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7.2.2.10: P-type Ca2+ transporter

This is an abbreviated version!
For detailed information about P-type Ca2+ transporter, go to the full flat file.

Word Map on EC 7.2.2.10

Reaction

ATP
+
H2O
 +
Ca2+[side 1]
=
ADP
 +
phosphate
 +
Ca2+[side 2]

Synonyms

ACA, ACA2, ACA8, adenosinetriphosphatase, AfPMR1, AtECA1, ATP-consuming plasma membrane calcium pump, ATP-dependent Ca(2+) pump PMR1, ATP-dependent Ca2+ pump PMR1, ATP-dependent calcium ATPase, Atp2b, ATP6, ATPase 2C1, auto-inhibited Ca2+-ATPase, autoinhibited Ca2+-ATPase, Ca(2+)-transporting ATPase, Ca-ATPase, Ca2+ -ATPase, Ca2+ ATPase, Ca2+ ATPase of sarcoplasmic reticulum, Ca2+ pump, Ca2+ pumping ATPase, Ca2+ transport ATPase, Ca2+ transport ATPase of sarco-endoplasmic reticulum, Ca2+,Mn2+-ATPase, Ca2+-ATPase, Ca2+-ATPase 6, Ca2+-ATPase 8, Ca2+-ATPase pump, Ca2+-ATPase, isoform 10, Ca2+-ATPase, isoform 11, Ca2+-ATPase, isoform 12, Ca2+-ATPase, isoform 13, Ca2+-dependent ATPase, Ca2+-Mg2+-ATPase, Ca2+-pumping ATPase, Ca2+-transporting ATPase, Ca2+/Mn2+ ATPase pump, Ca2+/Mn2+ P-type ATPase, Ca2+/Mn2+-ATPase 1, Ca2+/Mn2+-ATPase 2, calcium and manganese transporting ATPase, calcium pump, calcium-dependent ATPase, 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, CePMR-1, ChkSERCA3, Cod1 protein, Cod1p, EC 3.6.1.3, EC 3.6.1.38, EC 3.6.3.8, eCA, ECA1, ECA2, ECA3, ECA4, endomembrane Ca2+-ATPase, endoplasmic reticulum class 1/2 Ca(2+) ATPase, endosomal Ca2+/Mn2+ pump, ER-type Ca2+-ATPase, Golgi Ca2+-ATPase, HUSSY-28, LCA, LCA1, Mn2+-transporting P-type ATPase, More, P-type ATPase, P-type Ca2+-ATPase, P-type Ca2+/Mn2+ ATPase, P-type Ca2+/Mn2+-ATPase, P-type calcium ATPase, P2A Ca2+ pump, P2A Ca2+-ATPase, P2B Ca2+ pump, P2B Ca2+-ATPase, PCA1, PCMA4b, PfATP6, phosphatase, adenosine tri, plasma membrane ATPase related 1, plasma membrane Ca-ATPase, plasma membrane Ca2+, plasma membrane Ca2+ ATPase, plasma membrane Ca2+ pump 4xb, plasma membrane Ca2+-ATPase, plasma membrane Ca2+-ATPase 1, plasma membrane Ca2+-ATPase 2, plasma membrane Ca2+-ATPase 4, plasma membrane Ca2+-ATPase 4xb, plasma membrane Ca2+-ATPase isoform 4, plasma membrane Ca2+-ATPase isoform ACA8, plasma membrane