Abstract
A cDNA clone coding for a protein-tyrosine phosphatase (PTPase) was isolated from a rat spleen cDNA library. Nucleotide sequence of the clone showed an open reading frame coding for a polypeptide of 363 amino acids. Expression of this clone in E. coli in an expression vector showed PTPase activity. The non-catalytic region of this PTPase located at the carboxy terminus shows homology with the basic domains of transcription factors Fos and Jun. Northern blot analysis showed that a 1.7 kb transcript was present in many tissues and cells, the highest level being in macrophages. This PTPase is a rat homolog of human T-cell PTPase although it shows 3 large deletions in the carboxy terminal non-catalytic region.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Binding Sites
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Cloning, Molecular
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DNA / metabolism
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DNA-Binding Proteins / biosynthesis
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DNA-Binding Proteins / genetics*
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Escherichia coli / genetics
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Gene Expression
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Genomic Library
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Molecular Sequence Data
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Open Reading Frames
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Phosphoprotein Phosphatases / genetics*
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Protein Tyrosine Phosphatases
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Proto-Oncogene Proteins / genetics*
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Proto-Oncogene Proteins c-fos
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Proto-Oncogene Proteins c-jun
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Rats
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Sequence Homology, Nucleic Acid
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Spleen
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Transcription Factors / biosynthesis
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Transcription Factors / genetics*
Substances
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DNA-Binding Proteins
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Proto-Oncogene Proteins
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Proto-Oncogene Proteins c-fos
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Proto-Oncogene Proteins c-jun
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Transcription Factors
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DNA
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Phosphoprotein Phosphatases
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Protein Tyrosine Phosphatases