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Information on EC 7.2.2.10 - P-type Ca2+ transporter and Organism(s) Homo sapiens and UniProt Accession Q01814

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IUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria. The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolysed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolysed. In muscle cells Ca2+ is transported from the cytosol (side 1) into the sarcoplasmic reticulum (side 2).
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Homo sapiens
UNIPROT: Q01814
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
serca, ca2+-atpase, serca2a, ca2+ pump, serca2, ca-atpase, calcium pump, ca2+ atpase, serca1, serca2b, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+ ATPase
-
plasma membrane calcium ATPase
-
PMCA pump
-
PMCA2
isoform
ATP-consuming plasma membrane calcium pump
-
-
ATP-dependent Ca(2+) pump PMR1
-
ATP-dependent Ca2+ pump PMR1
-
-
-
-
ATPase 2C1
Ca2+ ATPase
Ca2+,Mn2+-ATPase
-
-
Ca2+-ATPase
-
-
Ca2+-ATPase pump
-
-
Ca2+-ATPase, isoform 10
-
-
-
-
Ca2+-ATPase, isoform 11
-
-
-
-
Ca2+-ATPase, isoform 12
-
-
-
-
Ca2+-ATPase, isoform 13
-
-
-
-
Ca2+-pumping ATPase
-
-
-
-
Ca2+-transporting ATPase
-
-
-
-
Ca2+/Mn2+-ATPase 1
-
Ca2+/Mn2+-ATPase 2
-
calcium pump
-
-
-
-
Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform
-
-
-
-
Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
-
-
-
-
calcium-transporting ATPase type 2C member 1
-
ChkSERCA3
-
-
-
-
endoplasmic reticulum class 1/2 Ca(2+) ATPase
-
-
-
-
Golgi Ca2+-ATPase
-
-
-
-
HUSSY-28
-
-
-
-
P-type calcium ATPase
-
-
-
-
PCMA4b
-
-
phosphatase, adenosine tri
-
-
-
-
plasma membrane Ca-ATPase
-
-
-
-
plasma membrane Ca2+
-
-
plasma membrane Ca2+ ATPase
-
-
plasma membrane Ca2+ pump 4xb
-
isoform
plasma membrane Ca2+-ATPase
-
-
plasma membrane Ca2+-ATPase 2
-
-
plasma membrane Ca2+-ATPase 4
-
-
plasma membrane Ca2+-ATPase 4xb
-
isoform
plasma membrane Ca2+-pump
-
-
plasma membrane calcium ATPase
plasma membrane calcium pump
-
-
plasma-membrane Ca2+-ATPase
-
-
plasmalemmal Ca2+ pump isoform 2
-
-
PMCA1
PMCA2
PMCA3
PMCA4
sarco(endo)plasmic reticulum ATPase
-
-
sarco(endo)plasmic reticulum Ca2+-ATPase
-
-
-
-
sarco/endoplasmic reticulum Ca2+ ATPase 3
-
-
sarcoendoplasmic reticulum calcium ATPase
-
-
sarcoplasmic reticulum ATPase
-
-
-
-
sarcoplasmic reticulum Ca2+ ATPase 2
-
-
sarcoplasmic reticulum Ca2+ ATPase pump
-
-
sarcoplasmic reticulum Ca2+-ATPase
-
-
sarcoplasmic reticulum Ca2+-ATPase 1
-
-
sarcoplasmic/endoplasmic reticulum Ca2+ ATPase
-
-
sarcoplasmic/endoplasmic reticulum calcium ATPase
-
-
Secretory pathway Ca2+ transporting ATPase
-
-
-
-
secretory pathway Ca2+/Mn2+-ATPase
-
-
SERCA
SERCA 1
-
-
SERCA1
SERCA1b
-
-
SERCA2
SERCA2a
-
isoform
SERCA2b
-
-
SERCA3
SERCA3a
-
isoform
SERCA3b
-
isoform
SERCA3c
-
isoform
SERCA3d
-
isoform
SERCA3f
-
isoform
SPCA1
SPCA2
-
-
SR Ca2+-ATPase
-
-
Vacuolar Ca2+-ATPase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, Ca2+-transporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria. The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolysed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolysed. In muscle cells Ca2+ is transported from the cytosol (side 1) into the sarcoplasmic reticulum (side 2).
