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{{Infobox_gene}}
{{PBB_Controls
'''Receptor-type tyrosine-protein phosphatase F''' is an [[enzyme]] that in humans is encoded by the ''PTPRF'' [[gene]].<ref name="pmid7558042">{{cite journal | vauthors = Harder KW, Saw J, Miki N, Jirik F | title = 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 | journal = Genomics | volume = 27 | issue = 3 | pages = 552–3 | date = Nov 1995 | pmid = 7558042 | pmc = | doi = 10.1006/geno.1995.1092 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PTPRF protein tyrosine phosphatase, receptor type, F| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5792| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
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 [[adherens junction]]s, 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 [[alternative splicing|alternatively spliced]] transcript variants of this gene, which encode distinct proteins, have been reported.<ref name="entrez"/>
{{GNF_Protein_box
| image = PBB_Protein_PTPRF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1lar.
| PDB = {{PDB2|1lar}}, {{PDB2|2dju}}, {{PDB2|2dn7}}
| Name = Protein tyrosine phosphatase, receptor type, F
| HGNCid = 9670
| Symbol = PTPRF
| AltSymbols =; FLJ43335; FLJ45062; FLJ45567; LAR
| OMIM = 179590
| ECnumber = 
| Homologene = 20623
| MGIid = 102695
| GeneAtlas_image1 = PBB_GE_PTPRF_200636_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PTPRF_200635_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PTPRF_200637_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005001 |text = transmembrane receptor protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007185 |text = transmembrane receptor protein tyrosine phosphatase signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5792
    | Hs_Ensembl = ENSG00000142949
    | Hs_RefseqProtein = NP_002831
    | Hs_RefseqmRNA = NM_002840
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 43769134
    | Hs_GenLoc_end = 43861924
    | Hs_Uniprot = P10586
    | Mm_EntrezGene = 19268
    | Mm_Ensembl = ENSMUSG00000033295
    | Mm_RefseqmRNA = NM_011213
    | Mm_RefseqProtein = NP_035343
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 117707733
    | Mm_GenLoc_end = 117775378
    | Mm_Uniprot = 
  }}
}}
'''Protein tyrosine phosphatase, receptor type, F''', also known as '''PTPRF''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPRF protein tyrosine phosphatase, receptor type, F| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5792| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{PBB_Summary
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: PTPRF protein tyrosine phosphatase, receptor type, F| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5792| accessdate = }}</ref>
}}


==References==
PTPRF has been shown to [[Protein-protein interaction|interact]] with [[Beta-catenin]]<ref name=pmid11245482>{{cite journal | vauthors = Bonvini P, An WG, Rosolen A, Nguyen P, Trepel J, Garcia de Herreros A, Dunach M, Neckers LM | title = Geldanamycin abrogates ErbB2 association with proteasome-resistant beta-catenin in melanoma cells, increases beta-catenin-E-cadherin association, and decreases beta-catenin-sensitive transcription | journal = Cancer Res. | volume = 61 | issue = 4 | pages = 1671–7 | date = Feb 2001 | pmid = 11245482 }}</ref><ref name=pmid9245795>{{cite journal | vauthors = Aicher B, Lerch MM, Müller T, Schilling J, Ullrich A | title = Cellular Redistribution of Protein Tyrosine Phosphatases LAR and PTPσ by Inducible Proteolytic Processing | journal = J. Cell Biol. | volume = 138 | issue = 3 | pages = 681–96 | date = Aug 1997 | pmid = 9245795 | pmc = 2141638 | doi = 10.1083/jcb.138.3.681 }}</ref> and [[liprin-alpha-1]].<ref name=pmid8524829>{{cite journal | vauthors = Pulido R, Serra-Pagès C, Tang M, Streuli M | title = 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 | journal = [[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] | volume = 92 | issue = 25 | pages = 11686–90 | date = Dec 1995 | pmid = 8524829 | pmc = 40467 | doi = 10.1073/pnas.92.25.11686 }}</ref><ref name=pmid7796809>{{cite journal | vauthors = Serra-Pagès C, Kedersha NL, Fazikas L, Medley Q, Debant A, Streuli M | title = The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions | journal = EMBO J. | volume = 14 | issue = 12 | pages = 2827–38 | date = Jun 1995 | pmid = 7796809 | pmc = 398401 }}</ref><ref name=pmid9624153>{{cite journal | vauthors = Serra-Pagès C, Medley QG, Tang M, Hart A, Streuli M | title = Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins | journal = J. Biol. Chem. | volume = 273 | issue = 25 | pages = 15611–20 | date = Jun 1998 | pmid = 9624153 | doi = 10.1074/jbc.273.25.15611 }}</ref>
{{reflist|2}}
 
