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receptor-type tyrosine-protein phosphatase U; R-PTP-U; pancreatic carcinoma phosphatase 2; PCP-2; protein-tyrosine phosphatase J; PTP-J; hPTP-J; protein-tyrosine phosphatase pi; PTP pi; protein-tyrosine phosphatase receptor omicron; PTP-RO; receptor-type protein-tyrosine phosphatase psi; R-PTP-psi (PTPRU, FMI, PCP2, PTPRO)

Function: - tyrosine-protein phosphatase which dephosphorylates CTNNB1 - regulates CTNNB1 function both in cell adhesion & signaling - may function in cell proliferation & migration & play a role in maintenance of epithelial integrity - may play a role in megakaryocytopoiesis - the extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain (putative) - beside the 190 kD full-length protein, proteolytic products of 100 kD, 80 kD & 73 kD are observed - phosphorylated on Tyr upon activation of KIT with stem cell factor (SCF) - the 73 kD proteolytic product is not phosphorylated - forms homooligomeric complexes which mediate cell homotypic adhesion (probable) - interacts (via the cytoplasmic juxtamembrane domain) with CTNNB1 - may mediate interaction with cadherin/catenin adhesion complex - interacts with KIT - may interact with AP3B1 protein tyrosine phosphate + H2O = protein tyrosine + phosphate Structure: - N-glycosylated - belongs to the protein-tyrosine phosphatase family receptor class 2B subfamily - contains 4 fibronectin F3 modules - contains 1 Ig-like C2-type domain - contains 1 MAM domain - contains 2 tyrosine-protein phosphatase domains Compartment: - cell junction, cell membrane - single-pass type 1 membrane protein Alternative splicing: named isoforms=4 Expression: - high expression in brain, pancreas, & skeletal muscle - less expression in colon, kidney, liver, stomach, & uterus - not expressed in placenta & spleen - also detected in heart, prostate, lung, thymus, testis & ovary - expressed througout the brain - expressed by hematopoietic stem cells - expressed in fetal brain, lung & kidney - induced by upon cell contact (at protein level) - down-regulated by phorbol ester (at protein level) & Ca+2 ionophore - up-regulated by phorbol ester in megakaryocytic cells [2]

General

glycoprotein receptor tyrosine phosphatase, receptor type

Properties

SIZE: entity length = 1446 aa MW = 162 kD COMPARTMENT: cellular membrane STATE: active state MOTIF: signal sequence {1-18} MAM domain {25-188} MOTIF: cysteine residue {*1} (2) MODIFICATION: cysteine residue {*2} cysteine residue {*2} (2) MODIFICATION: cysteine residue {*1} N-glycosylation site {N75} immunoglobulin superfamily domain {190-275} MOTIF: cysteine residue {C210} MODIFICATION: cysteine residue {C264} cysteine residue {C264} MODIFICATION: cysteine residue {C210} fibronectin type III domain or F3 module {285-377} fibronectin type III domain or F3 module {383-481} MOTIF: N-glycosylation site {N410} fibronectin type III domain or F3 module {482-585} fibronectin type III domain or F3 module {592-674} N-glycosylation site {N685} transmembrane domain {750-770} Mediates interaction with CTNNB1 {771-887} MOTIF: Ser phosphorylation site {S848} Ser phosphorylation site {S853} Tyrosine-protein phosphatase 1 {888-1144} MOTIF: binding site SITE: 1053-1053 FOR-BINDING-OF: Substrate Substrate binding {1085-1091} cysteine residue {C1085} binding site SITE: 1129-1129 FOR-BINDING-OF: Substrate Tyrosine-protein phosphatase 2 {1176-1439} MOTIF: cysteine residue {C1380}

Database Correlations

OMIM 602454 UniProt Q92729 PFAM correlations Entrez Gene 10076 Kegg hsa:10076 ENZYME 3.1.3.48

References

  1. UniProt :accession Q92729
  2. Taniguchi Y et al The receptor protein tyrosine phosphatase, PTP-RO, is upregulated during megakaryocyte differentiation and Is associated with the c-Kit receptor. Blood. 1999 Jul 15;94(2):539-49. PMID: 10397721