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Showing Protein Lysophospholipid acyltransferase 5 (HMDBP13917)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP13917
Secondary Accession Numbers None
Name Lysophospholipid acyltransferase 5
Synonyms
  1. LPLAT 5
  2. 1-acylglycerophosphocholine O-acyltransferase
  3. 1-acylglycerophosphoethanolamine O-acyltransferase
  4. 1-acylglycerophosphoserine O-acyltransferase
  5. Lysophosphatidylcholine acyltransferase
  6. Lysophosphatidylcholine acyltransferase 3
  7. Lysophosphatidylethanolamine acyltransferase
  8. Lysophosphatidylserine acyltransferase
  9. Membrane-bound O-acyltransferase domain-containing protein 5
  10. LPCAT
  11. Lyso-PC acyltransferase
  12. Lyso-PC acyltransferase 3
  13. mLPCAT3
  14. LPEAT
  15. Lyso-PE acyltransferase
  16. LPSAT
  17. Lyso-PS acyltransferase
  18. O-acyltransferase domain-containing protein 5
Gene Name LPCAT3
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Lysophospholipid O-acyltransferase (LPLAT) that catalyzes the reacylation step of the phospholipid remodeling process also known as the Lands cycle (PubMed:18287005, PubMed:25898003). 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). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs (PubMed:18287005, PubMed:25898003). Has higher activity for LPC acyl acceptors compared to LPEs and LPSs (PubMed:18287005). Can also transfer the fatty acyl chain from fatty acyl-CoA to 1-O-alkyl lysophospholipid or 1-O-alkenyl lysophospholipid with lower efficiency (PubMed:18287005). Acts as a major LPC O-acyltransferase in liver and intestine (PubMed:25898003, PubMed:26833026). 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 (PubMed:25806685). Promotes processing of sterol regulatory protein SREBF1 in hepatocytes, likely by facilitating the translocation of SREBF1-SCAP complex from ER to the Golgi apparatus (PubMed:28846071). Participates in mechanisms by which the liver X receptor/NR1H3 or NR1H2 signaling pathway counteracts lipid-induced ER stress response and inflammation (PubMed:24206663). Downregulates hepatic inflammation by limiting arachidonic acid availability for synthesis of inflammatory eicosanoids, such as prostaglandins (PubMed:24206663). In enterocytes, acts as a component of a gut-brain feedback loop that coordinates dietary lipid absorption and food intake. Regulates the abundance of PCs containing linoleate and arachidonate in enterocyte membranes, enabling passive diffusion of fatty acids and cholesterol across the membrane for efficient chylomicron assembly (PubMed:26833026). In the intestinal crypt, acts as a component of dietary-responsive phospholipid-cholesterol axis, regulating the biosynthesis of cholesterol and its mitogenic effects on intestinal stem cells (PubMed:29395055).
Pathways
  • Ferroptosis
  • Glycerophospholipid metabolism
  • phospholipid metabolism
Reactions Not Available
GO Classification
Biological Process
intestinal stem cell homeostasis
phosphatidylcholine acyl-chain remodeling
phosphatidylethanolamine acyl-chain remodeling
phosphatidylserine acyl-chain remodeling
negative regulation of inflammatory response
phosphatidylcholine biosynthetic process
regulation of plasma lipoprotein particle levels
positive regulation of intestinal cholesterol absorption
very-low-density lipoprotein particle assembly
regulation of cholesterol biosynthetic process
chylomicron assembly
endoplasmic reticulum membrane organization
lipid modification
negative regulation of response to endoplasmic reticulum stress
positive regulation of sterol regulatory element binding protein cleavage
positive regulation of triglyceride transport
Cellular Component
endoplasmic reticulum membrane
membrane
integral to membrane
Molecular Function
1-acylglycerophosphocholine O-acyltransferase activity
transferase activity, transferring acyl groups
1-acylglycerophosphoethanolamine O-acyltransferase activity
1-acylglycerophosphoserine O-acyltransferase activity
lysophospholipid acyltransferase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 487
Molecular Weight 56146.35
Theoretical pI 8.562
Pfam Domain Function
Signals Not Available
Transmembrane Regions
  • 44-64;84-104;111-131;180-200;236-256;285-305;364-384;422-442;453-473;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q91V01
UniProtKB/Swiss-Prot Entry Name MBOA5_MOUSE
