Receptor-type tyrosine-protein phosphatase alpha (PTPRA)
The protein contains 802 amino acids for an estimated molecular weight of 90719 Da.
Tyrosine protein phosphatase which is involved in integrin-mediated focal adhesion formation (By similarity). Following integrin engagement, specifically recruits BCAR3, BCAR1 and CRK to focal adhesions thereby promoting SRC-mediated phosphorylation of BRAC1 and the subsequent activation of PAK and small GTPase RAC1 and CDC42 (By similarity). (updated: Feb. 26, 2020)
Protein identification was indicated in the following studies:
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs1178027 |
Biological Process
Axon guidance
Insulin receptor signaling pathway
Integrin-mediated signaling pathway
MAPK cascade
Modulation of chemical synaptic transmission
Protein dephosphorylation
Protein phosphorylation
Regulation of focal adhesion assembly
The reference OMIM entry for this protein is 176884
Protein-tyrosine phosphatase, receptor-type, alpha; ptpra
Ptp-alpha; ptpa
Rptpase-alpha
Lca-related phosphatase; lrp
DESCRIPTION
Vital cellular functions, such as cell proliferation and signal transduction, are regulated in part by the balance between the activities of protein-tyrosine kinases (PTKs; see 147795) and protein-tyrosine phosphatases (PTPases; EC 3.1.3.48). PTPases can be divided into 2 classes: small, soluble enzymes containing a single conserved PTPase domain, such as T-cell protein-tyrosine phosphatase (PTPT; 176887), and larger, more complex receptor-linked PTPases containing 2 tandem PTPase domains. PTPRA belongs to the latter group, which also includes leukocyte common antigen (LCA, or PTPRC; 151460) and leukocyte antigen-related tyrosine phosphatase (LAR, or PTPRF; 179590) (summary by Kaplan et al. (1990)).CLONING
By screening a hepatoblastoma cell line cDNA library with probes corresponding to the PTPase domains of mouse Ptprc, Jirik et al. (1990) cloned human PTPRA, which they called LRP. The predicted 793-amino acid protein has a calculated molecular mass of 87.5 kD (unglycosylated). The protein contains a leader peptide, followed by a 121-residue extracellular domain, a single transmembrane segment, and 2 tandem intracytoplasmic catalytic domains. The extracellular region has 8 potential N-glycosylation sites and multiple O-glycosylation sites. Northern blot analysis detected 2 LRP transcripts of 3.0 to 3.5 kb in all human cell cell lines examined. Ubiquitous expression was also detected in mouse tissues and cell lines. By screening a human placenta cDNA library with Drosophila Ptp, Krueger et al. (1990) cloned several PTPases, including PTPRA, which they called PTP-alpha. The deduced 793-amino acid protein has an N-terminal signal peptide, followed by an extracellular domain, a transmembrane segment, and a cytoplasmic region containing duplicate PTPase-like domains. PTP-alpha is rich in serine and threonine and has multiple potential N-glycosylation sites. By screening a human brainstem cDNA library with a leukocyte common antigen (LCA, or PTPRC; 151460) probe, Kaplan et al. (1990) cloned PTPRA, which they called RPTPase-alpha. The deduced protein contains 802 amino acids. Outside of the extracellular domain, where some variability exists, human PTPRA differs from mouse Ptpra at only 5 amino acids. Northern blot analysis detected 4.3- and 6.3-kb transcripts in various human cell lines and tissues, with the larger transcript being more prevalent in fetal tissues. Matthews et al. (1990) cloned mouse Ptpra, which they called Lrp. The deduced 793-amino acid protein has an N-terminal leader sequence, followed by an extracellular domain, a membrane-spanning region, and a cytoplasmic domain with 2 conserved tyrosine phosphatase catalytic domains. The extracellular region was predicted to be highly glycosylated. Matthews et al. (1990) also identified an Lrp splice variant containing an insertion that preserves the reading frame but disrupts the first tyrosine phosphatase domain. RNA transfer blot analysis detected wide expression of Lrp in mouse tissues.GENE FUNCTION
Using the cytoplasmic segment of human PTP-alpha expressed in E. coli, Krueger et al. (1990) confirmed that PTP-alpha had robust PTPase activity against phosphorylated test substrates.MAPPING
By study of rodent-human somatic cell hybrids, Jirik et al. (1990) mapped the PTPRA gene to chromosome 20p13. Other family members located on chromosome 20 include SRC (190090), HCK (142370), and PTP1B (176885). Kaplan et al. (1990) local ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 176884 was added.
March 3, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).