Aliases for ATP2A3 Gene
External Ids for ATP2A3 Gene
Previous GeneCards Identifiers for ATP2A3 Gene
This gene encodes one of the SERCA Ca(2+)-ATPases, which are intracellular pumps located in the sarcoplasmic or endoplasmic reticula of muscle cells. This enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen, and is involved in calcium sequestration associated with muscular excitation and contraction. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008]
GeneCards Summary for ATP2A3 Gene
ATP2A3 (ATPase, Ca++ Transporting, Ubiquitous) is a Protein Coding gene. Diseases associated with ATP2A3 include darier disease. Among its related pathways are Signaling by GPCR and CREB Pathway. GO annotations related to this gene include calcium-transporting ATPase activity. An important paralog of this gene is ATP2A2.
UniProtKB/Swiss-Prot for ATP2A3 Gene
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction.
Ca2+-ATPases function to maintain a low cytoplasmic conentration of Ca2+ ions. They are high affinity, low capacitance transporters and compliment the actions of the low affinity, high capacitance Na+/Ca2+ exchanger. Ca2+-ATPases are P-type ATPases and there are two varients; a plasma membrane-bound Ca2+-ATPase (PMCA) and a sacroplasmic reticulum Ca2+-ATPase (SERCA). PMCA exists as a dimer within the plasma membrane of a wide variety of cell types and, using the energy released from ATP hydrolysis, transports Ca2+ ions out of the cell against the concentration gradient. SERCA is located in the sarcoplasmic reticulum (SR) of muscle cells and transports Ca2+ ions from the cytoplasm into the SR lumen during muscle relaxation. PMCA transports one Ca2+ ion per ATP molecule hydrolyzed, whilst SERCA can transport two. PMCAs are regulated by calmodulin and the phospholipid composition of the surrounding plasma membrane. Furthermore, PMCA can be phosphorylated by PKA, PKC, Src and FAK at specific residues to influence activity. So far, only one human pathology has been linked to PMCA defects; deafness. However, SERCA defects have been implicated in a wide array of pathologies including heart failure, sperm motility defects, cataract formation, carcinogenesis, diabetes, and cardiac hypertension and hypertrophy.