| Primary information |
|---|
| ID | 30161 |
| Uniprot ID | P09103 |
| Description | Protein disulfide-isomerase precursor (EC 5.3.4.1) (PDI) (Prolyl 4-hydroxylase subunit beta) (Cellular thyroid hormone-binding protein)(p55) (Erp59). |
| Organism | Mus musculus |
| Txonomy | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;Muroidea; Muridae; Murinae; Mus. |
| Subcellular Location | Endoplasmic reticulum; endoplasmic reticulum lumen. Melanosome. Note=Highly abundant. In some cell t |
| Developmental Stage | NA |
| Similarity | Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains. |
| Post Translational Modification | NA |
| Function | This multifunctional protein catalyzes the formation; breakage and rearrangement of disulfide bonds. At the cell surface; seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell; seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations; functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations; facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. |
| Length | 509 |
| Molecular Weight | 57144 |
| Reference | NA |
| Hormone | NA |
| PDB ID | NA
|