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DNA Research 2003 10(3):123-128; doi:10.1093/dnares/10.3.123
© 2003 by Kazusa DNA Research Institute
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Identification of a Human cDNA Sequence Which Encodes a Novel Membrane-associated Protein Containing a Zinc Metalloprotease Motif

Ying-Chun Bao1, Hiromichi Tsuruga2, Momoki Hirai3, Kazuki Yasuda4, Norihide Yokoi4, Toshio Kitamura1 and Hidetoshi Kumagai2,5,*

1Division of Cell Therapy 6-1 Shirokanedai 4-chome, Minato-ku, Tokyo 108-8639, Japan
2Division of Hematopoietic Factors, The Advanced Clinical Research Center, The Institute of Medical Science, University of Tokyo 6-1 Shirokanedai 4-chome, Minato-ku, Tokyo 108-8639, Japan
3Department of Biological Sciences, Graduate School of Science, University of Tokyo 3-1 Hongo 7-chome, Bunkyo-ku, Tokyo 113-8655, Japan
4Department of Metabolic Disorder Research Institute, International Medical Center of Japan 21-1 Toyama 1-chome, Shinjuku-ku, Tokyo 162-8655, Japan
5Chugai Pharmaceutical Co., Ltd. 41-8 Takada 3-chome, Toshima-ku, Tokyo 171-8545, Japan

* To whom correspondence should be addressed. Tel. +81-3-3987-3490, Fax. +81-3-3984-7874, E-mail: kumagaihdt{at}chugai-pharm.co.jp

We report the cloning and characterization of a human cDNA predicted to encode a novel hydrophobic protein containing four transmembrane domains and a zinc metalloprotease motif, HEXXH, between the third and fourth transmembrane domains, and have named the molecule metalloprotease-related protein-1 (MPRP-1). The MPRP-1 gene was localized to chromosome 1-p32.3 by radiation hybrid mapping, and Northern blot analysis revealed expression in many organs, with strong expression in the heart, skeletal muscle, kidney and liver. Immunohistochemical analyisis showed that MPRP-1 was localized in the endoplasmic reticulum (ER), and not in the Golgi compartment. Fragments of DNA encoding a segment homologous to the HEXXH motif of MPRP-1 are widely found in bacteria, yeast, plants, and animals. These results suggest that the MPRP-1 may have highly conserved functions, such as in intracellular proteolytic processing in the ER.

Key words: metalloprotease; membrane protein; endoplasmic reticulum


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