Ca2+-ATPase-4, plasma membrane Ca2+-pump, plasma membrane calcium ATPase, plasma membrane calcium ATPase 2 calcium pump, plasma membrane calcium pump, plasma-membrane Ca2+-ATPase, plasmalemmal Ca2+ pump isoform 2, plasmalemmal Ca2+-ATPase, PM Ca2+-ATPase, PMCA, PMCA pump, PMCA1, PMCA2, PMCA3, PMCA4, PMCA4a, PMCA4b, PMR1, PMR1-like calcium ATPase, Pmr1p, sarco(endo)plasmic reticulum ATPase, sarco(endo)plasmic reticulum Ca2+ ATPase, sarco(endo)plasmic reticulum Ca2+-ATPase, sarco(endo)plasmic reticulum Ca2+-ATPase 2b, sarco(endo)plasmic reticulum calcium ATPase, sarco-endoplasmic reticulum Ca2+ ATPase, sarco-endoplasmic reticulum Ca2+-ATPase, sarco/endoplasmic reticulum Ca2+ ATPase, sarco/endoplasmic reticulum Ca2+ ATPase 3, sarco/endoplasmic reticulum Ca2+-ATPase, sarco/endoplasmic reticulum calcium ATPase, sarcoendoplasmic reticulum Ca2+ ATPase6, sarcoendoplasmic reticulum Ca2+-ATPase, sarcoendoplasmic reticulum Ca2+-ATPase isoform 1a, sarcoendoplasmic reticulum calcium ATPase, sarcolemmal Ca2+-ATPase, sarcoplasmic reticulum (Ca2+)-ATPase, sarcoplasmic reticulum ATPase, sarcoplasmic reticulum Ca(2+)-ATPase, sarcoplasmic reticulum Ca-ATPase, sarcoplasmic reticulum Ca2+ ATPase, sarcoplasmic reticulum Ca2+ ATPase 1, sarcoplasmic reticulum Ca2+ ATPase 2, sarcoplasmic reticulum Ca2+ ATPase pump, sarcoplasmic reticulum Ca2+-ATPase, sarcoplasmic reticulum Ca2+-ATPase 1, sarcoplasmic reticulum Ca2+-pump ATPase, sarcoplasmic reticulum calcium ATPase, sarcoplasmic reticulum calcium pump, sarcoplasmic reticulum calcium-dependent adenosine triphosphatase, sarcoplasmic-endoplasmic reticulum Ca2+-ATPase, sarcoplasmic/endoplasmic reticulum Ca2+ ATPase, sarcoplasmic/endoplasmic reticulum Ca2+-ATPase, sarcoplasmic/endoplasmic reticulum calcium ATPase, secretory pathway Ca-ATPase, Secretory pathway Ca2+ transporting ATPase, secretory pathway Ca2+-ATPase, secretory pathway Ca2+-ATPase 1, secretory pathway Ca2+/Mn2+-ATPase, SERCA, SERCA 1, SERCA 2, SERCA 3, SERCA pump, SERCA-1, SERCA-like calcium ATPase, SERCA1, SERCA1a, SERCA1b, SERCA2, SERCA2a, SERCA2b, SERCA3, SERCA3a, SERCA3b, SERCA3c, SERCA3d, SERCA3f, SMA1, SPCA, SPCA1, SPCA2, Spf1, SR Ca-ATPase, SR Ca2+-ATPase, Vacuolar Ca2+-ATPase

