@article{5528ffbf22c04986b0755e4d54a9349f,
title = "Nucleotide sequence of the human 70 kDa peroxisomal membrane protein: a member of ATP-binding cassette transporters",
abstract = "The cDNA sequence of human liver 70 kDa peroxisomal membrane protein (hPMP70) was determined. The nucleotide sequence contains an open reading frame of 1977 base pairs and encodes an amino acid sequence of 659 residues which exhibits 95.0% identity with that of rat liver PMP70. hPMP70 shares close similarity to the members of a superfamily of ATP-binding transport proteins.",
keywords = "ATP-binding cassette, Multi-drug resistance P-glycoprotein, PMP70, Peroxisome",
author = "Keiju Kamijo and Takehiko Kamijo and Ichiro Ueno and Takashi Osumi and Takashi Hashimoto",
note = "Funding Information: ABC superfamily are composed of two hydrophobic and two ATP-binding domains [6]. PMP70 contains one hydrophobic and one ATP-binding domain in a single polypcptide. Thus, PMP70 seems to act as ho-modimer. Recently, a carboxy-terminai tripeptide, serine-lysine-leucine-COOH (SKL), was characterized to be a peroxisome targeting signal [14,15]. However, hPMP70 and rPMP70 do not contain this SKL motif. The carbox'y-terminal region of PMP70, which corresponds to the ATP-binding domain, is supposed to be exposed to cytosol [4], thus the peroxisome targeting signal of PMP70 may reside on its amino-terminal domain. We thank Drs. Y. Ebina and M. Mori for providing us with a human hepatic cDNA library. This work was supported in part by Grants-in-Aid for Scientific Research from the Ministry of Education, Science, and Culture of Japan. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",
year = "1992",
month = feb,
day = "11",
doi = "10.1016/0167-4781(92)90510-7",
language = "English",
volume = "1129",
pages = "323--327",
journal = "Biochimica et Biophysica Acta - Gene Structure and Expression",
issn = "0167-4781",
publisher = "Elsevier BV",
number = "3",
}