5.3.4.1: protein disulfide-isomerase
This is an abbreviated version!
For detailed information about protein disulfide-isomerase, go to the full flat file.
Reaction
catalyses the rearrangement of -S-S- bonds in proteins
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Synonyms
5'-MD, 58 kDa glucose regulated protein, 58 kDa microsomal protein, AGR2, anterior gradient homolog 2, BPA-binding protein, CaBP1, CaBP2, Cellular thyroid hormone binding protein, cotyledon-specific chloroplast biogenesis factor CYO1, CYO1, DbsG, disulfide bond isomerase, disulfide bond-forming enzyme, Disulfide interchange enzyme, disulfide isomerase, Disulfide isomerase ER-60, disulfide-bond isomerase, dithiol-disulfide isomerase, Dsb, DsbA, DsbB, DsbC, DsbD, DsbG, ECaSt/PDI, endoplasmic reticulum protein EUG1, Eps1p, ER protein 57, ER58, ER60, ERcalcistorin/protein-disulfide isomerase, ERdj5, Ero1, Erp, ERP-57, ERp-72 homolog, ERp18, ERp27, ERp28, ERp44, Erp46, ERp5, ERp57, ERP59, ERP60, ERp72, Eug1p, fibronectin, gPDI-1, gPDI-2, gPDI-3, HIP-70, HlPDI-1, HlPDI-2, HlPDI-3, Iodothyronine 5'-monodeiodinase, More, Mpd1p, Mpd2p, multifunctional protein disulfide isomerase, ncgl2478, P5, P55, P58, pancreas-specific protein disulfide isomerase, PDI, PDI A4, PDI I, PDI II, pdi-15, PDI-1a, pdi-40, pdi-47, pdi-52, PDI-A, PDI-M, PDI-P5, PDI-related protein, PDI1, PDI11, PDI2, PDI7, PDI8, PDIA1, PDIA2, PDIA3, PDIA4, PDIA6, PDIL-1, PDIL-2, PDIL1-1, PDIL1;1, PDIL1Aalpha, PDIL1B, PDIL2, PDIL2-3, PDIL3A, PDIL4D, PDIL5A, PDILT, PDIp, PDIr, protein disulfide isomerase, protein disulfide isomerase 1, protein disulfide isomerase 2, protein disulfide isomerase 3, protein disulfide isomerase A1, protein disulfide isomerase A3, protein disulfide isomerase A5, protein disulfide isomerase A6, protein disulfide isomerase associated 3, Protein disulfide isomerase P5, protein disulfide isomerase-1, protein disulfide isomerase-11, protein disulfide isomerase-2, protein disulfide isomerase-3, protein disulfide isomerase-8, protein disulfide isomerase-like protein of the testis, protein disulfide isomerase-P5, protein disulfide isomerase-related chaperone Wind, Protein disulfide isomerase-related protein, protein disulfide oxidoreductase, protein disulfide reductase/isomerase, protein disulfide-isomerase A4, Protein disulphide isomerase, Protein ERp-72, protein-disulfide isomerase, R-cognin, RB60, Rearrangease, Reduced ribonuclease reactivating enzyme, Retina cognin, S-S rearrangase, SSO0192, SsPDO, thiol-disulfide oxidoreductase, thiol-protein oxidoreductase, thioredoxin domain-containing protein 5, Thyroid hormone-binding protein, Thyroxine deiodinase, TXNDC5, yPDI
ECTree
Localization
Localization on EC 5.3.4.1 - protein disulfide-isomerase
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in endothelial cells. On activation of endothelial cells, PDI remains confined to the intracellular stores of the dense tubular system and is neither released nor targeted to the cell surface
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presence of isoforms P5 and Erp57. P5 localizes to the inner side of the inner membrane
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cell surface protein
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in presence of light, level of protein disulfide isomerase protein decreases by 80%. The effect of chemical treatments coincides with the effect of the light/dark cycle
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RB60 contains an N-terminal sequence of 50 amino acids that are sufficient for chloroplast and enodplasmic reticulum targeting, after translocation to the ER the leader sequence is cleaved while it remains intact after import into chloroplasts
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RB60 contains an N-terminal sequence of 50 amino acids that are sufficient for chloroplast and enodplasmic reticulum targeting, after translocation to the ER the leader sequence is cleaved while it remains intact after import into chloroplasts
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PDI contains an endoplasmic reticulum-retention KEEL signal
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lumen
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surface-associated
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lumen, high concentration in the ER
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the enzyme contains a C-terminal endoplasmic reticulum retention signal, RB60 contains an N-terminal leader sequence of 50 amino acids that are sufficient for chloroplast and enodplasmic reticulum targeting, after translocation to the ER the leader sequence is cleaved while it remains intact after import into chloroplasts
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the enzyme contains a C-terminal endoplasmic reticulum retention signal, RB60 contains an N-terminal leader sequence of 50 amino acids that are sufficient for chloroplast and enodplasmic reticulum targeting, after translocation to the ER the leader sequence is cleaved while it remains intact after import into chloroplasts
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the enzyme contains an N-terminal ER retention signal sequence
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lumen
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ER retention/retrieval signal KQRL
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gPDI-3 has a ER retention/retrieval signal KQRL, gPDI-2 has a KRKK motif
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KRKK motif
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PDIS-1 and PDIS-2 lack the C-terminal, endoplasmic reticulum-retrieval signal, KDEL
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expression is up-regulated in ER-stress conditions
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PDI contains an endoplasmic reticulum-retention DEL signal
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PDI contains an endoplasmic reticulum-retention EEL signal
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PDI contains an endoplasmic reticulum-retention VEL signal
