Basic Information

Symbol
PDIA5
RNA class
mRNA
Alias
Protein Disulfide Isomerase Family A Member 5 PDIR Protein Disulfide Isomerase-Related Protein Protein Disulfide Isomerase-Associated 5 Protein Disulfide-Isomerase A5 EC 5.3.4.1 FLJ30401 Protein Disulfide Isomerase Family A, Member 5
Location (GRCh38)
3:123067025-123225227
UCSC Genome Browser Search in Marker Scope
Forensic tag(s)
Mechanical injury analysis
External database
HGNC NCBI Ensembl OMIM UniProt GTEx

MANE select

Transcript ID
NM_006810.4
Sequence length
1844.0 nt
GC content
0.5228

Transcripts

ID Sequence Length GC content
NM_006810.4 NCBI
AGACGUGGCACCGGGAACUCGGAGGCGGGGAGCGGCUGGGAAGUGGCCG… 1844 nt 0.5228
Summary

This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has 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 other proteins and substrates as well. Alternative splicing results in multiple protein- and non-protein-coding transcript variants. [provided by RefSeq, Dec 2016]

Forensic Context

A study in humans demonstrated that the PDIA5 mRNA was up-regulated by 76% in pericontusional brain tissue from a patient with traumatic brain injury (TBI) compared to control tissue, indicating its differential expression in the context of neural trauma [Michael et al. DOI:10.1016/j.jocn.2004.11.003].