Lysophospholipase-like protein 1 (LYPLAL1)
The protein contains 237 amino acids for an estimated molecular weight of 26316 Da.
Has depalmitoylating activity toward KCNMA1. Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site. (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- 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.
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| Variant | Description |
|---|---|
| dbSNP:rs940570 | |
| dbSNP:rs34201999 |
The reference OMIM entry for this protein is 616548
Lysophospholipase-like 1; lyplal1
DESCRIPTION
LYPLAL1 shares similarity with acyl protein thioesterases (APTs; see 605599). However, it does not function as a phospholipase or triacylglycerol lipase, but rather hydrolyzes short-chain substrates (Burger et al., 2012).GENE FUNCTION
Using an in vitro assay of recombinant human LYPLAL1 expressed in E. coli, Burger et al. (2012) found that LYPLAL1 showed no phospholipase activity. LYPLAL1 hydrolyzed short-chain substrates, such as 4-nitrophenyl acetate.BIOCHEMICAL FEATURES
Burger et al. (2012) reported the crystal structure of human LYPLAL1 at 1.72-angstrom resolution. The structure revealed a typical alpha/beta hydrolase fold and featured the classical catalytic triad of serine, aspartate, and histidine. However, compared with other APT family members, the typical hydrophobic tunnel was closed in LYPLAL1. In addition, the crystal packing of LYPLAL1 suggested that it functions as a monomer rather than as a dimer, like most APTs.MAPPING
Hartz (2015) mapped the LYPLAL1 gene to chromosome 1q41 based on an alignment of the LYPLAL1 sequence (GenBank GENBANK BC016711) with the genomic sequence (GRCh38). ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 616548 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).