Information on EC 7.2.2.10 - P-type Ca2+ transporter and Organism(s) Oryctolagus cuniculus and UniProt Accession P04191

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ATP + H2O + Ca2+/cis

ADP + phosphate + Ca2+/trans

6 entries

ATP + H2O + Ca2+/out

ADP + phosphate + Ca2+/in

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?

ATP + H2O + Ca2+[side 1]

ADP + phosphate + Ca2+[side 2]

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734209, 734516, 750543, 751099

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?

ATP + H2O + Mn2+[side 1]

ADP + phosphate + Mn2+[side 2]

the enzyme has a much lower affinity for Mn2+ than for Ca2+

750543

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?

2,4-dinitrophenyl phosphate + H2O + Ca2+/in

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?

acyl-carrier protein + H2O + Ca2+/in

?

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?

ADP + phosphate + Ca2+/in

ATP + H2O + Ca2+/out

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r

ATP + H2O

ADP + phosphate

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?

ATP + H2O + 2 Ca2+[cytoplasm side]

ADP + phosphate + 2 Ca2+[lumen side]

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?

ATP + H2O + 2 Ca2+[side 1]

ADP + phosphate + 2 Ca2+[side 2]

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733861

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?

ATP + H2O + Ca2+/cis

ADP + phosphate + Ca2+/trans

11 entries

ATP + H2O + Ca2+/out

ADP + phosphate + Ca2+/in

11 entries

ATP + H2O + Ca2+[side 1]

ADP + phosphate + Ca2+[side 2]

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733829, 750181, 750217

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?

ATP + H2O + Sr2+/in

ADP + phosphate + Sr2+/out

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?

ATP + Sr2+/cis + H2O

ADP + phosphate + Sr2+/trans

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?

GTP + H2O + Ca2+/in

GDP + phosphate + Ca2+/out

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?

p-nitrophenyl phosphate + H2O + Ca2+/in

?

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?

UTP + H2O + Ca2+/in

UDP + phosphate + Ca2+/out

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?

additional information

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11 entries

ATP + H2O + 2 Ca2+[side 1]

ADP + phosphate + 2 Ca2+[side 2]

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?

ATP + H2O + Ca2+/cis

ADP + phosphate + Ca2+/trans

ATP + H2O + Ca2+[side 1]

ADP + phosphate + Ca2+[side 2]

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734209, 734516, 750543, 751099

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?

ATP + H2O

ADP + phosphate

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?

ATP + H2O + 2 Ca2+[cytoplasm side]

ADP + phosphate + 2 Ca2+[lumen side]

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?

ATP + H2O + 2 Ca2+[side 1]

ADP + phosphate + 2 Ca2+[side 2]

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733861

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?

ATP + H2O + Ca2+/cis

ADP + phosphate + Ca2+/trans

5 entries

ATP + H2O + Ca2+[side 1]

ADP + phosphate + Ca2+[side 2]

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733829, 750181, 750217

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?

additional information

?

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Ca2+

Mg2+

Ca2+

Mg2+

(4-chlorophenyl)(pyridin-2-yl)[4-(pyrrolidin-1-ylmethyl)phenyl]methanol

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(4-chlorophenyl)[4-([[3-(4-[3-[(7-chloroquinolin-4-yl)amino]propyl]piperazin-1-yl)propyl]amino]methyl)phenyl]methanone

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(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

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1,3-dibromo-2,4,6-tri(methylisothiouronium)benzene

micromolar inhibitor of SERCA

700293

1-(naphthalen-1-ylmethyl)naphthalen-2-ol

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1-[(4-chlorophenyl)(phenyl)[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-1H-1,2,4-triazole

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1-[(4-chlorophenyl)(phenyl)[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-1H-imidazole

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2,2',2''-methanetriyltris(4-tert-butylphenol)

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2,2'-methanediylbis(4-tert-butylphenol)

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2,4-di-tert-butyl-6-(1-phenylethyl)phenol

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2,4-di-tert-butyl-6-[1-(4-methoxyphenyl)ethyl]phenol

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2,5-bis(2-methylpropyl)phenol

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2,5-bis(cyclopenta-2,4-dien-1-ylmethyl)benzene-1,4-diol

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2,5-di(tert-butyl)hydroquinone

micromolar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation

700293

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

670677

2,5-di-tert-butylhydroquinone

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2,6-di-tert-butyl-4-[1-(4-methoxyphenyl)ethyl]phenol

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2-(cyclopenta-2,4-dien-1-ylmethyl)benzene-1,4-diol

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2-cyclooctylbenzene-1,4-diol

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3-(1,1-diphenylethyl)cyclopentanol