==Further reading==
== References ==
{{reflist}}
{{Clear}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Chernoff J | title = Protein tyrosine phosphatases as negative regulators of mitogenic signaling | journal = J. Cell. Physiol. | volume = 180 | issue = 2 | pages = 173–81 | year = 1999 | pmid = 10395287 | doi = 10.1002/(SICI)1097-4652(199908)180:2<173::AID-JCP5>3.0.CO;2-Y }}
| citations =
* {{cite journal | vauthors = Hashimoto N, Feener EP, Zhang WR, Goldstein BJ | title = Insulin receptor protein-tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin receptor kinase by preferential dephosphorylation of the receptor regulatory domain | journal = J. Biol. Chem. | volume = 267 | issue = 20 | pages = 13811–4 | year = 1992 | pmid = 1321126 | doi =  }}
*{{cite journal | author=Chernoff J |title=Protein tyrosine phosphatases as negative regulators of mitogenic signaling. |journal=J. Cell. Physiol. |volume=180 |issue= 2 |pages= 173-81 |year= 1999 |pmid= 10395287 |doi= 10.1002/(SICI)1097-4652(199908)180:2<173::AID-JCP5>3.0.CO;2-Y }}
* {{cite journal | vauthors = Jirik FR, Harder KW, Melhado IG, Anderson LL, Duncan AM | title = The gene for leukocyte antigen-related tyrosine phosphatase (LAR) is localized to human chromosome 1p32, a region frequently deleted in tumors of neuroectodermal origin | journal = Cytogenet. Cell Genet. | volume = 61 | issue = 4 | pages = 266–8 | year = 1993 | pmid = 1486801 | doi = 10.1159/000133418 }}
*{{cite journal | author=Hashimoto N, Feener EP, Zhang WR, Goldstein BJ |title=Insulin receptor protein-tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin receptor kinase by preferential dephosphorylation of the receptor regulatory domain. |journal=J. Biol. Chem. |volume=267 |issue= 20 |pages= 13811-4 |year= 1992 |pmid= 1321126 |doi=  }}
* {{cite journal | vauthors = Streuli M, Krueger NX, Thai T, Tang M, Saito H | title = Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR | journal = EMBO J. | volume = 9 | issue = 8 | pages = 2399–407 | year = 1990 | pmid = 1695146 | pmc = 552264 | doi =  }}
*{{cite journal | author=Jirik FR, Harder KW, Melhado IG, ''et al.'' |title=The gene for leukocyte antigen-related tyrosine phosphatase (LAR) is localized to human chromosome 1p32, a region frequently deleted in tumors of neuroectodermal origin. |journal=Cytogenet. Cell Genet. |volume=61 |issue= 4 |pages= 266-8 |year= 1993 |pmid= 1486801 |doi= }}
* {{cite journal | vauthors = Streuli M, Krueger NX, Tsai AY, Saito H | title = A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 86 | issue = 22 | pages = 8698–702 | year = 1989 | pmid = 2554325 | pmc = 298355 | doi = 10.1073/pnas.86.22.8698 }}
*{{cite journal | author=Streuli M, Krueger NX, Thai T, ''et al.'' |title=Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR. |journal=EMBO J. |volume=9 |issue= 8 |pages= 2399-407 |year= 1990 |pmid= 1695146 |doi=  }}
* {{cite journal | vauthors = Streuli M, Krueger NX, Hall LR, Schlossman SF, Saito H | title = A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen | journal = J. Exp. Med. | volume = 168 | issue = 5 | pages = 1523–30 | year = 1988 | pmid = 2972792 | pmc = 2189122 | doi = 10.1084/jem.168.5.1523 }}
*{{cite journal | author=Streuli M, Krueger NX, Tsai AY, Saito H |title=A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 22 |pages= 8698-702 |year= 1989 |pmid= 2554325 |doi= }}
* {{cite journal | vauthors = Schaapveld RQ, van den Maagdenberg AM, Schepens JT, Weghuis DO, Geurts van Kessel A, Wieringa B, Hendriks WJ | title = The mouse gene Ptprf encoding the leukocyte common antigen-related molecule LAR: cloning, characterization, and chromosomal localization | journal = Genomics | volume = 27 | issue = 1 | pages = 124–30 | year = 1995 | pmid = 7665159 | doi = 10.1006/geno.1995.1014 }}
*{{cite journal | author=Streuli M, Krueger NX, Hall LR, ''et al.'' |title=A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen. |journal=J. Exp. Med. |volume=168 |issue= 5 |pages= 1523-30 |year= 1988 |pmid= 2972792 |doi= }}
* {{cite journal | vauthors = Serra-Pagès C, Kedersha NL, Fazikas L, Medley Q, Debant A, Streuli M | title = The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions | journal = EMBO J. | volume = 14 | issue = 12 | pages = 2827–38 | year = 1995 | pmid = 7796809 | pmc = 398401 | doi =  }}
