CGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates . The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase .
The taxonomic range for the selected organisms is: Drosophila melanogaster The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
cgmp-dependent protein kinase, protein kinase g, cyclic gmp-dependent protein kinase, cgkii, pkg-i, cgmp kinase, prkg1, pkg ii, cgk ii, cgmp-dependent protein kinase i, more
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SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (cGMP-dependent)
CGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates [3]. The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase [4].
the enzyme is involved in locomotion behaviour of the larvae in presence of food, so-called rover and sitter gene ecoding an isozyme termed forager, overview
reduced enzyme activity leads to increased thermotolerance of synaptic transmission at the larval neuromuscular junction, PKG and the for gene polymorphism associated with the allelic variation in for may provide populationswith natural variantion in heat stress tolerance, the for gene function in behaviour is conserved across most organisms, overview
the enzyme is involved in locomotion behaviour of the larvae in presence of food, so-called rover and sitter gene ecoding an isozyme termed forager, overview
reduced enzyme activity leads to increased thermotolerance of synaptic transmission at the larval neuromuscular junction, PKG and the for gene polymorphism associated with the allelic variation in for may provide populationswith natural variantion in heat stress tolerance, the for gene function in behaviour is conserved across most organisms, overview
the enzyme is required for CNS axon guidance. Enzyme overexpression leads to the cytoplasmic retention of transcription factor LolaT in S2 cells, suggesting a role for the enzyme in mediating the nucleocytoplasmic trafficking of Lola. The enzyme plays a role in regulating the establishment of neuronal connectivity by sequestering transcription factor Lola in the cytoplasm
the presynaptic, but not postsynaptic or glial, enzyme gene is required for synaptic vesicle recycling. The enzyme gene FOR inhibits synaptic vesicle exocytosis during low-frequency stimulation by negatively regulating presynaptic Ca2+ levels and maintains neurotransmission during high-frequency stimulation by facilitating synaptic vesicle endocytosis. Additionally, glial FOR gene negatively regulated nerve terminal growth through TGF-beta signalling, and this developmental effect is independent of the effects of the enzyme gene on neurotransmission. Overall, the enzyme gene plays a critical role in coupling synaptic vesicle exocytosis and endocytosis, thereby balancing these two components to maintain sustained neurotransmission
construction of transgenic flies by targeted expression of DG2P1 and DG2P2, and DG1 in malpigian tubule using the UAS/GAL4 system, differential localization of all 3 enzyme forms in transgenic flies, phenotypes, overview
in vitro transcription of DG2P1 and DG2P2, and DG1 by RT-PCR of cDNAs from tubule cells, targeted expression of DG2P1 and DG2P2, and DG1 in malpigian tubule using the UAS/GAL4 system, differential localization of all 3 enzyme forms in transgenic flies