Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain

Journal Article · Sat Sep 01 00:00:00 EDT 1990 · Proceedings of the National Academy of Sciences of the United States of America; (United States)

DOI:https://doi.org/10.1073/pnas.87.18.7000· OSTI ID:5464364

Kaplan, R; Morse, B; Howk, R; Ravera, M; Ricca, G; Jaye, M ^[1]; Huebner, K; Croce, C ^[2]; Schlessinger, J ^[3]

---

1. Rorer Biotechnology, Inc., King of Prussia, PA (USA)
2. Temple Univ., Philadephia, PA (USA)
3. New York Univ., NY (USA)

A human brainstem cDNA library in bacteriophage {lambda}gt11 was screened under conditions of reduced bybridization stringency with a leukocyte common antigen (LCA) probe that spanned both conserved cytoplasmic domains. cDNA encoding a receptor-linked protein-tyrosinephosphatase (protein-tyrosine-phosphate phosphohydrolase, EC 3.1.3.48), RPTPase {alpha}, has been cloned and sequenced. Human RPTPase {alpha} consists of 802 amino acids. The extracellular domain of 150 residues includes a hydrophobic signal peptide and eight potential N-glycosylation sites. This is followed by a transmembrane region and two tandemly repeated conserved domains characteristic of all RPTPases identified thus far. The gene for RPTPase {alpha} has been localized to human chromosome region 20pter-20q12 by analysis of its segregation pattern in rodent-human somatic cell hybrids. Northern blot analysis revealed the presence of two major transcripts of 4.3 and 6.3 kilobases. In addition to PRTPase {alpha}, two other RPTPases ({beta} and {gamma}), identified in the same screen, have been partially cloned and sequenced. Analysis of sequence comparisons among LCA, the LCA-related protein LAR, and RPTP-ases {alpha}, {beta}, and {gamma} reveals the existence of a multigene family encoding different RPTPases, each containing a distinct extracellular domain, a single hydrophobic transmembrane region, and two tandemly repeated conserved cytoplasmic domains.

• OSTI ID: 5464364
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 87:18; ISSN 0027-8424
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
PHOSPHATASES
GENE REGULATION
PHOSPHOTRANSFERASES
RECOMBINANT DNA
DNA SEQUENCING
AMINO ACID SEQUENCE
BACTERIOPHAGES
BRAIN
DNA HYBRIDIZATION
DNA-CLONING
ENDONUCLEASES
GENES
HETEROCHROMOSOMES
RECEPTORS
TYROSINE
AMINO ACIDS
BODY
CARBOXYLIC ACIDS
CENTRAL NERVOUS SYSTEM
CHROMOSOMES
CLONING
DNA
DNA-ASE
ENZYMES
ESTERASES
HYBRIDIZATION
HYDROLASES
HYDROXY ACIDS
MEMBRANE PROTEINS
MICROORGANISMS
MOLECULAR STRUCTURE
NERVOUS SYSTEM
NUCLEIC ACIDS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANS
PARASITES
PHOSPHODIESTERASES
PHOSPHORUS-GROUP TRANSFERASES
PROTEINS
STRUCTURAL CHEMICAL ANALYSIS
TRANSFERASES
VIRUSES
550201* - Biochemistry- Tracer Techniques