Protein disulfide-isomerase precursor341)
From DrugPedia: A Wikipedia for Drug discovery
Contents |
[edit] Source Organism
Mus musculus (Mouse).
[edit] Taxomomy
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;Muroidea; Muridae; Murinae; Mus.
[edit] Subcellular Localization
Endoplasmic reticulum; endoplasmic reticulum lumen (By similarity). Melanosome (By similarity). Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces (By similarity).
[edit] Developmental Stage
[edit] Similarity
Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.
[edit] Post translational Modification
[edit] 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 (By similarity).