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4,4'-butane-2,2-diylbis(2-methylphenol)

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4,4'-butane-2,3-diyldiphenol

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4,4'-propane-2,2-diylbis(2,6-dimethylphenol)

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4,5-dibenzylbenzene-1,2-diol

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4-(7-methyloctyl)phenol

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6-tert-butyl-2,3-dihydro-1H-inden-5-ol

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7-chloro-4-(piperazin-1-yl)quinoline

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biphenyl-2,5-diol

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clotrimazole

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cyclopiazonic acid

N-((3-chlorophenyl)(4-((4-(7-chloroquinolin-4-yl)piperazin-1-yl)methyl)phenyl)methyl)-7-chloro-4-aminoquinoline

NF1442

phospholamban

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rutin

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rutin 4'''-O-arachidonate

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rutin 4'''-O-erucate

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rutin 4'''-O-linoleate

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rutin 4'''-O-linolenate

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rutin 4'''-O-oleate

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rutin 4'''-O-stearate

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rutin palmitate

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thapsigargin

1,2-dichlorobenzene

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at concentrations of 0.25-0.75 mM, 1,2-dichlorobenzene inhibits the ATP hydrolysis to about 80%. Starting at 0.05 mM, 1,2-dichlorobenzene is able to uncouple the ratio of hydrolysis/Ca2+transporte

bis(maltolato)oxovanadium(IV)

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bis(N-hydroxylamidoiminodiacetato)vanadium(IV)

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bupivacaine

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inhibition by bupivacaine is not competitive with respect to the specific transport and catalytic sites of the enzyme

Ca2+

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above 0.1 mM, Ca2+-dependent ATPase

detergent C12E8

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inhibition of mutant D813A/D818A

lidocaine

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inhibition by lidocaine is not competitive with respect to the specific transport and catalytic sites of the enzyme

Mg2+

N,N-dimethylalkylamine N-oxide

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slight stimulation at low concentrations, inhibition at higher concentrations, maximal inhibition for the homologue with the alkyl chain length n=16

210496

N-alkyl-N,N-dimethylamine-N-oxide

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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

670493

orthovanadate

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palytoxin

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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

695863

polysubstituted fullerene C60-II

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noncompetitive and reversible inhibition, complete inhibition at 0.05 mM

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polysubstituted fullerene C60-III

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complete inhibition at 0.05 mM

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polysubstituted fullerene C60-IV

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76% inhibition of Ca2+ transport and 91% inhibition of ATP hydrolysis at 0.05 mM

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polysubstituted fullerene C60-IX

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complete inhibition at 0.05 mM

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polysubstituted fullerene C60-V

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complete inhibition at 0.05 mM

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polysubstituted fullerene C60-VI

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63% inhibition of Ca2+ transport and 38% inhibition of ATP hydrolysis at 0.05 mM

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polysubstituted fullerene C60-VII

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60% inhibition of Ca2+ transport and 38% inhibition of ATP hydrolysis at 0.05 mM

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polysubstituted fullerene C60-VIII

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82% inhibition of Ca2+ transport and 67% inhibition of ATP hydrolysis at 0.05 mM

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polysubstituted fullerene C60-X

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complete inhibition at 0.05 mM

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polysubstituted fullerene C60-XI

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complete inhibition at 0.05 mM

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pyridine-2,6-dicarboxylatodioxovanadium

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thapsigargin

vanadate

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656099, 698270

[(dihydroindenyl)oxy]acetic acid

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DIOA

1,2-dichlorobenzene

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concentrations of 0.05-0.2 mM of 1,2-dichlorobenzene stimulate the hydrolytic activity of the enzyme in a medium-containing Ca2+-ionophore

Ca2+

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656099

N,N-dimethylalkylamine N-oxide

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slight stimulation at low concentrations, inhibition at higher concentrations

210496

N-alkyl-N,N-dimethylamine-N-oxide

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CnNO with n = 10-20, stimulate at low concentrations and inhibit at high concentrations dependent on the compound alkyl chain length, overview

670493

potassium oxalate

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Ca2+ uptake is supported by potassium oxalate

additional information

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0.0003 - 0.002

Ca2+

0.015 - 0.035

Sr2+

additional information

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detailed de-/phosphorylation reaction kinetics, kinetic modelling

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9.5 - 128

Ca2+

additional information

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0.0023

polysubstituted fullerene C60-II

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pH and temperature not specified in the publication

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0.000023 - 0.000045

thapsigargin

additional information

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0.152

(4-chlorophenyl)(pyridin-2-yl)[4-(pyrrolidin-1-ylmethyl)phenyl]methanol

Oryctolagus cuniculus

in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C

0.022 - 0.029

(4-chlorophenyl)[4-([[3-(4-[3-[(7-chloroquinolin-4-yl)amino]propyl]piperazin-1-yl)propyl]amino]methyl)phenyl]methanone

