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Identification
HMDB Protein ID HMDBP07290
Secondary Accession Numbers
  • 12910
Name Lysophosphatidylcholine acyltransferase 2
Synonyms
  1. 1-acylglycerophosphocholine O-acyltransferase
  2. 1-alkylglycerophosphocholine O-acetyltransferase
  3. Acetyl-CoA:lyso-PAF acetyltransferase
  4. Acetyl-CoA:lyso-platelet-activating factor acetyltransferase
  5. Acyltransferase-like 1
  6. LPC acyltransferase 2
  7. LPCAT-2
  8. Lyso-PAF acetyltransferase
  9. LysoPAFAT
  10. LysoPC acyltransferase 2
Gene Name LPCAT2
Protein Type Enzyme
Biological Properties
General Function Involved in acyltransferase activity
Specific Function Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-dependent. Involved in platelet-activating factor (PAF) biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF). Also converts lyso-PAF to 1-alkyl-phosphatidylcholine (PC), a major component of cell membranes and a PAF precursor. Under resting conditions, acyltransferase activity is preferred. Upon acute inflammatory stimulus, acetyltransferase activity is enhanced and PAF synthesis increases (By similarity).
Pathways
  • Ether lipid metabolism
  • Glycerophospholipid metabolism
  • phospholipid metabolism
Reactions
Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine → Coenzyme A + 1,2-diacyl-sn-glycero-3-phosphocholine details
Acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine → Coenzyme A + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine details
Acyl-CoA + 1-Acyl-sn-glycero-3-phosphocholine → Coenzyme A + Phosphatidylcholine details
Acetyl-CoA + 1-Organyl-2-lyso-sn-glycero-3-phosphocholine → Coenzyme A + 2-Acetyl-1-alkyl-sn-glycero-3-phosphocholine details
Acyl-CoA + 1-Organyl-2-lyso-sn-glycero-3-phosphocholine → Coenzyme A + 1-Radyl-2-acyl-sn-glycero-3-phosphocholine details
Acyl-CoA + 1-Acyl-sn-glycero-3-phosphoglycerol → Coenzyme A + Phosphatidylglycerol details
GO Classification
Biological Process
phosphatidylcholine acyl-chain remodeling
platelet activating factor biosynthetic process
cellular membrane organization
Cellular Component
endoplasmic reticulum membrane
Golgi stack
integral to membrane
Golgi membrane
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
acyltransferase activity
calcium ion binding
Molecular Function
1-acylglycerophosphocholine O-acyltransferase activity
calcium ion binding
1-alkylglycerophosphocholine O-acetyltransferase activity
Process
metabolic process
Cellular Location
  1. Golgi apparatus membrane
  2. Endoplasmic reticulum membrane
  3. Single-pass type II membrane protein
  4. Single-pass type II membrane protein
Gene Properties
Chromosome Location 16
Locus 16q12.2
SNPs LPCAT2
Gene Sequence
>1635 bp
ATGAGCCGGTGCGCCCAGGCGGCGGAAGTGGCGGCCACAGTGCCAGGTGCCGGCGTCGGG
AACGTGGGGCTGCGGCCGCCCATGGTGCCCCGTCAGGCGTCCTTCTTCCCGCCGCCGGTG
CCGAACCCCTTCGTGCAGCAGACGCAGATCGGCTCCGCGAGGCGGGTCCAGATTGTCCTT
CTTGGGATTATCTTGCTTCCAATTCGTGTCTTATTGGTTGCGTTAATTTTATTACTTGCA
