Information on EC 3.6.3.8 - Ca2+-transporting ATPase

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

EC NUMBER
COMMENTARY
3.6.3.8
-
RECOMMENDED NAME
GeneOntology No.
Ca2+-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
show the reaction diagram
mechanism
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
show the reaction diagram
phosphoenzyme intermediate formation
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
show the reaction diagram
formation of a phosphorylated intermediate
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
show the reaction diagram
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]
show the reaction diagram
the enzyme is a Ca2+-dependent phosphoprotein intermediate
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
show the reaction diagram
Ca2+ binding site structure and mechanism
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
show the reaction diagram
isozyme SPCA2 shows Ca2+- and Mn2+-dependent phosphoprotein intermediate formation
O75185
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
show the reaction diagram
kinetic mechanism of isozymes SPCA1 and SPCA2, phosphorylated intermediate, overview
-
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
show the reaction diagram
reaction and kinetic mechanism, phosphorylated intermediate, detailed overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (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 and in yeast. The first and third transport one ion per ATP hydrolysed, whereas the second transports two ions. Ca2+ is transported from the cytosol [side 1] into the sarcoplasmic reticulum in muscle cells [side 2].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ATP-dependent Ca2+ pump PMR1
-
-
-
-
ATPase 2C1
-
-
-
-
Ca2+ ATPase
-
-
-
-
Ca2+-ATPase, isoform 10
-
-
-
-
Ca2+-ATPase, isoform 11
-
-
-
-
Ca2+-ATPase, isoform 12
-
-
-
-
Ca2+-ATPase, isoform 13
-
-
-
-
Ca2+-pumping 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
-
-
-
-
Endoplasmic reticulum class 1/2 Ca(2+) ATPase
-
-
-
-
Golgi Ca2+-ATPase
-
-
-
-
HUSSY-28
-
-
-
-
P-type calcium ATPase
-
-
-
-
phosphatase, adenosine tri
-
-
-
-
plasma membrane Ca-ATPase
-
-
-
-
PMCA1
-
-
-
-
PMCA2
-
-
-
-
PMCA3
-
-
-
-
PMCA4
-
-
-
-
sarco(endo)plasmic reticulum Ca2+-ATPase
-
-
-
-
sarcoplasmic reticulum ATPase
-
-
-
-
Secretory pathway Ca2+ transporting ATPase
-
-
-
-
SERCA
-
-
-
-
SERCA1
-
-
-
-
SERCA2
-
-
-
-
SERCA3
-
-
-
-
Vacuolar Ca2+-ATPase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene Afpmr1
-
-
Manually annotated by BRENDA team
strain PS832, derived from strain 168
-
-
Manually annotated by BRENDA team
enzyme isoform PMCA 5
-
-
Manually annotated by BRENDA team
strains N2, daf-16(m26), and daf-2(e1370)III, gene pmr1
-
-
Manually annotated by BRENDA team
several strains, gene PMR1 homologue
SwissProt
Manually annotated by BRENDA team
Dorytheutis plei
-
-
-
Manually annotated by BRENDA team
Homarus sp.
lobster
-
-
Manually annotated by BRENDA team
enzyme isoforms PMCA 1, PMCA 2, PMCA 4
-
-
Manually annotated by BRENDA team
gene ATP2C2; gene ATP2C2
SwissProt
Manually annotated by BRENDA team
genes ATP2C1 and ATP2C2, isoenzymes SPCA 1 and 2
-
-
Manually annotated by BRENDA team
isoform 4b
-
-
Manually annotated by BRENDA team
isozyme 1
-
-
Manually annotated by BRENDA team
isozyme SERCA1
-
-
Manually annotated by BRENDA team
isozymes SPCA1 and SPCA2, genes ATP2C1 and ATP2C2
-
-
Manually annotated by BRENDA team
isozymes SPCA1a-SPCA1d; isozymes 1a-d
SwissProt
Manually annotated by BRENDA team
isoform PMCA2
UniProt
Manually annotated by BRENDA team
adult male New Zealand rabbits
-
-
Manually annotated by BRENDA team
adult New Zealand rabbits
-
-
Manually annotated by BRENDA team
isozyme 1a
UniProt
Manually annotated by BRENDA team
New Zealand rabbits
-
-
Manually annotated by BRENDA team
young female New Zealand rabbit
-
-
Manually annotated by BRENDA team
Paramecium tetraurelia 7S
strain 7S
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
Plasmodium falciparum W-2
-
UniProt
Manually annotated by BRENDA team
red swamp crayfish
SwissProt
Manually annotated by BRENDA team
enzyme isoform PMCA 1, PMCA 2 and PMCA3
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
-
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
-
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
P11506
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
O55143
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4-dinitrophenyl phosphate + H2O + Ca2+/in
?
show the reaction diagram
-
-
-
-
?
acyl-carrier protein + H2O + Ca2+/in
?
show the reaction diagram
-
-
-
-
?
ADP + phosphate + Ca2+/in
ATP + H2O + Ca2+/out
show the reaction diagram
-
-
-
r
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
Ca2+-independent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
P20647
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
Q6SLH6
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
Homarus sp.
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
P23220
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
O23087, P92939, Q9SY55, Q9XES1
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
Q42883
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
recombinant enzyme
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
P98194
ATPase activity and Ca2+ transport activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
O75185
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
Q9P872
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is the Ca2+ pump in sarcoplasmic reticulum membranes
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
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
show the reaction diagram
P04191
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
Homarus sp.
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
assay with labeled ATP substrate
-
-
r
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
ATPase activity and Ca2+ uptake into artificial proteoliposomes activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
Ca2+ transport
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
Ca2+-dependent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
the enzyme performs ATP-dependent Ca2+/H+ antiport and Ca2+-dependent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
P20020, Q01814, Q16720
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
show the reaction diagram
Q9R0K7
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
show the reaction diagram
-
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
show the reaction diagram
-
SERCA1 is responsible for ATPase activity and intermediate reactions, as well as ATP-dependent Ca2+ transport, 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
show the reaction diagram
-
the enzyme has one high affinity ATP binding site (catalytic site) and two calcium-binding sites
-
-
?
ATP + H2O + Ca2+/in
ADP + phosphate + Ca2+/out
show the reaction diagram
-
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
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
r
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
Pigeon
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
Dorytheutis plei
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
O55143
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
Q08853
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
Q9LF79
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
P11506
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
B6CAM1
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
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+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
Plasmodium falciparum W-2
Q08853
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
Paramecium tetraurelia 7S
-
-
-
?
ATP + H2O + Ca2+/out
?
show the reaction diagram
-
filling of the Ca2+ pool in the endoplasmic reticulum
-
-
?
ATP + H2O + Ca2+/out
?
show the reaction diagram
-
high affinity (Ca2+-Mg2+)-ATPase is responsible for Ca2+ transport
-
-
?
ATP + H2O + Ca2+/out
?
show the reaction diagram
Paramecium tetraurelia, Paramecium tetraurelia 7S
-
responsible for Ca2+ uptake into the alveolar sac
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
show the reaction diagram
-
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
show the reaction diagram
-
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
show the reaction diagram
O75185
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
show the reaction diagram
Q9P872
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Sr2+/in
ADP + phosphate + Sr2+/out
show the reaction diagram
-
-
-
?
ATP + Sr2+/cis + H2O
ADP + phosphate + Sr2+/trans
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O + Ca2+/in
?
show the reaction diagram
-
-
-
-
?
UTP + H2O + Ca2+/in
UDP + phosphate + Ca2+/out
show the reaction diagram
-
-
-
?
UTP + H2O + Ca2+/in
UDP + phosphate + Ca2+/out
show the reaction diagram
-
-
-
?
GTP + H2O + Ca2+/in
GDP + phosphate + Ca2+/out
show the reaction diagram
-
-
-
?
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
?
-
-
the enzyme is responsible for the Ca2+ sequestering
-
-
-
additional information
?
