Lysophospholipid acyltransferase 5 (LPCAT3)

The protein contains 487 amino acids for an estimated molecular weight of 56035 Da.

 

Lysophospholipid O-acyltransferase (LPLAT) that catalyzes the reacylation step of the phospholipid remodeling process also known as the Lands cycle (PubMed:18782225, PubMed:18195019, PubMed:18772128). Catalyzes transfer of the fatty acyl chain from fatty acyl-CoA to 1-acyl lysophospholipid to form various classes of phospholipids. Converts 1-acyl lysophosphatidylcholine (LPC) into phosphatidylcholine (PC) (LPCAT activity), 1-acyl lysophosphatidylserine (LPS) into phosphatidylserine (PS) (LPSAT activity) and 1-acyl lysophosphatidylethanolamine (LPE) into phosphatidylethanolamine (PE) (LPEAT activity) (PubMed:18782225, PubMed:18195019, PubMed:18772128). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs (PubMed:18195019, PubMed:18772128). Has higher activity for LPC acyl acceptors compared to LPEs and LPSs. Can also transfer the fatty acyl chain from fatty acyl-CoA to 1-O-alkyl lysophospholipid or 1-O-alkenyl lysophospholipid with lower efficiency (By similarity). Acts as a major LPC O-acyltransferase in liver and intestine. As a component of the liver X receptor/NR1H3 or NR1H2 signaling pathway, mainly catalyzes the incorporation of arachidonate into PCs of endoplasmic reticulum (ER) membranes, increasing membrane dynamics and enabling triacylglycerols transfer to nascent very low-density lipoprotein (VLDL) particles. Promotes processing of sterol regulatory protein SREBF1 in hepatocytes, likely by facilitating the translocation of SRE (updated: Aug. 12, 2020)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. 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.
  3. 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.
  4. 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.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. 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.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

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.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

This protein is predicted to be membranous by TOPCONS.

Topcons

Interpro domains
Total structural coverage: 39%
Model score: 31
MODL_I-TASSER-3.0

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VariantDescription
dbSNP:rs34196984
dbSNP:rs1984564

No binding partner found

The reference OMIM entry for this protein is 611950

Membrane-bound o-acyltransferase domain-containing 5; mboat5
Membrane-bound o-acyltransferase 5
Lysophosphatidylcholine acyltransferase 3; lpcat3
Nessy, drosophila, homolog of

CLONING

Maurel-Zaffran et al. (1999) identified human and mouse MBOAT5 as homologs of Drosophila nessy. The deduced 487-amino acid human and mouse MBOAT5 proteins contain 11 predicted transmembrane domains and share 88% amino acid identity. Human MBOAT5 shares 35% amino acid identity with Drosophila nessy. Hishikawa et al. (2008) cloned mouse Mboat5, which they called Lpcat3. The deduced protein contains 10 putative transmembrane domains and a C-terminal endoplasmic reticulum (ER) retention motif (KKxx). RT-PCR detected ubiquitous Lpcat3 expression, with highest level in testis. Lpcat3 colocalized with an ER marker protein in transfected Chinese hamster ovary cells.

GENE FUNCTION

Hishikawa et al. (2008) found that mouse Lpcat3 converted lysophosphatidylcholine, lysophosphatidylethanolamine, and lysophosphatidylserine to phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine, respectively, using polyunsaturated fatty acyl-CoAs as acyl donors. Knockdown of Lpcat3 in mouse melanoma cells with small interfering RNA significantly reduced cellular acyltransferase activity toward endogenous lysophosphatidylcholine, lysophosphatidylethanolamine, and lysophosphatidylserine. Maurel-Zaffran et al. (1999) found that expression of Drosophila nessy was controlled by Hox proteins (e.g., HOXA7; 142950) during embryogenesis.

MAPPING

Maurel-Zaffran et al. (1999) stated that the MBOAT5 gene maps to chromosome 12p13. ... More on the omim web site

Subscribe to this protein entry history

Aug. 24, 2020: 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 611950 was added.