*{{cite journal | author=Harder KW, Saw J, Miki N, Jirik F |title=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. |journal=Genomics |volume=27 |issue= 3 |pages= 552-3 |year= 1995 |pmid= 7558042 |doi= 10.1006/geno.1995.1092 }}
* {{cite journal | vauthors = O'Grady P, Krueger NX, Streuli M, Saito H | title = Genomic organization of the human LAR protein tyrosine phosphatase gene and alternative splicing in the extracellular fibronectin type-III domains | journal = J. Biol. Chem. | volume = 269 | issue = 40 | pages = 25193–9 | year = 1994 | pmid = 7929208 | doi =  }}
*{{cite journal | author=Schaapveld RQ, van den Maagdenberg AM, Schepens JT, ''et al.'' |title=The mouse gene Ptprf encoding the leukocyte common antigen-related molecule LAR: cloning, characterization, and chromosomal localization. |journal=Genomics |volume=27 |issue= 1 |pages= 124-30 |year= 1995 |pmid= 7665159 |doi=  }}
* {{cite journal | vauthors = Pulido R, Serra-Pagès C, Tang M, Streuli M | title = 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 | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 25 | pages = 11686–90 | year = 1996 | pmid = 8524829 | pmc = 40467 | doi = 10.1073/pnas.92.25.11686 }}
*{{cite journal | author=Serra-Pagès C, Kedersha NL, Fazikas L, ''et al.'' |title=The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions. |journal=EMBO J. |volume=14 |issue= 12 |pages= 2827-38 |year= 1995 |pmid= 7796809 |doi=  }}
* {{cite journal | vauthors = Liu X, Vega QC, Decker RA, Pandey A, Worby CA, Dixon JE | title = Oncogenic RET receptors display different autophosphorylation sites and substrate binding specificities | journal = J. Biol. Chem. | volume = 271 | issue = 10 | pages = 5309–12 | year = 1996 | pmid = 8621380 | doi = 10.1074/jbc.271.10.5309 }}
*{{cite journal | author=O'Grady P, Krueger NX, Streuli M, Saito H |title=Genomic organization of the human LAR protein tyrosine phosphatase gene and alternative splicing in the extracellular fibronectin type-III domains. |journal=J. Biol. Chem. |volume=269 |issue= 40 |pages= 25193-9 |year= 1994 |pmid= 7929208 |doi= }}
* {{cite journal | vauthors = Debant A, Serra-Pagès C, Seipel K, O'Brien S, Tang M, Park SH, Streuli M | title = 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 | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 11 | pages = 5466–71 | year = 1996 | pmid = 8643598 | pmc = 39269 | doi = 10.1073/pnas.93.11.5466 }}
*{{cite journal | author=Pulido R, Serra-Pagès C, Tang M, Streuli M |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 25 |pages= 11686-90 |year= 1996 |pmid= 8524829 |doi= }}
* {{cite journal | vauthors = Zhang WR, Li PM, Oswald MA, Goldstein BJ | title = Modulation of insulin signal transduction by eutopic overexpression of the receptor-type protein-tyrosine phosphatase LAR | journal = Mol. Endocrinol. | volume = 10 | issue = 5 | pages = 575–84 | year = 1996 | pmid = 8732688 | doi = 10.1210/me.10.5.575 }}
*{{cite journal | author=Liu X, Vega QC, Decker RA, ''et al.'' |title=Oncogenic RET receptors display different autophosphorylation sites and substrate binding specificities. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5309-12 |year= 1996 |pmid= 8621380 |doi= }}
* {{cite journal | vauthors = Tabiti K, Cui L, Chhatwal VJ, Moochhala S, Ngoi SS, Pallen CJ | title = Novel alternative splicing predicts a secreted extracellular isoform of the human receptor-like protein tyrosine phosphatase LAR | journal = Gene | volume = 175 | issue = 1–2 | pages = 7–13 | year = 1996 | pmid = 8917069 | doi = 10.1016/0378-1119(96)00113-8 }}
*{{cite journal | author=Debant A, Serra-Pagès C, Seipel K, ''et al.'' |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 11 |pages= 5466-71 |year= 1996 |pmid= 8643598 |doi= }}
* {{cite journal | vauthors = Ahmad F, Goldstein BJ | title = Functional association between the insulin receptor and the transmembrane protein-tyrosine phosphatase LAR in intact cells | journal = J. Biol. Chem. | volume = 272 | issue = 1 | pages = 448–57 | year = 1997 | pmid = 8995282 | doi = 10.1074/jbc.272.1.448 }}
