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Gene Review

PDIA4  -  protein disulfide isomerase family A,...

Homo sapiens

Synonyms: ER protein 70, ER protein 72, ERP70, ERP72, ERp-72, ...
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High impact information on PDIA4

  • NH2-terminal sequence and/or Western blot analysis revealed the identity of two of the proteins as the endoplasmic reticulum (ER) resident stress proteins GRP94 and ERp72 [1].
  • In vitro analysis revealed that PDI and ERp72 alter CT's conformation in a manner consistent with their roles in retrotranslocation and ER retention [2].
  • ERp72 was identified as one of the ER-resident oxidoreductases associating with the orphan ERp57 substrates to maintain their folding competence [3].
  • However, beta-chaperone complexes containing the ER chaperones BiP, ERp72, and ERp94 have been detected in slow folding mutants of hCG-beta subunit that lack both of the N-linked oligosaccharides (Feng, W., Matzuk, M [4].
  • The gene for the protein associated with neutrophil priming was sequenced and identified as the endoplasmic reticulum protein, ERp72, which contains three copies of the active site sequences of protein disulfide isomerase [5].

Biological context of PDIA4


Anatomical context of PDIA4


Associations of PDIA4 with chemical compounds


Other interactions of PDIA4

  • In addition, the molecular chaperones BiP, ERp72, and ERp94, but not calnexin, were found in a complex with unglycosylated, unfolded hCG-beta and may be involved in the folding of this beta form [12].
  • The identification of the genes for endoplasmic reticulum (ER)-resident GRP78, ERp72, and p58IPK proteins connected TFF1 deficiency to the unfolded protein response (UPR) [13].

Analytical, diagnostic and therapeutic context of PDIA4

  • Sequential immunoprecipitation with antibodies to MTP and apoB revealed the presence of ternary complexes containing apoB-100, MTP, and ERp72 [14].


  1. HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. Schaiff, W.T., Hruska, K.A., McCourt, D.W., Green, M., Schwartz, B.D. J. Exp. Med. (1992) [Pubmed]
  2. Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation. Forster, M.L., Sivick, K., Park, Y.N., Arvan, P., Lencer, W.I., Tsai, B. J. Cell Biol. (2006) [Pubmed]
  3. Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle. Soldà, T., Garbi, N., Hämmerling, G.J., Molinari, M. J. Biol. Chem. (2006) [Pubmed]
  4. Novel covalent chaperone complexes associated with human chorionic gonadotropin beta subunit folding intermediates. Feng, W., Bedows, E., Norton, S.E., Ruddon, R.W. J. Biol. Chem. (1996) [Pubmed]
  5. An antibody that binds a neutrophil membrane protein, ERp72, primes human neutrophils for enhanced oxidative metabolism in response to formyl-methionyl-leucyl-phenylalanine. Implications for ERp72 in the signal transduction pathway for neutrophil priming. Weisbart, R.H. J. Immunol. (1992) [Pubmed]
  6. Competitive inhibition of a set of endoplasmic reticulum protein genes (GRP78, GRP94, and ERp72) retards cell growth and lowers viability after ionophore treatment. Li, X.A., Lee, A.S. Mol. Cell. Biol. (1991) [Pubmed]
  7. Accumulation and degradation in the endoplasmic reticulum of a truncated ER-60 devoid of C-terminal amino acid residues. Urade, R., Kusunose, M., Moriyama, T., Higasa, T., Kito, M. J. Biochem. (2000) [Pubmed]
  8. Serum antibodies from halothane hepatitis patients react with the rat endoplasmic reticulum protein ERp72. Pumford, N.R., Martin, B.M., Thomassen, D., Burris, J.A., Kenna, J.G., Martin, J.L., Pohl, L.R. Chem. Res. Toxicol. (1993) [Pubmed]
  9. Isolation of ERp72 from guinea pig term placentae using heparin Sepharose affinity chromatography. Bonifacio, M.D., Steeves, T., Saunders, D.M., Sinosich, M.J. Biochem. Mol. Biol. Int. (1995) [Pubmed]
  10. Molecular characterization and expression of an alfalfa protein with sequence similarity to mammalian ERp72, a glucose-regulated endoplasmic reticulum protein containing active site sequences of protein disulphide isomerase. Shorrosh, B.S., Dixon, R.A. Plant J. (1992) [Pubmed]
  11. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. Mazzarella, R.A., Srinivasan, M., Haugejorden, S.M., Green, M. J. Biol. Chem. (1990) [Pubmed]
  12. The asparagine-linked oligosaccharides of the human chorionic gonadotropin beta subunit facilitate correct disulfide bond pairing. Feng, W., Matzuk, M.M., Mountjoy, K., Bedows, E., Ruddon, R.W., Boime, I. J. Biol. Chem. (1995) [Pubmed]
  13. Trefoil factor 1 (TFF1/pS2) deficiency activates the unfolded protein response. Torres, L.F., Karam, S.M., Wendling, C., Chenard, M.P., Kershenobich, D., Tomasetto, C., Rio, M.C. Mol. Med. (2002) [Pubmed]
  14. Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state. Linnik, K.M., Herscovitz, H. J. Biol. Chem. (1998) [Pubmed]
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