PDIA5
PDIA5 (protein disulfide isomerase family A member 5, also known as PDIR) is an endoplasmic reticulum protein of the protein disulfide isomerase family. It catalyses protein folding and thiol-disulfide interchange reactions in the ER lumen. Browse Assay Genie's current range of PDIA5 research reagents below, or read on for the biology behind the target.
PDIA5 belongs to the disulfide isomerase (PDI) family of endoplasmic reticulum proteins that catalyse protein folding and thiol-disulfide interchange reactions. These reactions help newly synthesised proteins reach their correct disulfide-bonded conformation within the ER lumen, where the protein is localised. The enzyme is classified under EC 5.3.4.1.
The PDIA5 protein has a defined domain architecture: an N-terminal ER-signal sequence, three catalytically active thioredoxin (TRX) domains, a TRX-like domain, and a C-terminal ER-retention sequence. The N-terminal TRX-like domain is the primary binding site for the major ER chaperone calreticulin, and possibly for other proteins and substrates as well. This links PDIA5 to the chaperone network that supports folding in the ER.
The PDIA5 gene is listed by HGNC within the protein disulfide isomerases group and also among the microRNA protein coding host genes. Alternative splicing produces multiple protein-coding and non-protein-coding transcript variants. The protein is also known as PDIR, and the gene has the previous symbol FLJ30401. Its earlier names were protein disulfide isomerase-associated 5 and protein disulfide isomerase family A, member 5. Mouse and rat orthologs are both named Pdia5, which allows comparative work in rodent models.
PDIA5 catalyses protein folding and thiol-disulfide interchange in the ER, so it is a relevant target for studying oxidative folding.
Its N-terminal TRX-like domain is the main binding site for calreticulin, making PDIA5 useful for studying ER chaperone complexes.
PDIA5 is one of several PDI family members, allowing comparison of thioredoxin-domain organisation and function across the family.
Alternative splicing gives protein-coding and non-coding transcripts, so PDIA5 is a subject for studying isoform-level gene regulation.
PDIA5 is an ER member of the disulfide isomerase family that catalyses protein folding and thiol-disulfide interchange reactions. It carries three catalytically active thioredoxin domains and a TRX-like domain, and it is retained in the ER lumen by a C-terminal retention sequence.
PDIA5 is also called PDIR, and its previous symbol was FLJ30401. Earlier names include protein disulfide isomerase-associated 5 and protein disulfide isomerase family A, member 5. UniProt lists it as protein disulfide-isomerase A5. Alternative splicing yields multiple transcript variants.
Yes. Mouse and rat both have an ortholog named Pdia5, so rodent systems can be used to study the gene. PDIA5 belongs to the protein disulfide isomerase family; check the datasheet of any product for its validated reactivity.
Other protein disulfide isomerase family members involved in ER protein folding, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q14554; product specifications from Assay Genie datasheets.