ATP2B4

ATP2B4
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1CFF, 2KNE
Identifiers
Aliases	ATP2B4, ATP2B2, MXRA1, PMCA4, PMCA4b, PMCA4x, ATPase plasma membrane Ca2+ transporting 4
External IDs	MGI: 88111 HomoloGene: 48034 GeneCards: ATP2B4
Genetically Related Diseases
malaria[1]
Gene ontology Molecular function • nucleotide binding • PDZ domain binding • sodium channel regulator activity • nitric-oxide synthase binding • scaffold protein binding • metal ion binding • calmodulin binding • nitric-oxide synthase inhibitor activity • protein binding • protein phosphatase 2B binding • ATP binding • hydrolase activity • calcium-transporting ATPase activity Cellular component • integral component of membrane • cell projection • membrane • intracellular membrane-bounded organelle • T-tubule • plasma membrane • integral component of plasma membrane • sperm flagellum • protein complex • sperm principal piece • basolateral plasma membrane • Z disc • caveola • neuron projection • sarcolemma Biological process • negative regulation of nitric oxide mediated signal transduction • flagellated sperm motility • negative regulation of adrenergic receptor signaling pathway involved in heart process • regulation of cardiac conduction • negative regulation of nitric-oxide synthase activity • negative regulation of calcineurin-NFAT signaling cascade • negative regulation of citrulline biosynthetic process • negative regulation of peptidyl-cysteine S-nitrosylation • regulation of transcription from RNA polymerase II promoter • calcium ion import across plasma membrane • response to hydrostatic pressure • cellular calcium ion homeostasis • ion transport • positive regulation of peptidyl-serine phosphorylation • cellular response to epinephrine stimulus • ion transmembrane transport • negative regulation of nitric oxide biosynthetic process • calcium ion transmembrane transport • calcium ion transmembrane import into cytosol • spermatogenesis • transport • positive regulation of cAMP-dependent protein kinase activity • regulation of cell cycle G1/S phase transition • regulation of sodium ion transmembrane transport • calcium ion export • hippocampus development • negative regulation of arginine catabolic process • neural retina development • negative regulation of the force of heart contraction • calcium ion transport • negative regulation of cardiac muscle hypertrophy in response to stress Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	493	381290
Ensembl	ENSG00000058668	ENSMUSG00000026463
UniProt	P23634	Q6Q477
RefSeq (mRNA)	NM_001684 NM_001001396	NM_001167949 NM_213616
RefSeq (protein)	NP_001001396.1 NP_001675.3	NP_001161421.1 NP_998781.1
Location (UCSC)	Chr 1: 203.63 – 203.74 Mb	Chr 1: 133.7 – 133.8 Mb
PubMed search	[2]	[3]
Wikidata

View/Edit Human

View/Edit Mouse

Plasma membrane calcium-transporting ATPase 4 is an enzyme that in humans is encoded by the ATP2B4 gene.^[4][5]

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.^[5]

Interactions

ATP2B4 has been shown to interact with CASK.^[6]

References

1. "Diseases that are genetically associated with ATP2B4 view/edit references on wikidata".
2. "Human PubMed Reference:".
3. "Mouse PubMed Reference:".
4. Olson S, Wang MG, Carafoli E, Strehler EE, McBride OW (Jul 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.
5. "Entrez Gene: ATP2B4 ATPase, Ca++ transporting, plasma membrane 4".
6. Schuh, Kai; Uldrijan Stjepan; Gambaryan Stepan; Roethlein Nicola; Neyses Ludwig (Mar 2003). "Interaction of the plasma membrane Ca²⁺ pump 4b/CI with the Ca²⁺/calmodulin-dependent membrane-associated kinase CASK". J. Biol. Chem. United States. 278 (11): 9778–83. doi:10.1074/jbc.M212507200. ISSN 0021-9258. PMID 12511555.

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. doi:10.1016/0304-4157(95)00017-8. 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. doi:10.2174/1566524043360735. 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. doi:10.1111/j.1432-1033.1992.tb16784.x. 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.
• 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. doi:10.1073/pnas.85.9.2914. PMC 280113. 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. doi:10.1042/bj3030275. PMC 1137587. 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. doi:10.1042/bj3140663. PMC 1217098. 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 Ca²⁺-ATPase splice variant in human heart". Mol. Cell. Biochem. 155 (2): 173–82. doi:10.1007/BF00229314. PMID 8700162.
• Zacharias DA, DeMarco SJ, Strehler EE (1997). "mRNA expression of the four isoforms of the human plasma membrane Ca²⁺-ATPase in the human hippocampus". Brain Res. Mol. Brain Res. 45 (1): 173–6. doi:10.1016/S0169-328X(97)00009-0. 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. doi:10.1074/jbc.272.24.15113. 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. doi:10.1074/jbc.273.3.1591. 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. doi:10.1074/jbc.274.3.1667. 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.