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This gene encodes a bifunctional signal transduction molecule. Dopaminergic and glutamatergic receptor stimulation regulates its phosphorylation and function as a kinase or phosphatase inhibitor. As a target for dopamine, this gene may serve as a therapeutic target for neurologic and psychiatric disorders. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2011].

The Annexins are a family of structurally similar proteins. Annexins bind to phospholipids and may be involved in regulation of membrane transport, membrane channel activity, and interaction of the cell membrane with the extracellular matrix. Annexin A7 is a member of the annexin family of calcium dependent phospholipid binding proteins. The Annexin A7 gene contains 14 exons and spans approximately 34 kb of DNA. Structural analysis of the protein suggests that Annexin A7 is a membrane bindin

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hema

The Annexins are a family of structurally similar proteins. Annexins bind to phospholipids and may be involved in regulation of membrane transport, membrane channel activity, and interaction of the cell membrane with the extracellular matrix. Annexin A7 is a member of the annexin family of calcium dependent phospholipid binding proteins. The Annexin A7 gene contains 14 exons and spans approximately 34 kb of DNA. Structural analysis of the protein suggests that Annexin A7 is a membrane bindin

Cathepsin D is a normal lysosomal protease that is expressed in all cells. It is an aspartyl protease with a pH optimum in the range of 3-5, and contains two N-linked oligosaccharides. Cathepsin D is synthesized as an inactive 52 kDa pro enzyme. Activation involves the proteolytic removal of the 43 amino acid profragment and an internal cleavage to generate the two-chain form made up of 34 and 14 kDa subunits. Cathepsin D contains the mannose-6-phosphate lysosomal localization signal that ta