cDNA cloning of a cytosolic protein tyrosine phosphatase (RKPTP) from rat kidney

FEBS Letters

Kaneko, Tetsuya²  Noguchi, Tamio¹  Ueda, Naohiko²  Kamada, Takenobu²  Xia, Chen²  Kawanishi, Sachio²  Moriyama, Toshiki²  Takenaka, Masaru²  Inoue, Takuya²  Imai, Enyu² 

[1] Department of Nutrition and Physiological Chemistry, Osaka University School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565, Japan;First Department of Medicine and Physiological Chemistry, Osaka University School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565, Japan

关键词: Protein tyrosine phosphatase;    Rat kidney;    Protein phosphorylation;    PTPase;    protein tyrosine phosphatase;    PTK;    protein tyrosine kinase;    PCR;    polymerase chain reaction;    GST;    glutathione-S-transferase;    MBP;    myelin basic protein;   

DOI  :  10.1016/0014-5793(94)01064-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A rat cDNA encoding a non-receptor type phosphotyrosine phosphatase (PTPase; EC 3.1.3.48) was identified. The 1608 bp cDNA contains a single open reading frame that predicts a 382 amino acid protein with M _r 44,438. The predicted protein has no apparent signal or transmembrane sequences, suggesting that it is a cytosolic protein. The C-terminal region has a PTPase catalytic domain that has 40–50% nucleic acid homology to other known PTPases. The N-terminal region has little amino acid sequence homology to any other known sequences. The recombinant protein of the cloned cDNA expressed in Escherichia coli was shown to possess PTPase activity using myelin basic protein, tyrosine phosphorylated by p43^ν-abl tyrosine kinase, as a substrate.

【 授权许可】

Unknown