-
-
the enzyme plays a significant role in cellular Ca2+ homeostasis
-
-
-
additional information
?
-
-
interaction of Ca2+-ATPase with phospholamban is involved in regulation of heart contractility, overview
-
-
-
additional information
?
-
-
the Ca2+,Mn2+-ATPase SPCA2 is involved in the secretory pathway
-
-
-
additional information
?
-
Q9P872
the enzyme is a P-type Ca2+/Mn2+-ATPase involved in the secretory pathway
-
-
-
additional information
?
-
P98194
the enzyme is important in the secretory pathway
-
-
-
additional information
?
-
-
the enzyme is involved in calcium and maganese homeostasis
-
-
-
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 enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
-
additional information
?
-
Q6SLH6
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, functional regulation by phospholamban
-
-
-
additional information
?
-
-
the P-type calcium ATPase is important for calcium/manganese homeostasis and oxidative stress response
-
-
-
additional information
?
-
-
dissection of the functional differences between secretory pathway Ca2+/Mn2+-ATPase isoenzymes SPCA 1 and 2
-
-
-
additional information
?
-
-
interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals, overview
-
-
-
additional information
?
-
-
the enzyme binds calmodulin with high affinity
-
-
-
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
?
-
O23087, P92939, Q9SY55, Q9XES1
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
?
-
P20020, Q01814, Q16720
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
-
additional information
?
-
Q9R0K7
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
-
additional information
?
-
P20647
SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
-
-
-
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
?
-
P20647
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
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
Q6SLH6
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
Homarus sp.
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
P98194
ATPase activity and Ca2+ transport activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
O75185
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
Q9P872
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is the Ca2+ pump in sarcoplasmic reticulum membranes
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
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
show the reaction diagram
P04191
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
-
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
show the reaction diagram
-
SERCA1 is responsible for ATPase activity and intermediate reactions, as well as ATP-dependent Ca2+ transport
-
-
?
ATP + H2O + Ca2+/in
ADP + phosphate + Ca2+/out
show the reaction diagram
-
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
ADP + phosphate + Ca2+/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+/out
?
show the reaction diagram
-
filling of the Ca2+ pool in the endoplasmic reticulum
-
-
?
ATP + H2O + Ca2+/out
?
show the reaction diagram
-
high affinity (Ca2+-Mg2+)-ATPase is responsible for Ca2+ transport
-
-
?
ATP + H2O + Ca2+/out
?
show the reaction diagram
Paramecium tetraurelia, Paramecium tetraurelia 7S
-
responsible for Ca2+ uptake into the alveolar sac
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
show the reaction diagram
-
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
show the reaction diagram
-
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
show the reaction diagram
O75185
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
show the reaction diagram
Q9P872
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
additional information
?
-
-
the enzyme is responsible for the Ca2+ sequestering
-
-
-
additional information
?
-
-
the enzyme plays a significant role in cellular Ca2+ homeostasis
-
-
-
additional information
?
-
-
interaction of Ca2+-ATPase with phospholamban is involved in regulation of heart contractility, overview
-
-
-
additional information
?
-
-
the Ca2+,Mn2+-ATPase SPCA2 is involved in the secretory pathway
-
-
-
additional information
?
-
Q9P872
the enzyme is a P-type Ca2+/Mn2+-ATPase involved in the secretory pathway
-
-
-
additional information
?
-
P98194
the enzyme is important in the secretory pathway
-
-
-
additional information
?
-
-
the enzyme is involved in calcium and maganese homeostasis
-
-
-
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 enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
-
additional information
?
-
Q6SLH6
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, functional regulation by phospholamban
-
-
-
additional information
?
-
-
the P-type calcium ATPase is important for calcium/manganese homeostasis and oxidative stress response
-
-
-
additional information
?
-
O23087, P92939, Q9SY55, Q9XES1
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
?
-
P20020, Q01814, Q16720
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
-
additional information
?
-
Q9R0K7
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
-
additional information
?
-
P20647
SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
-
-
-
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
?
-
P20647
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.
-
-
-
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+
-
activates at 0.001 mM
Ca2+
-
required, activates the ATP hydrolysis activity
Ca2+
-
-
Ca2+
-
required
Ca2+
-
binding structure and kinetics in the crystallized enzyme-phospholamban complex, overview
Ca2+
-
required
Ca2+
-
isozyme SPCA1 shows the Ca2+-preferring phenotype
Ca2+
O75185
the enzyme shows high affinity for Ca2+
Ca2+
P98194
; quantitative Ca2+ flux analysis of recombinant isozymes in COS-1 cells permeabilized by saponin
Ca2+
-
SPCA1d shows a 2.5fold higher affinity for Ca2+ compared to SPCA2
Ca2+
-
optimal at 0.008-0.01 mM, the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
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+
-
dependent on
Ca2+
-
required
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+
-
required
Ca2+
-
SERCA1 has two high affinity transmembrane Ca2+-binding sites
Ca2+
P20020, Q01814, Q16720
dependent on, at very low Ca2+ concentrations the PMCA is nearly inactive, unstimulated PMCA pumps have poor affinity for Ca2+; dependent on, at very low Ca2+ concentrations the PMCA is nearly inactive, unstimulated PMCA pumps have poor affinity for Ca2+; dependent on, at very low Ca2+ concentrations the PMCA is nearly inactive, unstimulated PMCA pumps have poor affinity for Ca2+; dependent on, at very low Ca2+ concentrations the PMCA is nearly inactive, unstimulated PMCA pumps have poor affinity for Ca2+
Ca2+
Q9R0K7
dependent on, at very low Ca2+ concentrations the PMCA is nearly inactive, unstimulated PMCA pumps have poor affinity for Ca2+
Ca2+
-
SERCA binds two Ca2+ per mole
Ca2+
Q42883
dependent on
Ca2+
-
hydrolyzes ATP in a Ca2+ dependent manner
Ca2+
-
dependent on, there are two binding sites for Ca2+; dependent on, there are two binding sites for Ca2+; dependent on, there are two binding sites for Ca2+
Ca2+
P23220
dependent on
Ca2+
-
dependent on
Ca2+
-
SERCA is dependent on 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+
-
dependent on
Ca2+
-
PMCA of neurons is electroneutral and exchanges 2 H+ for each Ca2+ or Ba2+ ion extruded
Ca2+
-
SPCA1 mediates the accumulation of Ca2+ with high affinity into Golgi reservoirs
Ca2+
-
dependent on
Ca2+
-
SERCA2a transfers Ca2+ from the cytosol of the cardiomyocyte to the lumen of the sarcoplasmic reticulum during muscle relaxation
Ca2+
O23087, P92939, Q9SY55, Q9XES1
dependent on; dependent on; dependent on; dependent on
Ca2+
-
dependent on
Ca2+
-
dependent on
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+
-
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
Calmodulin
-
PMCA is dependent on Ca2+-calmodulin
K+
-
slightly stimulates the dephosphorylation reaction
Mg2+
-
required
Mg2+
-
plasma membrane vesicles from the optic nerve accumulate Ca2+ in the presence of Mg2+
Mg2+
-
3 mM Mg2+ required for optimal activity; required
Mg2+
-
greatest activity at 10 mM Mg2+
Mg2+
-
binding structure in the crystallized enzyme-phospholamban complex, overview
Mg2+
-
required
Mg2+
-
required for ATPase activity
Mg2+
-
required, best at 0.09 mM in all muscle tissue, higher concentration are inhibitory
Mg2+
-
required
Mg2+
-
required
Mg2+
-
1 mM Mg2+ (a concentration equivalent to that of ATP) is an absolute requirement for ATPase activity
Mg2+
-
