MGP Database

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MGP002189

UniProt Annotations

Entry Information
Gene Nameprolyl 4-hydroxylase, beta polypeptide
Protein EntryPDIA1_HUMAN
UniProt IDP07237
SpeciesHuman
Comments
Comment typeDescription
Catalytic ActivityCatalyzes the rearrangement of -S-S- bonds in proteins.
FunctionThis 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. {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:12485997}.
InteractionQ96HE7:ERO1L; NbExp=2; IntAct=EBI-395883, EBI-2564539; Q8TCT9:HM13; NbExp=3; IntAct=EBI-395883, EBI-347472; Q13162:PRDX4; NbExp=2; IntAct=EBI-395883, EBI-2211957; Q03518:TAP1; NbExp=4; IntAct=EBI-395883, EBI-747259;
MiscellaneousReduces and may activate fusogenic properties of HIV-1 gp120 surface protein, thereby enabling HIV-1 entry into the cell.
SimilarityBelongs to the protein disulfide isomerase family. {ECO:0000305}.
SimilarityContains 2 thioredoxin domains. {ECO:0000255|PROSITE- ProRule:PRU00691}.
Subcellular LocationEndoplasmic reticulum lumen. Melanosome. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources (Probable). Localizes near CD4-enriched regions on lymphoid cell surfaces. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000305}.
SubunitHomodimer. 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 (By similarity). Binds UBQLN1. Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex. {ECO:0000250}.
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