PTPRF

Receptor-type tyrosine-protein phosphatase F is an enzyme that, in humans, is encoded by the PTPRF 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 those of the neural cell adhesion molecule. This PTP was shown to function in the regulation of epithelial cell-cell contacts at adherens 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.

Protein-coding gene in the species Homo sapiens

PTPRF
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1LAR, 2DJU, 2EDX, 2EDY, 2YD5, 2YD8, 4N5U, 2DN7
Identifiers
Aliases	PTPRF, LAR, BNAH2, protein tyrosine phosphatase, receptor type F, protein tyrosine phosphatase receptor type F
External IDs	OMIM: 179590; MGI: 102695; HomoloGene: 20623; GeneCards: PTPRF; OMA:PTPRF - orthologs
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p34.2 Start 43,525,187 bp[1] End 43,623,666 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 D2.1 Start 118,208,213 bp[2] End 118,291,405 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gingival epithelium bronchial epithelial cell nipple parotid gland hair follicle germinal epithelium jejunal mucosa skin of arm skin of thigh epithelium of nasopharynx Top expressed in medullary collecting duct epithelium of lens transitional epithelium of urinary bladder hair follicle vestibular sensory epithelium vestibular membrane of cochlear duct external carotid artery conjunctival fornix left lung left lung lobe More reference expression data BioGPS More reference expression data
Gene ontology Molecular function chondroitin sulfate proteoglycan binding heparin binding phosphoprotein phosphatase activity phosphatase activity protein-containing complex binding protein tyrosine phosphatase activity transmembrane receptor protein tyrosine phosphatase activity hydrolase activity cell adhesion molecule binding Cellular component integral component of membrane membrane integral component of plasma membrane soma neuron projection extracellular exosome plasma membrane Biological process neuron projection regeneration regulation of axon regeneration negative regulation of receptor binding regulation of neuron projection development protein dephosphorylation transmembrane receptor protein tyrosine phosphatase signaling pathway cell adhesion peptidyl-tyrosine dephosphorylation cell migration dephosphorylation synaptic membrane adhesion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5792 19268 Ensembl ENSG00000142949 ENSMUSG00000033295 UniProt P10586 A2A8L5 RefSeq (mRNA) NM_002840 NM_130440 NM_001329137 NM_001329138 NM_001329139 NM_001329140 NM_011213 RefSeq (protein) NP_001316066 NP_001316067 NP_001316068 NP_001316069 NP_002831 NP_569707 NP_035343 Location (UCSC) Chr 1: 43.53 – 43.62 Mb Chr 4: 118.21 – 118.29 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Receptor-type tyrosine-protein phosphatase F is an enzyme that, in humans, is encoded by the PTPRF gene.^[5][6]

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 those of the neural cell adhesion molecule. This PTP was shown to function in the regulation of epithelial cell-cell contacts at adherens 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.^[6]

Interactions

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PTPRF has been shown to interact with Beta-catenin^[7][8] and liprin-alpha-1.^[9][10][11]

References

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1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000142949 – Ensembl, May 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000033295 – Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ Harder KW, Saw J, Miki N, Jirik F (Nov 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.
6. ^ ^{a b} "Entrez Gene: PTPRF protein tyrosine phosphatase, receptor type, F".
7. ^ Bonvini P, An WG, Rosolen A, Nguyen P, Trepel J, Garcia de Herreros A, Dunach M, Neckers LM (Feb 2001). "Geldanamycin abrogates ErbB2 association with proteasome-resistant beta-catenin in melanoma cells, increases beta-catenin-E-cadherin association, and decreases beta-catenin-sensitive transcription". Cancer Res. 61 (4): 1671–7. PMID 11245482.
8. ^ Aicher B, Lerch MM, Müller T, Schilling J, Ullrich A (Aug 1997). "Cellular Redistribution of Protein Tyrosine Phosphatases LAR and PTPσ by Inducible Proteolytic Processing". J. Cell Biol. 138 (3): 681–96. doi:10.1083/jcb.138.3.681. PMC 2141638. PMID 9245795.
9. ^ Pulido R, Serra-Pagès C, Tang M, Streuli M (Dec 1995). "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. Bibcode:1995PNAS...9211686P. doi:10.1073/pnas.92.25.11686. PMC 40467. PMID 8524829.
10. ^ Serra-Pagès C, Kedersha NL, Fazikas L, Medley Q, Debant A, Streuli M (Jun 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. doi:10.1002/j.1460-2075.1995.tb07282.x. PMC 398401. PMID 7796809.
11. ^ Serra-Pagès C, Medley QG, Tang M, Hart A, Streuli M (Jun 1998). "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins". J. Biol. Chem. 273 (25): 15611–20. doi:10.1074/jbc.273.25.15611. PMID 9624153.