competitive Mg2+ binding can occur at Ca2+ binding site I but not at site II
Mn2+
-
isozyme SPCA2 shows the Mn2+-preferring phenotype
Mn2+
-
required, less effective than Ca2+
Mn2+
Q42883
LCA1 may also act as a Mn2+ pump, consistent with a possible role in secretory pathway divalent cation homeostasis
Mn2+
-
SPCA1 mediates the accumulation Mn2+ with high affinity into Golgi reservoirs
Mn2+
-
ER-type Ca2+-ATPases can transport, beside Ca2+, also Mn2+ and Zn2+ ions
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(12S,12aR)-3-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(1R,9aR)-9-[2-[(4-fluorobenzyl)oxy]ethyl]-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepine
Q08853
-
(1S,6R,9aS)-3,6-dimethyloctahydro-3,9a-epidioxy-2-benzoxepin-1(1H)-yl phenylacetate
Q08853
-
(1S,9aR)-1-methoxy-3-methyl-9-[2-(phenylperoxy)ethyl]octahydro-3,9a-epidioxy-2-benzoxepine
Q08853
-
(1S,9aR)-1-methoxy-3-methyl-9-[2-(prop-2-en-1-yloxy)ethyl]octahydro-3,9a-epidioxy-2-benzoxepine
Q08853
-
(1S,9aR)-9-[2-(benzyloxy)ethyl]-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepine
Q08853
-
(1S,9aS)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepine
Q08853
-
(1S,9aS)-1-[2-(benzyloxy)ethyl]-1,3,9-trimethyloctahydro-3,9a-epidioxy-2-benzoxepine
Q08853
-
(3R,5aS,6R,8aS,12aS)-11-benzyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
Q08853
-
(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
Q08853
-
(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
Q08853
-
(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
Q08853
-
(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
Q08853
-
(3R,5aS,6R,8aS,12aS)-3,6-dimethyl-11-pentyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
Q08853
-
(3R,5aS,6R,8aS,12aS)-3-butyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(3R,5aS,6R,8aS,12aS)-3-ethyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(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
Q08853
-
(3R,5aS,6R,8aS,12aS)-6-methyl-3-(3-phenylpropyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(3R,5aS,6R,8aS,12aS)-6-methyl-3-propyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(3R,5aS,6R,8aS,9R,12aR)-3,9-dibutyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(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
Q08853
-
(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
Q08853
-
(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
Q08853
-
(3R,5aS,6R,8aS,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-ol
Q08853
-
(3R,5aS,6R,8aS,9R,12S,12aR)-3,6,9-trimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(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
Q08853
-
(3R,6R,9S,12R,12aR)-10-ethoxy-6,9-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-9-ol
Q08853
-
(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
Q08853
-
(3R,6R,9S,12R,12aR)-6,9-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,10-diol
Q08853
-
(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
Q08853
-
(3S,5aS,6R,8aS,12aS)-6-methyl-3-(2-methylpropyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(3S,5aS,6R,8aS,12aS)-6-methyl-3-(2-phenylethyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(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
Q08853
-
(3S,6R,12R,12aS)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(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
Q08853
-
(4aS)-3,3-dimethylhexahydro-6H-[1,2,4]trioxino[6,5-j]isochromen-6-one
Q08853
-
(4aS)-hexahydro-6H-[1,2,4]trioxino[6,5-j]isochromen-6-one
Q08853
-
(5S,6R,9R,10S,12R,12aS)-10-ethoxy-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-5-ol
Q08853
-
(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
Q08853
-
(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
Q08853
-
(6R,10R,12R,12aR)-3,6-dimethyl-9-methylidenedecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl hydroperoxide
Q08853
-
(6R,10R,12R,12aR)-3,6-dimethyloctahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,2'-oxiran]-10-ol
Q08853
-
(6R,10R,12R,12aR)-3,6-dimethyloctahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,2'-oxiran]-10-yl hydroperoxide
Q08853
-
(6R,10S,12R,12aR)-3,6-dimethyl-9-methylidenedecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-ol
Q08853
-
(6R,12aS)-11-(4-chlorobenzyl)-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
Q08853
-
(6R,12aS)-11-acetyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
Q08853
-
(6R,12aS)-11-benzyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
Q08853
-
(6R,12aS)-3,6-dimethyl-11-(2-phenylethyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
Q08853
-
(6R,12aS)-3,6-dimethyl-11-(3-phenylpropyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
Q08853
-
(6R,12aS)-3,6-dimethyl-11-(pyridin-2-ylmethyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
Q08853
-
(6R,12aS)-3,6-dimethyl-11-(thiophen-2-yl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
Q08853
-
(6R,12aS)-3,6-dimethyl-11-pentyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
Q08853
-
(6R,12R,12aR)-3,6-dimethyl-9-methylidenedecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl hydroperoxide
Q08853
-
(6R,12R,12aS)-3-butyl-6-methyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,12R,12aS)-3-ethyl-6-methyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,12R,12aS)-3-[3-(4-chlorophenyl)propyl]-6-methyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,12R,12aS)-6-methyl-3-(2-methylpropyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,12R,12aS)-6-methyl-3-(4-phenylbutyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,12R,12aS)-6-methyl-3-propyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,12S,12aS)-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(6R,12S,12aS)-3-ethyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(6R,12S,12aS)-6-methyl-3-(4-phenylbutyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(6R,12S,12aS)-6-methyl-3-propyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(6R,8aR,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,8aR,9R,12aR)-3,6,9-trimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(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
Q08853
-
(6R,8aS,9S,10R,12R,12aR)-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,10-diol
Q08853
-
(6R,8aS,9Z,12S,12aR)-9-ethylidene-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(6R,9aS)-3,6-dimethyloctahydro-3,9a-epidioxy-2-benzoxepine
Q08853
-
(6R,9R,12R,12aR)-10-(tert-butylperoxy)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,9R,12R,12aR)-10-ethoxy-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,9R,12R,12aR)-10-ethoxy-3,6-dimethyl-9-propyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,9R,12R,12aR)-10-ethoxy-9-ethyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,9R,12R,12aR)-10-methoxy-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-ol
Q08853
-
(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,9R,12R,12aR)-3,6-dimethyl-9-(3-phenylpropyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,9R,12R,12aR)-3,6-dimethyl-9-pentyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,9R,12R,12aR)-3,6-dimethyl-9-propyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,9R,12R,12aR)-3,6-dimethyloctahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,2'-oxiran]-10-yl hydroperoxide
Q08853
-
(6R,9R,12R,12aR)-9-butyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,9R,12R,12aR)-9-ethyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6R,9R,12S,12aR)-3,6,9-trimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(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
Q08853
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(2-methylpropyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(2-phenylethyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(3-phenylpropyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(4-phenylbutyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(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
Q08853
-
(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
Q08853
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-pentyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(6R,9R,12S,12aR)-9-butyl-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(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
Q08853
-
(6R,9R,12S,12aR)-9-ethyl-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(6R,9R,12S,12aR)-9-hexyl-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
Q08853
-
(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
Q08853
-
(6R,9S,10R,12R,12aR)-3,6-dimethyloctahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,2'-oxiran]-10-yl hydroperoxide