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
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
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
show the reaction diagram
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+[side 1] + H+[side 2]
ADP + phosphate + Ca2+[side 2] + H+[side 1]
show the reaction diagram
-
-
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
show the reaction diagram
UTP + H2O + Ca2+/in
UDP + phosphate + Ca2+/out
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
show the reaction diagram
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
show the reaction diagram
-
-
-
-
?
ATP + H2O + Ca2+[side 1] + H+[side 2]
ADP + phosphate + Ca2+[side 2] + H+[side 1]
show the reaction diagram
-
-
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
dependent on, at very low Ca2+ concentrations the PMCA is nearly inactive, unstimulated PMCA pumps have poor affinity for Ca2+
Calmodulin
-
PMCA is dependent on Ca2+-calmodulin
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4,4'-diisothiocyano-2,2'-stilbenedisulfonic acid
-
-
aluminium fluoride
-
the inhibition by aluminium fluoride is dependend on Mg2+ concentration
amyloid beta-peptide
-
the addition of amyloid beta-peptide to normal brain decreases the PMCA activity resulting in the same Ca2+ dependency as that seen in Alzheimer's disease brain, whereas the addition of amyloid beta-peptide to Alzheimer's disease brain has no effect on PMCA activity, in the absence of cholesterol, the level of inhibition of cerebrum PMCA is 60%, but levels of inhibition decreases with increasing concentrations of cholesterol
-
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.
-
beryllium fluoride
-
the inhibition by beryllium fluoride is dependend on Mg2+ concentration
calmodulin antagonist compound 48/80
-
inhibits phosphatase activity
chlorpromazine
-
non-competitive inhibition, complete inhibition at 1 mM
cyclopiazonic acid
-
specific inhibitor
dimethyl sulfoxide
-
-
erythrosine B
-
-
magnesium fluoride
-
the inhibition by magnesium fluoride is dependend on Mg2+ concentration
Mg2+
-
competitive Mg2+ binding can occur at Ca2+ binding site I but not at site II
N-4-(azido-2-nitrophenyl)-2-aminoethylsulfonate
-
-
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
-
sarcolipin
-
-
-
Sodium fluoride
-
the inhibition by magnesium fluoride is dependend on Mg2+ concentration. The enzyme is totally inhibited by NaF at total Mg2+ concentrations higher than 3.5 mM
thapsigargin
-
inhibits SERCA activity
vanadate
Zn2+
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
activated by calmodulin
calpain
cleavage of PMCA by calpain activates it irreversibly
-
phosphatidylinositol bisphosphate
the most active in stimulating PMCA activity
Ca2+
-
-
Calmodulin
calpain
cleavage of PMCA by calpain activates it irreversibly
-
G-actin
-
when purified enzyme is incubated with increasing concentrations of G-actin, an increase in the rate of ATP hydrolysis is observed
-
phosphatidylinositol bisphosphate
the most active in stimulating PMCA activity
phosphatidylserine
-
can replace calmodulin in shifting the enzyme to the high-affinity form
Trypsin
-
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000021
ATP
-
enzyme from liver
0.000013 - 0.02
Ca2+
0.000037
UTP
-
enzyme from liver
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5 - 130
ATP
90 - 149
Ca2+
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012
aluminium fluoride
-
in the presence of 4 mM Mg2+, at pH 7.2 and 37°C
0.00382
beryllium fluoride
-
in the presence of 4 mM Mg2+, at pH 7.2 and 37°C
0.00314
Sodium fluoride
-
in the presence of 4 mM Mg2+, at pH 7.2 and 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.085 - 0.42
chlorpromazine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.19
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
