Phospholipase A-2-activating protein (PLAA)
The protein contains 795 amino acids for an estimated molecular weight of 87157 Da.
Plays a role in protein ubiquitination, sorting and degradation through its association with VCP (PubMed:27753622). Involved in ubiquitin-mediated membrane proteins trafficking to late endosomes in an ESCRT-dependent manner, and hence plays a role in synaptic vesicle recycling (By similarity). May play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes (PubMed:27753622). Plays a role in cerebellar Purkinje cell development (By similarity). Positively regulates cytosolic and calcium-independent phospholipase A2 activities in a tumor necrosis factor alpha (TNF-alpha)- or lipopolysaccharide (LPS)-dependent manner, and hence prostaglandin E2 biosynthesis (PubMed:18291623, PubMed:28007986). (updated: Jan. 31, 2018)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
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.
Biological Process
Cellular response to lipopolysaccharide
Inflammatory response
Macroautophagy
Negative regulation of protein K63-linked ubiquitination
Nervous system development
Phospholipid metabolic process
Positive regulation of dendrite extension
Positive regulation of neuron migration
Positive regulation of phospholipase A2 activity
Positive regulation of synaptic vesicle recycling
Prostaglandin metabolic process
Proteasome-mediated ubiquitin-dependent protein catabolic process
Signal transduction
Ubiquitin recycling
Ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway
The reference OMIM entry for this protein is 603873
Phospholipase a2-activating protein; plaa
Plap
Phospholipase A2-activating protein (PLAP) is potentially important in regulating the inflammatory response through its activation of phospholipase A2 (e.g., 600522), which catalyzes the release of arachidonic acid. By screening a human monocyte cDNA library with a mouse Plap cDNA, Chopra et al. (1999) isolated human PLAP cDNAs. The 738-amino acid human PLAP protein predicted by the cDNA sequence has a molecular mass of 80,826 kD; however, immunoblot analysis using antibodies against PLAP detected a 72- to 74-kD protein in human monocyte cell lysates. In mouse macrophages, an antisense Plap oligonucleotide blocked cholera toxin-induced arachidonic acid release, indicating a role for PLAP in the regulation of phospholipase A2 activation. ... More on the omim web site
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 603873 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed