Cloned (Comment) | Organism |
---|---|
expression in COS-7 cells | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
isoform pancreas-specific protein disulfide isomerase homolog, PDIp | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | PDIp exists predominantly as monomer under reducing conditions, but the dimeric form is significantly increased following the removal of the reducing agent, due to the formation of an inter-subunit disulfide bond. The oxidized PDIp exposes more hydrophobic patches and is more sensitive to protease digestion. The formation of the inter-subunit disulfide bond is mainly contributed by its non-active cysteine residue C4. The formation of the inter-subunit disulfide bond is redox-dependent and is favored under oxidizing conditions. PDIp can function as a chaperone to form stable complexes with various non-native cellular proteins, particularly under oxidizing conditions | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
pancreas | - |
Homo sapiens | - |
Subunits | Comment | Organism |
---|---|---|
More | PDIp exists predominantly as monomer under reducing conditions, but the dimeric form is significantly increased following the removal of the reducing agent, due to the formation of an inter-subunit disulfide bond. The oxidized PDIp exposes more hydrophobic patches and is more sensitive to protease digestion. The formation of the inter-subunit disulfide bond is mainly contributed by its non-active cysteine residue C4. The formation of the inter-subunit disulfide bond is redox-dependent and is favored under oxidizing conditions. PDIp can function as a chaperone to form stable complexes with various non-native cellular proteins, particularly under oxidizing conditions | Homo sapiens |