<p>ERp29 (<db_xref db="SWISSPROT" dbkey="P52555"/>) is a ubiquitously expressed endoplasmic reticulum protein, and is involved in the processes of protein maturation and protein secretion in this organelle [<cite idref="PUB00016490"/>, <cite idref="PUB00014099"/>]. The protein exists as a homodimer, with each monomer being composed of two domains. The N-terminal domain featured in this family is organised into a thioredoxin-like fold that resembles the a domain of human protein disulphide isomerase (PDI) [<cite idref="PUB00014099"/>]. However, this domain lacks the C-X-X-C motif required for the redox function of PDI; it is therefore thought that the function of ERp29 is similar to the chaperone function of PDI [<cite idref="PUB00014099"/>]. The N-terminal domain is exclusively responsible for the homodimerisation of the protein, without covalent linkages or additional contacts with other domains [<cite idref="PUB00014099"/>]. </p> ERp29, N-terminal