Plasma membrane calcium-transporting ATPase 3 is an enzyme that in humans is encoded by the ATP2B3gene.[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 3. Alternatively spliced transcript variants encoding different isoforms have been identified.[2]
References
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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. PMID8634322.
Strehler EE, Zacharias DA (2001). "Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps". Physiol. Rev. 81 (1): 21–50. PMID11152753.
Strehler EE, Treiman M (2004). "Calcium pumps of plasma membrane and cell interior". Curr. Mol. Med. 4 (3): 323–35. doi:10.2174/1566524043360735. PMID15101689.
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. PMID1531651.
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. PMID7989379.
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. PMID8245032.
Brown BJ, Hilfiker H, DeMarco SJ, et al. (1996). "Primary structure of human plasma membrane Ca(2+)-ATPase isoform 3". Biochim. Biophys. Acta. 1283 (1): 10–3. doi:10.1016/0005-2736(96)00108-3. PMID8765088.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID8889548.
Moreau R, Daoud G, Masse A, et al. (2004). "Expression and role of calcium-ATPase pump and sodium-calcium exchanger in differentiated trophoblasts from human term placenta". Mol. Reprod. Dev. 65 (3): 283–8. doi:10.1002/mrd.10303. PMID12784250.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Martin R, Harvey NC, Crozier SR, et al. (2007). "Placental calcium transporter (PMCA3) gene expression predicts intrauterine bone mineral accrual". Bone. 40 (5): 1203–8. doi:10.1016/j.bone.2006.12.060. PMID17336174.
