Protein Disulfide Isomerase (PDI)

P4HB; ERBA2L; PDIA1; PO4DB; PROHB, DSI, GIT, PDI, PO4HB, P4Hbeta; Prolyl 4-Hydroxylase Subunit Beta; Procollagen-Proline 2-Oxoglutarate 4-Dioxygenase Beta Polypeptide

SPN	V751
HGNC	8548
MGI	97464
PubMed	19476414
RGD	3244
UniProt	P07237
Wiki	PDI

PROHB is the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex.

Reference

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"Promoter of the gene for the multifunctional protein disulfide isomerase polypeptide. Functional significance of the six CCAAT boxes and other promoter elements."
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, Submitted (FEB-1996) to UniProtKB

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, Submitted (DEC-2008) to UniProtKB

"Characterization of a cDNA for human glutathione-insulin transhydrogenase (protein-disulfide isomerase/oxidoreductase)."
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"Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death."
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"Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry."
J. Biol. Chem. 277:50579-50588(2002) [PubMed] [Europe PMC] [Abstract]

"Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion."
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"Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase."
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"Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy."
Biochemistry 35:7684-7691(1996) [PubMed] [Europe PMC] [Abstract]

"The structure in solution of the B domain of protein disulfide isomerase."
J. Biomol. NMR 13:357-368(1999) [PubMed] [Europe PMC] [Abstract]

"The solution structure of the second thioredoxin-like domain of human protein disulfide-isomerase."
Submitted (NOV-2005) to the PDB data bank