TGGCCATTTGCTGCAATTTCAACAGTATGCTGTCCTGAAAAGCTGACCCACCCAATAACT
GGTTGGAGGAGGAAAATTACTCAAACAGCTTTGAAATTTCTGGGTCGTGCTATGTTCTTT
TCAATGGGATTTATAGTTGCTGTAAAAGGAAAGATTGCAAGTCCTTTGGAAGCACCAGTT
TTTGTTGCTGCCCCTCATTCAACATTCTTTGATGGAATTGCCTGTGTTGTAGCTGGGTTA
CCTTCTATGGTATCTCGAAATGAGAATGCACAAGTCCCTCTGATTGGCAGACTGTTACGG
GCTGTGCAACCAGTTTTGGTGTCCCGTGTAGATCCGGATTCCCGAAAAAACACAATAAAT
GAAATAATAAAGCGAACAACATCAGGAGGAGAATGGCCCCAGATACTAGTTTTCCCAGAA
GGTACTTGTACTAATCGTTCCTGTTTGATTACTTTTAAACCAGGAGCCTTCATTCCAGGA
GTTCCAGTGCAGCCAGTCCTCCTCAGATACCCAAACAAGCTGGATACTGTGACCTGGACA
TGGCAAGGATATACATTCATTCAGCTTTGTATGCTTACTTTCTGCCAGCTCTTCACAAAG
GTAGAAGTTGAGTTTATGCCAGTTCAAGTACCAAATGATGAAGAAAAAAATGATCCTGTC
CTTTTTGCCAATAAAGTCCGGAATTTAATGGCAGAAGCTCTGGGAATACCAGTAACAGAT
CATACCTATGAAGACTGCAGATTGATGATTTCAGCAGGACAGCTAACATTGCCTATGGAA
GCTGGGCTGGTGGAATTTACTAAAATTAGCCGAAAATTGAAATTAGATTGGGATGGTGTT
CGTAAGCATTTGGATGAATATGCATCTATTGCGAGTTCCTCAAAAGGAGGAAGAATTGGA
ATTGAAGAATTCGCCAAGTATTTAAAGTTGCCTGTTTCAGATGTCTTGAGACAACTTTTT
GCACTCTTTGACAGGAACCATGATGGCAGCATTGACTTCCGAGAGTATGTGATTGGCCTG
GCTGTCTTGTGCAACCCTTCCAACACAGAGGAGATCATCCAGGTGGCATTTAAGCTGTTT
GACGTTGATGAGGATGGCTACATAACGGAGGAAGAGTTCTCCACCATTCTACAGGCTTCC
CTTGGAGTGCCTGACCTTGATGTTTCTGGTCTCTTCAAGGAAATAGCCCAAGGGGACTCA
ATTTCCTATGAGGAATTTAAAAGTTTTGCCTTAAAGCATCCAGAATATGCTAAGATATTT
ACAACATACCTAGACCTCCAGACGTGCCATGTGTTTTCATTACCAAAAGAAGTCCAGACA
ACCCCCTCCACCGCCAGTAATAAAGTCAGCCCTGAAAAGCATGAAGAGAGTACCTCAGAC
AAAAAAGATGACTGA
Protein Properties
Number of Residues 544
Molecular Weight 60207.295
Theoretical pI 6.551
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Lysophosphatidylcholine acyltransferase 2
MSRCAQAAEVAATVPGAGVGNVGLRPPMVPRQASFFPPPVPNPFVQQTQIGSARRVQIVL
LGIILLPIRVLLVALILLLAWPFAAISTVCCPEKLTHPITGWRRKITQTALKFLGRAMFF
SMGFIVAVKGKIASPLEAPVFVAAPHSTFFDGIACVVAGLPSMVSRNENAQVPLIGRLLR
AVQPVLVSRVDPDSRKNTINEIIKRTTSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPG
VPVQPVLLRYPNKLDTVTWTWQGYTFIQLCMLTFCQLFTKVEVEFMPVQVPNDEEKNDPV
LFANKVRNLMAEALGIPVTDHTYEDCRLMISAGQLTLPMEAGLVEFTKISRKLKLDWDGV
RKHLDEYASIASSSKGGRIGIEEFAKYLKLPVSDVLRQLFALFDRNHDGSIDFREYVIGL
AVLCNPSNTEEIIQVAFKLFDVDEDGYITEEEFSTILQASLGVPDLDVSGLFKEIAQGDS
ISYEEFKSFALKHPEYAKIFTTYLDLQTCHVFSLPKEVQTTPSTASNKVSPEKHEESTSD
KKDD
GenBank ID Protein 126364244
UniProtKB/Swiss-Prot ID Q7L5N7
UniProtKB/Swiss-Prot Entry Name PCAT2_HUMAN
PDB IDs Not Available
GenBank Gene ID AB244718
GeneCard ID LPCAT2
GenAtlas ID LPCAT2
HGNC ID HGNC:26032
References
General References
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  2. 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 ]
  3. 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. [PubMed:17974005 ]
  4. Shindou H, Hishikawa D, Nakanishi H, Harayama T, Ishii S, Taguchi R, Shimizu T: A single enzyme catalyzes both platelet-activating factor production and membrane biogenesis of inflammatory cells. Cloning and characterization of acetyl-CoA:LYSO-PAF acetyltransferase. J Biol Chem. 2007 Mar 2;282(9):6532-9. Epub 2006 Dec 20. [PubMed:17182612 ]