-d, expression of isozymes 1a-1d using an SV40 vector, in HEK-293 and COS-1 cells
genes ATP2C1 and ATP2C2, transient overexpression of isozymes SPCA1 and SPCA2 in HEK293 cell microsomal membranes
-
isoforms 3a, b and c, transfection in HEK-293 or COS-1 cells using the calcium phosphate precipitation method
-
mutant enzymes are expressed in Saccharomyces cerevisiae strain K616 (devoid of endogenous Ca2+-ATPases) and His-tagged N-termini of wild type and mutant proteins are expressed in Escherichia coli strain DH5alpha
overexpression of C-terminally biotinylated SERCA1a, with introduced thrombin cleavage site, in Saccharomyces cerevisiae
overexpression of wild-type and mutant SERCA-1s in COS-1 cells membranes using an SV40 vector for transfection
-
PMCA3 DNA and amino acid sequence determination and analysis, phylogenetic tree, expression analysis during molting cycle
SERCA1 expression in COS-1 cells targeted extensively to intracellular membranes using an adenoviral vector. Higher transcription and expression are obtained in the presence of a His6 tag at the amino terminus, as compared with a His6 tag at the carboxyl SERCA terminus, or no tag. Optimization of expression method, overview
-
the pmr1+ gene has strong genetic interactions with pdt1+ gene that encodes the Nramp-related divalent metal transporter
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of Mn2+, as well as Ca2+, to the medium induces pmr1+ gene expression in a calcineurin/Prz1-dependent manner
after 20 h of anoxic submergence, enzyme protein levels remain unchanged in skeletal muscle, liver and heart, but decreases by 36% and 24% in kidney and brain, respectively. Vmax decreases by 46% in muscle, 47% in liver and 35% in heart of anoxic turtles, but does not change significantly in other tissues
-
enzyme protein expression is up-regulated after 30 min in CCL21-treated dendritic cells
-
expression of SERCA proteins is about 4times higher in the heart of cold-acclimated burbot than warm-acclimated burbot
-
in the presence of protein kinase C, inhibition with 100 nM 3-[1-[3-(dimethylamino)propyl]-5-methoxy-1H-indol-3-yl]-4-(1H-indol-3-yl)-1H-pyrrole-2,5-dione (Goe 6983) maintains adequate isoform SERCA2 levels
-
isoform SERCA2 downregulation (30-60%) occurs following infection of myocytes with adenovirus vectors carrying luciferase or isoform SERCA1 cDNA under control of nuclear factor of activated T cells (NFAT)-dependent promoters. Competitive engagement of the CN/NFAT pathway by endogenous genes involved in hypertrophy produces downregulation of SERCA2
-
isoform SERCA2b protein and mRNA levels are dramatically reduced in the liver of obese mice
placental explants cultured under hypoxia in the presence of 4mM MgSO4 show similar values of Ca2+-ATPase activity of their membranes compared to those of explants cultured under normoxia
-
splice varianta PMCA4e and PMCA4a show higher expression level in injured carotids compared to uninjured carotids
stimulation of protein kinase C activity has no effect on SERCA enzyme activity
-
syncytiotrophoblast plasma membranes of placental explants cultured under hypoxia diminish their Ca2+-ATPase activity
-
the expression of the P2B Ca2+ pumps in potato virus X-inoculated plants is significantly higher than in control plants
-
addition of Mn2+, as well as Ca2+, to the medium induces pmr1+ gene expression in a calcineurin/Prz1-dependent manner
addition of Mn2+, as well as Ca2+, to the medium induces pmr1+ gene expression in a calcineurin/Prz1-dependent manner
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of purified enzyme into dioleoyl-phosphatidylcholine, in a buffer containing 50 mM MOPS, 0.25 M sucrose, 1 M KCl, 1 mM MgCl2, 0.1 mM CaCl2, 1 mM DTT, and 0.025% NaN3, at pH 7.5
-
reconstitution of purified enzyme into proteoliposomes using 1,2-dioleoyl-sn-glycero-3-phosphocholine in a cholate buffer containing 30 mM Tris, pH 7.0, 0.4 M NaCl, 0.4 M sucrose, 1 mM MgCl2, 1 mM NaN3, 1% w/v sodium cholate, and 50 mM DTT, the enzyme shows nearly full activity
reconstitution of purified enzyme into proteoliposomes using microbeads, the enzyme is mixed with lipid in a 1:5000 protein to lipid molar ratio, removal of detergent, sealing of vesicles
-
reconstitution of purified enzyme with phospholamban in proteoliposomes, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
the ability to manipulate metal transporters, such as by altering substrate specificity, is an essential step in developing genetically engineered plants that can be used for phytoremediation strategies for specific metals
biotechnology
the ability to manipulate metal transporters, such as by altering substrate specificity, is an essential step in developing genetically engineered plants that can be used for phytoremediation strategies for specific metals
medicine
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
additional information
-
determination of enzyme activity and Ca2+ transport rates in different human muscles types are important for the local anesthetics strategy in dentistry
medicine
-
isoform SERCA2-mediated Ca2+-regulation decreases in the failing heart, isoform SERCA2a overexpression can potentially reduce arrhythmias and is a therapy for heart failure and cardiac hypertrophy
medicine
-
isoform SERCA3f may account for the mechanism of endoplasmic reticulum stress in vivo in heart failure
medicine
-
PMCA4b overexpression significantly reduces cardiac hypertrophy following pressure overload
medicine
-
SERCA2 expression and activity are decreased in cycstic fibrosis airway epithelium resulting in enhanced susceptibility to oxidants, reduced SERCA2 expression may alter calcium signalling and apoptosis in cystic fibrosis
medicine
-
plasmalemmal Ca2+ pump isoform 2 mRNA levels are a potential tool in identifying poor responders to therapy in women with basal breast cancer
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EXTERNAL LINKS (specific for EC-Number 7.2.2.10)
Transporter Classification Database (TCDB): 3.A.3.2.10, 3.A.3.2.14, 3.A.3.2.17, 3.A.3.2.34, 3.A.3.2.3, 3.A.3.2.1, 3.A.3.2.5, 3.A.3.2.9, 3.A.3.2.35, 3.A.3.2.2, 3.A.3.9.2, 3.A.3.2.19, 3.A.3.2.25, 3.A.3.2.40, 3.A.3.2.31, 3.A.3.2.42, 3.A.3.2.11, 3.A.3.2.12, 3.A.3.2.43, 3.A.3.2.7, 3.A.3.2.13, 3.A.3.2.27, 3.A.3.2.6, 3.A.3.2.26, 3.A.3.2.21, 3.A.3.2.44, 3.A.3.2.33, 3.A.3.2.30, 3.A.3.2.32
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Release 2023.1 (January 2023)
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