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Molecular cloning of a novel protein‐tyrosine phosphatase containing a membrane‐binding domain and GLGF repeats
Author(s) -
Maekawa Kazuhiko,
Imagawa Noriko,
Nagamatsu Masaaki,
Harada Shigenori
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80273-4
Subject(s) - gene isoform , amino acid , complementary dna , microbiology and biotechnology , protein tyrosine phosphatase , peptide sequence , biology , biochemistry , coding region , tyrosine , gene
A full‐length cDNA encoding a novel cytosolic protein‐tyrosine phosphatase (PTP), PTP‐BAS, was cloned from human basophils. Due to in‐frame deletions in the coding region, PTP‐BAS exists in three isoforms: 7,455 bp (2,485 aa) for type 1, 7,398 bp (2,466 aa) for type 2 and 6,882 bp (2,294 aa) for type 3. All three isoforms contain a single PTP catalytic domain at the carboxyl termini as well as two distinct structural sequences. Amino terminal sequences of 300 amino acids are homologous to membrane‐binding domains of eytoskeleton‐associated proteins. Three 90 amino acid internal repetitive sequences are homologous to the GLGF repeats found in guanylate kinase proteins. PTP‐BAS was expressed in various human tissues, especially highly in the kidney and lung. Interestingly, the BAS mRNA level in the fetal brain was remarkably high.