Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
apical plasma membrane | luminal acidification is required for the cell to redirect ATP7B to the apical domain and maintain it there under conditions of high Cu. Deacidification prevents Cu-directed delivery to apical domain | Homo sapiens | 16324 | - |
endosome | Cu2+ directs ATP7B to the apical domain of hepatic cells via basolateral endosomes | Homo sapiens | 5768 | - |
plasma membrane | enzyme localization at high copper concentration | Homo sapiens | 5886 | - |
plasma membrane | enzyme localization at high copper concentration. Deacidification prevents Cu-directed delivery to apical domain | Homo sapiens | 5886 | - |
trans-Golgi network | enzyme localization at low copper concentration | Homo sapiens | 5802 | - |
vesicle | - |
Homo sapiens | 31982 | - |
vesicle | Cu induces an increase in the number of ATP7B vesicles, which traverse large basolateral endosomes en route to the apical domain | Homo sapiens | 31982 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | copper directs ATP7B to the apical domain of hepatic cells via basolateral endosomes | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P35670 | ATP7B | - |
Homo sapiens | Q04656 | ATP7A | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
hepatocyte | Cu-regulated localization in hepatocytes | Homo sapiens | - |
liver | Cu2+ directs ATP7B to the apical domain of hepatic cells via basolateral endosomes | Homo sapiens | - |
additional information | Cu-directed trafficking of both endogenous and exogenous ATP7B | Homo sapiens | - |
WIF-B cell | Cu levels regulate the reversible trafficking of endogenous ATP7B in polarized WIF-B cells | Homo sapiens | - |
Synonyms | Comment | Organism |
---|---|---|
ATP7A | - |
Homo sapiens |
ATP7B | - |
Homo sapiens |
Cu ATPase | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | Menkes disease results from loss-of-function mutations in ATP7A | Homo sapiens |
malfunction | Wilson's disease results from loss-of-function mutations in ATP7B. Loss of ATP7B function leads to excess Cu accumulation in the brain, kidney and particularly in the liver, owing to defective biliary Cu excretion across the apical surface of hepatocytes. Wilson's disease mutation affects the intracellular trafficking of ATP7B, while having little effect on ATPase activity itself, indicating that a mislocalization of ATP7B is sufficient to cause the disease | Homo sapiens |
additional information | Cu-directed trans-Golgi network-to-apical trafficking occurs via a basolateral compartment in hepatocytes in vivo | Homo sapiens |
physiological function | cellular Cu homeostasis is highly regulated and is achieved in part by two intracellular Cu-transporting P-type ATPases, ATP7A and ATP7B. When Cu is low, the enzymes pump cytosolic Cu into the luminal spaces in the secretory pathway to supply Cu to newly synthesized cuproenzymes. When Cu is high, Cu ATPases exit the trans-Golgi network in vesicles and move near the plasma membrane, where they extrude Cu from the cell | Homo sapiens |
physiological function | cellular Cu homeostasis is highly regulated and is achieved in part by two intracellular Cu-transporting P-type ATPases, ATP7A and ATP7B. When Cu is low, the enzymes pump cytosolic Cu into the luminal spaces in the secretory pathway to supply Cu to newly synthesized cuproenzymes. When Cu is high, Cu ATPases exit the trans-Golgi network in vesicles and move near the plasma membrane, where they extrude Cu from the cell. Cu induces an increase in the number of ATP7B vesicles, which traverse large basolateral endosomes en route to the apical domain | Homo sapiens |