Lysophosphatidylcholine acyltransferase 1

NameLysophosphatidylcholine acyltransferase 1
Synonyms
  • 1-acylglycerophosphocholine O-acyltransferase
  • 1-alkylglycerophosphocholine O-acetyltransferase
  • 2.3.1.23
  • Acetyl-CoA:lyso-PAF acetyltransferase
  • Acetyl-CoA:lyso-platelet-activating factor acetyltransferase
  • Acyltransferase-like 2
  • AYTL2
  • LPC acyltransferase 1
  • Lyso-PAF acetyltransferase
  • LysoPAFAT
  • PFAAP3
  • Phosphonoformate immuno-associated protein 3
Gene NameLPCAT1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0008840|Lysophosphatidylcholine acyltransferase 1
MRLRGCGPRAAPASSAGASDARLLAPPGRNPFVHELRLSALQKAQVALMTLTLFPVRLLV
AAAMMLLAWPLALVASLGSAEKEPEQPPALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGR
QALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQ
DSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPN
KLDTITWTWQGPGALEILWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAE
ALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPEKLEKDLDRYSERAR
MKGGEKIGIAEFAASLEVPVSDLLEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDT
IQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELTVTDLFRAIDQEEKGKITFADFHRFA
EMYPAFAEEYLYPDQTHFESCAETSPAPIPNGFCADFSPENSDAGRKPVRKKLD
Number of residues534
Molecular Weight59150.675
Theoretical pINot Available
GO Classification
Functions
  • calcium ion binding
  • 1-acylglycerophosphocholine O-acyltransferase activity
  • 1-alkenylglycerophosphocholine O-acyltransferase activity
  • 1-alkylglycerophosphocholine O-acetyltransferase activity
  • 1-alkylglycerophosphocholine O-acyltransferase activity
Processes
  • phosphatidylglycerol acyl-chain remodeling
  • triglyceride biosynthetic process
  • phospholipid biosynthetic process
  • surfactant homeostasis
  • small molecule metabolic process
  • negative regulation of phosphatidylcholine biosynthetic process
  • cellular lipid metabolic process
  • glycerophospholipid biosynthetic process
  • phospholipid metabolic process
  • retina development in camera-type eye
  • positive regulation of protein catabolic process
  • phosphatidic acid biosynthetic process
  • phosphatidylcholine acyl-chain remodeling
Components
  • membrane
  • endoplasmic reticulum
  • endoplasmic reticulum membrane
  • Golgi apparatus
  • integral component of membrane
  • Golgi membrane
  • lipid particle
General FunctionCalcium ion binding
Specific FunctionPossesses both acyltransferase and acetyltransferase activities. Activity is calcium-independent. Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology.
Pfam Domain Function
Transmembrane Regions58-78
GenBank Protein IDNot Available
UniProtKB IDQ8NF37
UniProtKB Entry NamePCAT1_HUMAN
Cellular LocationEndoplasmic reticulum membrane
Gene sequence
>lcl|BSEQ0013448|Lysophosphatidylcholine acyltransferase 1 (LPCAT1)
ATGAGGCTGCGGGGATGCGGACCCCGGGCCGCCCCTGCCTCCAGCGCAGGGGCCAGCGAC