Q08853
-
(6R,9S,11aR)-3,6,9-trimethyloctahydro-3H-3,11-epoxyfuro[3,4-j][1,2]benzodioxepine
Q08853
-
(6R,9S,12R,12aR)-9-bromo-3,6,9-trimethyl-N-phenyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-amine
Q08853
-
(6R,9S,12R,12aR)-9-bromo-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(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
Q08853
-
(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
Q08853
-
(6S,7S,10S,12aS)-10-ethoxy-7-fluoro-3,6,7-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(6S,7S,10S,12R,12aS)-10-ethoxy-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-7-ol
Q08853
-
(6S,9R,10S,12aS)-10-ethoxy-3,6,9-trimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-7(3H)-one
Q08853
-
(6S,9R,10S,12aS)-10-ethoxy-7,7-difluoro-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
Q08853
-
(7R,12aR)-7,10-dimethyldodecahydro-2H-10,13-epoxy[1,2]dioxepino[4,3-i]pyrano[2,3-c]isochromene
Q08853
-
(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
-
1,1'-methanediyldinaphthalen-2-ol
-
-
1,3-dibromo-2,4,6-tri(methylisothiouronium)benzene
-
micromolar inhibitor of SERCA
1,5-bis(4-methoxyphenyl)-6,7-dioxabicyclo[3.2.2]nonane
Q08853
-
1,5-diphenyl-3,6,7-trioxabicyclo[3.2.2]nonane
Q08853
-
1-(naphthalen-1-ylmethyl)naphthalen-2-ol
-
-
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
Q08853
-
2,2',2''-methanetriyltris(4-tert-butylphenol)
-
-
2,2'-methanediylbis(4-tert-butylphenol)
-
-
2,4-di-tert-butyl-6-(1-phenylethyl)phenol
-
-
2,4-di-tert-butyl-6-[1-(4-methoxyphenyl)ethyl]phenol
-
-
2,5-bis(2-methylpropyl)phenol
-
-
2,5-bis(cyclopenta-2,4-dien-1-ylmethyl)benzene-1,4-diol
-
-
2,5-di(tert-butyl)hydroquinone
-
micromolar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation
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
2,6-di-tert-butyl-4-[1-(4-methoxyphenyl)ethyl]phenol
-
-
2-(cyclopenta-2,4-dien-1-ylmethyl)benzene-1,4-diol
-
-
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
Q08853
-
2-(dimethylamino)ethyl 4-[([2-[(1S,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethyl]peroxy)methyl]benzoate
Q08853
-
2-cyclooctylbenzene-1,4-diol
-
-
2-[(1R,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethyl diethylcarbamate
Q08853
-
2-[(1R,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethyl diphenylcarbamate
Q08853
-
2-[(1S,9aS)-1,3,9-trimethyloctahydro-3,9a-epidioxy-2-benzoxepin-1(1H)-yl]ethanol
Q08853
-
2-[(1S,9aS)-1,3-dimethyloctahydro-3,9a-epidioxy-2-benzoxepin-1(1H)-yl]ethanol
Q08853
-
2-[(1S,9aS)-3,9-dimethyloctahydro-3,9a-epidioxy-2-benzoxepin-1(1H)-yl]ethanol
Q08853
-
3-(1,1-diphenylethyl)cyclopentanol
-
-
3-[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]propan-1-ol
Q08853
-
4,4'-butane-2,2-diylbis(2-methylphenol)
-
-
4,4'-butane-2,3-diyldiphenol
-
-
4,4'-diisothiocyano-2,2'-stilbenedisulfonic acid
-
-
4,4'-propane-2,2-diylbis(2,6-dimethylphenol)
-
-
4,5-dibenzylbenzene-1,2-diol
-
-
4-(2-[2-[(1S,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethoxy]ethyl)pyridine
Q08853
-
4-(7-methyloctyl)phenol
-
-
4-([2-[(1R,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethoxy]methyl)pyrimidine
Q08853
-
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
Q08853
-
6-tert-butyl-2,3-dihydro-1H-inden-5-ol
-
-
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
Q08853
-
7-chloro-4-(piperazin-1-yl)quinoline
-
-
A23187
-
Ca2+ ionophore
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
-
amyloid beta-peptide 1-40
P23220
-
-
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
P23220
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
Q08853
-
-
biphenyl-2,5-diol
-
-
bis(maltolato)oxovanadium(IV)
-
-
bis(N-hydroxylamidoiminodiacetato)vanadium(IV)
-
-
bupivacaine
-
inhibition by bupivacaine is not competitive with respect to the specific transport and catalytic sites of the enzyme
Ca2+
-
above 0.1 mM, Ca2+-dependent ATPase
Calmidazolium
-
-
calmodulin antagonist compound 48/80
-
inhibits phosphatase activity
carboxyeosin
-
blocker of PMCA
Cd2+
-
1 mM, 39% inhibition
clotrimazole
-
-
Cu2+
Homarus sp.
-
reduces the Ca2+ content in the cytosol
Cu2+
-
0.5 mM, 50% inhibition
cyclopiazonic acid
-
weak
cyclopiazonic acid
Q42883
highly sensitive to the specific inhibitor cyclopiazonic acid
cyclopiazonic acid
-
nanomalar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation
cyclopiazonic acid
-
inhibitor of ER-type Ca2+-ATPases
detergent C12E8
-
inhibition of mutant D813A/D818A
eosin
Q42883
potent inhibitor
eosin Y
-
auto-inhibited Ca2+-ATPases are particularly sensitive to inhibition by eosin Y
erythrosin B
-
auto-inhibited Ca2+-ATPases are particularly sensitive to inhibition by erythrosin B
erythrosine B
-
-
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
Q08853
-
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
Q08853
-
ethyl 3-[(6R,12R,12aS)-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propanoate
Q08853
-
ethyl 3-[(6R,12S,12aS)-6-methyl-10-oxooctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propanoate
Q08853
-
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
Q08853
-
ethyl [[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]acetate
Q08853
-
Hg2+
-
0.25 mM, 50% inhibition
hydroxylamine
-
the enzyme is sensitive to treatment with hydroxylamine
iononphore A 23187
-
-
La3+
Q9R0K7
-
La3+
-
prevents the Mg2+-dependent transition E1P->E2P, acting noncompetitively with respect to Ca2+ and ATP
lidocaine
-
inhibition by lidocaine is not competitive with respect to the specific transport and catalytic sites of the enzyme
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
Q08853
-
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
Q08853
-
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
Q08853
-
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
Q08853
-
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
Q08853
-
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
Q08853
-
methyl 3-[[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]propanoate
Q08853
-
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
Q08853
-
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
Q08853
-
methyl 4-[[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]butanoate
Q08853
-
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
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-4-(azido-2-nitrophenyl)-2-aminoethylsulfonate
-
-
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
Q08853
-
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
Q08853
-
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
Q08853
-
Ni2+
-
1 mM, 28% inhibition
orthovanadate
-
50% inhibition at 0.13 mM
orthovanadate
-
-
orthovanadate
P20020, Q01814, Q16720
-
orthovanadate
Q9R0K7
-
orthovanadate
-
the Ca2+ pump is inhibited by orthovanadate (0.1 mM) once sufficient Ca2+ accumulation has occurred
orthovanadate
-
-
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
PCMB
Pigeon
-
-
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
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+
-
phospholamban
-
complex formation with the recombinant SERCA2a in transfected insect cells, regulatory function, overiew
-
phospholamban
-
-
-
phospholamban
-
phospholamban inhibits SERCA2a activity in its dephosphorylated state
-
pyridine-2,6-dicarboxylatodioxovanadium
-
-
ruthenium red
-
slight inhibition
Sodium vanadate
-
slight inhibition
tert-butyl [(1E)-1-([2-[(1S,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethyl]peroxy)ethylidene]carbamate
Q08853
-
tert-butylhydroquinone
-
-
tetrabromobisphenol A
-
can inhibit SERCA at low concentrations (IC50, 0.0004-0.0012 mM)
thapsigargin
-
-
thapsigargin
-
no effect up to 0.005 mM
thapsigargin
-
80% inhibition at 0.003 mM
thapsigargin
-
complete inhibition at 0.001 mM
thapsigargin
-
inhibits Ca2+ uptake in musles
thapsigargin
Homarus sp.
-
-
thapsigargin
-
-
thapsigargin
-
stabilizes the enzyme structure in absence of Ca2+
thapsigargin
Q42883
only mildly sensitive to the ER-type pump inhibitor thapsigargin
thapsigargin
-
inhibits SERCA activity
thapsigargin
-
SERCA is inhibited by 0.001 mM thapsigargin
thapsigargin
-
nanomalar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation
thapsigargin
-
specific inhibitor, complete inhibition at 50 nM
thapsigargin
Q08853
highly specific inhibitor
thapsigargin
-
-
Trifluoperazine
-
-
vanadate
-
orthovanadate
vanadate
-
orthovanadate
vanadate
-
-
vanadate
P98194
inhibits the phosphorylation reaction; inhibits the phosphorylation reaction
vanadate
-
inhibits the phosphorylation reaction
vanadate
Homarus sp.