7.4
-
assay at
7.5
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 hide
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the PMCA2 pump is a brain isoform
Manually annotated by BRENDA team
PMCA2 is highly expressed in cerebellar Purkinje cells
Manually annotated by BRENDA team
PMCA2 is expressed at a lower level in the heart
Manually annotated by BRENDA team
PMCA2 is highly expressed in the hair cells of the inner ear
Manually annotated by BRENDA team
the brain isoform PMCA2 pump is also expressed in the lactating mammary glands
Manually annotated by BRENDA team
-
CF-41o cell, CF-45o cell
Manually annotated by BRENDA team
-
and nonpolarized cells, isozyme SPCA1
Manually annotated by BRENDA team
-
primary, isozyme SPCA2 shows a highly punctate distribution
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
SERCA2a transfers Ca2+ from the cytosol of the cardiomyocyte to the lumen of the sarcoplasmic reticulum during muscle relaxation
Manually annotated by BRENDA team
-
isoform SERCA3d is observed around the nucleus
Manually annotated by BRENDA team
-
from the trans-Golgi network, isozyme SPCA2
Manually annotated by BRENDA team
additional information
-
uniform distribution of SERCA3a
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AT2B2_HUMAN
1243
8
136876
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
109200
-
isoform SERCA3a, SDS-PAGE
112600
-
isoform SERCA3f, SDS-PAGE
114100
-
isoform SERCA3d, SDS-PAGE
138000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
no glycoprotein
-
-
phosphoprotein
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D351N
-
a phosphorylation site mutant, catalytically inactive
E309Q
-
the mutation of Ca2+-binding site II leads to non-cooperative binding of only one Ca2+, and loss of ATPase activation, catalytically inactive mutant
E771Q
-
the mutation of Ca2+-binding site I leads to no Ca2+ binding to either site, catalytically inactive mutant
F1110A
-
2-chloro-(epsilon-amino-Lys75)-[6-(4-[N,N-diethylamino]phenyl)-1,3,5-triazin]-4-yl-calmodulin-labeled calmodulin is used for determination of enzyme amino acids essential for binding, peptide mapping with full-length binding site peptide 28 and truncated and mutated versions, overview
I274V
-
Darier disease causing, 64% activity in comparison to wild-type enzyme
L321F
-
Darier disease causing mutant, the mutant has the dramatically reduced sensitivity to the feedback inhibition by the accumulated lumenal Ca2+, the insensitivity to luminal Ca2+ raises this ion to an abnormally elevated level, 100% activity in comparison to wild-type enzyme
M719I
-
Darier disease causing, 69% activity in comparison to wild-type enzyme
R268Q
-
the mutation in isoform PMCA4 is likely causative for autosomal dominant familial spastic paraplegia
V1107A
-
2-chloro-(epsilon-amino-Lys75)-[6-(4-[N,N-diethylamino]phenyl)-1,3,5-triazin]-4-yl-calmodulin-labeled calmodulin is used for determination of enzyme amino acids essential for binding, peptide mapping with full-length binding site peptide 28 and truncated and mutated versions, overview
additional information
-
2-chloro-(epsilon-amino-Lys75)-[6-(4-[N,N-diethylamino]phenyl)-1,3,5-triazin]-4-yl-calmodulin-labeled calmodulin is used for determination of enzyme amino acids essential for binding, peptide mapping with full-length binding site peptide 28 and truncated and mutated versions, overview
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
-80°C, 10 mM HEPES pH 7.4, no loss in activity
-
4°C, purified enzyme in the detergent-solubilized form, several days, rapid loss of activity
-
4°C, purified enzyme in the reconstituted form, several days, little loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
Sepharose-calmodulin column chromatography, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293 cells
-
