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	OMIM: 108732; MGI: 88111; HomoloGene: 48034; GeneCards: ATP2B4; OMA:ATP2B4 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q32.1 Start 203,626,787 bp End 203,744,081 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 E4|1 57.95 cM Start 133,627,195 bp End 133,728,779 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in saphenous vein tail of epididymis body of uterus myometrium epithelium of colon smooth muscle tissue left uterine tube muscle layer of sigmoid colon superficial temporal artery skin of arm Top expressed in spermatocyte superior frontal gyrus primary visual cortex dentate gyrus of hippocampal formation granule cell lip spermatid Rostral migratory stream esophagus genital tubercle ascending aorta More reference expression data BioGPS More reference expression data
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 P-type calcium transporter activity protein kinase binding Cellular component integral component of membrane cell projection membrane intracellular membrane-bounded organelle T-tubule plasma membrane integral component of plasma membrane sperm flagellum sperm principal piece basolateral plasma membrane Z discdkac caveola neuron projection sarcolemma cilium motile cilium protein-containing complex glutamatergic synapse integral component of presynaptic active zone membrane Biological process negative regulation of nitric oxide mediated signal transduction flagellated sperm motility 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 by RNA polymerase II 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 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 transport regulation of cytosolic calcium ion concentration negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process urinary bladder smooth muscle contraction cellular response to acetylcholine Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 493 381290 Ensembl ENSG00000058668 ENSMUSG00000026463 UniProt P23634 Q6Q477 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
Wikidata
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Plasma membrane calcium-transporting ATPase 4 is an enzyme that in humans is encoded by the ATP2B4 gene.

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.

Interactions

ATP2B4 has been shown to interact with CASK.

Further reading

• Møller JV, Juul B, le Maire M (May 1996). "Structural organization, ion transport, and energy transduction of P-type ATPases". Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes. 1286 (1): 1–51. doi:10.1016/0304-4157(95)00017-8. PMID 8634322.
• Strehler EE, Zacharias DA (January 2001). "Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps". Physiological Reviews. 81 (1): 21–50. doi:10.1152/physrev.2001.81.1.21. PMID 11152753. S2CID 9062253.
• Strehler EE, Treiman M (May 2004). "Calcium pumps of plasma membrane and cell interior". Current Molecular Medicine. 4 (3): 323–35. doi:10.2174/1566524043360735. PMID 15101689.
• Heim R, Hug M, Iwata T, Strehler EE, Carafoli E (April 1992). "Microdiversity of human-plasma-membrane calcium-pump isoform 2 generated by alternative RNA splicing in the N-terminal coding region". European Journal of Biochemistry. 205 (1): 333–40. doi:10.1111/j.1432-1033.1992.tb16784.x. PMID 1313367.
• Brandt P, Neve RL, Kammesheidt A, Rhoads RE, Vanaman TC (March 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". The Journal of Biological Chemistry. 267 (7): 4376–85. doi:10.1016/S0021-9258(18)42846-3. PMID 1531651.
• Strehler EE, James P, Fischer R, Heim R, Vorherr T, Filoteo AG, Penniston JT, Carafoli E (February 1990). "Peptide sequence analysis and molecular cloning reveal two calcium pump isoforms in the human erythrocyte membrane". The Journal of Biological Chemistry. 265 (5): 2835–42. doi:10.1016/S0021-9258(19)39877-1. PMID 2137451.
• James P, Maeda M, Fischer R, Verma AK, Krebs J, Penniston JT, Carafoli E (February 1988). "Identification and primary structure of a calmodulin binding domain of the Ca2+ pump of human erythrocytes". The Journal of Biological Chemistry. 263 (6): 2905–10. doi:10.1016/S0021-9258(18)69154-9. PMID 2963820.
• Brandt P, Zurini M, Neve RL, Rhoads RE, Vanaman TC (May 1988). "A C-terminal, calmodulin-like regulatory domain from the plasma membrane Ca2+-pumping ATPase". Proceedings of the National Academy of Sciences of the United States of America. 85 (9): 2914–8. Bibcode:1988PNAS...85.2914B. doi:10.1073/pnas.85.9.2914. PMC 280113. PMID 2966397.
• Howard A, Barley NF, Legon S, Walters JR (October 1994). "Plasma-membrane calcium-pump isoforms in human and rat liver". The Biochemical Journal. 303 ( Pt 1) (Pt 1): 275–9. doi:10.1042/bj3030275. PMC 1137587. PMID 7945253.
• Stauffer TP, Hilfiker H, Carafoli E, Strehler EE (December 1994). "Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes". The Journal of Biological Chemistry. 269 (50): 32022. doi:10.1016/S0021-9258(18)31797-6. PMID 7989379.
• Stauffer TP, Hilfiker H, Carafoli E, Strehler EE (December 1993). "Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes". The Journal of Biological Chemistry. 268 (34): 25993–6003. doi:10.1016/S0021-9258(19)74484-6. PMID 8245032.
• Váradi A, Molnár E, Ashcroft SJ (March 1996). "A unique combination of plasma membrane Ca2+-ATPase isoforms is expressed in islets of Langerhans and pancreatic beta-cell lines". The Biochemical Journal. 314 ( Pt 2) (Pt 2): 663–9. doi:10.1042/bj3140663. PMC 1217098. PMID 8670083.
• Santiago-García J, Mas-Oliva J, Saavedra D, Zarain-Herzberg A (February 1996). "Analysis of mRNA expression and cloning of a novel plasma membrane Ca(2+)-ATPase splice variant in human heart". Molecular and Cellular Biochemistry. 155 (2): 173–82. doi:10.1007/BF00229314. PMID 8700162. S2CID 33539531.
• Zacharias DA, DeMarco SJ, Strehler EE (April 1997). "mRNA expression of the four isoforms of the human plasma membrane Ca(2+)-ATPase in the human hippocampus". Brain Research. Molecular Brain Research. 45 (1): 173–6. doi:10.1016/S0169-328X(97)00009-0. PMID 9105688.
• Dean WL, Chen D, Brandt PC, Vanaman TC (June 1997). "Regulation of platelet plasma membrane Ca2+-ATPase by cAMP-dependent and tyrosine phosphorylation". The Journal of Biological Chemistry. 272 (24): 15113–9. doi:10.1074/jbc.272.24.15113. PMID 9182531.
• Kim E, DeMarco SJ, Marfatia SM, Chishti AH, Sheng M, Strehler EE (January 1998). "Plasma membrane Ca2+ ATPase isoform 4b binds to membrane-associated guanylate kinase (MAGUK) proteins via their PDZ (PSD-95/Dlg/ZO-1) domains". The Journal of Biological Chemistry. 273 (3): 1591–5. doi:10.1074/jbc.273.3.1591. PMID 9430700.
• Guerini D, García-Martin E, Gerber A, Volbracht C, Leist M, Merino CG, Carafoli E (January 1999). "The expression of plasma membrane Ca2+ pump isoforms in cerebellar granule neurons is modulated by Ca2+". The Journal of Biological Chemistry. 274 (3): 1667–76. doi:10.1074/jbc.274.3.1667. PMID 9880546.
• Rosado JA, Sage SO (June 2000). "Regulation of plasma membrane Ca2+-ATPase by small GTPases and phosphoinositides in human platelets". The Journal of Biological Chemistry. 275 (26): 19529–35. doi:10.1074/jbc.M001319200. PMID 10748016.

External links

• Human ATP2B2 genome location and ATP2B2 gene details page in the UCSC Genome Browser.
• Human ATP2B4 genome location and ATP2B4 gene details page in the UCSC Genome Browser.