-
-
vanadate
Q42883
potent inhibitor
Zn2+
-
-
Zn2+
Homarus sp.
-
reduces the Ca2+ content in the cytosol
Zn2+
-
1 mM, 50% inhibition
[(dihydroindenyl)oxy]acetic acid
-
DIOA
[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
Q08853
-
Mg2+
-
competitive Mg2+ binding can occur at Ca2+ binding site I but not at site II
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
O75185
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
-
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
-
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
P23220
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
-
PMCA is inhibited by acutely lowering extracellular proton concentration (pH raised to 9.0)
-
additional information
-
PMCA is insensitive to increases in membrane potential
-
additional information
-
PCA1 contains a N-terminal autoinhibitory domain
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
shifts the Ca2+-ATPase to the high-affinity form
Calmodulin
-
slight stimulation
Calmodulin
-
calmodulin depletion results in the transition of the Ca2+-pumping ATPase to a low Ca2+-affinity form
Calmodulin
-
stimulates
Calmodulin
-
no stimulation by bovine calmodulin
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
P20020, Q01814, Q16720
activated by calmodulin; activated by calmodulin; activated by calmodulin; activated by calmodulin
Calmodulin
Q9R0K7
activated by calmodulin
Calmodulin
-
enhances the Ca2+ transport
Calmodulin
-
-
Calmodulin
-
Pmr1p is positively controlled by the calmodulin and calcineurin complex in the presence of an elevated Ca2+ level
Calmodulin
-
strongly activated by calmodulin
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
-
the fully auto-inhibited enzyme has a very low basal Ca2+-ATPase activity which is stimulated more than 5fold by calmodulin
Calmodulin
-
0.001 mM calmodulin stimulates the activity of wild type enzyme by about 300%
Calmodulin
-
auto-inhibited Ca2+-ATPase
calpain
P20020, Q01814, Q16720
cleavage of PMCA by calpain activates it irreversibly; cleavage of PMCA by calpain activates it irreversibly; cleavage of PMCA by calpain activates it irreversibly; cleavage of PMCA by calpain activates it irreversibly
-
calpain
Q9R0K7
cleavage of PMCA by calpain activates it irreversibly
-
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
phosphatidylinositol bisphosphate
P20020, Q01814, Q16720
the most active in stimulating PMCA activity; the most active in stimulating PMCA activity; the most active in stimulating PMCA activity; the most active in stimulating PMCA activity
phosphatidylinositol bisphosphate
Q9R0K7
the most active in stimulating PMCA activity
phosphatidylserine
-
can replace calmodulin in shifting the enzyme to the high-affinity form
phosphatidylserine
-
465% 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
additional information
-
activation by controlled proteolysis
-
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
-
native and recombinant enzymes achieve maximal activity when supplemented with acidic phospholipids
-
additional information
-
isoform SERCA3f mRNA is up-regulated in failing hearts
-
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
-
PMCA isoform ACA8 activity is hardly affected by phosphatidylcholine or phosphatidylethanolamine
-
additional information
-
PCA1 mRNA levels are up-regulated by dehydration, NaCl, and abscisic acid
-
additional information
-
calcium occupancy of site I is required to trigger cooperative binding to site II and catalytic activation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000021
ATP
-
enzyme from liver
0.016
ATP
-
-
0.000013
Ca2+
-
enzyme from liver
0.0002
Ca2+
-
-
0.0003
Ca2+
-
-
0.0003
Ca2+
-
wild-type enzyme in absence of detergent
0.0004
Ca2+
-
-
0.0005
Ca2+
-
phosphatidylserine environment with or without calmodulin, enzyme from erythrocytes
0.001 - 0.002
Ca2+
-
mutant D813A/D818A in absence of detergent
0.0013
Ca2+
-
isoform3b
0.0017
Ca2+
-
isoform3a
0.0018
Ca2+
-
isoform3c
0.0075
Ca2+
-
-
0.02
Ca2+
-
phosphatidylcholine environment with or without calmodulin, enzyme from erythrocytes
0.00071
Ca2+/cis
-
PMCA from undifferentiated PC-12 cells
0.00097
Ca2+/cis
-
PMCA from differentiated PC-12 cells
0.015
Sr2+
-
mutant D813A/D818A in absence of detergent
0.035
Sr2+
-
wild-type enzyme in absence of detergent
0.000037
UTP
-
enzyme from liver
0.0013
Ca2+/cis
-
SERCA from undifferentiated or differentiated PC-12 cells
additional information
additional information
-
detailed de-/phosphorylation reaction kinetics, kinetic modelling
-
additional information
additional information
-
binding kinetics of calmodulin and labeled calmodulin to enzyme binding site-derived peptides, overview
-
additional information
additional information
P98194
ATPase and phosphorylation kinetics, kinetics of activation by Ca2+, and binding and transport of Ca2+; ATPase and phosphorylation kinetics, kinetics of isozymes of activation by Ca2+, and binding and transport of Ca2+
-
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
Homarus sp.
-
kinetics
-
additional information
additional information
-
kinetics of Ca2+ uptake and efflux, overview
-
additional information
additional information
-
charge transfer and current transients measurements, kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.5
ATP
P98194
ATPase turnover rate, pH 7.0, 37C, isozyme SPCA1a
15.9
ATP
P98194
ATPase turnover rate, pH 7.0, 37C, isozyme SPCA1d
20.27
ATP
P98194
ATPase turnover rate, pH 7.0, 37C, isozyme SPCA1a
22.5
ATP
P98194
ATPase turnover rate, pH 7.0, 37C, isozyme SPCA1b
27.44
ATP
P98194
ATPase turnover rate, pH 7.0, 37C, isozyme SPCA1d
130
ATP
P98194
ATPase turnover rate, pH 7.0, 37C, isozyme SERCA1a
9.5
Ca2+
-
calcium pump activity, pH 7.2, 37C
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
-
-
-
additional information
additional information
P98194
Ca2+ binding transition rate; Ca2+ binding transition rates of isozymes, overview
-
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000023
thapsigargin
-
pH 7.2, 37C, enzyme from medial pterygoid muscles
0.000026
thapsigargin
-
pH 7.2, 37C, enzyme from masseter muscles
0.000045
thapsigargin
-
pH 7.2, 37C, enzyme from fast 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
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.152
(4-chlorophenyl)(pyridin-2-yl)[4-(pyrrolidin-1-ylmethyl)phenyl]methanol
-
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 37C
0.022
(4-chlorophenyl)[4-([[3-(4-[3-[(7-chloroquinolin-4-yl)amino]propyl]piperazin-1-yl)propyl]amino]methyl)phenyl]methanone
-
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 37C
0.029
(4-chlorophenyl)[4-([[3-(4-[3-[(7-chloroquinolin-4-yl)amino]propyl]piperazin-1-yl)propyl]amino]methyl)phenyl]methanone
-
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 37C
0.0013
(N-((3-chlorophenyl)(4-(pyrrolidin-1-yl)methyl)phenyl)methyl)-7-chloro-4-aminoquinoline
-
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 37C
-
0.015
1,1'-methanediyldinaphthalen-2-ol
-
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
-
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
-
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 37C
0.057
1-[(4-chlorophenyl)(phenyl)[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-1H-imidazole
-
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 37C
0.0213
2,2',2''-methanetriyltris(4-tert-butylphenol)
-
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)