expressed in PC-12 cells
-
expressed in Saccharomyces cerevisiae strain DBY 2062
-
expressed in Sf9 cells
-
gene ATP2C2, expression pattern, chromosomal localization 16q24.1, the genes ATP2C1 and ATP2C2 present an identical exon/intron layout, overview, functional expression of SPCA2 in COS-1 cell microsomes
gene ATP2C2, isozyme SPCA2, DNA and amino acid sequence determination and analysis, expression in Mn2+-sensitive pmr1 null mutant strain K616 of Saccharomyces cerevisiae, isozyme SPCA2 complements better than isozyme SPCA1
-
genes ATP2C genes encoding isozymes 1a-d, expression of isozymes 1a-1d using an SV40 vector, in HEK-293 and COS-1 cells
genes ATP2C1 and ATP2C2, transient overexpression of isozymes SPCA1 and SPCA2 in HEK293 cell microsomal membranes
-
isoforms 3a, b and c, transfection in HEK-293 or COS-1 cells using the calcium phosphate precipitation method
-
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
-
wild-type and mutant enzymes are transfected in COS-1 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CCL21 does not affect the mRNA levels of the enzyme
-
CCL21 inhibits enzyme expression through phospholipase C and protein kinase C
-
enzyme protein expression is up-regulated after 30 min in CCL21-treated dendritic cells
-
placental explants cultured under hypoxia in the presence of 4mM MgSO4 show similar values of Ca2+-ATPase activity of their membranes compared to those of explants cultured under normoxia
-
PMCA2 mRNA levels are enriched in basal breast cancer cells
-
syncytiotrophoblast plasma membranes of placental explants cultured under hypoxia diminish their Ca2+-ATPase activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Carafoli, E.; Zurini, M.
The Ca2+-pumping ATPase of plasma membranes. Purification, reconstitution and properties
Biochim. Biophys. Acta
683
279-301
1982
Homo sapiens
Manually annotated by BRENDA team
Rossi, J.P.F.C.; Garrahan, P.J.; Rega, A.F.
Differential effects of compound 48/80 on the ATPase and phosphatase activities of the Ca2+ pump of red cells
Biochim. Biophys. Acta
902
101-108
1987
Homo sapiens
Manually annotated by BRENDA team
Vicenzi, F.F.; Ashleman, B.T.
Calmodulin stimulated calcium pump ATPase: inhibition by zinc and vanadate
Calcium-binding Proteins, Structure and Function (Siegel, F. L. , Carafoli, E. , Kretsinger, R. H. , MacLennan, D. H. , Wasserman, R. H. , eds. )
173-179
1980
Homo sapiens
-
Manually annotated by BRENDA team
Carafoli, E.
The Ca2+ pump of the plasma membrane
J. Biol. Chem.
267
2115-2118
1992
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Dean, W.L.
Isolation and reconstitution of Ca2+-pump from human and porcine platelets
Methods Enzymol.
157
351-360
1988
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Dode, L.; Vilsen, B.; Van Baelen, K.; Wuytack, F.; Clausen, J.D.; Andersen, J.P.
Dissection of the functional differences between sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) 1 and 3 isoforms by steady-state and transient kinetic analyses
J. Biol. Chem.
277
45579-45591
2002
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Sato, K.; Yamasaki, K.; Daiho, T.; Miyauchi, Y.; Takahashi, H.; Ishida-Yamamoto, A.; Nakamura, S.; Iizuka, H.; Suzuki, H.
Distinct types of abnormality in kinetic properties of three Darier disease-causing sarco(endo)plasmic reticulum Ca2+-ATPase mutants that exhibit normal expression and high Ca2+ transport activity
J. Biol. Chem.
279
35595-35603
2004
Homo sapiens
Manually annotated by BRENDA team
Moreau, R.; Daoud, G.; Masse, A.; Simoneau, L.; Lafond, J.
Expression and role of calcium-ATPase pump and sodium-calcium exchanger in differentiated trophoblasts from human term placenta
Mol. Reprod. Dev.
65
283-288
2003
Homo sapiens
Manually annotated by BRENDA team
Osborn, K.D.; Zaidi, A.; Urbauer, R.J.; Michaelis, M.L.; Johnson, C.K.
