Ca-1D

Drosophila melanogaster

Ca[2+]-channel protein alpha[[1]] subunit D (Ca-alpha1D) encodes the pore-forming alpha subunit of an L-type voltage-gated Ca[2+] channel expressed in neurons. It mediates Ca[2+] influx, affecting action potential generation and muscle contraction.

Calx

Drosophila melanogaster

Na/Ca-exchange protein (Calx) encodes a Na-Ca exchanger involved in phototransduction and response to endoplasmic reticulum stress.

Rbm20

Mus musculus

PHENOTYPE: Mice homozygous for an allele lacking the RNA recognition motif exhibit increased titin compliance, and attenuated Frank-Starling mechanism. [provided by MGI curators]

ca

Drosophila melanogaster

claret (ca) encodes a protein that is required for wild-type eye color. ca mutant flies show a wine-red eye color.

Sln

Homo sapiens

Sarcoplasmic reticulum Ca(2+)-ATPases are transmembrane proteins that catalyze the ATP-dependent transport of Ca(2+) from the cytosol into the lumen of the sarcoplasmic reticulum in muscle cells. This gene encodes a small proteolipid that regulates several sarcoplasmic reticulum Ca(2+)-ATPases. The transmembrane protein interacts with Ca(2+)-ATPases and reduces the accumulation of Ca(2+) in the sarcoplasmic reticulum without affecting the rate of ATP hydrolysis. [provided by RefSeq, Jul 2008]

Slc8a1

Homo sapiens

In cardiac myocytes, Ca(2+) concentrations alternate between high levels during contraction and low levels during relaxation. The increase in Ca(2+) concentration during contraction is primarily due to release of Ca(2+) from intracellular stores. However, some Ca(2+) also enters the cell through the sarcolemma (plasma membrane). During relaxation, Ca(2+) is sequestered within the intracellular stores. To prevent overloading of intracellular stores, the Ca(2+) that entered across the sarcolemma must be extruded from the cell. The Na(+)-Ca(2+) exchanger is the primary mechanism by which the Ca(2+) is extruded from the cell during relaxation. In the heart, the exchanger may play a key role in digitalis action. The exchanger is the dominant mechanism in returning the cardiac myocyte to its resting state following excitation.[supplied by OMIM, Apr 2004]

ncx-3

Caenorhabditis elegans

Predicted to enable calcium:sodium antiporter activity; calmodulin binding activity; and metal ion binding activity. Predicted to be involved in metal ion transport. Predicted to be located in membrane. Expressed in dorsal nerve cord; head neurons; phasmid neurons; and ventral nerve cord.

PMCA

Drosophila melanogaster

plasma membrane calcium ATPase (PMCA) encodes a P-type ion pump found in the plasma membrane. It functions as a low-capacity, high-affinity Ca[2+]-extrusion mechanism, which is required for maintaining resting Ca[2+] levels in all cells. In the larval neuromuscular junction it plays an important role in restoring resting Ca[2+] levels after pre- or post-synaptic Ca[2+] influx.

Nrxn1

Mus musculus

PHENOTYPE: Mice homozygous for a knock-out allele exhibit reduced Ca(2+)-dependent binding of alpha-latrotoxin to brain membranes. Isolated synaptosomes display only a small reduction in alpha-latrotoxin -triggered glutamate release in the absence of Ca(2+) but show a major decrease in the presence of Ca(2+). [provided by MGI curators]

CA11

Homo sapiens

Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. They show extensive diversity in tissue distribution and in their subcellular localization. CA XI is likely a secreted protein, however, radical changes at active site residues completely conserved in CA isozymes with catalytic activity, make it unlikely that it has carbonic anhydrase activity. It shares properties in common with two other acatalytic CA isoforms, CA VIII and CA X. CA XI is most abundantly expressed in brain, and may play a general role in the central nervous system. [provided by RefSeq, Jul 2008]