Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis (By similarity). H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate Forms homooligomeric complexes which mediate cell homotypic adhesion (Probable). Interacts (via the cytoplasmic juxtamembrane domain) with CTNNB1; may mediate interaction with the cadherin/catenin adhesion complex. Interacts with KIT (By similarity). May interact with AP3B1 (By similarity). Transcripts of different sizes are differentially expressed in a subset of tissues. Detected in brain, lung, skeletal muscle, heart, kidney and placenta. In brain; expressed in olfactory bulb, cerebral cortex, hippocampus and cerebellum. Expressed throughout embryonic development. First detected at 7 dpc. The extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain. In addition to the 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa and 73 kDa are observed (By similarity). N-glycosylated. Phosphorylated on tyrosine residues upon activation of KIT with stem cell factor (SCF). The 73 kDa proteolytic product is not phosphorylated (By similarity). Belongs to the protein-tyrosine phosphatase family. Receptor class 2B subfamily. Truncated C-terminus. Contaminating sequence. Potential poly-A sequence. Intron retention.