ATP2B4

From Wikipedia, the free encyclopedia

ATPase, Ca++ transporting, plasma membrane 4

Identifiers

ATP2B4; ATP2B2; DKFZp686G08106; DKFZp686M088; MXRA1; PMCA4

External IDs

OMIM: 108732 MGI: 88111 HomoloGene: 48034

Gene ontology
Molecular Function:	• nucleotide binding • magnesium ion binding • calcium-transporting ATPase activity • calcium ion binding • calmodulin binding • ATP binding • hydrolase activity • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
Cellular Component:	• plasma membrane • integral to plasma membrane
Biological Process:	• cation transport • calcium ion transport • metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_001001396 (mRNA)
NP_001001396 (protein)

XM_981196 (mRNA)
XP_986290 (protein)

Location

Chr 1: 201.86 - 201.98 Mb

Chr 1: 135.52 - 135.57 Mb

Pubmed search

[1]

[2]

ATPase, Ca++ transporting, plasma membrane 4, also known as ATP2B4, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: ATP2B4 ATPase, Ca++ transporting, plasma membrane 4.

[edit] Further reading

Møller JV, Juul B, le Maire M (1996). "Structural organization, ion transport, and energy transduction of P-type ATPases.". Biochim. Biophys. Acta 1286 (1): 1–51. PMID 8634322.
Strehler EE, Zacharias DA (2001). "Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps.". Physiol. Rev. 81 (1): 21–50. PMID 11152753.
Strehler EE, Treiman M (2004). "Calcium pumps of plasma membrane and cell interior.". Curr. Mol. Med. 4 (3): 323–35. PMID 15101689.
Heim R, Hug M, Iwata T, et al. (1992). "Microdiversity of human-plasma-membrane calcium-pump isoform 2 generated by alternative RNA splicing in the N-terminal coding region.". Eur. J. Biochem. 205 (1): 333–40. PMID 1313367.
Brandt P, Neve RL, Kammesheidt A, et al. (1992). "Analysis of the tissue-specific distribution of mRNAs encoding the plasma membrane calcium-pumping ATPases and characterization of an alternately spliced form of PMCA4 at the cDNA and genomic levels.". J. Biol. Chem. 267 (7): 4376–85. PMID 1531651.
Olson S, Wang MG, Carafoli E, et al. (1991). "Localization of two genes encoding plasma membrane Ca2(+)-transporting ATPases to human chromosomes 1q25-32 and 12q21-23.". Genomics 9 (4): 629–41. PMID 1674727.
Strehler EE, James P, Fischer R, et al. (1990). "Peptide sequence analysis and molecular cloning reveal two calcium pump isoforms in the human erythrocyte membrane.". J. Biol. Chem. 265 (5): 2835–42. PMID 2137451.
James P, Maeda M, Fischer R, et al. (1988). "Identification and primary structure of a calmodulin binding domain of the Ca2+ pump of human erythrocytes.". J. Biol. Chem. 263 (6): 2905–10. PMID 2963820.
Brandt P, Zurini M, Neve RL, et al. (1988). "A C-terminal, calmodulin-like regulatory domain from the plasma membrane Ca2+-pumping ATPase.". Proc. Natl. Acad. Sci. U.S.A. 85 (9): 2914–8. PMID 2966397.
Howard A, Barley NF, Legon S, Walters JR (1994). "Plasma-membrane calcium-pump isoforms in human and rat liver.". Biochem. J. 303 ( Pt 1): 275–9. PMID 7945253.
Stauffer TP, Hilfiker H, Carafoli E, Strehler EE (1995). "Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes.". J. Biol. Chem. 269 (50): 32022. PMID 7989379.
Stauffer TP, Hilfiker H, Carafoli E, Strehler EE (1994). "Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes.". J. Biol. Chem. 268 (34): 25993–6003. PMID 8245032.
Váradi A, Molnár E, Ashcroft SJ (1996). "A unique combination of plasma membrane Ca2+-ATPase isoforms is expressed in islets of Langerhans and pancreatic beta-cell lines.". Biochem. J. 314 ( Pt 2): 663–9. PMID 8670083.
Santiago-García J, Mas-Oliva J, Saavedra D, Zarain-Herzberg A (1996). "Analysis of mRNA expression and cloning of a novel plasma membrane Ca(2+)-ATPase splice variant in human heart.". Mol. Cell. Biochem. 155 (2): 173–82. PMID 8700162.
Zacharias DA, DeMarco SJ, Strehler EE (1997). "mRNA expression of the four isoforms of the human plasma membrane Ca(2+)-ATPase in the human hippocampus.". Brain Res. Mol. Brain Res. 45 (1): 173–6. PMID 9105688.
Dean WL, Chen D, Brandt PC, Vanaman TC (1997). "Regulation of platelet plasma membrane Ca2+-ATPase by cAMP-dependent and tyrosine phosphorylation.". J. Biol. Chem. 272 (24): 15113–9. PMID 9182531.
Kim E, DeMarco SJ, Marfatia SM, et al. (1998). "Plasma membrane Ca2+ ATPase isoform 4b binds to membrane-associated guanylate kinase (MAGUK) proteins via their PDZ (PSD-95/Dlg/ZO-1) domains.". J. Biol. Chem. 273 (3): 1591–5. PMID 9430700.
Guerini D, García-Martin E, Gerber A, et al. (1999). "The expression of plasma membrane Ca2+ pump isoforms in cerebellar granule neurons is modulated by Ca2+.". J. Biol. Chem. 274 (3): 1667–76. PMID 9880546.
Rosado JA, Sage SO (2000). "Regulation of plasma membrane Ca2+-ATPase by small GTPases and phosphoinositides in human platelets.". J. Biol. Chem. 275 (26): 19529–35. doi:10.1074/jbc.M001319200. PMID 10748016.