Human ERp29: Isolation, primary structural characterisation and two-dimensional gel mapping

• Published in: Electrophoresis 2000-11, Vol.21 (17), p.3785-3796
• Main Authors: Hubbard, Michael J., McHugh, Nicola J.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Cell Extracts; Electrophoresis, Gel, Two-Dimensional - methods; Endoplasmic reticulum; Endoplasmic Reticulum - chemistry; Functional genomics; Heat-Shock Proteins - analysis; Humans; Molecular Sequence Data; Peptide Mapping; Proteome; Rats; Reticuloplasmin; Two-dimensional gel
• ISSN: 0173-0835; 1522-2683
• DOI: 10.1002/1522-2683(200011)21:17<3785::AID-ELPS3785>3.0.CO;2-2

Recently we characterised a novel 29 kDa endoplasmic reticulum protein that is widely expressed in rat tissues, and named it ERp29. Several ERp29‐like gene products have been reported in human tissues but uncertainty surrounds their relationships with each other and rat ERp29. To clarify these issues, ERp29 was isolated from human liver and characterised by primary structural analysis and two‐dimensional gel mapping. Comparisons with rat ERp29 revealed striking homologies both in sequence and physical properties. Characterisation of the isoelectric heterogeneity and anomalous mass on two‐dimensional gels enabled two reported homologues (UL35 and ERp31) to be identified as ERp29. Resolution of a sequence discrepancy led to unequivocal correlation of human ERp29 with the cognate cDNA previously named ERp31 and ERp28. Consequent links established to human genome and proteome projects showed that ERp29 is encoded by a gene on chromosome 12 that is expressed universally in human tissues. Together, these findings unified various ERp29 homologues as products of a single gene orthologous to rat ERp29 and established ERp29 as the only known member of a new protein class. Investigations of ERp29 function in human health and disease should benefit from the integrated links between genome, proteome and murine model organisms established here.*