AAB22262.2
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
57,116 Da
NCBI Official Full Name
protein disulfide isomerase, partial
NCBI Official Synonym Full Names
prolyl 4-hydroxylase, beta polypeptide
NCBI Official Synonym Symbols
DSI; GIT; PDI; PHDB; PDIA1; PO4DB; PO4HB; PROHB; ERBA2L; P4Hbeta [Similar Products]
NCBI Protein Information
protein disulfide-isomerase; cellular thyroid hormone-binding protein; collagen prolyl 4-hydroxylase beta; glutathione-insulin transhydrogenase; p55; procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide; prolyl 4-hydroxylase subunit beta; protein disulfide isomerase family A, member 1; protein disulfide isomerase-associated 1; protein disulfide isomerase/oxidoreductase; protocollagen hydroxylase; thyroid hormone-binding protein p55
UniProt Protein Name
Protein disulfide-isomerase
UniProt Synonym Protein Names
Cellular thyroid hormone-binding protein; Prolyl 4-hydroxylase subunit beta; p55
UniProt Synonym Gene Names
UniProt Entry Name
PDIA1_HUMAN
NCBI Summary for PDI
This gene encodes 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. [provided by RefSeq, Jul 2008]
UniProt Comments for PDI
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. Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1. Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex. Belongs to the protein disulfide isomerase family.
Protein type: Nuclear receptor co-regulator; Isomerase; Oxidoreductase; EC 5.3.4.1; Endoplasmic reticulum
Chromosomal Location of Human Ortholog: 17q25
Cellular Component: focal adhesion; endoplasmic reticulum; endoplasmic reticulum lumen; melanosome; extracellular region; ER-Golgi intermediate compartment; plasma membrane
Molecular Function: protein binding; enzyme binding; procollagen-proline 4-dioxygenase activity; protein heterodimerization activity; endopeptidase activity; protein disulfide isomerase activity
Biological Process: response to reactive oxygen species; extracellular matrix organization and biogenesis; protein folding; cell redox homeostasis; lipoprotein metabolic process; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; proteolysis
Disease: Cole-carpenter Syndrome 1
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