-
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)
0.0338
2,4-di-tert-butyl-6-(1-phenylethyl)phenol
-
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
-
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
-
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
-
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
-
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
-
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
-
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)
0.0497
3-(1,1-diphenylethyl)cyclopentanol
-
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)
-
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
-
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)
-
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
-
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)
0.0172
4-(7-methyloctyl)phenol
-
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)
0.0281
6-tert-butyl-2,3-dihydro-1H-inden-5-ol
-
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)
0.0025
amyloid beta-peptide 25-35
P23220
-
-
0.00229
biphenyl-2,5-diol
-
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)
-
in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25C
0.325
bis(N-hydroxylamidoiminodiacetato)vanadium(IV)
-
in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25C
35
clotrimazole
-
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 37C
0.00016
cyclopiazonic acid
Q42883
in 1 mM EGTA, 130 mM NaCl, 3 mM MgCl2, at 37C
0.0036
eosin
Q42883
in 1 mM EGTA, 130 mM NaCl, 3 mM MgCl2, at 37C
0.0008
N-((3-chlorophenyl)(4-((4-(7-chloroquinolin-4-yl)piperazin-1-yl)methyl)phenyl)methyl)-7-chloro-4-aminoquinoline
-
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 37C
-
0.0004
palytoxin
-
in 20 mM MOPS, pH 7.0, 80 mM KC1, 5 mM MgCl2, 0.5 mM EGTA, 0.55 mM CaC12, at 25C
0.025
pyridine-2,6-dicarboxylatodioxovanadium
-
in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25C
0.000635
thapsigargin
Q42883
recombinant enzyme expressed in Saccharomyces cerevisiae strain HI227, in 1 mM EGTA, 130 mM NaCl, 3 mM MgCl2, at 37C
0.00095
thapsigargin
Q42883
recombinant enzyme expressed in Saccharomyces cerevisiae strain K616, in 1 mM EGTA, 130 mM NaCl, 3 mM MgCl2, at 37C
0.0057
vanadate
Q42883
in 1 mM EGTA, 130 mM NaCl, 3 mM MgCl2, at 37C
0.08
vanadate
-
in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25C
0.127
[(dihydroindenyl)oxy]acetic acid
-
-
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 25C
0.1181
-
recombinant wild type enzyme, in the presence of Ca2+ and 0.001 mM calmodulin, pH not specified in the publication, at 25C
0.19
-
-
0.49
-
purified recombinant SERCA2a
4.07
-
purified enzyme
5.2
-
purified calcium pump activity
9
-
avidin affinity chromatography purified enzyme
additional information
-
-
additional information
-
activity during purification and after solubilization/reconstitution with different detergents, 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
additional information
P98194
Ca2+ ionophore A23187 effect, Ca2+ transport rate isozymes, overview; Ca2+ ionophore A23187 effect, Ca2+ transport rate, overview
additional information
-
determination of enzyme activity distribution in different muscle types, overview
additional information
-
Ca2+ uptake and efflux activity of recombinant enzyme in membrane vesicles of transfected insect cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
P98194
assay at; assay at
7
P04191
assay at
7
-
assay at
7
-
Ca2+-ATPase activity assay
7.2 - 7.4
Pigeon
-
-
7.2
-
assay at
7.2
-
assay at
7.2
-
assay at
7.23
-
in presence of Ca2+ ionophore
7.4
-
assay at
7.4
-
ATPase activity assay
7.5
O75185
assay at
7.7 - 8
-
isoform 3c in presence of Ca2+ ionophore
7.72
-
isoform 3a in presence of Ca2+ ionophore
7.74
-
isoform 3b in presence of Ca2+ ionophore
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
5.5 - 8
-
about 35% of maximal activity at pH 5.5 and at pH 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
-
different types of proton participation in E1 to E2 transition and in calcium binding
additional information
-
pH profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 21
-
assay at 2C and at 21C
37
-
assay at
37
-
assay at
37
-
assay at
37
P98194
assay at; assay at
37
-
assay at
37
-
assay at
37
-
ATPase activity assay
37
-
Ca2+-ATPase activity assay
50
Pigeon
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 60
-
maximal enzyme activation between 30-40C
30 - 55
Pigeon
-
30C: about 20% of maximal activity, 55C: about 55% of maximal activity, 60C: about 5% of maximal activity
additional information
-
temperature dependence of the Ca2+ transport at different pH values, overview
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
only isoform SPCA1
Manually annotated by BRENDA team
-
CF-41o cell, CF-45o cell
Manually annotated by BRENDA team
-
exclusively located in
Manually annotated by BRENDA team
Paramecium tetraurelia 7S
-
exclusively located in
-
Manually annotated by BRENDA team
Q6SLH6
expression and activity during molting cycle, overview
Manually annotated by BRENDA team
-
isoform SERCA 2, isoform SERCA 3
Manually annotated by BRENDA team
-
isozyme SPCA2
Manually annotated by BRENDA team
P20020, Q01814, Q16720
PMCA1 is ubiquitous, but is expressed most abundantly in brain, lung and intestine
Manually annotated by BRENDA team
Q9R0K7
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.
Manually annotated by BRENDA team
P20020, Q01814, Q16720
the PMCA2 pump is a brain isoform
Manually annotated by BRENDA team
P20020, Q01814, Q16720
the PMCA3 pump is expressed in brain
Manually annotated by BRENDA team
-
strongest expression of isoform SPCA2
Manually annotated by BRENDA team
Q6SLH6
expression and activity during molting cycle, overview
Manually annotated by BRENDA team
Q9R0K7
PMCA2 is highly expressed in cerebellar Purkinje cells
Manually annotated by BRENDA team
P20020, Q01814, Q16720
PMCA2 is highly expressed in cerebellar Purkinje cells
Manually annotated by BRENDA team
P23220
isoform PMCA 2 is more abundant in the cerebellum than in the cerebrum
Manually annotated by BRENDA team
-
strongest expression of isoform SPCA2
Manually annotated by BRENDA team
Q9R0K7
the PMCA4 pump is expressed in erythrocyte
Manually annotated by BRENDA team
Q6SLH6
expression and activity during molting cycle, overview
Manually annotated by BRENDA team
Pigeon
-
-
Manually annotated by BRENDA team
-
methods to employ tissue homogenates to study sarcoplasmatic reticulum Ca2+ transport function in individual mouse hearts
Manually annotated by BRENDA team
P20020, Q01814, Q16720
PMCA2 is expressed at a lower level in the heart
Manually annotated by BRENDA team
Q9R0K7
the PMCA4 pump is expressed in heart, PMCA2 is expressed at a lower level in the heart
Manually annotated by BRENDA team
Homarus sp.
-
-
Manually annotated by BRENDA team
Q9R0K7
PMCA2 is highly expressed in the hair cells of the inner ear
Manually annotated by BRENDA team
P20020, Q01814, Q16720
PMCA2 is highly expressed in the hair cells of the inner ear
Manually annotated by BRENDA team
P20020, Q01814, Q16720
-
Manually annotated by BRENDA team
P20020, Q01814, Q16720
PMCA1 is ubiquitous, but is expressed most abundantly in brain, lung and intestine
Manually annotated by BRENDA team
Q9R0K7
PMCA1 is ubiquitous, but is expressed most abundantly in brain, lung and intestine. The PMCA4 pump is expressed in intestine.
