cDNA cloning of a cytosolic protein tyrosine phosphatase (RKPTP) from rat kidney
Open Access
- 19 October 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 353 (3) , 305-308
- https://doi.org/10.1016/0014-5793(94)01064-1
Abstract
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 p43ν‐abl tyrosine kinase, as a substrate.Keywords
This publication has 17 references indexed in Scilit:
- The role of protein tyrosine phosphatases in density‐dependent growth control of normal rat kidney cellsFEBS Letters, 1993
- 1002 Protein Phosphatases?Annual Review of Cell Biology, 1992
- cDNA cloning of rat LRP, a receptor like protein tyrosine phosphatase, and evidence for its gene regulation in cultured rat niesangial cellsBiochemical and Biophysical Research Communications, 1992
- Molecular cloning and chromosomal mapping of a human protein-tyrosine phosphatase LC-PTPBiochemical and Biophysical Research Communications, 1992
- Cloning and characterization of a mouse cDNA encoding a cytoplasmic protein-tyrosine-phosphatase.Proceedings of the National Academy of Sciences, 1992
- A protein-tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinasesNature, 1991
- Molecular cloning and expresion of a protein‐tyrosine phosphatase showing homology with transcription factors Fos and JunFEBS Letters, 1991
- Human placenta protein-tyrosine-phosphatase: amino acid sequence and relationship to a family of receptor-like proteins.Proceedings of the National Academy of Sciences, 1989
- Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferaseGene, 1988
- A simple and very efficient method for generating cDNA librariesGene, 1983