0.0013

(N-((3-chlorophenyl)(4-(pyrrolidin-1-yl)methyl)phenyl)methyl)-7-chloro-4-aminoquinoline

Oryctolagus cuniculus

in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C

0.015

1,1'-methanediyldinaphthalen-2-ol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0273

1-(naphthalen-1-ylmethyl)naphthalen-2-ol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.032

1-[(4-chlorophenyl)(phenyl)[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-1H-1,2,4-triazole

Oryctolagus cuniculus

in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C

0.057

1-[(4-chlorophenyl)(phenyl)[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-1H-imidazole

Oryctolagus cuniculus

in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C

0.0213

2,2',2''-methanetriyltris(4-tert-butylphenol)

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0118

2,2'-methanediylbis(4-tert-butylphenol)

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0338

2,4-di-tert-butyl-6-(1-phenylethyl)phenol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0353

2,4-di-tert-butyl-6-[1-(4-methoxyphenyl)ethyl]phenol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0188

2,5-bis(2-methylpropyl)phenol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0094

2,5-bis(cyclopenta-2,4-dien-1-ylmethyl)benzene-1,4-diol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0454

2,6-di-tert-butyl-4-[1-(4-methoxyphenyl)ethyl]phenol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0202

2-(cyclopenta-2,4-dien-1-ylmethyl)benzene-1,4-diol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0115

2-cyclooctylbenzene-1,4-diol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0497

3-(1,1-diphenylethyl)cyclopentanol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0393

4,4'-butane-2,2-diylbis(2-methylphenol)

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0283

4,4'-butane-2,3-diyldiphenol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0195

4,4'-propane-2,2-diylbis(2,6-dimethylphenol)

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0238

4,5-dibenzylbenzene-1,2-diol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0172

4-(7-methyloctyl)phenol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.0281

6-tert-butyl-2,3-dihydro-1H-inden-5-ol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

0.00229

biphenyl-2,5-diol

Oryctolagus cuniculus

In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)

35

clotrimazole

Oryctolagus cuniculus

IC50 about 0.035 mM, in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C

0.0008

N-((3-chlorophenyl)(4-((4-(7-chloroquinolin-4-yl)piperazin-1-yl)methyl)phenyl)methyl)-7-chloro-4-aminoquinoline

Oryctolagus cuniculus

in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C

0.023

rutin 4'''-O-arachidonate

Oryctolagus cuniculus

at 37°C and pH 7.4

0.05

rutin 4'''-O-erucate

Oryctolagus cuniculus

at 37°C and pH 7.4

0.025

rutin 4'''-O-linoleate

Oryctolagus cuniculus

at 37°C and pH 7.4

0.062

rutin 4'''-O-linolenate

Oryctolagus cuniculus

at 37°C and pH 7.4

0.05

rutin 4'''-O-oleate

Oryctolagus cuniculus

at 37°C and pH 7.4

0.035

rutin 4'''-O-stearate

Oryctolagus cuniculus

at 37°C and pH 7.4

0.064

rutin palmitate

Oryctolagus cuniculus

at 37°C and pH 7.4

0.04

bis(maltolato)oxovanadium(IV)

Oryctolagus cuniculus

-

in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25°C

0.325

bis(N-hydroxylamidoiminodiacetato)vanadium(IV)

Oryctolagus cuniculus

-

in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25°C

0.0004

palytoxin

Oryctolagus cuniculus

-

in 20 mM MOPS, pH 7.0, 80 mM KC1, 5 mM MgCl2, 0.5 mM EGTA, 0.55 mM CaC12, at 25°C

695863

0.025

pyridine-2,6-dicarboxylatodioxovanadium

Oryctolagus cuniculus

-

in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25°C

0.08

vanadate

Oryctolagus cuniculus

-

in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25°C

0.127

[(dihydroindenyl)oxy]acetic acid

Oryctolagus cuniculus

-

10.06

-

at pH 7.2 and 37°C

5.2

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purified calcium pump activity

9

-

avidin affinity chromatography purified enzyme

additional information

7

assay at

7

7.2

7.23

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in presence of Ca2+ ionophore

