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Identification
HMDB Protein ID HMDBP01543
Secondary Accession Numbers
  • 6839
Name Dihydroxyacetone phosphate acyltransferase
Synonyms
  1. Acyl-CoA:dihydroxyacetonephosphateacyltransferase
  2. DAP-AT
  3. DHAP-AT
  4. Glycerone-phosphate O-acyltransferase
Gene Name GNPAT
Protein Type Enzyme
Biological Properties
General Function Lipid transport and metabolism
Specific Function Not Available
Pathways
  • Glycerophospholipid metabolism
  • Peroxisome
  • Plasmalogen Synthesis
Reactions
Acyl-CoA + Dihydroxyacetone phosphate → Coenzyme A + acylglycerone phosphate details
GO Classification
Biological Process
synapse assembly
response to drug
response to nutrient
response to starvation
paranodal junction assembly
phosphatidic acid biosynthetic process
response to fatty acid
ether lipid biosynthetic process
cellular membrane organization
cerebellum morphogenesis
Cellular Component
mitochondrion
peroxisomal matrix
peroxisomal membrane
Function
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
acyltransferase activity
Molecular Function
palmitoyl-CoA hydrolase activity
glycerol-3-phosphate O-acyltransferase activity
glycerone-phosphate O-acyltransferase activity
Process
metabolic process
Cellular Location
  1. Peripheral membrane protein
  2. Matrix side
  3. Peroxisome membrane
Gene Properties
Chromosome Location 1
Locus 1q42
SNPs GNPAT
Gene Sequence
>2043 bp
ATGGAGTCTTCCAGTTCATCTAACTCTTATTTCTCCGTTGGCCCAACCAGTCCCAGCGCT
GTCGTGCTCCTCTACTCGAAGGAGCTCAAAAAGTGGGATGAGTTTGAAGATATTTTAGAA
GAGAGGAGGCATGTCAGTGACTTGAAATTTGCAATGAAATGCTACACACCTCTTGTCTAT
AAGGGAATTACTCCATGTAAACCAATTGATATTAAATGTAGTGTTCTCAATTCTGAGGAG
ATTCATTATGTCATTAAACAGCTTTCCAAGGAATCCCTTCAATCTGTGGATGTCCTCCGA
GAGGAAGTGAGTGAGATCTTAGATGAAATGAGTCACAAACTGCGTCTTGGAGCCATTCGG
TTTTGTGCCTTCACCCTGAGCAAAGTATTTAAACAAATTTTCTCGAAGGTGTGTGTAAAT
GAAGAAGGTATTCAGAAACTACAAAGAGCCATCCAGGAGCATCCTGTTGTTCTGCTGCCT
AGTCATCGAAGTTACATTGACTTCCTCATGTTGTCTTTTCTTCTATACAATTATGATTTG
CCTGTGCCAGTTATAGCAGCAGGAATGGACTTCCTGGGAATGAAAATGGTTGGTGAGCTG
CTACGAATGTCGGGTGCCTTTTTCATGCGGCGTACCTTTGGTGGCAATAAACTCTACTGG
GCTGTATTCTCTGAATATGTAAAAACTATGTTACGGAATGGTTATGCTCCTGTTGAATTT
TTCCTCGAAGGGACAAGAAGCCGCTCTGCCAAGACATTGACTCCTAAATTTGGTCTTCTG
AATATTGTGATGGAGCCATTTTTTAAAAGAGAAGTTTTTGATACCTACCTTGTCCCAATT
AGTATCAGTTATGATAAGATCTTGGAAGAAACTCTTTATGTGTATGAGCTTCTAGGGGTT
CCTAAACCAAAAGAATCTACAACTGGGTTGCTGAAAGCCAGAAAGATTCTCTCTGAAAAT
TTTGGAAGCATCCATGTGTACTTTGGAGATCCTGTGTCACTTCGATCTTTGGCAGCTGGG
AGGATGAGTCGGAGCTCATATAACTTGGTTCCAAGATACATTCCTCAGAAACAGTCTGAG
GACATGCATGCCTTTGTCACTGAAGTTGCCTACAAAATGGAGCTTCTGCAAATTGAAAAC
ATGGTTTTGAGCCCCTGGACCCTAATAGTTGCTGTTCTGCTTCAGAACCGGCCATCCATG
GACTTTGATGCTCTGGTGGAAAAGACTTTATGGCTAAAAGGCTTAACCCAGGCATTTGGA
GGGTTTCTCATTTGGCCTGATAATAAACCTGCTGAAGAAGTTGTCCCGGCCAGCATTCTT
CTGCATTCCAACATTGCCAGCCTTGTCAAAGACCAGGTGATTCTGAAAGTGGACTCCGGA