*{{cite journal | author=Zhang WR, Li PM, Oswald MA, Goldstein BJ |title=Modulation of insulin signal transduction by eutopic overexpression of the receptor-type protein-tyrosine phosphatase LAR. |journal=Mol. Endocrinol. |volume=10 |issue= 5 |pages= 575-84 |year= 1996 |pmid= 8732688 |doi= }}
* {{cite journal | vauthors = Aicher B, Lerch MM, Müller T, Schilling J, Ullrich A | title = Cellular Redistribution of Protein Tyrosine Phosphatases LAR and PTPσ by Inducible Proteolytic Processing | journal = J. Cell Biol. | volume = 138 | issue = 3 | pages = 681–96 | year = 1997 | pmid = 9245795 | pmc = 2141638 | doi = 10.1083/jcb.138.3.681 }}
*{{cite journal | author=Tabiti K, Cui L, Chhatwal VJ, ''et al.'' |title=Novel alternative splicing predicts a secreted extracellular isoform of the human receptor-like protein tyrosine phosphatase LAR. |journal=Gene |volume=175 |issue= 1-2 |pages= 7-13 |year= 1996 |pmid= 8917069 |doi= }}
* {{cite journal | vauthors = Serra-Pagès C, Medley QG, Tang M, Hart A, Streuli M | title = Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins | journal = J. Biol. Chem. | volume = 273 | issue = 25 | pages = 15611–20 | year = 1998 | pmid = 9624153 | doi = 10.1074/jbc.273.25.15611 }}
*{{cite journal | author=Ahmad F, Goldstein BJ |title=Functional association between the insulin receptor and the transmembrane protein-tyrosine phosphatase LAR in intact cells. |journal=J. Biol. Chem. |volume=272 |issue= 1 |pages= 448-57 |year= 1997 |pmid= 8995282 |doi= }}
* {{cite journal | vauthors = O'Grady P, Thai TC, Saito H | title = The Laminin–Nidogen Complex is a Ligand for a Specific Splice Isoform of the Transmembrane Protein Tyrosine Phosphatase LAR | journal = J. Cell Biol. | volume = 141 | issue = 7 | pages = 1675–84 | year = 1998 | pmid = 9647658 | pmc = 2133008 | doi = 10.1083/jcb.141.7.1675 }}
*{{cite journal | author=Aicher B, Lerch MM, Müller T, ''et al.'' |title=Cellular redistribution of protein tyrosine phosphatases LAR and PTPsigma by inducible proteolytic processing. |journal=J. Cell Biol. |volume=138 |issue= 3 |pages= 681-96 |year= 1997 |pmid= 9245795 |doi= }}
* {{cite journal | vauthors = Chiplunkar S, Chamblis K, Chwa M, Rosenberg S, Kenney MC, Brown DJ | title = Enhanced expression of a transmembrane phosphotyrosine phosphatase (LAR) in keratoconus cultures and corneas | journal = Exp. Eye Res. | volume = 68 | issue = 3 | pages = 283–93 | year = 1999 | pmid = 10079136 | doi = 10.1006/exer.1998.0604 }}
*{{cite journal | author=Serra-Pagès C, Medley QG, Tang M, ''et al.'' |title=Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins. |journal=J. Biol. Chem. |volume=273 |issue= 25 |pages= 15611-20 |year= 1998 |pmid= 9624153 |doi= }}
*{{cite journal | author=O'Grady P, Thai TC, Saito H |title=The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR. |journal=J. Cell Biol. |volume=141 |issue= 7 |pages= 1675-84 |year= 1998 |pmid= 9647658 |doi=  }}
*{{cite journal  | author=Chiplunkar S, Chamblis K, Chwa M, ''et al.'' |title=Enhanced expression of a transmembrane phosphotyrosine phosphatase (LAR) in keratoconus cultures and corneas. |journal=Exp. Eye Res. |volume=68 |issue= 3 |pages= 283-93 |year= 1999 |pmid= 10079136 |doi= 10.1006/exer.1998.0604 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=5792}}
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{{Protein tyrosine phosphatases}}

Latest revision as of 01:47, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Receptor-type tyrosine-protein phosphatase F is an enzyme that in humans is encoded by the PTPRF gene.[1][2]

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 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.[2]

Interactions

PTPRF has been shown to interact with Beta-catenin[3][4] and liprin-alpha-1.[5][6][7]

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: PTPRF protein tyrosine phosphatase, receptor type, F".
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ 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. doi:10.1073/pnas.92.25.11686. PMC 40467. PMID 8524829.
  6. ↑ 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. PMC 398401. PMID 7796809.
  7. ↑ 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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