Activating Compound | Comment | Organism | Structure |
---|---|---|---|
curcumin | molecular basis for Fe(III)-independent curcumin potentiation of cystic fibrosis transmembrane conductance regulator activity, overview. Highly conserved aromatic and positively charged residues at the ICL1/ICL4 interface and phosphorylation site S813 are sensitive to curcumin regardless of whether Fe3+ and nucleotide-binding domain 2 are removed. Spontaneous disulfide cross-linking between curcumin-sensitive ICL1 and S795 is observed to be enough to promote channel opening as curcumin does. Curcumin may potentiate CFTR activity not only by removing inhibitory Fe3+ to release the R domain from ICL3 but also by stabilizing the stimulatory R-ICL1/ICL4 interactions | Homo sapiens | |
additional information | phosphorylation-dependent enzyme activity | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
transient expression of the enzyme in HEK-293T cells | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Fe3+ | binds at the interface of the regulatory (R) domain and intracellular loop (ICL) 3 | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | transmembrane protein | Homo sapiens | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P13569 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | stimulatory phosphorylation site S795 and S813 at the C-terminus of the R domain. The phosphorylated R domain, once released from ICL3, may function as a length- and gating-regulatory cross-linker between two transmembrane domains to promote the stimulatory interactions between the R domain and the ICL1/ICL4 interface | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
CFTR | - |
Homo sapiens |
cystic fibrosis transmembrane conductance regulator | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | the phosphorylated R domain, once released from ICL3, may function as a length- and gating-regulatory cross-linker between two transmembrane domains to promote the stimulatory interactions between the R domain and the ICL1/ICL4 interface | Homo sapiens |