Any feedback?
Information on EC 7.2.2.10 - P-type Ca2+ transporter and Organism(s) Mus musculus and UniProt Accession O55143
for references in articles please use BRENDA:EC7.2.2.10Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
7.2.2.10 P-type Ca2+ transporterIUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria. The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolysed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolysed. In muscle cells Ca2+ is transported from the cytosol (side 1) into the sarcoplasmic reticulum (side 2).
Specify your search results
Word Map
- 7.2.2.10
- cardiac
- thapsigargin
-
contractile
- ventricular
- phospholamban
- myocardial
- cardiomyocytes
- calmodulin
-
ryanodine
- myocytes
- na+
- myosin
-
pmcas
- atpases
- hypertrophy
-
blocker
-
cyclopiazonic
- inositol
-
diastolic
- caffeine
-
ca2+-free
-
fura-2
-
l-type
- vanadate
-
extrusion
- plb
- overload
- phosphoenzyme
-
systolic
- nifedipine
- cpa
-
excitation-contraction
- ouabain
-
store-operated
-
1,4,5-trisphosphate
-
ca2+-binding
-
calmodulin-dependent
-
twitch
- na+-k+-atpase
-
slow-twitch
-
ca2+-sensitive
- na,k-atpase
-
refilling
-
inotropic
- myofibrillar
-
k+-atpase
-
fast-twitch
-
ca2+-induced
- medicine
- insp3
-
actin-activated
- biotechnology
- pharmacology
- agriculture
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
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
-
-
-
-
Ca2+-transporting 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
-
-
-
-
plasma membrane calcium ATPase
PMCA1
PMCA2
PMCA3
PMCA4
PMCA4b
sarco(endo)plasmic reticulum Ca2+-ATPase
-
-
-
-
sarcoplasmic reticulum ATPase
-
-
-
-
Secretory pathway Ca2+ transporting ATPase
-
-
-
-
SERCA
SERCA1
-
-
-
-
SERCA2
-
-
-
-
SERCA3
-
-
-
-
Vacuolar Ca2+-ATPase
-
-
-
-
Ca2+ ATPase
-
-
-
-
PMCA1
-
-
-
-
PMCA2
-
-
-
-
PMCA3
-
-
-
-
PMCA4
-
-
-
-
SERCA
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
9000-83-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
the PMCA pump uses a molecule of ATP to transport one molecule of Ca2+ from the cytosol to the external environment
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mn2+
-
SPCA1 mediates the accumulation Mn2+ with high affinity into Golgi reservoirs
Ca2+
dependent on, at very low Ca2+ concentrations the PMCA is nearly inactive, unstimulated PMCA pumps have poor affinity for Ca2+
Ca2+
-
PMCA extrudes Ca2+ but has little effect on excitation-contraction coupling, Pmca4b likely reduces the local Ca2+ signals involved in reactive cardiomyocyte hypertrophy via calcineurin regulation
Ca2+
-
SPCA1 mediates the accumulation of Ca2+ with high affinity into Golgi reservoirs
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tetrabromobisphenol A
-
can inhibit SERCA at low concentrations (IC50, 0.0004-0.0012 mM)
orthovanadate
-
the Ca2+ pump is inhibited by orthovanadate (0.1 mM) once sufficient Ca2+ accumulation has occurred
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphatidylinositol bisphosphate
the most active in stimulating PMCA activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
PMCA2 is highly expressed in cerebellar Purkinje cells
PMCA1 is ubiquitous, but is expressed most abundantly in brain, lung and intestine
-
SPCA1 localizes in the initial part of primary dendritic trunk in main cortical, hippocampal and cerebellar neurons from the earliest postnatal stages
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.
-
methods to employ tissue homogenates to study sarcoplasmatic reticulum Ca2+ transport function in individual mouse hearts
the PMCA4 pump is expressed in heart, PMCA2 is expressed at a lower level in the heart
PMCA1 is ubiquitous, but is expressed most abundantly in brain, lung and intestine. The PMCA4 pump is expressed in intestine.
-
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
the brain isoform PMCA2 pump is also expressed in the lactating mammary glands
the PMCA3 and PMCA4 pumps are expressed in skeletal muscles
PMCA4 is expressed at particularly high levels in the testis (more than 90% of PMCA protein expressed there is isoform 4)
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
isoform SERCA2b plays an important role in dysregulated glucose and lipid homeostasis in the liver of obese mice. Overexpression of isoform SERCA2b in the liver of obese mice significantly reduces the lipogenic gene expression and the triglyceride content in the liver and reduces steatohepatitis. Increasing the levels of isoform SERCA2b greatly reduces endoplasmic reticulum stress in the liver, increases glucose tolerance, and establishes euglycemia in severely obese and diabetic mice. Isoform SERCA2b can increase endoplasmic reticulum folding capacity
malfunction
-
plasma membrane Ca2+-ATPase 1 deficiency increases susceptibility to atrial tachyarrhythmia in Langendorff-perfused hearts under stress conditions. Enzyme deficiency produces instabilities in membrane potentials and Ca2+ handling in atrial myocytes
physiological function
physiological function
-
sarcoplasmic reticulum Ca2+ ATPase pump is a major regulator of glucose transport in the healthy and diabetic heart. Cardiac-specific enzyme expression increases active cell-surface GLUT4 and glucose uptake in the myocardium, as well as whole body glucose tolerance. The enzyme regulates cardiac GLUT4 translocation
physiological function
the combination of the functional attributes of both PMCA4 variants leads to heightened efficiency of the pump in the maintenance of Ca2+ homeostasis, which is crucial for normal motility and male fertility
physiological function
-
the enzyme is responsible for intracellular Ca2+ homeostasis. Enzyme uncoupling of Ca2+ transport from ATP hydrolysis by sarcolipin increases heat production implicating sarcolipin-enzyme interaction in muscle thermogenesis
physiological function
-
plasma membrane Ca2+-ATPase 1 is required for maintaining atrial Ca2+ homeostasis and electrophysiological stability in mouse atria under stress conditions
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AT2A2_MOUSE
1044
8
114858
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
a splice variant PMCA4b-Asp mutant exhibits 10% of the Ca2+ efflux activity of wild type isoform PMCA4
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform SERCA2b protein and mRNA levels are dramatically reduced in the liver of obese mice
splice varianta PMCA4e and PMCA4a show higher expression level in injured carotids compared to uninjured carotids
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
PMCA4b overexpression significantly reduces cardiac hypertrophy following pressure overload
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ji, Y.; Loukianov, E.; Periasamy, M.
