1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (AGPAT1)
The protein contains 283 amino acids for an estimated molecular weight of 31717 Da.
Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. (updated: July 3, 2019)
Protein identification was indicated in the following studies:
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
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 predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs11964847 |
No binding partner found
Biological Process
CDP-diacylglycerol biosynthetic process
Phosphatidic acid biosynthetic process
Phospholipid metabolic process
Positive regulation of cellular metabolic process
Positive regulation of cytokine production
Positive regulation of cytokine-mediated signaling pathway
The reference OMIM entry for this protein is 603099
1-@acylglycerol-3-phosphate o-acyltransferase 1; agpat1
Lysophosphatidic acid acyltransferase-alpha
Lpaat-alpha
CLONING
Lysophosphatidic acid (LPA) and phosphatidic acid (PA) are 2 phospholipids involved in signal transduction and in lipid biosynthesis in cells. LPA acyltransferase (LPAAT), or 1-acyl-sn-glycerol-3-phosphate acetyltransferase (EC 2.3.1.51), catalyzes the conversion of LPA to PA. By searching an EST database for human homologs of yeast LPAAT, West et al. (1997) identified cDNAs encoding 2 proteins that they designated LPAAT-alpha and LPAAT-beta (603100). The predicted LPAAT-alpha protein is 283 amino acids long. Northern blot analysis revealed LPAAT-alpha expression in all tissues tested, with highest expression in skeletal muscle. West et al. (1997) demonstrated that both human LPAATs complemented an E. coli LPAAT mutation. Overexpression of the human LPAATs in mammalian cell lines led to increased enzyme activity. This increase in activity correlated with enhanced transcription and synthesis of IL6 (147620) and TNF-alpha (191160), suggesting that LPAAT overexpression may amplify the cellular response to cytokine stimulation. Independently, Stamps et al. (1997) and Aguado and Campbell (1998) isolated LPAAT-alpha cDNAs. Aguado and Campbell (1998) reported that the sequence of the LPAAT-alpha protein shares 48% and 31% identity with those of LPAAT-beta and yeast LPAAT, respectively. They proposed that, based on sequence analysis and immunofluorescence studies, LPAAT-alpha is an endoplasmic reticulum (ER) transmembrane protein with 4 transmembrane domains. The potential active center of the enzyme is located between the third and fourth domains, facing the cytosolic part of the ER. Analysis of expression in insect and Chinese hamster ovary (CHO) cells suggested that a 58-amino acid signal sequence is cleaved from LPAAT-alpha to form a mature protein that migrates at 26 kD by SDS-PAGE. The recombinant protein has affinity for fatty acids of acyl-chain lengths of 12 to 18 carbons, with a slight dependence on the degree of saturation.MAPPING
Aguado and Campbell (1998) determined that the LPAAT-alpha gene is located within a 220-kb segment separating the major histocompatibility complex class II region and the complement C4 genes of the class III region on chromosome 6p21.3. The authors noted that the LPAAT-alpha, NOTCH4 (164951), PBX2 (176311), and TNXA (see 600985) genes have respective family members LPAAT-beta, NOTCH1 (190198), PBX3 (176312), and TN-C (187380) located on 9q34, suggesting that these 2 regions arose from duplication of an ancestral chromosomal segment. ... More on the omim web site
June 29, 2020: Protein entry updated
Automatic update: OMIM entry 603099 was added.
July 4, 2019: 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).