656099

6.3 - 8.2

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additional information

2 - 21

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assay at 2°C and at 21°C

30

-

assay at

37

additional information

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temperature dependence of the Ca2+ transport at different pH values, overview

fast twitch muscle fiber

P04191, P20647

isoform SERCA 1

697684

muscle

-

-

masseter and medial pterygoid

slow twitch muscle fiber

P04191, P20647

isoform SERCA 2

697684

endoplasmic reticulum

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sarcoplasmic reticulum

8 entries

endoplasmic reticulum

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-

a microsomal fraction enriched in the transverse tubular system (T-tubule)/sarcoplasmic reticulum, SR, complex is prepared

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sarcoplasmic reticulum membrane

sarcoplasmic reticulum

5 entries

-

33017

695863, 712588

physiological function

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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

P04191 pBLAST

AT2A1_RABIT

1001

7

110459

Swiss-Prot

Show Sequence

other Location (Reliability: 3), other Location (Reliability: 2)

100000

-

x * 100000, SDS-PAGE

110000

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x * 110000, isoform SERCA1, SDS-PAGE

additional information

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?

additional information

phosphoprotein

nitrosylation

-

at Tyr122

phosphoprotein

-

-

695857

crystal structure

656867

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

670677

purified enzyme in complex with purified recombinant phospholamban, from 20 mM imidazole, pH 7.4, 100 mM KCl, 35 mM MgCl2, 0.5 mM EGTA, 0.25 mM Na3VO4, 0.03 mM thapsigargin, three freeze-thaw cycles using liquid nitrogen and thawing in hand, reconstitution at 4°C for several days to 1 week, analysis of interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals, overview

purified enzyme is crystallized preserving natural and essential lipids, high resolution crystal structure determination and analysis, crystallization method optimization

669559

purified recombinant enzyme, hanging drop vapour diffusion method, 12 mg/ml protein in a solution containing 10 mM Ca2+, 1 mm beta,gamma-methyleneadenosine 5'-triphosphate, and 1,2-dioleoyl-sn-glycero-3-phosphocholine, 0.002 ml is mixed with 0.002 ml well solution containing 0.2 M sodium acetate, 10-14% w/v PEG 6000, 10% glycerol, and 4% tert-butanol, crystals grow within 1 to 14 days at 19°C, X-ray diffraction structure determination and analysis at 3.3 A resolution

-

-

210475

hanging drop vapor diffusion method, using 220 mM sodium acetate, 4% (v/v) tert-butanol, 5 mM 2-mercaptoethanol, 15% (v/v) glycerol, and 6-7% (w/v) PEG 6000

-

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

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

N34A

loss-of-function mutation

696294

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

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

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

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

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

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

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+

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

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

-

210498

native enzyme from sekeletal muscle sarcoplasmic reticulum membranes by adsorption chromatography

purified on a sucrose step-gradient

696294

Reactive Red 120 resin column chromatography

751099

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

avidin resin column chromatography

-

native enzyme from psoas muscle

-

partially by preparation of sarcoplasmic reticulum vesicles

-

partially, preparation of sarcoplasmic reticulum membrane vesicles

-

667604, 669646

recombinant biotinylated SERCA1a 92fold from Saccharomyces cerevisiae light membrane fraction by avidin affinity chromatography, cleavage of the biotin tag by thrombin, and gel filtration

-

wild type and mutant D813A/D818A of the L6-7 loop of enzyme

-

expressed in COS-1 cells

overexpression of C-terminally biotinylated SERCA1a, with introduced thrombin cleavage site, in Saccharomyces cerevisiae

-

-

210492

expressed in Saccharomyces cerevisiae

-

expression of C-terminally biotinylated SERCA1a in Saccharomyces cerevisiae strain W3031.b/Gal4, a thrombin cleavage site is inserted

-

expression of wild type and mutant D813A/D818A of L6-7 loop of enzyme in yeast

-

mutants are expressed in COS-1 cells

-

698857, 698885

reconstitution of purified enzyme into proteoliposomes using 1,2-dioleoyl-sn-glycero-3-phosphocholine in a cholate buffer containing 30 mM Tris, pH 7.0, 0.4 M NaCl, 0.4 M sucrose, 1 mM MgCl2, 1 mM NaN3, 1% w/v sodium cholate, and 50 mM DTT, the enzyme shows nearly full activity

reconstitution of purified enzyme with phospholamban in proteoliposomes, overview

pharmacology

-

lower concentration of [(dihydroindenyl)oxy]acetic acid should be used for evaluation of the activity of K+-Cl- cotranporter without affecting the activities of coexisting Na+,K+-ATPase and H+,K+-ATPase in cells

additional information

-

determination of enzyme activity and Ca2+ transport rates in different human muscles types are important for the local anesthetics strategy in dentistry

Hasselbach, W.