Analysis of sarcoplasmic reticulum Ca2+ transport and Ca2+ ATPase enzymatic properties using mouse cardiac tissue homogenates
Anal. Biochem.
269
236-244
1999
Mus musculus
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)
Faddy, H.M.; Smart, C.E.; Xu, R.; Lee, G.Y.; Kenny, P.A.; Feng, M.; Rao, R.; Brown, M.A.; Bissell, M.J.; Roberts-Thomson, S.J.; Monteith, G.R.
Localization of plasma membrane and secretory calcium pumps in the mammary gland
Biochem. Biophys. Res. Commun.
369
977-981
2008
Mus musculus
Wu, X.; Chang, B.; Blair, N.S.; Sargent, M.; York, A.J.; Robbins, J.; Shull, G.E.; Molkentin, J.D.
Plasma membrane Ca2+-ATPase isoform 4 antagonizes cardiac hypertrophy in association with calcineurin inhibition in rodents
J. Clin. Invest.
119
976-985
2009
Mus musculus
Sepulveda, M.R.; Marcos, D.; Berrocal, M.; Raeymaekers, L.; Mata, A.M.; Wuytack, F.
Activity and localization of the secretory pathway Ca2+-ATPase isoform 1 (SPCA1) in different areas of the mouse brain during postnatal development
Mol. Cell. Neurosci.
38
461-473
2008
Mus musculus
Ogunbayo, O.A.; Lai, P.F.; Connolly, T.J.; Michelangeli, F.
Tetrabromobisphenol A (TBBPA), induces cell death in TM4 Sertoli cells by modulating Ca2+ transport proteins and causing dysregulation of Ca2+ homeostasis
Toxicol. In Vitro
22
943-952
2008
Mus musculus
Park, S.W.; Zhou, Y.; Lee, J.; Lee, J.; Ozcan, U.
Sarco(endo)plasmic reticulum Ca2+-ATPase 2b is a major regulator of endoplasmic reticulum stress and glucose homeostasis in obesity
Proc. Natl. Acad. Sci. USA
107
19320-19325
2010
Mus musculus (O55143)
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
Waller, A.P.; Kalyanasundaram, A.; Hayes, S.; Periasamy, M.; Lacombe, V.A.
Sarcoplasmic reticulum Ca2+ ATPase pump is a major regulator of glucose transport in the healthy and diabetic heart
Biochim. Biophys. Acta
1852
873-881
2015
Mus musculus
Patel, R.; Al-Dossary, A.A.; Stabley, D.L.; Barone, C.; Galileo, D.S.; Strehler, E.E.; Martin-DeLeon, P.A.
Plasma membrane Ca2+-ATPase 4 in murine epididymis: secretion of splice variants in the luminal fluid and a role in sperm maturation
Biol. Reprod.
89
6-6
2013
Mus musculus (Q6Q477), Mus musculus
Afroze, T.; Yang, G.; Khoshbin, A.; Tanwir, M.; Tabish, T.; Momen, A.; Husain, M.
Calcium efflux activity of plasma membrane Ca2+ ATPase-4 (PMCA4) mediates cell cycle progression in vascular smooth muscle cells
J. Biol. Chem.
289
7221-7231
2014
Mus musculus (H2BL43)
Sahoo, S.K.; Shaikh, S.A.; Sopariwala, D.H.; Bal, N.C.; Bruhn, D.S.; Kopec, W.; Khandelia, H.; Periasamy, M.
The N terminus of sarcolipin plays an important role in uncoupling sarco-endoplasmic reticulum Ca2+-ATPase (SERCA) ATP hydrolysis from Ca2+ Transport
J. Biol. Chem.
290
14057-14067
2015
Mus musculus
EXTERNAL LINKS (specific for EC-Number 7.2.2.10)
Transporter Classification Database (TCDB): 3.A.3.2.10, 3.A.3.2.14, 3.A.3.2.17, 3.A.3.2.34, 3.A.3.2.3, 3.A.3.2.1, 3.A.3.2.5, 3.A.3.2.9, 3.A.3.2.35, 3.A.3.2.2, 3.A.3.9.2, 3.A.3.2.19, 3.A.3.2.25, 3.A.3.2.40, 3.A.3.2.31, 3.A.3.2.42, 3.A.3.2.11, 3.A.3.2.12, 3.A.3.2.43, 3.A.3.2.7, 3.A.3.2.13, 3.A.3.2.27, 3.A.3.2.6, 3.A.3.2.26, 3.A.3.2.21, 3.A.3.2.44, 3.A.3.2.33, 3.A.3.2.30, 3.A.3.2.32
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
