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receptor-type tyrosine-protein phosphatase R; R-PTP-R; Ch-1PTPase; NC-PTPCOM1; protein-tyrosine phosphatase PCPTP1 (PTPRR ECPTP PTPRQ)

Function: - sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 & MAPK14 in the cytoplasm in an inactive form - the MAPKs bind to a dephosphorylated kinase-interacting motif, phosphorylation of which by protein kinase A releases the MAPKs for activation & translocation into the nucleus (putative) - interacts with MAPKs (putative) protein tyrosine phosphate + H2O = protein tyrosine + phosphate Structure: - belongs to the protein-tyrosine phosphatase family receptor class 7 subfamily - contains 1 tyrosine-protein phosphatase domain Compartment: - isoform alpha: - cell membrane; single-pass type 1 membrane protein - isoform delta: - cytoplasm, perinuclear region - locates to the perinuclear areas within the cytoplasm - isoform gamma - cytoplasm, perinuclear region - locates to the perinuclear areas within the cytoplasm Alternative splicing: named isoforms=3; alpha, gamma, delta Expression: - expressed in brain, placenta, small intestine, stomach, uterus - weakly expressed in the prostate - isoform alpha has been observed only in the brain - isoform gamma is expressed in brain, placenta & uterus - isoform delta is expressed in brain, kidney, placenta, prostate, small intestine & uterus

General

receptor tyrosine phosphatase, receptor type

Properties

SIZE: entity length = 657 aa MW = 74 kD COMPARTMENT: cytoplasm cell nucleus cellular membrane STATE: active state MOTIF: signal sequence {1-21} N-glycosylation site {N129} transmembrane domain {228-248} Ser phosphorylation site {S339} Tyr phosphorylation site {Y370} Tyrosine-protein phosphatase {393-647} MOTIF: binding site SITE: 554-554 FOR-BINDING-OF: Substrate Substrate binding {588-594} cysteine residue {C588} binding site SITE: 632-632 FOR-BINDING-OF: Substrate

Database Correlations

OMIM 602853 UniProt Q15256 Pfam PF00102 Entrez Gene 5801 KEGG correlations ENZYME 3.1.3.48

References

UniProt :accession Q15256