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Plasma membrane-type Ca2+-ATPases (PMCAs) mediate the export of bivalent calcium ions from eukaryotic cells. As members of the P class of ion-motive ATPases, PMCAs are a functionally diverse group of proteins that are derived from alternatively spliced transcripts originating from four distinct genes, PMCA1, 2, 3, and 4. The expression of different PMCA isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, and with respect to the physiological

Dickkopf 3, like DKK1, DKK2, and DKK4, possesses an N terminal signal peptide and 2 conserved cysteine rich domains, which are separated by a linker region and contain 10 cysteine residues each. The second cysteine region has a putative lipid binding function that may facilitate WNT/DKK interactions at the plasma membrane. The linker region contains 50 to 55 amino acids in DKK1, DKK2, and DKK4, whereas in DKK3 it contains only 12 amino acids. All DKKs have several potential sites for cleava

Direct ligand for the ERBB4 tyrosine kinase receptor. Binding results in ligand-stimulated tyrosine phosphorylation and activation of the receptor. Does not bind to the EGF receptor, ERBB2 or ERBB3 receptors. May be a survival factor for oligodendrocytes.

Caspase-activated deoxyribonuclease(CAD) also designated DNA fragmentation factor 45 kDa subunit (DFF-45)and Caspase-activated DNase. CAD is a nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology. ICAD (DNA fragmentation factor alpha subunit) (DNA fragmentation factor 45 kDa subunit) (DFF-45) (Inhibitor of CAD) is inhibitor of the caspase-activated DNase (DFF44).