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Carninci P, Kasukawa T, Katayama S, Gough J, Frith MC, Maeda N, Oyama R, Ravasi T, Lenhard B, Wells C, Kodzius R, Shimokawa K, Bajic VB, Brenner SE, Batalov S, Forrest AR, Zavolan M, Davis MJ, Wilming LG, Aidinis V, Allen JE, Ambesi-Impiombato A, Apweiler R, Aturaliya RN, Bailey TL, Bansal M, Baxter L, Beisel KW, Bersano T, Bono H, Chalk AM, Chiu KP, Choudhary V, Christoffels A, Clutterbuck DR, Crowe ML, Dalla E, Dalrymple BP, de Bono B, Della Gatta G, di Bernardo D, Down T, Engstrom P, Fagiolini M, Faulkner G, Fletcher CF, Fukushima T, Furuno M, Futaki S, Gariboldi M, Georgii-Hemming P, Gingeras TR, Gojobori T, Green RE, Gustincich S, Harbers M, Hayashi Y, Hensch TK, Hirokawa N, Hill D, Huminiecki L, Iacono M, Ikeo K, Iwama A, Ishikawa T, Jakt M, Kanapin A, Katoh M, Kawasawa Y, Kelso J, Kitamura H, Kitano H, Kollias G, Krishnan SP, Kruger A, Kummerfeld SK, Kurochkin IV, Lareau LF, Lazarevic D, Lipovich L, Liu J, Liuni S, McWilliam S, Madan Babu M, Madera M, Marchionni L, Matsuda H, Matsuzawa S, Miki H, Mignone F, Miyake S, Morris K, Mottagui-Tabar S, Mulder N, Nakano N, Nakauchi H, Ng P, Nilsson R, Nishiguchi S, Nishikawa S, Nori F, Ohara O, Okazaki Y, Orlando V, Pang KC, Pavan WJ, Pavesi G, Pesole G, Petrovsky N, Piazza S, Reed J, Reid JF, Ring BZ, Ringwald M, Rost B, Ruan Y, Salzberg SL, Sandelin A, Schneider C, Schonbach C, Sekiguchi K, Semple CA, Seno S, Sessa L, Sheng Y, Shibata Y, Shimada H, Shimada K, Silva D, Sinclair B, Sperling S, Stupka E, Sugiura K, Sultana R, Takenaka Y, Taki K, Tammoja K, Tan SL, Tang S, Taylor MS, Tegner J, Teichmann SA, Ueda HR, van Nimwegen E, Verardo R, Wei CL, Yagi K, Yamanishi H, Zabarovsky E, Zhu S, Zimmer A, Hide W, Bult C, Grimmond SM, Teasdale RD, Liu ET, Brusic V, Quackenbush J, Wahlestedt C, Mattick JS, Hume DA, Kai C, Sasaki D, Tomaru Y, Fukuda S, Kanamori-Katayama M, Suzuki M, Aoki J, Arakawa T, Iida J, Imamura K, Itoh M, Kato T, Kawaji H, Kawagashira N, Kawashima T, Kojima M, Kondo S, Konno H, Nakano K, Ninomiya N, Nishio T, Okada M, Plessy C, Shibata K, Shiraki T, Suzuki S, Tagami M, Waki K, Watahiki A, Okamura-Oho Y, Suzuki H, Kawai J, Hayashizaki Y: The transcriptional landscape of the mammalian genome. Science. 2005 Sep 2;309(5740):1559-63. [PubMed:16141072 ]
  3. Huttlin EL, Jedrychowski MP, Elias JE, Goswami T, Rad R, Beausoleil SA, Villen J, Haas W, Sowa ME, Gygi SP: A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89. doi: 10.1016/j.cell.2010.12.001. [PubMed:21183079 ]
  4. Ansari-Lari MA, Oeltjen JC, Schwartz S, Zhang Z, Muzny DM, Lu J, Gorrell JH, Chinault AC, Belmont JW, Miller W, Gibbs RA: Comparative sequence analysis of a gene-rich cluster at human chromosome 12p13 and its syntenic region in mouse chromosome 6. Genome Res. 1998 Jan;8(1):29-40. [PubMed:9445485 ]
  5. Hishikawa D, Shindou H, Kobayashi S, Nakanishi H, Taguchi R, Shimizu T: Discovery of a lysophospholipid acyltransferase family essential for membrane asymmetry and diversity. Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):2830-5. doi: 10.1073/pnas.0712245105. Epub 2008 Feb 20. [PubMed:18287005 ]
  6. Rong X, Albert CJ, Hong C, Duerr MA, Chamberlain BT, Tarling EJ, Ito A, Gao J, Wang B, Edwards PA, Jung ME, Ford DA, Tontonoz P: LXRs regulate ER stress and inflammation through dynamic modulation of membrane phospholipid composition. Cell Metab. 2013 Nov 5;18(5):685-97. doi: 10.1016/j.cmet.2013.10.002. [PubMed:24206663 ]
  7. Hashidate-Yoshida T, Harayama T, Hishikawa D, Morimoto R, Hamano F, Tokuoka SM, Eto M, Tamura-Nakano M, Yanobu-Takanashi R, Mukumoto Y, Kiyonari H, Okamura T, Kita Y, Shindou H, Shimizu T: Fatty acid remodeling by LPCAT3 enriches arachidonate in phospholipid membranes and regulates triglyceride transport. Elife. 2015 Apr 21;4. doi: 10.7554/eLife.06328. [PubMed:25898003 ]
  8. Rong X, Wang B, Dunham MM, Hedde PN, Wong JS, Gratton E, Young SG, Ford DA, Tontonoz P: Lpcat3-dependent production of arachidonoyl phospholipids is a key determinant of triglyceride secretion. Elife. 2015 Mar 25;4. doi: 10.7554/eLife.06557. [PubMed:25806685 ]
  9. Wang B, Rong X, Duerr MA, Hermanson DJ, Hedde PN, Wong JS, Vallim TQ, Cravatt BF, Gratton E, Ford DA, Tontonoz P: Intestinal Phospholipid Remodeling Is Required for Dietary-Lipid Uptake and Survival on a High-Fat Diet. Cell Metab. 2016 Mar 8;23(3):492-504. doi: 10.1016/j.cmet.2016.01.001. Epub 2016 Jan 28. [PubMed:26833026 ]
  10. Rong X, Wang B, Palladino EN, de Aguiar Vallim TQ, Ford DA, Tontonoz P: ER phospholipid composition modulates lipogenesis during feeding and in obesity. J Clin Invest. 2017 Oct 2;127(10):3640-3651. doi: 10.1172/JCI93616. Epub 2017 Aug 28. [PubMed:28846071 ]
  11. Wang B, Rong X, Palladino END, Wang J, Fogelman AM, Martin MG, Alrefai WA, Ford DA, Tontonoz P: Phospholipid Remodeling and Cholesterol Availability Regulate Intestinal Stemness and Tumorigenesis. Cell Stem Cell. 2018 Feb 1;22(2):206-220.e4. doi: 10.1016/j.stem.2017.12.017. [PubMed:29395055 ]