This product is an active protein and may elicit a biological response in vivo, handle with caution.
Leukocyte common antigen
Ly5, homolog of
Protein tyrosine phosphatase receptor type c polypeptide
Protein tyrosine phosphatase, receptor type C
protein tyrosine phosphatase, receptor type, C
Receptor-type tyrosine-protein phosphatase C
T200 leukocyte common antigen
FunctionProtein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN.
Involvement in diseaseDefects in PTPRC are a cause of severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID) [MIM:608971]. A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. Genetic variations in PTPRC are involved in multiple sclerosis susceptibility (MS) [MIM:126200]. MS is a neurodegenerative disorder characterized by the gradual accumulation of focal plaques of demyelination particularly in the periventricular areas of the brain. Peripheral nerves are not affected. Onset usually in third or fourth decade with intermittent progression over an extended period. The cause is still uncertain.
Sequence similaritiesBelongs to the protein-tyrosine phosphatase family. Receptor class 1/6 subfamily. Contains 2 fibronectin type-III domains. Contains 2 tyrosine-protein phosphatase domains.
DomainThe first PTPase domain interacts with SKAP1.
Post-translational modificationsHeavily N- and O-glycosylated.
Cellular localizationMembrane. Membrane raft. Colocalized with DPP4 in membrane rafts.