PDIA1_HUMAN
Source: hRBCD ; ID: IPI00010796PM19886704
PM23856902
BSc_CH
PM22954596
Marked as 'Membrane associated protein'
Confidence: high (present in two of the MS resources) Search PubMed for
(RBC AND this entry)
Gene names: P4HB , ERBA2L, PDI, PDIA1, PO4DB
Protein names and data: PDIA1_HUMAN , Protein disulfide-isomerase; PDI; 5.3.4.1 , Cellular thyroid hormone-binding protein; Prolyl 4-hydroxylase subunit beta; p55; Flags: Precursor Lenght: 508 a.a.
Mass: 57116 Da
fasta formatted sequence
Function: 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.
Catalytic activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Cellular location: Endoplasmic reticulum lumen. Melanosome. Cell membrane; Peripheral membrane protein (Potential). 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.
Database cross-references
UniProt: P07237Ensembl: ENST00000331483
MIM: 176790
neXtProt: NX_P07237
Antibodypedia: P07237 (may not find the protein thus also not any antibody)
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