PDIA1 This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration. Belongs to the protein disulfide isomerase family. Note: This description may include information from UniProtKB.
Protein type: EC; Endoplasmic reticulum; Isomerase; Nuclear receptor co-regulator; Oxidoreductase
Chromosomal Location of Human Ortholog: 17q25.3
Cellular Component:  endoplasmic reticulum; endoplasmic reticulum chaperone complex; endoplasmic reticulum lumen; endoplasmic reticulum-Golgi intermediate compartment; external side of plasma membrane; extracellular region; melanosome; procollagen-proline 4-dioxygenase complex
Molecular Function:  enzyme binding; integrin binding; peptide disulfide oxidoreductase activity; protein binding; protein disulfide isomerase activity; protein heterodimerization activity
Biological Process:  cell redox homeostasis; cellular protein metabolic process; cellular response to hypoxia; cellular response to interleukin-7; chylomicron assembly; interleukin-12-mediated signaling pathway; interleukin-23-mediated signaling pathway; oxidation-reduction process; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; positive regulation of viral entry into host cell; post-translational protein modification; regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; response to endoplasmic reticulum stress; very-low-density lipoprotein particle assembly
Disease: Cole-carpenter Syndrome 1
Reference #:  P07237 (UniProtKB)
Alt. Names/Synonyms: Cellular thyroid hormone-binding protein; CLCRP1; collagen prolyl 4-hydroxylase beta; DSI; ERBA2L; GIT; glutathione-insulin transhydrogenase; P4HB; P4Hbeta; p55; PDI; PDIA1; PHDB; PO4DB; PO4HB; procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide; PROHB; Prolyl 4-hydroxylase subunit beta; prolyl 4-hydroxylase, beta polypeptide; protein disulfide isomerase family A, member 1; protein disulfide isomerase-associated 1; protein disulfide isomerase/oxidoreductase; Protein disulfide-isomerase; protocollagen hydroxylase; testicular secretory protein Li 32; thyroid hormone-binding protein p55; v-erb-a avian erythroblastic leukemia viral oncogene homolog 2-like
Gene Symbols: P4HB
Molecular weight: 57,116 Da
Basal Isoelectric point: 4.76  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.

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