Plasma membrane calcium-transporting ATPase 1 is an enzyme that in humans is encoded by the ATP2B1 gene.[5][6]

ATP2B1
Identifiers
AliasesATP2B1, ATPase, Ca++ transporting, plasma membrane 1, PMCA1, PMCA1kb, ATPase plasma membrane Ca2+ transporting 1
External IDsMGI: 104653 HomoloGene: 55597 GeneCards: ATP2B1
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for ATP2B1
Genomic location for ATP2B1
Band12q21.33Start89,588,049 bp[1]
End89,709,300 bp[1]
RNA expression pattern
PBB GE ATP2B1 215716 s at fs.png

PBB GE ATP2B1 212930 at fs.png

PBB GE ATP2B1 209281 s at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001001323
NM_001682

NM_026482
NM_001359506
NM_001359507
NM_001359508
NM_001359509

RefSeq (protein)

NP_080758
NP_001346435
NP_001346436
NP_001346437
NP_001346438

Location (UCSC)Chr 12: 89.59 – 89.71 MbChr 10: 98.91 – 99.03 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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 1. Alternatively spliced transcript variants encoding different isoforms have been identified.[6]

ReferencesEdit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000070961 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019943 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:".
  4. ^ "Mouse PubMed Reference:".
  5. ^ 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.
  6. ^ a b "Entrez Gene: ATP2B1 ATPase, Ca++ transporting, plasma membrane 1".

External linksEdit

Further readingEdit

  • 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.
  • Kessler F, Falchetto R, Heim R, et al. (1992). "Study of calmodulin binding to the alternatively spliced C-terminal domain of the plasma membrane Ca2+ pump". Biochemistry. 31 (47): 11785–92. doi:10.1021/bi00162a016. PMID 1332771.
  • Wang KK, Wright LC, Machan CL, et al. (1991). "Protein kinase C phosphorylates the carboxyl terminus of the plasma membrane Ca(2+)-ATPase from human erythrocytes". J. Biol. Chem. 266 (14): 9078–85. PMID 1827443.
  • Strehler EE, Strehler-Page MA, Vogel G, Carafoli E (1989). "mRNAs for plasma membrane calcium pump isoforms differing in their regulatory domain are generated by alternative splicing that involves two internal donor sites in a single exon". Proc. Natl. Acad. Sci. U.S.A. 86 (18): 6908–12. doi:10.1073/pnas.86.18.6908. PMC 297959. PMID 2528729.
  • James PH, Pruschy M, Vorherr TE, et al. (1989). "Primary structure of the cAMP-dependent phosphorylation site of the plasma membrane calcium pump". Biochemistry. 28 (10): 4253–8. doi:10.1021/bi00436a020. PMID 2548572.
  • Verma AK, Filoteo AG, Stanford DR, et al. (1988). "Complete primary structure of a human plasma membrane Ca2+ pump". J. Biol. Chem. 263 (28): 14152–9. PMID 2844759.
  • Howard A, Legon S, Walters JR (1993). "Human and rat intestinal plasma membrane calcium pump isoforms". Am. J. Physiol. 265 (5 Pt 1): G917–25. PMID 7694502.
  • 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.
  • Kumar R, Haugen JD, Penniston JT (1993). "Molecular cloning of a plasma membrane calcium pump from human osteoblasts". J. Bone Miner. Res. 8 (4): 505–13. doi:10.1002/jbmr.5650080415. PMID 8386431.
  • Hilfiker H, Strehler-Page MA, Stauffer TP, et al. (1993). "Structure of the gene encoding the human plasma membrane calcium pump isoform 1". J. Biol. Chem. 268 (26): 19717–25. PMID 8396145.
  • Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • 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. PMID 8889548.
  • Benkwitz C, Kubisch C, Kraft K, Neyses L (1997). "Investigation of the Met-267 Arg exchange in isoform 1 of the human plasma membrane calcium pump in patients with essential hypertension by the amplification-created restriction site technique". J. Mol. Med. 75 (1): 62–6. doi:10.1007/s001090050088. PMID 9020386.
  • Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
  • Elshorst B, Hennig M, Försterling H, et al. (1999). "NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump". Biochemistry. 38 (38): 12320–32. doi:10.1021/bi9908235. PMID 10493800.