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Symbol report for DGAT1

Stable symbol

HGNC data for DGAT1

Approved symbol
DGAT1
Approved name

diacylglycerol O-acyltransferase 1

Locus type
gene with protein product
HGNC ID
HGNC:2843
Symbol status
Approved
Previous symbols
DGAT
Previous names
diacylglycerol O-acyltransferase (mouse) homolog
Alias symbols
ARGP1
Chromosomal location
8q24.3
UCSC
Alliance of Genome Resources
Bos taurus
DGAT1 VGNC:28020 VGNC
Canis familiaris
DGAT1 VGNC:39912 VGNC
Equus caballus
DGAT1 VGNC:17144 VGNC
Felis catus
DGAT1 VGNC:61455 VGNC
Macaca mulatta
DGAT1 VGNC:71776 VGNC
Mus musculus
Dgat1 MGI:1333825 Curated
Pan troglodytes
DGAT1 VGNC:891 VGNC
Rattus norvegicus
Dgat1 RGD:628673
Sus scrofa
DGAT1 VGNC:87267 VGNC
IUPHAR/BPS Guide to PHARMACOLOGY
Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes.
Oelkers P et al. J Biol Chem 1998 Oct;273(41)26765-26771
Oelkers P, Behari A, Cromley D, Billheimer JT, Sturley SL.
J Biol Chem 1998 Oct;273(41)26765-26771
Abstract: The enzyme acyl coenzyme A:cholesterol acyltransferase 1 (ACAT1) mediates sterol esterification, a crucial component of intracellular lipid homeostasis. Two enzymes catalyze this activity in Saccharomyces cerevisiae (yeast), and several lines of evidence suggest multigene families may also exist in mammals. Using the human ACAT1 sequence to screen data bases of expressed sequence tags, we identified two novel and distinct partial human cDNAs. Full-length cDNA clones for these ACAT related gene products (ARGP) 1 and 2 were isolated from a hepatocyte (HepG2) cDNA library. ARGP1 was expressed in numerous human adult tissues and tissue culture cell lines, whereas expression of ARGP2 was more restricted. In vitro microsomal assays in a yeast strain deleted for both esterification genes and completely deficient in sterol esterification indicated that ARGP2 esterified cholesterol while ARGP1 did not. In contrast to ACAT1 and similar to liver esterification, the activity of ARGP2 was relatively resistant to a histidine active site modifier. ARGP2 is therefore a tissue-specific sterol esterification enzyme which we thus designated ACAT2. We speculate that ARGP1 participates in the coenzyme A-dependent acylation of substrate(s) other than cholesterol. Consistent with this hypothesis, ARGP1, unlike any other member of this multigene family, possesses a predicted diacylglycerol binding motif suggesting that it may perform the last acylation in triglyceride biosynthesis.