Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum

FEBS Letters

Demmer, Jerome¹  Zhou, ChaoMing¹  Hubbard, Michael J¹ 

[1] Department of Biochemistry, University of Otago, P.O. Box 56, Dunedin, New Zealand

关键词: Endoplasmic reticulum;    Reticuloplasmin;    Protein disulfide isomerase;    Stress response;    Enamel cell;    ER;    endoplasmic reticulum;    RT;    reverse transcription;    PCR;    polymerase chain reaction;    kb;    kilobase(s);    bp;    base pair(s);   

DOI  :  10.1016/S0014-5793(96)01513-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have isolated a full-length cDNA clone for a novel 29 kDa protein that is highly expressed in rat enamel cells. The clone encodes a 259-residue protein, here named ERp29, with structural features (signal peptide and a variant endoplasmic reticulum-retention motif, KEEL) that indicate it is a reticuloplasmin. ERp29 has limited homology with protein disulfide isomerase and its cognates, but lacks their characteristic thioredoxin-like catalytic moiety and calcium-binding motifs. ERp29 mRNA was expressed in all rat tissues tested, and a homologous transcript was detected in other animal livers (primate, ruminant, marsupial). In human hepatoma cells, ERp29 mRNA expression was not increased by stresses (tunicamycin, calcium ionophore) that induced other reticuloplasmins. We conclude that ERp29 is a new, highly conserved member of the reticuloplasmin family which is widely expressed. The apparent lack of both calcium binding properties and stress responsiveness distinguish ERp29 from all major reticuloplasmins characterised to date.

【 授权许可】

Unknown