Further reading

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• 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. S2CID 24952421.
• 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. doi:10.1016/S0021-9258(19)49639-7. PMID 1321126.
• Jirik FR, Harder KW, Melhado IG, Anderson LL, Duncan AM (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. doi:10.1159/000133418. PMID 1486801.
• Streuli M, Krueger NX, Thai T, Tang M, Saito H (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. doi:10.1002/j.1460-2075.1990.tb07415.x. PMC 552264. PMID 1695146.
• 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. Bibcode:1989PNAS...86.8698S. doi:10.1073/pnas.86.22.8698. PMC 298355. PMID 2554325.
• Streuli M, Krueger NX, Hall LR, Schlossman SF, Saito H (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. doi:10.1084/jem.168.5.1523. PMC 2189122. PMID 2972792.
• Schaapveld RQ, van den Maagdenberg AM, Schepens JT, Weghuis DO, Geurts van Kessel A, Wieringa B, Hendriks WJ (1995). "The mouse gene Ptprf encoding the leukocyte common antigen-related molecule LAR: cloning, characterization, and chromosomal localization". Genomics. 27 (1): 124–30. doi:10.1006/geno.1995.1014. hdl:2066/21329. PMID 7665159.
• Serra-Pagès C, Kedersha NL, Fazikas L, Medley Q, Debant A, Streuli M (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. doi:10.1002/j.1460-2075.1995.tb07282.x. PMC 398401. PMID 7796809.
• 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. doi:10.1016/S0021-9258(17)31516-8. PMID 7929208.
• 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. Bibcode:1995PNAS...9211686P. doi:10.1073/pnas.92.25.11686. PMC 40467. PMID 8524829.
• Liu X, Vega QC, Decker RA, Pandey A, Worby CA, Dixon JE (1996). "Oncogenic RET receptors display different autophosphorylation sites and substrate binding specificities". J. Biol. Chem. 271 (10): 5309–12. doi:10.1074/jbc.271.10.5309. PMID 8621380.
• Debant A, Serra-Pagès C, Seipel K, O'Brien S, Tang M, Park SH, Streuli M (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. Bibcode:1996PNAS...93.5466D. doi:10.1073/pnas.93.11.5466. PMC 39269. PMID 8643598.
• 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. doi:10.1210/mend.10.5.8732688. PMID 8732688. S2CID 42128485.
• Tabiti K, Cui L, Chhatwal VJ, Moochhala S, Ngoi SS, Pallen CJ (1996). "Novel alternative splicing predicts a secreted extracellular isoform of the human receptor-like protein tyrosine phosphatase LAR". Gene. 175 (1–2): 7–13. doi:10.1016/0378-1119(96)00113-8. PMID 8917069.
• 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. doi:10.1074/jbc.272.1.448. PMID 8995282.
• Aicher B, Lerch MM, Müller T, Schilling J, Ullrich A (1997). "Cellular Redistribution of Protein Tyrosine Phosphatases LAR and PTPσ by Inducible Proteolytic Processing". J. Cell Biol. 138 (3): 681–96. doi:10.1083/jcb.138.3.681. PMC 2141638. PMID 9245795.
• Serra-Pagès C, Medley QG, Tang M, Hart A, Streuli M (1998). "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins". J. Biol. Chem. 273 (25): 15611–20. doi:10.1074/jbc.273.25.15611. PMID 9624153.
• 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. doi:10.1083/jcb.141.7.1675. PMC 2133008. PMID 9647658.
• Chiplunkar S, Chamblis K, Chwa M, Rosenberg S, Kenney MC, Brown DJ (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.