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3070, 649629, 651957, 651990, 652425, 652930, 702795, 702970, 703096, 704784, 704927, 705291, 714600, 715531, 727573, 728766, 746919, 747197, 747829, 747833, 747835, 747836 brenda
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lumen
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lumen, high concentration in the ER
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ERp27 contains a putative secretory pathway signal sequence and a putative endoplasmic reticulum-retention signal, overview
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exclusively in human umbilical vein endothelial cells. In endothelium, PDI remains exclusively localized in the endoplasmic reticulum, both at steady state and after thrombin stimulation
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the enzyme contains a C-terminal endoplasmic reticulum retrieval signal, SEEL
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lumen
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loosely associated with the luminal surface
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lumen, high concentration in the ER
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PDI possesses an anomalously low thiol pKa and is fine-tuned to catalyze oxidative folding in the lumen of the endoplasmic reticulum where the ambient pH of about 7 would otherwise retard thioldisulfide exchange reactions and hinder acquisition of the native fold
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lumen
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lumen, high concentration in the ER
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enzyme exists as an interconvertible mixture of monomers and dimers
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lumen
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the enzyme is among the most abundant proteins within the endoplasmic reticulum of developing grains
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GmPDIL-3a and GmPDIL-3b form protein complexes in the endoplasmic reticulum
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integral, the catalytic reaction takes place on the periplasmic side, PDI contains four transmembrane helices that surround the bound ubiquinone cofactor, overview
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associated
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associated
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associated
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of the P2 fraction
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rough. The enzyme associates with the membrane via electrostatic interactions between the acidic enzyme and the basic groups on the membrane
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membrane
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located on both sides of the membrane. The inside-located enzyme is immunochemically different from the outside-located enzyme
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rough and smooth
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PDIL1-1 is uniformly distributed in the lumen
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PDIL2-3 is localized mainly on the surface of the endoplasmic reticulum
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protein storage vacuoles
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additional information
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dual localization of RB60 via two different conserved transport mechanisms, overview
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additional information
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dual localization of RB60 via two different conserved transport mechanisms, overview
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additional information
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PDIS-1 and PDIS-2 both possess a putative N-terminal secretory signal sequence and two tandem thioredoxin-like motifs, with a CGHC active site
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additional information
subcellular localization study with wild-type and mutant enzyme, overview
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additional information
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subcellular localization study with wild-type and mutant enzyme, overview
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additional information
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presence of protein disulfide isomerase on the surface of platelet-derived microparticles. Enzyme is catalytically active and capable of both promoting platelet aggregation and disrupting insulin signaling. Platelet-derived microparticles increase the initial rates of aggregation by 4fold and the pro-aggregatory activity of micrparticles can be attenuated with an anti-PDI antibody. Anti-PDI antibodies are able to block the degradation of insulin, thereby restoring insulin signaling
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additional information
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semiquantitative analysis of the endogenous PDI distribution, overview
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additional information
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stage-specific expression and cellular localization of isozymes, overview
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additional information
cullular enzyme distribution, immunohistochemic detection, overview
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additional information
both enzyme forms co-localized with markers of the endocytic pathway and concentrate at the posterior end of the cell between the nucleus and the kinetoplast
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additional information
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both enzyme forms co-localized with markers of the endocytic pathway and concentrate at the posterior end of the cell between the nucleus and the kinetoplast
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