ATP2B4

ATPase, Ca++ transporting, plasma membrane 4

Rendering of ATP2B4 from PDB 1CFF

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1CFF, 2KNE

Identifiers

Symbols

ATP2B4 ; ATP2B2; MXRA1; PMCA4; PMCA4b; PMCA4x

External IDs

OMIM: 108732 MGI: 88111 HomoloGene: 48034 GeneCards: ATP2B4 Gene

EC number

3.6.3.8

Gene ontology
Molecular function	• calcium-transporting ATPase activity • protein binding • calmodulin binding • ATP binding • sodium channel regulator activity • PDZ domain binding • protein phosphatase 2B binding • nitric-oxide synthase inhibitor activity • metal ion binding • nitric-oxide synthase binding • scaffold protein binding
Cellular component	• plasma membrane • integral component of plasma membrane • caveola • membrane • basolateral plasma membrane • Z disc • T-tubule • neuron projection • protein complex • sperm principal piece
Biological process	• neural retina development • regulation of transcription from RNA polymerase II promoter • cellular calcium ion homeostasis • spermatogenesis • blood coagulation • metabolic process • negative regulation of nitric oxide mediated signal transduction • hippocampus development • positive regulation of peptidyl-serine phosphorylation • ion transmembrane transport • negative regulation of nitric oxide biosynthetic process • negative regulation of nitric-oxide synthase activity • response to hydrostatic pressure • transmembrane transport • calcium ion transmembrane transport • negative regulation of calcineurin-NFAT signaling cascade • cellular response to epinephrine stimulus • calcium ion transmembrane import into cytosol • calcium ion import across plasma membrane • negative regulation of the force of heart contraction • negative regulation of arginine catabolic process • negative regulation of adrenergic receptor signaling pathway involved in heart process • calcium ion export • negative regulation of peptidyl-cysteine S-nitrosylation • regulation of sodium ion transmembrane transport • regulation of cell cycle G1/S phase transition • negative regulation of cardiac muscle hypertrophy in response to stress • negative regulation of citrulline biosynthetic process • positive regulation of cAMP-dependent protein kinase activity
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

493

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
203.63 – 203.74 Mb

Chr 1:
133.7 – 133.8 Mb

PubMed search

Plasma membrane calcium-transporting ATPase 4 is an enzyme that in humans is encoded by the ATP2B4 gene.^[1]^[2]

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.^[2]

Interactions

ATP2B4 has been shown to interact with CASK.^[3]

References

↑ 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.
1 2 "Entrez Gene: ATP2B4 ATPase, Ca++ transporting, plasma membrane 4".
↑ 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.

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) (Pt 1): 275–9. 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) (Pt 2): 663–9. 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.

Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1

3.6.2

3.6.3-4: ATPase

3.6.3

Cu++ (3.6.3.4)	Menkes/ATP7A Wilson/ATP7B

Ca+ (3.6.3.8)	SERCA ATP2A1 ATP2A2 ATP2A3 Plasma membrane ATP2B1 ATP2B2 ATP2B3 ATP2B4 SPCA ATP2C1 ATP2C2

Na+/K+ (3.6.3.9)	ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4

H+/K+ (3.6.3.10)	ATP4A

Other P-type ATPase	ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3

3.6.4

3.6.5: GTPase

3.6.5.1: Heterotrimeric G protein	G_αs G_αi GNAI1 GNAI2 GNAI3 G_αq/11 GNAQ GNA11 G_α12/13 GNA12 GNA13 Transducin GNAT1 GNAT2

3.6.5.2: Small GTPase > Ras superfamily	Rho family of GTPases: Cdc42 CDC42 TC10 TCL RhoUV RhoU RhoV Rac Rac1 2 3 RhoG RhoBTB 1 2 RhoH Rho A B C Rnd 1 2 3 RhoDF RhoF RhoD other: Ras HRAS KRAS NRAS Rab RAB23 RAB27 Arf ARF6 SAR1B ARL13B ARL6 Ran Rheb Rap RGK

3.6.5.3: Protein-synthesizing GTPase	Prokaryotic IF-2 EF-Tu EF-G Eukaryotic

3.6.5.5-6: Polymerization motors	Dynamin Tubulin

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ATP2B4

Interactions

References

Further reading