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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | This entry represents the pseudokinase domain found in membrane Guanylate Cyclase receptor guanylyl cyclase C (GC-C, also known as heat-stable enterotoxin receptor). This domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding.GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt [ , , ].Membrane (or particulate) guanylate cyclases (GCs) consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyses the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins [ , , ]. | Name | Membrane Guanylate Cyclase receptor GC-C, pseudokinase domain |
| Short Name | GC-C_PK | Type | Domain |
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