Calcium-activated ATPase of the sarcoplasmic reticulum membranes

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Oryctolagus cuniculus

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Oryctolagus cuniculus, Homo sapiens

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15155750

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Biochemistry

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Oryctolagus cuniculus

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Crystals of sarcoplasmic reticulum Ca2+-ATPase

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Characteristics of the sarcoplasmic reticulum Ca2+-dependent ATPase from masticatory muscles

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83

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2004

Oryctolagus cuniculus

15218046

670493

Karlovska, J.; Hammel, M.; Laggner, P.; Lacko, I.; Devinsky, F.; Balgavy, P.

Effects of N-alkyl-N,N-dimethylamine-N-oxides on the activity of purified sarcoplasmic reticulum Ca(2+)-transporting ATPase

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60

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Oryctolagus cuniculus

15739903

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Proc. Natl. Acad. Sci. USA

102

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Oryctolagus cuniculus (P04191), Oryctolagus cuniculus

16087876

670677

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Proc. Natl. Acad. Sci. USA

102

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2005

Gallus gallus, Oryctolagus cuniculus (P04191)

16150713

Jidenko, M.; Lenoir, G.; Fuentes, J.M.; le Maire, M.; Jaxel, C.

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48

32-42

2006

Oryctolagus cuniculus

16603381

Fujii, T.; Ohira, Y.; Itomi, Y.; Takahashi, Y.; Asano, S.; Morii, M.; Takeguchi, N.; Sakai, H.

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560

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2007

Oryctolagus cuniculus

17303113

695857

Toyoshima, C.

Structural aspects of ion pumping by Ca2+-ATPase of sarcoplasmic reticulum

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476

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Oryctolagus cuniculus (P04191)

18455499

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476

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2008

Oryctolagus cuniculus

18485884

695863

Coca, R.; Soler, F.; Fernandez-Belda, F.

Characterization of the palytoxin effect on Ca2+-ATPase from sarcoplasmic reticulum (SERCA)

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478

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Oryctolagus cuniculus

18675777

696294

Afara, M.R.; Trieber, C.A.; Ceholski, D.K.; Young, H.S.

Peptide inhibitors use two related mechanisms to alter the apparent calcium affinity of the sarcoplasmic reticulum calcium pump

Biochemistry

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2008

Oryctolagus cuniculus (P04191)

18702513

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17

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19117760

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Arruda, A.P.; Ketzer, L.A.; Nigro, M.; Galina, A.; Carvalho, D.P.; de Meis, L.

Cold tolerance in hypothyroid rabbits: role of skeletal muscle mitochondria and sarcoplasmic reticulum Ca2+ ATPase isoform 1 heat production

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149

6262-6271

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Oryctolagus cuniculus (P04191), Oryctolagus cuniculus

18703625

697684

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Is the Ca2+-ATPase from sarcoplasmic reticulum also a heat pump?

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Oryctolagus cuniculus, Oryctolagus cuniculus (P04191), Oryctolagus cuniculus (P20647)

18679670

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Sarcoplasmic reticulum calcium ATPase is inhibited by organic vanadium coordination compounds: pyridine-2,6-dicarboxylatodioxovanadium(V), BMOV, and an amavadine analogue

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47

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2008

Oryctolagus cuniculus

18510311

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2008

Oryctolagus cuniculus

18930923

Holdensen, A.N.; Andersen, J.P.

The length of the A-M3 linker is a crucial determinant of the rate of the Ca2+ transport cycle of sarcoplasmic reticulum Ca2+-ATPase

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284

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Oryctolagus cuniculus

19278994

698973

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

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284

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Homo sapiens, Oryctolagus cuniculus (P20647)

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Oryctolagus cuniculus (P04191)

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Local anesthetics inhibit Ca-ATPase in masticatory muscles

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89

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2010

Oryctolagus cuniculus

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Clausen, J.D.; Andersen, J.P.

Glutamate 90 at the luminal ion gate of sarcoplasmic reticulum Ca2+-ATPase is critical for Ca2+ binding on both sides of the membrane

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Oryctolagus cuniculus (B6CAM1)

20421308

Bartolommei, G.; Tadini-Buoninsegni, F.; Moncelli, M.R.; Gemma, S.; Camodeca, C.; Butini, S.; Campiani, G.; Lewis, D.; Inesi, G.

The Ca2+-ATPase (SERCA1) is inhibited by 4-aminoquinoline derivatives through interference with catalytic activation by Ca2+, whereas the ATPase E2 state remains functional

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286

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Oryctolagus cuniculus (P04191), Oryctolagus cuniculus

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Conformational changes of recombinant Ca2+-ATPase studied by reaction-induced infrared difference spectroscopy

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23331704

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Inhibition of the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA1) by rutin derivatives

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26968444