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• W2002588081 abstract "Protein disulphide isomerases belong to the thioredoxin superfamily of protein-thiol oxidoreductases that have two double-cysteine redox-active sites and take part in protein folding in the endoplasmic reticulum (ER). We report here the cloning of a Pichia pastoris genomic DNA fragment (2919 bp) that encodes the full length of a protein disulphide isomerase (PpPDI). The deduced amino acid sequence of PDI consists of 517 residues and carries the two characteristic PDI-type redox-active domains -CGHC-, separated by 338 residues, and two potential N-glycosylation sites. The N-terminal end forms a putative signal sequence, and an acidic C-terminal region represents a possible calcium-binding domain. Together with the -HDEL ER retrieval sequence at the C-terminus, these features indicate that the gene encodes a redox-active ER-resident protein disulphide isomerase. The nucleotide sequence, which also contains two other open reading frames, has been submitted to the EMBL Nucleotide Sequence Database, Accession No. AJ302014." @default.
• W2002588081 created "2016-06-24" @default.
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• W2002588081 date "2001-03-01" @default.
• W2002588081 modified "2023-10-18" @default.
• W2002588081 title "Characterization of a Gene Encoding a Pichia pastoris Protein Disulfide Isomerase" @default.
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• W2002588081 doi "https://doi.org/10.1006/bbrc.2001.4479" @default.
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