PDIA6
PDIA6 (protein disulfide isomerase family A member 6, also known as P5, ERp5 and TXNDC7) is an endoplasmic reticulum protein of the protein disulfide isomerase family. It catalyses protein folding and thiol-disulfide interchange, and it also acts as a chaperone. Browse Assay Genie's current range of PDIA6 research reagents below, or read on for the biology behind the target.
PDIA6 belongs to the protein disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyse protein folding and thiol-disulfide interchange reactions. The protein inhibits the aggregation of misfolded proteins and shows both isomerase and chaperone activity. Beyond folding, PDIA6 negatively regulates the unfolded protein response (UPR): it binds UPR sensors such as ERN1, which in turn inactivates ERN1 signalling. It may also regulate the UPR through the EIF2AK3 sensor. PDIA6 additionally plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.
The PDIA6 gene encodes a protein with an N-terminal ER-signal sequence, two catalytically active thioredoxin (TRX) domains, a TRX-like domain and a C-terminal ER-retention sequence. Alternative splicing gives rise to multiple transcript variants that encode different isoforms. Within the ER lumen, PDIA6 is the main site of activity, but UniProt also records it at the cell membrane and in melanosomes.
PDIA6 is classed by HGNC in the protein disulfide isomerase and thioredoxin domain containing gene groups. Its alternative names reflect that history: P5 and ERp5 are in common use, and the earlier symbol TXNDC7 derives from the previous name thioredoxin domain containing 7. Mouse and rat each have a Pdia6 ortholog, which supports comparative work on ER proteostasis.
PDIA6 catalyses thiol-disulfide interchange and inhibits aggregation of misfolded proteins, making it a focus for studies of protein folding in the ER.
PDIA6 binds UPR sensors such as ERN1 to inactivate ERN1 signalling, and may also act through EIF2AK3, so it is relevant to UPR regulation.
PDIA6 plays a role in platelet aggregation and activation by agonists including convulxin, collagen and thrombin.
With isomerase and chaperone activities and multiple thioredoxin domains, PDIA6 is a useful model for how PDI family members combine functions.
PDIA6 is an ER protein disulfide isomerase that catalyses protein folding and thiol-disulfide interchange, and inhibits aggregation of misfolded proteins. It negatively regulates the unfolded protein response by binding sensors such as ERN1, and it contributes to platelet aggregation and activation.
PDIA6 is also called P5, ERp5 and TXNDC7, the last from the earlier name thioredoxin domain containing 7. The UniProt entry is the protein disulfide-isomerase A6. Alternative splicing of the gene produces multiple transcript variants that encode different isoforms.
Yes. Mouse and rat both have a Pdia6 ortholog, which allows PDIA6 biology to be studied in rodent systems. Researchers should check the datasheet of any product for its validated reactivity before use in a given species.
Other protein disulfide isomerase family members and ER proteostasis targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q15084; product specifications from Assay Genie datasheets.