GCTCGGCTGCTGGCGCCCCCGGGGCGGAACCCCTTCGTGCACGAGCTGCGCCTCAGCGCC
CTGCAGAAGGCCCAGGTGGCCCTCATGACACTGACGCTCTTCCCGGTCCGGCTCCTGGTT
GCCGCTGCCATGATGCTGCTGGCCTGGCCCCTCGCACTTGTCGCATCCCTGGGCTCTGCG
GAGAAGGAACCCGAGCAGCCCCCGGCCCTGTGGAGGAAGGTTGTGGACTTCCTGCTGAAG
GCCATCATGCGCACCATGTGGTTCGCCGGCGGCTTCCACCGGGTGGCCGTGAAGGGGCGG
CAGGCGCTGCCCACCGAGGCGGCCATCCTCACGCTCGCGCCTCACTCGTCCTACTTCGAC
GCCATCCCTGTGACCATGACGATGTCCTCCATCGTGATGAAGGCAGAGAGCAGAGACATC
CCGATCTGGGGAACTCTGATCCAGTATATACGGCCTGTGTTCGTGTCCCGGTCAGACCAG
GATTCTCGCAGGAAAACAGTAGAAGAAATCAAGAGACGGGCGCAGTCCAACGGAAAGTGG
CCACAGATAATGATTTTTCCAGAAGGAACTTGTACAAACAGGACCTGCCTAATTACCTTC
AAACCTGGTGCATTCATCCCTGGAGCGCCCGTCCAGCCTGTGGTTTTACGATATCCAAAT
AAACTGGACACCATCACATGGACGTGGCAAGGACCTGGAGCGCTGGAAATCCTGTGGCTC
ACGCTGTGTCAGTTTCACAACCAAGTGGAAATCGAGTTCCTTCCTGTGTACAGCCCTTCT
GAGGAGGAGAAGAGGAACCCCGCGCTGTATGCCAGCAACGTGCGGCGAGTCATGGCCGAG
GCCTTGGGTGTCTCCGTGACTGACTACACGTTCGAGGACTGCCAGCTGGCCCTGGCGGAA
GGACAGCTCCGTCTCCCCGCTGACACTTGCCTTTTAGAATTTGCCAGGCTCGTGCGGGGC
CTCGGGCTAAAACCAGAAAAGCTTGAAAAAGATCTGGACAGATACTCAGAAAGAGCCAGG
ATGAAGGGAGGAGAGAAGATAGGTATTGCGGAGTTTGCCGCCTCCCTGGAAGTCCCCGTT
TCTGACTTGCTGGAAGACATGTTTTCACTGTTCGACGAGAGCGGCAGCGGCGAGGTGGAC
CTGCGAGAGTGTGTGGTTGCCCTGTCTGTCGTCTGCCGGCCGGCCCGGACCCTGGACACC
ATCCAGCTGGCTTTCAAGATGTACGGAGCGCAAGAGGACGGCAGCGTCGGCGAAGGTGAC
CTGTCCTGCATCCTCAAGACGGCCCTGGGGGTGGCAGAGCTCACCGTGACCGACCTATTC
CGAGCCATTGACCAAGAGGAGAAGGGGAAGATCACATTCGCTGACTTCCACAGGTTTGCA
GAAATGTACCCTGCCTTCGCAGAGGAATACCTGTACCCGGATCAGACACATTTCGAAAGC
TGTGCAGAGACCTCACCTGCGCCAATCCCAAACGGCTTCTGTGCCGATTTCAGCCCGGAA
AACTCAGACGCTGGGCGGAAGCCTGTTCGCAAGAAGCTGGATTAG
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:25718
Chromosome Location5
LocusNot Available
References
  1. Nakanishi H, Shindou H, Hishikawa D, Harayama T, Ogasawara R, Suwabe A, Taguchi R, Shimizu T: Cloning and characterization of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1). Expression in alveolar type II cells and possible involvement in surfactant production. J Biol Chem. 2006 Jul 21;281(29):20140-7. Epub 2006 May 16. 16704971
  2. Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. 12693554
  3. 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. 15489334
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. 14702039
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. 17974005
  6. Chen X, Hyatt BA, Mucenski ML, Mason RJ, Shannon JM: Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells. Proc Natl Acad Sci U S A. 2006 Aug 1;103(31):11724-9. Epub 2006 Jul 24. 16864775
  7. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. 21269460
  8. Moessinger C, Kuerschner L, Spandl J, Shevchenko A, Thiele C: Human lysophosphatidylcholine acyltransferases 1 and 2 are located in lipid droplets where they catalyze the formation of phosphatidylcholine. J Biol Chem. 2011 Jun 17;286(24):21330-9. doi: 10.1074/jbc.M110.202424. Epub 2011 Apr 15. 21498505
  9. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. 25944712