Target intelligence / Profile preview

Receptor-type tyrosine-protein phosphatase alpha (PTPRA)

Target
PTPRA
Molecular classification
Enzyme, Receptor, Protein tyrosine phosphatase (Classical, receptor-type)
01

Overview

Receptor-type tyrosine-protein phosphatase alpha (PTPRA) is a cell-surface receptor-type protein tyrosine phosphatase enzyme that regulates key cellular processes such as cell growth, differentiation, and the cell cycle[1][2][4]. It consists of an extracellular domain, a single transmembrane segment, and two intracytoplasmic catalytic domains (D1—active, D2—regulatory)[1][4]. PTPRA is best known for dephosphorylating and activating Src family tyrosine kinases, implicating it in signal transduction mechanisms that control integrin signaling, cell adhesion, and proliferation[1][2][4]. Dysregulation of PTPRA function has been noted in oncogenic transformation, fibrosis, arthritis, and other diseases[2][4]. While not yet a major direct drug target, its structural domains and regulatory mechanisms suggest emerging interest in selective allosteric inhibition for therapeutic purposes[4].

Other names
Protein tyrosine phosphatase receptor type APTPAPTPRL2Protein-tyrosine phosphatase alphaR-PTP-alphaLRPHLPRHPTPARPTPAHEPTPreceptor-type tyrosine-protein phosphatase alphaLeukocyte common antigen-related peptidePTPLCA-related phosphatasePTPase-alphaprotein tyrosine phosphatase, receptor type, alpha polypeptidetyrosine phosphatase alphaRPTPα
02

Mechanism of action

Inhibition or allosteric modulation of phosphatase activity (potential, not clinically validated)

03

Biological functions

Signal transductionRegulation of cell proliferationRegulation of cell growthDifferentiationMitotic cycle controlRegulation of integrin signalingCell adhesion
04

Disease associations

CancerAtherosclerosisDystonia 30FibrosisArthritis
05

Safety considerations

Potential for off-target effects due to broad substrate signaling impactOncogenic risk if dysregulatedChallenge in selective targeting due to structural similarity with other PTPs

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