Manually annotated by BRENDA team
-
and nonpolarized cells, isozyme SPCA1
Manually annotated by BRENDA team
P20020, Q01814, Q16720
-
Manually annotated by BRENDA team
Q6SLH6
expression and activity during molting cycle, overview
Manually annotated by BRENDA team
Q9R0K7
the PMCA4 pump is expressed in kidney
Manually annotated by BRENDA team
-
lowest protein content and activity in kidney
Manually annotated by BRENDA team
-
only isoform SPCA1
Manually annotated by BRENDA team
Q9R0K7
PMCA1 is ubiquitous, but is expressed most abundantly in brain, lung and intestine
Manually annotated by BRENDA team
P20020, Q01814, Q16720
PMCA1 is ubiquitous, but is expressed most abundantly in brain, lung and intestine
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Q9R0K7
the brain isoform PMCA2 pump is also expressed in the lactating mammary glands
Manually annotated by BRENDA team
P20020, Q01814, Q16720
the brain isoform PMCA2 pump is also expressed in the lactating mammary glands
Manually annotated by BRENDA team
-
strongest expression of isoform PMCA1 in the prelactating mammary gland
Manually annotated by BRENDA team
-
masseter and medial pterygoid
Manually annotated by BRENDA team
Q6SLH6
axial abdominal muscle, expression and activity during molting cycle, overview
Manually annotated by BRENDA team
-
masticatory, fast, masseter, and pterygoid muscles, determination of enzyme activity distribution in different muscle types, overview
Manually annotated by BRENDA team
-
back and leg muscles
Manually annotated by BRENDA team
-
highest protein content and activity in muscle
Manually annotated by BRENDA team
-
only isoform PMCA1
Manually annotated by BRENDA team
-
SPCA1 localizes in the initial part of primary dendritic trunk in main cortical, hippocampal and cerebellar neurons from the earliest postnatal stages
Manually annotated by BRENDA team
-
primary, isozyme SPCA2 shows a highly punctate distribution
Manually annotated by BRENDA team
-
only isoform SPCA1
Manually annotated by BRENDA team
-
hind-leg white muscle
Manually annotated by BRENDA team
-
fast twitch skeletal muscle
Manually annotated by BRENDA team
P20020, Q01814, Q16720
the PMCA3 and PMCA4 pumps are expressed in skeletal muscles
Manually annotated by BRENDA team
Q9R0K7
the PMCA3 and PMCA4 pumps are expressed in skeletal muscles
Manually annotated by BRENDA team
P20020, Q01814, Q16720
the PMCA3 pump is expressed in skeletal muscles
Manually annotated by BRENDA team
P20020, Q01814, Q16720
PMCA4 is the most abundant isoform in smooth muscles
Manually annotated by BRENDA team
Q9R0K7
PMCA4 is the most abundant isoform in smooth muscles
Manually annotated by BRENDA team
P20020, Q01814, Q16720
-
Manually annotated by BRENDA team
Q9R0K7
the PMCA4 pump is expressed in spermatozoa
Manually annotated by BRENDA team
P20020, Q01814, Q16720
-
Manually annotated by BRENDA team
Q9R0K7
the PMCA4 pump is expressed in stomach
Manually annotated by BRENDA team
P23220
isoform PMCA 4 is more abundant in the cerebrum than in the cerebellum
Manually annotated by BRENDA team
-
isozyme SPCA2
Manually annotated by BRENDA team
P20020, Q01814, Q16720
PMCA4 is expressed at particularly high levels in the testis (more than 90% of PMCA protein expressed there is isoform 4)
Manually annotated by BRENDA team
Q9R0K7
PMCA4 is expressed at particularly high levels in the testis (more than 90% of PMCA protein expressed there is isoform 4)
Manually annotated by BRENDA team
additional information
-
enzyme expression pattern, overview
Manually annotated by BRENDA team
additional information
-
isozyme SPCA1 is ubiquitously expressed, while SPCA2 is limited to some tissues
Manually annotated by BRENDA team
additional information
-
isozyme SPCA1 shows a less limited tissue distribution than isozyme SPCA2
Manually annotated by BRENDA team
additional information
O75185
SPCA2 expression pattern, overview
Manually annotated by BRENDA team
additional information
-
PMCA1 and PMCA4 isoforms are distributed ubiquitously, PMCA2 and 3 are found mainly in excitable cell types
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Dorytheutis plei
-
giant axon
Manually annotated by BRENDA team
-
SERCA2a transfers Ca2+ from the cytosol of the cardiomyocyte to the lumen of the sarcoplasmic reticulum during muscle relaxation
Manually annotated by BRENDA team
-
the main part of activity of total membrane vesicles results from the enzyme of the Golgi
Manually annotated by BRENDA team
-
the enzyme is intracellular in epidermal keratinocytes
Manually annotated by BRENDA team
-
integral membrane protein
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
in membranes isolated from sporulating bacteria but not from vegetative cells, the expression of enzyme is dependent on the sporulating time
Manually annotated by BRENDA team
-
isozymes SPCA1 and SPCA2
Manually annotated by BRENDA team
-
isoform SERCA3d is observed around the nucleus
Manually annotated by BRENDA team
-
the enzyme has 10 transmembrane helices
Manually annotated by BRENDA team
-
isoform SERCA3f is observed in close vicinity of plasma membrane
Manually annotated by BRENDA team
-
P2B type pumps are expressed at the plasma membrane
Manually annotated by BRENDA team
-
the enzyme is enriched in plasma membranes of the intestinal epithelium
Manually annotated by BRENDA team
-
SERCA2a transfers Ca2+ from the cytosol of the cardiomyocyte to the lumen of the sarcoplasmic reticulum during muscle relaxation
Manually annotated by BRENDA team
-
from the trans-Golgi network, isozyme SPCA2
-
Manually annotated by BRENDA team
-
cortical synaptosome
-
Manually annotated by BRENDA team
-
PCA1 resides in membranes of small vacuoles
Manually annotated by BRENDA team
-
a microsomal fraction enriched in the transverse tubular system (T-tubule)/sarcoplasmic reticulum, SR, complex is prepared
-
Manually annotated by BRENDA team
additional information
-
uniform distribution of SERCA3a
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
-
SDS-PAGE
700190
109200
-
isoform SERCA3a, SDS-PAGE
697167
112600
-
isoform SERCA3f, SDS-PAGE
697167
114100
-
isoform SERCA3d, SDS-PAGE
697167
115000
-
gel filtration
667825
138000
-
-
667623
additional information
-
-
667995
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 120000, SDS-PAGE
?
P11506
x * 135000, SDS-PAGE
?
Q6SLH6
x * 130000, SDS-PAGE
?
-
x * 106000, SDS-PAGE
?
-
x * 115000, SDS-PAGE
?
-
x * 150000, SDS-PAGE
?
-
x * 114700, calculation from nucleotide sequence, SDS-PAGE
?
-
x * 138000, enzyme may exist in both the monomeric and dimeric enzyme form, SDS-PAGE
?
-
x * 100000, isoform SPCA1, SDS-PAGE
?
-
x * 103000, isoform SPCA2, SDS-PAGE
?