Single-molecule characterization of the dynamics of calmodulin bound to oxidatively modified plasma-membrane Ca2+-ATPase
Biochemistry
44
11074-11081
2005
Homo sapiens
Manually annotated by BRENDA team
Penheiter, A.R.; Filoteo, A.G.; Penniston, J.T.; Caride, A.J.
Kinetic analysis of the calmodulin-binding region of the plasma membrane calcium pump isoform 4b
Biochemistry
44
2009-2020
2005
Homo sapiens
Manually annotated by BRENDA team
Xiang, M.; Mohamalawari, D.; Rao, R.
A novel isoform of the secretory pathway Ca2+,Mn(2+)-ATPase, hSPCA2, has unusual properties and is expressed in the brain
J. Biol. Chem.
280
11608-11614
2005
Homo sapiens
Manually annotated by BRENDA team
Vanoevelen, J.; Dode, L.; Van Baelen, K.; Fairclough, R.J.; Missiaen, L.; Raeymaekers, L.; Wuytack, F.
The secretory pathway Ca2+/Mn2+-ATPase 2 is a Golgi-localized pump with high affinity for Ca2+ ions
J. Biol. Chem.
280
22800-22808
2005
Homo sapiens (O75185), Homo sapiens
Manually annotated by BRENDA team
Dode, L.; Andersen, J.P.; Raeymaekers, L.; Missiaen, L.; Vilsen, B.; Wuytack, F.
Functional comparison between secretory pathway Ca2+/Mn2+-ATPase (SPCA) 1 and sarcoplasmic reticulum Ca2+-ATPase (SERCA) 1 isoforms by steady-state and transient kinetic analyses
J. Biol. Chem.
280
39124-39134
2005
Homo sapiens, Homo sapiens (P98194)
Manually annotated by BRENDA team
Dode, L.; Andersen, J.P.; Vanoevelen, J.; Raeymaekers, L.; Missiaen, L.; Vilsen, B.; Wuytack, F.
Dissection of the functional differences between human secretory pathway Ca2+/Mn2+-ATPase (SPCA) 1 and 2 isoenzymes by steady-state and transient kinetic analyses
J. Biol. Chem.
281
3182-3189
2006
Homo sapiens
Manually annotated by BRENDA team
Ahmad, S.; Ahmad, A.; Dremina, E.S.; Sharov, V.S.; Guo, X.; Jones, T.N.; Loader, J.E.; Tatreau, J.R.; Perraud, A.L.; Schoeneich, C.; Randell, S.H.; White, C.W.
Bcl-2 suppresses sarcoplasmic/endoplasmic reticulum Ca2+-ATPase expression in cystic fibrosis airways: role in oxidant-mediated cell death
Am. J. Respir. Crit. Care Med.
179
816-826
2009
Homo sapiens
Manually annotated by BRENDA team
Di Leva, F.; Domi, T.; Fedrizzi, L.; Lim, D.; Carafoli, E.
The plasma membrane Ca2+ ATPase of animal cells: structure, function and regulation
Arch. Biochem. Biophys.
476
65-74
2008
Homo sapiens, Homo sapiens (P20020), Homo sapiens (Q01814), Homo sapiens (Q16720), Mus musculus (Q9R0K7)
Manually annotated by BRENDA team
Cura, C.I.; Corradi, G.R.; Rinaldi, D.E.; Adamo, H.P.
High sensibility to reactivation by acidic lipids of the recombinant human plasma membrane Ca2+-ATPase isoform 4xb purified from Saccharomyces cerevisiae
Biochim. Biophys. Acta
1778
2757-2764
2008
Homo sapiens
Manually annotated by BRENDA team
Zylinska, L.; Kowalska, I.; Ferenc, B.
Calmodulin effects on steroids-regulated plasma membrane calcium pump activity
Cell Biochem. Funct.
27
111-117
2009
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Dally, S.; Monceau, V.; Corvazier, E.; Bredoux, R.; Raies, A.; Bobe, R.; del Monte, F.; Enouf, J.