ECTree

     7 Translocases
         7.2 Catalysing the translocation of inorganic cations
             7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
                7.2.2.10 P-type Ca2+ transporter

Engineering

Engineering on EC 7.2.2.10 - P-type Ca2+ transporter

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A56S
-
the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
R123I
site-directed mutagenesis, when Arg123 of ShMTP1 is mutated to Ile, the ability to confer Mn tolerance to either yeast or Arabidopsis is completely lost
R59A
-
the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
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
the mutant with wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus
S27A
the mutant shows 127% of wild type activity
S27D
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
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
the mutant with 77% of wild type activity shows half of the wild type affinity towards calmodulin
Y62A
-
the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
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
D203R
the mutant shows an about 5fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
D203R/R678D
the mutant shows an about 3.5fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
D813A/D818A
-
the mutant displays a very low activity in presence of detergent, but the same maximal velocity and apparent affinity for Ca2+ as the wild-type enzyme in absence of detergent, the mutation affects pronotation-dependent winding and unwinding events in the nearby M6 transmembrane segment
E243G/Q244G
-
the mutant shows wild type-like Ca2+-ATPase activity
E439A
the mutant shows an about 15fold basal dephosphorylation rate constant compared to the wild type enzyme
E439S
the mutant shows an about 10fold basal dephosphorylation rate constant compared to the wild type enzyme
E90A
the mutant shows a reduction of the apparent affinity for luminal Ca2+ and exhibits 19% of wild type activity
E90L
the mutant shows a reduction of the apparent affinity for luminal Ca2+ and exhibits less than 10% of wild type activity
E90R
the mutation allows E2P formation from phosphate even at luminal Ca2+ concentrations much too small to support phosphorylation in wild type. The mutant with less than 10% of wild type activity further displays a blocked dephosphorylation of E2P and an increased rate of conversion of the ADP-sensitive E1P phosphoenzyme intermediate to ADP-insensitive E2P as well as insensitivity of the E2-BeF3-complex to luminal Ca2+
I188A
-
displays about 30% reduced ATP turnover rate relative to wild type, whereas the ATP turnover rate is reduced by about 80%
I188F
-
the molecular rate of Ca2+-activated ATP hydrolysis at 37°C with 5 mM MgATP is slightly lower (by less than 15%) than that of wild type enzyme, the mutant displays reduced MgATP affinity
K204A
-
the mutant displays around 40% Ca2+ transport, compared with its about 70% rate of ATP turnover relative to the wild type enzyme
K205A
-
the molecular rate of Ca2+-activated ATP hydrolysis at 37°C with 5 mM MgATP slightly lower than that of wild type enzyme
K205E
-
the molecular rate of Ca2+-activated ATP hydrolysis at 37°C with 5 mM MgATP is slightly lower (by less than 15%) than that of wild type enzyme, the mutant displays reduced MgATP affinity
K234A
-
the mutant shows reduced relative Ca2+ ATPase activiy compared to the wild type enzyme
K234G
-
the mutant shows reduced relative Ca2+ ATPase activiy compared to the wild type enzyme
K297A
the mutant exhibits 87% of wild type activity
N34A
loss-of-function mutation
Q202A
th mutation causes reduced Ca2+ transport and ATPase activity
Q202A/D203A
the mutant shows an about 4fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
R174A
-
the molecular rate of Ca2+-activated ATP hydrolysis at 37°C with 5 mM MgATP is similar to, or slightly lower than (by less than 15%) that of wild type enzyme, the mutant displays wild type-like MgATP affinity
R174E
-
the mutant displays wild type-like MgATP affinity
R678A
the mutant shows a reduced basal dephosphorylation rate constant compared to the wild type enzyme
R678D
the mutant shows an about 6fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
R678Q
the mutant shows an about 1.4fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
S186A
the mutant shows an about 6fold increased basal dephosphorylation rate constant compared to the wild type enzyme
S186E
the mutant shows an about 1,2fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
S186E/E439S
the mutant restores the basal dephosphorylation rate to a level about 2fold faster than that of the wild type. Little stimulation of the dephosphorylation by ATPis seen in this mutant
S186P
the mutant shows an about 18fold increased basal dephosphorylation rate constant compared to the wild type enzyme
S72A
the mutant exhibits 80% of wild type activity
S72R
the mutation allows E2P formation from phosphate even at luminal Ca2+ concentrations much too small to support phosphorylation in wild type. The mutant with less than 10% of wild type activity further displays a blocked dephosphorylation of E2P and an increased rate of conversion of the ADP-sensitive E1P phosphoenzyme intermediate to ADP-insensitive E2P as well as insensitivity of the E2-BeF3-complex to luminal Ca2+
S766C
the mutation of isoform SERCA1a strongly reduces the apparent Ca2+ affinity and ATPase activity of the enzyme
S766L
the mutation of isoform SERCA1a strongly reduces the apparent Ca2+ affinity and ATPase activity of the enzyme
S766V
the mutation of isoform SERCA1a strongly reduces the apparent Ca2+ affinity and ATPase activity of the enzyme
D100A
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
D136A
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
D100A
-
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
-
D136A
-
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
-
D354A
-
the mutant enzyme is not getting phosphorylated
D366A
catalytically inactive
additional information