ATP2B4

Last updated
ATP2B4
PDB 1cff EBI.jpg
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases ATP2B4 , ATP2B2, MXRA1, PMCA4, PMCA4b, PMCA4x, ATPase plasma membrane Ca2+ transporting 4
External IDs OMIM: 108732 MGI: 88111 HomoloGene: 48034 GeneCards: ATP2B4
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001684
NM_001001396
NM_001365783
NM_001365784

NM_001167949
NM_213616

RefSeq (protein)

NP_001001396
NP_001675
NP_001352712
NP_001352713

NP_001161421
NP_998781

Location (UCSC) Chr 1: 203.63 – 203.74 Mb Chr 1: 133.63 – 133.73 Mb
PubMed search [3] [4]
Wikidata
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Plasma membrane calcium-transporting ATPase 4 is an enzyme that in humans is encoded by the ATP2B4 gene. [5] [6]

Contents

The protein encoded by this gene belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle. These enzymes remove bivalent calcium ions from eukaryotic cells against very large concentration gradients and play a critical role in intracellular calcium homeostasis. The mammalian plasma membrane calcium ATPase isoforms are encoded by at least four separate genes and the diversity of these enzymes is further increased by alternative splicing of transcripts. The expression of different isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, suggesting that these pumps are functionally adapted to the physiological needs of particular cells and tissues. This gene encodes the plasma membrane calcium ATPase isoform 4. Alternatively spliced transcript variants encoding different isoforms have been identified. [6]

Interactions

ATP2B4 has been shown to interact with CASK. [7]

Related Research Articles

<span class="mw-page-title-main">V-ATPase</span> Family of transport protein complexes

Vacuolar-type ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pumps protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that uses the energy from ATP hydrolysis to produce a proton gradient.

<span class="mw-page-title-main">Calcium ATPase</span> Class of enzymes

Ca2+ ATPase is a form of P-ATPase that transfers calcium after a muscle has contracted. The two kinds of calcium ATPase are:

Plasma membrane Ca<sup>2+</sup> ATPase Transport protein

The plasma membrane Ca2+ ATPase (PMCA) is a transport protein in the plasma membrane of cells and functions to remove calcium (Ca2+) from the cell. PMCA function is vital for regulating the amount of Ca2+ within all eukaryotic cells. There is a very large transmembrane electrochemical gradient of Ca2+ driving the entry of the ion into cells, yet it is very important that they maintain low concentrations of Ca2+ for proper cell signalling. Thus, it is necessary for cells to employ ion pumps to remove the Ca2+. The PMCA and the sodium calcium exchanger (NCX) are together the main regulators of intracellular Ca2+ concentrations. Since it transports Ca2+ into the extracellular space, the PMCA is also an important regulator of the calcium concentration in the extracellular space.

ATPase, Na<sup>+</sup>/K<sup>+</sup> transporting, alpha 1 Protein-coding gene in the species Homo sapiens

Sodium/potassium-transporting ATPase subunit alpha-1 is an enzyme that in humans is encoded by the ATP1A1 gene.

<span class="mw-page-title-main">ATP1A2</span> Protein-coding gene in the species Homo sapiens

Sodium/potassium-transporting ATPase subunit alpha-2 is a protein which in humans is encoded by the ATP1A2 gene.

<span class="mw-page-title-main">ATP2C1</span> Protein-coding gene in the species Homo sapiens

Calcium-transporting ATPase type 2C member 1 is an enzyme that in humans is encoded by the ATP2C1 gene.

<span class="mw-page-title-main">ATP2B1</span> Protein-coding gene in the species Homo sapiens

Plasma membrane calcium-transporting ATPase 1 is a plasma membrane Ca2+
ATPase
, an enzyme that in humans is encoded by the ATP2B1 gene. It's a transport protein, a translocase, a calcium pump EC 7.2.2.10.

<span class="mw-page-title-main">ATP2B2</span> Protein-coding gene in the species Homo sapiens

Plasma membrane calcium-transporting ATPase 2 is an enzyme that in humans is encoded by the ATP2B2 gene.

<span class="mw-page-title-main">ATP1B1</span> Protein-coding gene in the species Homo sapiens

Sodium/potassium-transporting ATPase subunit beta-1 is an enzyme that in humans is encoded by the ATP1B1 gene.

<span class="mw-page-title-main">ATP6V0C</span>

V-type proton ATPase 16 kDa proteolipid subunit is an enzyme that in humans is encoded by the ATP6V0C gene.

<span class="mw-page-title-main">ATP2A3</span>

Sarcoplasmic/endoplasmic reticulum calcium ATPase 3 is an enzyme that in humans is encoded by the ATP2A3 gene.

<span class="mw-page-title-main">ATP6V1B2</span>

V-type proton ATPase subunit B, brain isoform is an enzyme that in humans is encoded by the ATP6V1B2 gene.

<span class="mw-page-title-main">ATP6V1C1</span>

V-type proton ATPase subunit C 1 is an enzyme that in humans is encoded by the ATP6V1C1 gene.

<span class="mw-page-title-main">ATPase, H+ transporting, lysosomal V0 subunit a1</span> Protein-coding gene in the species Homo sapiens

V-type proton ATPase 116 kDa subunit a isoform 1 is an enzyme that in humans is encoded by the ATP6V0A1 gene.

<span class="mw-page-title-main">ATP6V1A</span> Protein-coding gene in the species Homo sapiens

V-type proton ATPase catalytic subunit A is an enzyme that in humans is encoded by the ATP6V1A gene.

<span class="mw-page-title-main">ATP6V1G2</span> Protein-coding gene in Homo sapiens

V-type proton ATPase subunit G 2 is an enzyme that in humans is encoded by the ATP6V1G2 gene.

<span class="mw-page-title-main">ATP6V1G3</span> Protein-coding gene in the species Homo sapiens

V-type proton ATPase subunit G 3 is an enzyme that in humans is encoded by the ATP6V1G3 gene.

<span class="mw-page-title-main">ATP6V0E1</span> Protein-coding gene in the species Homo sapiens

V-type proton ATPase subunit e 1 is an enzyme that in humans is encoded by the ATP6V0E1 gene.

<span class="mw-page-title-main">ATP2B3</span> Protein-coding gene in the species Homo sapiens

Plasma membrane calcium-transporting ATPase 3 is an enzyme that in humans is encoded by the ATP2B3 gene.

Calcium pumps are a family of ion transporters found in the cell membrane of all animal cells. They are responsible for the active transport of calcium out of the cell for the maintenance of the steep Ca2+ electrochemical gradient across the cell membrane. Calcium pumps play a crucial role in proper cell signalling by keeping the intracellular calcium concentration roughly 10,000 times lower than the extracellular concentration. Failure to do so is one cause of muscle cramps.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000058668 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026463 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Olson S, Wang MG, Carafoli E, Strehler EE, McBride OW (April 1991). "Localization of two genes encoding plasma membrane Ca2(+)-transporting ATPases to human chromosomes 1q25-32 and 12q21-23". Genomics. 9 (4): 629–41. doi:10.1016/0888-7543(91)90356-J. PMID   1674727.
  6. 1 2 "Entrez Gene: ATP2B4 ATPase, Ca++ transporting, plasma membrane 4".
  7. Schuh K, Uldrijan S, Gambaryan S, Roethlein N, Neyses L (March 2003). "Interaction of the plasma membrane Ca2+ pump 4b/CI with the Ca2+/calmodulin-dependent membrane-associated kinase CASK". The Journal of Biological Chemistry. 278 (11): 9778–83. doi: 10.1074/jbc.M212507200 . PMID   12511555.

Further reading