PDIA6 Proteins

Protein Information

P5 is a novel protein that was originally identified in humans. Functionally, P5 has been shown to have peptide binding ability and chaperone activity specific to certain proteins. P5 shares several structural similarities to PDI, an important protein of the ER. The deduced amino acid sequence of P5 shows that it contains the ER retention signal KDEL. P5 also contains two CXXC-like motifs, a motif responsible for oxidoreductase activity. These two CXXC motifs are found on the N- and C-terminus of the protein, one at each end. Studies suggest that the N-terminal CXXC motif is more important than the second for isomerase activity. Contrary to most of the PDI-like proteins, P5 is not stress-inducible.

Synonyms

1700015E05Rik; AL023058; C77895; CaBP1; CaBP5; Calcium-binding protein 1; endoplasmic reticulum protein 5; ER protein 5; ERP5; P5; Pdia6; protein disulfide isomerase A6; protein disulfide isomerase associated 6; protein disulfide isomerase family A member 6; protein disulfide isomerase family A, member 6; protein disulfide isomerase P5; protein disulfide isomerase-associated 6; protein disulfide isomerase-related protein; protein disulfide-isomerase A6; thioredoxin domain containing 7; thioredoxin domain containing 7 (protein disulfide isomerase); thioredoxin domain-containing protein 7; TXNDC7