Compartmentalized expression of three novel sarco/endoplasmic reticulum Ca2+ ATPase 3 isoforms including the switch to ER stress, SERCA3f, in non-failing and failing human heart
Cell Calcium
45
144-154
2009
Homo sapiens
Manually annotated by BRENDA team
Bookchin, R.M.; Etzion, Z.; Lew, V.L.; Tiffert, T.
Preserved function of the plasma membrane calcium pump of red blood cells from diabetic subjects with high levels of glycated haemoglobin
Cell Calcium
45
260-263
2009
Homo sapiens
Manually annotated by BRENDA team
Berrocal, M.; Marcos, D.; Sepulveda, M.R.; Perez, M.; Avila, J.; Mata, A.M.
Altered Ca2+ dependence of synaptosomal plasma membrane Ca2+-ATPase in human brain affected by Alzheimers disease
FASEB J.
23
1826-1834
2009
Homo sapiens, Sus scrofa (P23220), Sus scrofa
Manually annotated by BRENDA team
Mangialavori, I.; Giraldo, A.M.; Buslje, C.M.; Gomes, M.F.; Caride, A.J.; Rossi, J.P.
A new conformation in sarcoplasmic reticulum calcium pump and plasma membrane Ca2+ pumps revealed by a photoactivatable phospholipidic probe
J. Biol. Chem.
284
4823-4828
2009
Homo sapiens, Oryctolagus cuniculus (P20647)
Manually annotated by BRENDA team
Kawase, Y.; Hajjar, R.J.
The cardiac sarcoplasmic/endoplasmic reticulum calcium ATPase: a potent target for cardiovascular diseases
Nat. Clin. Pract. Cardiovasc. Med.
5
554-565
2008
Homo sapiens
Manually annotated by BRENDA team
Mandal, A.; Liyanage, M.R.; Zaidi, A.; Johnson, C.K.
Interchange of autoinhibitory domain conformations in plasma-membrane Ca2+-ATPase-calmodulin complexes
Protein Sci.
17
555-562
2008
Homo sapiens
Manually annotated by BRENDA team
Liu, Y.; Pilankatta, R.; Lewis, D.; Inesi, G.; Tadini-Buoninsegni, F.; Bartolommei, G.; Moncelli, M.R.
High-yield heterologous expression of wild type and mutant Ca2+ ATPase: characterization of Ca(2+) binding sites by charge transfer
J. Mol. Biol.
391
858-871
2009
Homo sapiens
Manually annotated by BRENDA team
Ferreira-Gomes, M.S.; Gonzalez-Lebrero, R.M.; de la Fuente, M.C.; Strehler, E.E.; Rossi, R.C.; Rossi, J.P.
Calcium occlusion in plasma membrane Ca2+-ATPase
J. Biol. Chem.
286
32018-32025
2011
Homo sapiens
Manually annotated by BRENDA team
Alexander, R.T.; Beggs, M.R.; Zamani, R.; Marcussen, N.; Frische, S.; Dimke, H.
Ultrastructural and immunohistochemical localization of plasma membrane Ca2+-ATPase 4 in Ca2+-transporting epithelia
Am. J. Physiol. Renal Physiol.
309
F604-F616
2015
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Strehler, E.E.
Plasma membrane calcium ATPases: From generic Ca2+ sump pumps to versatile systems for fine-tuning cellular Ca2+
Biochem. Biophys. Res. Commun.
460
26-33
2015
Homo sapiens
Manually annotated by BRENDA team
Chiarello, D.I.; Marin, R.; Proverbio, F.; Benzo, Z.; Pinero, S.; Botana, D.; Abad, C.
Effect of hypoxia on the calcium and magnesium content, lipid peroxidation level, and Ca2+-ATPase activity of syncytiotrophoblast plasma membranes from placental explants
BioMed Res. Int.
2014
597357
2014
Homo sapiens
Manually annotated by BRENDA team
Dalghi, M.G.; Fernandez, M.M.; Ferreira-Gomes, M.; Mangialavori, I.C.; Malchiodi, E.L.; Strehler, E.E.; Rossi, J.P.