GACTCGGAAGTGGTCGATGGGCTTATGCTCCAGCACATCACTCTCCTCATGTGCTCAGCT
TATAGGAACCAGCTGCTCAACATTTTTGTGCGCCCATCCTTAGTAGCAGTAGCATTGCAG
ATGACACCAGGGTTCAGGAAAGAGGATGTCTACAGTTGCTTTCGCTTCCTACGTGATGTT
TTTGCAGATGAGTTCATCTTCCTTCCAGGAAACACACTAAAGGACTTTGAAGAAGGCTGT
TACCTGCTTTGTAAAAGTGAAGCCATACAAGTGACTACGAAAGACATCCTAGTTACAGAG
AAAGGAAATACTGTGTTAGAATTTTTAGTAGGACTCTTTAAACCTTTTGTGGAAAGCTAT
CAGATAATTTGCAAGTACCTTTTGAGTGAAGAAGAGGACCACTTCAGTGAGGAACAGTAC
TTGGCTGCAGTCAGAAAATTCACAAGTCAGCTTCTCGATCAAGGTACCTCTCAATGTTAT
GATGTATTATCTTCTGATGTGCAGAAAAACGCCTTAGCAGCCTGTGTGAGGCTCGGAGTA
GTGGAGAAGAAGAAGATAAATAATAACTGTATATTTAATGTGAATGAACCTGCCACAACC
AAATTAGAAGAAATGCTTGGTTGTAAGACACCAATAGGAAAACCAGCCACTGCAAAACTT
TAA
Protein Properties
Number of Residues 680
Molecular Weight 77187.185
Theoretical pI 6.559
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Dihydroxyacetone phosphate acyltransferase
MESSSSSNSYFSVGPTSPSAVVLLYSKELKKWDEFEDILEERRHVSDLKFAMKCYTPLVY
KGITPCKPIDIKCSVLNSEEIHYVIKQLSKESLQSVDVLREEVSEILDEMSHKLRLGAIR
FCAFTLSKVFKQIFSKVCVNEEGIQKLQRAIQEHPVVLLPSHRSYIDFLMLSFLLYNYDL
PVPVIAAGMDFLGMKMVGELLRMSGAFFMRRTFGGNKLYWAVFSEYVKTMLRNGYAPVEF
FLEGTRSRSAKTLTPKFGLLNIVMEPFFKREVFDTYLVPISISYDKILEETLYVYELLGV
PKPKESTTGLLKARKILSENFGSIHVYFGDPVSLRSLAAGRMSRSSYNLVPRYIPQKQSE
DMHAFVTEVAYKMELLQIENMVLSPWTLIVAVLLQNRPSMDFDALVEKTLWLKGLTQAFG
GFLIWPDNKPAEEVVPASILLHSNIASLVKDQVILKVDSGDSEVVDGLMLQHITLLMCSA
YRNQLLNIFVRPSLVAVALQMTPGFRKEDVYSCFRFLRDVFADEFIFLPGNTLKDFEEGC
YLLCKSEAIQVTTKDILVTEKGNTVLEFLVGLFKPFVESYQIICKYLLSEEEDHFSEEQY
LAAVRKFTSQLLDQGTSQCYDVLSSDVQKNALAACVRLGVVEKKKINNNCIFNVNEPATT
KLEEMLGCKTPIGKPATAKL
GenBank ID Protein 3258645
UniProtKB/Swiss-Prot ID O15228
UniProtKB/Swiss-Prot Entry Name GNPAT_HUMAN
PDB IDs Not Available
GenBank Gene ID AF043937
GeneCard ID GNPAT
GenAtlas ID Not Available
HGNC ID HGNC:4416
References
General References
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  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Thai TP, Rodemer C, Jauch A, Hunziker A, Moser A, Gorgas K, Just WW: Impaired membrane traffic in defective ether lipid biosynthesis. Hum Mol Genet. 2001 Jan 15;10(2):127-36. [PubMed:11152660 ]
  5. Thai TP, Heid H, Rackwitz HR, Hunziker A, Gorgas K, Just WW: Ether lipid biosynthesis: isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase. FEBS Lett. 1997 Dec 29;420(2-3):205-11. [PubMed:9459311 ]
  6. Ofman R, Hettema EH, Hogenhout EM, Caruso U, Muijsers AO, Wanders RJ: Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the human cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia punctata type 2. Hum Mol Genet. 1998 May;7(5):847-53. [PubMed:9536089 ]
  7. Ofman R, Lajmir S, Wanders RJ: Etherphospholipid biosynthesis and dihydroxyactetone-phosphate acyltransferase: resolution of the genomic organization of the human gnpat gene and its use in the identification of novel mutations. Biochem Biophys Res Commun. 2001 Mar 2;281(3):754-60. [PubMed:11237722 ]