PTPRF

Protein tyrosine phosphatase, receptor type, F
File:PBB Protein PTPRF image.jpg PDB rendering based on 1lar.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1lar​, 2dju​, 2dn7​
Identifiers
Symbols	PTPRF ; FLJ43335; FLJ45062; FLJ45567; LAR
External IDs	Template:OMIM5 Template:MGI HomoloGene: 20623
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE PTPRF 200636 s at tn.png
File:PBB GE PTPRF 200635 s at tn.png
File:PBB GE PTPRF 200637 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Protein tyrosine phosphatase, receptor type, F, also known as PTPRF, is a human gene.

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains three Ig-like domains, and nine non-Ig like domains similar to that of neural-cell adhesion molecule. This PTP was shown to function in the regulation of epithelial cell-cell contacts at adherents junctions, as well as in the control of beta-catenin signaling. An increased expression level of this protein was found in the insulin-responsive tissue of obese, insulin-resistant individuals, and may contribute to the pathogenesis of insulin resistance. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported.

Further reading

• Chernoff J (1999). "Protein tyrosine phosphatases as negative regulators of mitogenic signaling". J. Cell. Physiol. 180 (2): 173–81. doi:10.1002/(SICI)1097-4652(199908)180:2<173::AID-JCP5>3.0.CO;2-Y. PMID 10395287.
• Hashimoto N, Feener EP, Zhang WR, Goldstein BJ (1992). "Insulin receptor protein-tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin receptor kinase by preferential dephosphorylation of the receptor regulatory domain". J. Biol. Chem. 267 (20): 13811–4. PMID 1321126.CS1 maint: Multiple names: authors list (link)
• Jirik FR, Harder KW, Melhado IG; et al. (1993). "The gene for leukocyte antigen-related tyrosine phosphatase (LAR) is localized to human chromosome 1p32, a region frequently deleted in tumors of neuroectodermal origin". Cytogenet. Cell Genet. 61 (4): 266–8. PMID 1486801.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Streuli M, Krueger NX, Thai T; et al. (1990). "Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR". EMBO J. 9 (8): 2399–407. PMID 1695146.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Streuli M, Krueger NX, Tsai AY, Saito H (1989). "A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila". Proc. Natl. Acad. Sci. U.S.A. 86 (22): 8698–702. PMID 2554325.CS1 maint: Multiple names: authors list (link)
• Streuli M, Krueger NX, Hall LR; et al. (1988). "A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen". J. Exp. Med. 168 (5): 1523–30. PMID 2972792.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Harder KW, Saw J, Miki N, Jirik F (1995). "Coexisting amplifications of the chromosome 1p32 genes (PTPRF and MYCL1) encoding protein tyrosine phosphatase LAR and L-myc in a small cell lung cancer line". Genomics. 27 (3): 552–3. doi:10.1006/geno.1995.1092. PMID 7558042.CS1 maint: Multiple names: authors list (link)
• Schaapveld RQ, van den Maagdenberg AM, Schepens JT; et al. (1995). "The mouse gene Ptprf encoding the leukocyte common antigen-related molecule LAR: cloning, characterization, and chromosomal localization". Genomics. 27 (1): 124–30. PMID 7665159.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Serra-Pagès C, Kedersha NL, Fazikas L; et al. (1995). "The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions". EMBO J. 14 (12): 2827–38. PMID 7796809.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• O'Grady P, Krueger NX, Streuli M, Saito H (1994). "Genomic organization of the human LAR protein tyrosine phosphatase gene and alternative splicing in the extracellular fibronectin type-III domains". J. Biol. Chem. 269 (40): 25193–9. PMID 7929208.CS1 maint: Multiple names: authors list (link)
• Pulido R, Serra-Pagès C, Tang M, Streuli M (1996). "The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1". Proc. Natl. Acad. Sci. U.S.A. 92 (25): 11686–90. PMID 8524829.CS1 maint: Multiple names: authors list (link)
• Liu X, Vega QC, Decker RA; et al. (1996). "Oncogenic RET receptors display different autophosphorylation sites and substrate binding specificities". J. Biol. Chem. 271 (10): 5309–12. PMID 8621380.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Debant A, Serra-Pagès C, Seipel K; et al. (1996). "The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains". Proc. Natl. Acad. Sci. U.S.A. 93 (11): 5466–71. PMID 8643598.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Zhang WR, Li PM, Oswald MA, Goldstein BJ (1996). "Modulation of insulin signal transduction by eutopic overexpression of the receptor-type protein-tyrosine phosphatase LAR". Mol. Endocrinol. 10 (5): 575–84. PMID 8732688.CS1 maint: Multiple names: authors list (link)
• Tabiti K, Cui L, Chhatwal VJ; et al. (1996). "Novel alternative splicing predicts a secreted extracellular isoform of the human receptor-like protein tyrosine phosphatase LAR". Gene. 175 (1–2): 7–13. PMID 8917069.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ahmad F, Goldstein BJ (1997). "Functional association between the insulin receptor and the transmembrane protein-tyrosine phosphatase LAR in intact cells". J. Biol. Chem. 272 (1): 448–57. PMID 8995282.
• Aicher B, Lerch MM, Müller T; et al. (1997). "Cellular redistribution of protein tyrosine phosphatases LAR and PTPsigma by inducible proteolytic processing". J. Cell Biol. 138 (3): 681–96. PMID 9245795.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Serra-Pagès C, Medley QG, Tang M; et al. (1998). "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins". J. Biol. Chem. 273 (25): 15611–20. PMID 9624153.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• O'Grady P, Thai TC, Saito H (1998). "The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR". J. Cell Biol. 141 (7): 1675–84. PMID 9647658.CS1 maint: Multiple names: authors list (link)
• Chiplunkar S, Chamblis K, Chwa M; et al. (1999). "Enhanced expression of a transmembrane phosphotyrosine phosphatase (LAR) in keratoconus cultures and corneas". Exp. Eye Res. 68 (3): 283–93. doi:10.1006/exer.1998.0604. PMID 10079136.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)