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PTPRF

From Wikipedia, the free encyclopedia
PTPRF
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPTPRF, LAR, BNAH2, protein tyrosine phosphatase, receptor type F, protein tyrosine phosphatase receptor type F
External IDsOMIM: 179590; MGI: 102695; HomoloGene: 20623; GeneCards: PTPRF; OMA:PTPRF - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_011213

RefSeq (protein)

NP_035343

Location (UCSC)Chr 1: 43.53 – 43.62 MbChr 4: 118.21 – 118.29 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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: ENSG00000142949Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033295Ensembl, 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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