Paramecium tetraurelia 7S
-
x * 106000, SDS-PAGE, x * 114700, calculation from nucleotide sequence, SDS-PAGE
-
monomer
-
x * 115000, SDS-PAGE
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
-
PMCA is rich in sphingomyelin-cholesterol domains
additional information
-
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
-
the enzyme contains P-type ATPase subdomains such as the phosphatase region, the phosphorylation site, the FITC labeling site, and the ATP binding site
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
-
phosphoprotein
-
auto-inhibited Ca2+-ATPase
no glycoprotein
-
-
phosphoprotein
-
-
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
proteolytic modification
-
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
side-chain modification
-
contains about 7 mol phosphate per mol of protein
phosphoprotein
Q9R0K7
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
-
-
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
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 20C, X-ray diffraction structure determination and analysis at 3.0 A resolution
-
crystal structure
-
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 4C 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 19C, X-ray diffraction structure determination and analysis at 3.3 A resolution
P04191
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
9
-
PMCA is inhibited at pH 9.0
699293
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the maximal activity is reduced progressively with increasing temperature and time of incubation
656262
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
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
-
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, 10 mM HEPES pH 7.4, no loss in activity
-
-80C, the activity of LCA1 prepared from yeast cells stored at -80C is dramatically reduced when compared to LCA1 prepared from freshly harvested cells
Q42883
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
calmodulin-Sepharose column chromatography
-
nickel-NTA-agarose column chromatography and glutathione-Sepharose column chromatography
-
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
-
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
-
transport-specific fractionation for purification
-
recombinant SERCA2a 3.61fold from insect cell microsomes
-
partially, recombinant enzyme in microsomes of transfected COS-1 cells
-
calmodulin-affinity chromatography
-
calmodulin-Sepharose column chromatography
-
native enzyme from blood by calmodulin affinity chromatography
-
native PMCA4b from erythrocytes by calmodulin affiniyt chromatography
-
partially recombinant isozymes SPCA1 and SPCA2 in HEK293 cell microsomal membranes by differential centrifugation
-
Sepharose-calmodulin column chromatography
-
the protein is purified from healthy mussels by homogenization, centrifugation and passing through sterile gauzes
-
native enzyme from psoas muscle
-
native nezyme from sekeletal muscle sarcoplasmic reticulum membranes by adsorption chromatography
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partially by preparation of sarcoplasmic reticulum vesicles
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partially, preparation of sarcoplasmic reticulum membrane vesicles
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purified on a sucrose step-gradient
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recombinant biotinylated SERCA1a 92fold from Saccharomyces cerevisiae light membrane fraction by avidin affinity chromatography, cleavage of the biotin tag by thrombin, and gel filtration
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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
P04191
wild type and mutant D813A/D818A of the L6-7 loop of enzyme
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Pigeon
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transport-specific fractionation for purification
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native enzyme from brain by calmodulin affinity chromatography to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ECA3 mutant defective in its endogenous Ca21 pumps is expressed in Saccharomyces cerevisiae strain K616; ECA3 mutant defective in its endogenous Ca21 pumps is expressed in Saccharomyces cerevisiae strain K616; ECA3 mutant defective in its endogenous Ca21 pumps is expressed in Saccharomyces cerevisiae strain K616; ECA3 mutant defective in its endogenous Ca21 pumps is expressed in Saccharomyces cerevisiae strain K616
O23087, P92939, Q9SY55, Q9XES1
expressed in Saccharomyces cerevisiae mutant strain K616 devoid of endogenous Ca2+-ATPases
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expressed in Saccharomyces cerevisiae strain K616
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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
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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
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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
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the enzyme is a product of the yloB gene
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gene pmr1, expression pattern, overexpression of truncated pmr1 in transgenic worms
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gene PM1 homologue, DNA and amino acid sequence determination and analysis
Q9P872
expression of wild-type SERCA2a in insect cell membranes using the baculovirus transfection system, process optimization, co-expression of phospholamban, overview
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overexpression of wild-type and mutant SERCA-1s in COS-1 cells membranes using an SV40 vector for transfection
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expressed in HEK-293 cells
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expressed in Saccharomyces cerevisiae strain DBY 2062
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expressed in Sf9 cells
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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
O75185
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
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genes ATP2C genes encoding isozymes 1a-d, expression of isozymes 1a-1d using an SV40 vector, in HEK-293 and COS-1 cells
P98194
genes ATP2C1 and ATP2C2, transient overexpression of isozymes SPCA1 and SPCA2 in HEK293 cell microsomal membranes
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isoforms 3a, b and c, transfection in HEK-293 or COS-1 cells using the calcium phosphate precipitation method
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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
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wild-type and mutant enzymes are transfected in COS-1 cells
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gene PMR1, DNA and amino acid sequence determination and analysis
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expression of C-terminally biotinylated SERCA1a in Saccharomyces cerevisiae strain W3031.b/Gal4, a thrombin cleavage site is inserted
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expression of wild type and mutant D813A/D818A of L6-7 loop of enzyme in yeast
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mutants are expressed in COS-1 cells
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overexpression of C-terminally biotinylated SERCA1a, with introduced thrombin cleavage site, in Saccharomyces cerevisiae
P04191
isolation of gene from the cDNA library
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expressed in a Ca2+ transport-deficient yeast mutant
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PMCA3 DNA and amino acid sequence determination and analysis, phylogenetic tree, expression analysis during molting cycle
Q6SLH6
expressed in Escherichia coli
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transfection in HEK-293 cells
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cloning of PMR1, string and inducible heat shock promoter to direct high level expression of PMR1 from a multicopy plasmid
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expressed in Escherichia coli XL1-Blue cells
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expressed in a Saccharomyces cerevisiae triple mutant defective in both a Golgi and vacuolar Ca2+ pump, strain K616 and strain HI227
Q42883
expressed in Escherichia coli
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expressed in HEK-293 cells
P23220
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform SERCA2b protein and mRNA levels are dramatically reduced in the liver of obese mice
O55143
the expression of the P2B Ca2+ pumps in potato virus X-inoculated plants is significantly higher than in control plants
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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
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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
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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
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stimulation of protein kinase C activity has no effect on SERCA enzyme activity
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R59A
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the mutation lead to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
S19A
-
the mutant shows 95% of wild type activity
S19D
-
the mutant with 163% of wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus
S22A
-
the mutant shows 70% of wild type activity
S22D
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the mutant with wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus
S27A
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the mutant shows 127% of wild type activity
S27D
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the mutant with 89% of wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus
S29A
-
the mutant shows 60% of wild type activity
S29D
-
the mutant shows 64% of wild type activity
S57A
-
the mutant shows 50% of wild type activity
S57D
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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
S99A
-
the mutant shows 78% of wild type activity
S99D
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the mutant with 77% of wild type activity shows half of the wild type affinity towards calmodulin
D351N
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a phosphorylation site mutant, catalytically inactive
E309Q
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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
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the mutation of Ca2+-binding site I leads to no Ca2+ binding to either site, catalytically inactive mutant
F1110A
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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
I274V
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Darier disease causing, 64% activity in comparison to wild-type enzyme
L321F
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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
D813A/D818A
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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
E243G/Q244G
-
the mutant shows wild type-like Ca2+-ATPase activity
E90A
B6CAM1
the mutant shows a reduction of the apparent affinity for luminal Ca2+ and exhibits 19% of wild type activity
E90L
B6CAM1
the mutant shows a reduction of the apparent affinity for luminal Ca2+ and exhibits less than 10% of wild type activity
E90R
B6CAM1
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
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displays about 30% reduced ATP turnover rate relative to wild type, whereas the ATP turnover rate is reduced by about 80%
I188F
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the molecular rate of Ca2+-activated ATP hydrolysis at 37C with 5 mM MgATP is slightly lower (by less than 15%) than that of wild type enzyme, the mutant displays reduced MgATP affinity
K204A
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the mutant displays around 40% Ca2+ transport, compared with its about 70% rate of ATP turnover relative to the wild type enzyme
K205A
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the molecular rate of Ca2+-activated ATP hydrolysis at 37C with 5 mM MgATP slightly lower than that of wild type enzyme
K205E
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the molecular rate of Ca2+-activated ATP hydrolysis at 37C with 5 mM MgATP is slightly lower (by less than 15%) than that of wild type enzyme, the mutant displays reduced MgATP affinity
K234A
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the mutant shows reduced relative Ca2+ ATPase activiy compared to the wild type enzyme
K234G
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the mutant shows reduced relative Ca2+ ATPase activiy compared to the wild type enzyme
N34A
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loss-of-function mutation
R174A
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the molecular rate of Ca2+-activated ATP hydrolysis at 37C 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
R174E
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the mutant displays wild type-like MgATP affinity
S72A
B6CAM1
the mutant exhibits 80% of wild type activity
D366A
Q42883
catalytically inactive
A56S
-
the mutation lead to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
additional information
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the N-deleted mutant DELTA74-ACA8 is also activated by acidic phospholipids
Y62A
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the mutation lead to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
additional information
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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
Q9P872
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
M719I
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Darier disease causing, 69% activity in comparison to wild-type enzyme
additional information
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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
V1107A
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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
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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
K297A
B6CAM1
the mutant exhibits 87% of wild type activity
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
S72R
B6CAM1
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+
additional information
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DELTAPCA1 mutants fail to restore resting Ca2+ levels after salt stress treatments
additional information
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the yeast strain K610, which has the pmr1DELTA mutation, has the highest sensitivity to CdCl2 at a final concentration of 0.02 mM
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
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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
P04191
reconstitution of purified enzyme with phospholamban in proteoliposomes, overview
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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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
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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
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
medicine
-
PMCA4b overexpression significantly reduces cardiac hypertrophy following pressure overload
additional information
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determination of enzyme activity and Ca2+ transport rates in different human muscles types are important for the local anesthetics strategy in dentistry