Plasma membrane calcium ATPase activity is regulated by actin oligomers through direct interaction
J. Biol. Chem.
288
23380-23393
2013
Homo sapiens
Manually annotated by BRENDA team
Kosa, M.; Brinyiczki, K.; van Damme, P.; Goemans, N.; Hancsak, K.; Mendler, L.; Zador, E.
The neonatal sarcoplasmic reticulum Ca2+-ATPase gives a clue to development and pathology in human muscles
J. Muscle Res. Cell Motil.
36
195-203
2015
Homo sapiens
Manually annotated by BRENDA team
Boczek, T.; Lisek, M.; Ferenc, B.; Kowalski, A.; Stepinski, D.; Wiktorska, M.; Zylinska, L.
Plasma membrane Ca2+-ATPase isoforms composition regulates cellular pH homeostasis in differentiating PC12 cells in a manner dependent on cytosolic Ca2+ elevations
PLoS ONE
9
e102352
2014
Homo sapiens
Manually annotated by BRENDA team
Niggli, V.; Carafoli, E.
The plasma membrane Ca2+ ATPase Purification by calmodulin affinity chromatography, and reconstitution of the purified protein
Methods Mol. Biol.
1377
57-70
2016
Homo sapiens
Manually annotated by BRENDA team
Saffioti, N.A.; de Sautu, M.; Ferreira-Gomes, M.S.; Rossi, R.C.; Berlin, J.; Rossi, J.P.F.C.; Mangialavori, I.C.
E2P-like states of plasma membrane Ca2+-ATPase characterization of vanadate and fluoride-stabilized phosphoenzyme analogues
Biochim. Biophys. Acta Biomembr.
1861
366-379
2019
Homo sapiens
Manually annotated by BRENDA team
Hong, C.; Lee, H.; Choi, N.; Jung, S.; Vo, M.; Hoang, M.; Kim, H.; Lee, J.
Sarcoplasmic reticulum Ca2+ ATPase 2 (SERCA2) reduces the migratory capacity of CCL21-treated monocyte-derived dendritic cells
Exp. Mol. Med.
48
e253
2016
Homo sapiens
Manually annotated by BRENDA team
Plenge-Tellechea, F.; Dominguez-Solis, C.A.; Diaz-Sanchez, A.G.; Melendez-Martinez, D.; Vargas-Medrano, J.; Sierra-Fonseca, J.A.
Chlorpromazine and dimethyl sulfoxide modulate the catalytic activity of the plasma membrane Ca2+-ATPase from human erythrocyte
J. Bioenerg. Biomembr.
50
59-69
2018
Homo sapiens
Manually annotated by BRENDA team
Espinoza-Fonseca, L.M.
The Ca2+-ATPase pump facilitates bidirectional proton transport across the sarco/endoplasmic reticulum
Mol. Biosyst.
13
633-637
2017
Homo sapiens
Manually annotated by BRENDA team
Guglielmi, V.; Oosterhof, A.; Voermans, N.; Cardani, R.; Molenaar, J.; van Kuppevelt, T.; Meola, G.; van Engelen, B.; Tomelleri, G.; Vattemi, G.
Characterization of sarcoplasmic reticulum Ca2+ ATPase pumps in muscle of patients with myotonic dystrophy and with hypothyroid myopathy
Neuromuscul. Disord.
26
378-385
2016
Homo sapiens
Manually annotated by BRENDA team
Peters, A.; Milevskiy, M.; Lee, W.; Curry, M.; Smart, C.; Saunus, J.; Reid, L.; Da Silva, L.; Marcial, D.; Dray, E.; Brown, M.; Lakhani, S.; Roberts-Thomson, S.; Monteith, G.
The calcium pump plasma membrane Ca2+-ATPase 2 (PMCA2) regulates breast cancer cell proliferation and sensitivity to doxorubicin
Sci. Rep.
6
25505
2016
Homo sapiens
Manually annotated by BRENDA team