| First Author | Sap J | Year | 1990 |
| Journal | Proc Natl Acad Sci U S A | Volume | 87 |
| Issue | 16 | Pages | 6112-6 |
| PubMed ID | 2166945 | Mgi Jnum | J:10677 |
| Mgi Id | MGI:59124 | Doi | 10.1073/pnas.87.16.6112 |
| Citation | Sap J, et al. (1990) Cloning and expression of a widely expressed receptor tyrosine phosphatase. Proc Natl Acad Sci U S A 87(16):6112-6 |
| abstractText | We describe the identification of a widely expressed receptor-type (transmembrane) protein tyrosine phosphatase (PTPase; EC 3.1.3.48). Screening of a mouse brain cDNA library under low-stringency conditions with a probe encompassing the intracellular (phosphatase) domain of the CD45 lymphocyte antigen yielded cDNA clones coding for a 794-amino acid transmembrane protein [hereafter referred to as receptor protein tyrosine phosphatase alpha (R-PTP-alpha)] with an intracellular domain displaying clear homology to the catalytic domains of CD45 and LAR (45% and 53%, respectively). The 142-amino acid extracellular domain (including signal peptide) of R-PTP-alpha is marked by a high serine/threonine content (32%) as well as eight potential N-glycosylation sites but displays no similarity to known proteins. Genetic mapping assigns the gene for R-PTP-alpha to mouse chromosome 2, closely linked to the Il-1a and Bmp-2a loci. The corresponding mRNA (3.0 kilobases) is expressed in most murine tissues and most abundantly expressed in brain and kidney. Antibodies against a synthetic peptide of R-PTP-alpha identified a 130-kDa protein in cells transfected with the R-PTP-alpha cDNA. |
