Q9DCV3 (DGAT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Diacylglycerol O-acyltransferase 2
EC=2.3.1.20

Alternative name(s):
Diglyceride acyltransferase 2

Gene names

Name:

Dgat2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation. Ref.1 Ref.9
Catalytic activity	Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol.
Enzyme regulation	Inhibited by niacin. Ref.7
Pathway	Glycerolipid metabolism; triacylglycerol biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.10.
Tissue specificity	Predominantly expressed in lver. Also expressed in testis. Ref.1
Induction	In white adipose tissue, it is regulated by leptin. By insulin. Up-regulated in diabetic mice. Down-regulated upon fasting and replenished upon refeeding in adipose tissue and liver. Down-regulation in obese animals can reduce hepatic lipogenesis and hepatic steatosis as well as attenuate hyperlipidemia, thereby leading to an improvement in metabolic syndrome. Ref.4 Ref.5 Ref.7 Ref.8
Disruption phenotype	Mice are lipopenic and die soon after birth, apparently from profound reductions in substrates for energy metabolism and from impaired permeability barrier function in the skin. Ref.6
Sequence similarities	Belongs to the diacylglycerol acyltransferase family.

Ontologies

Keywords
Biological process	Glycerol metabolism Lipid metabolism Lipid synthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glycerol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW triglyceride biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from direct assay Ref.1. Source: MGI
Molecular function	2-acylglycerol O-acyltransferase activity Inferred from direct assay. Source: MGI diacylglycerol O-acyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 388	388	Diacylglycerol O-acyltransferase 2		PRO_0000249046
Regions
	Topological domain	1 – 69	69	Cytoplasmic Potential
	Transmembrane	70 – 88	19	Helical; Potential
	Topological domain	89 – 92	4	Lumenal Potential
	Transmembrane	93 – 112	20	Helical; Potential
	Topological domain	113 – 388	276	Cytoplasmic Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9DCV3 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 9C35C37DCAF61D55	FASTA	388	43,770
	10 20 30 40 50 60 MKTLIAAYSG VLRGERRAEA ARSENKNKGS ALSREGSGRW GTGSSILSAL QDIFSVTWLN 70 80 90 100 110 120 RSKVEKQLQV ISVLQWVLSF LVLGVACSVI LMYTFCTDCW LIAVLYFTWL AFDWNTPKKG 130 140 150 160 170 180 GRRSQWVRNW AVWRYFRDYF PIQLVKTHNL LTTRNYIFGY HPHGIMGLGA FCNFSTEATE 190 200 210 220 230 240 VSKKFPGIRP YLATLAGNFR MPVLREYLMS GGICPVNRDT IDYLLSKNGS GNAIIIVVGG 250 260 270 280 290 300 AAESLSSMPG KNAVTLKNRK GFVKLALRHG ADLVPTYSFG ENEVYKQVIF EEGSWGRWVQ 310 320 330 340 350 360 KKFQKYIGFA PCIFHGRGLF SSDTWGLVPY SKPITTVVGE PITVPKLEHP TQKDIDLYHA 370 380 MYMEALVKLF DNHKTKFGLP ETEVLEVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members." Cases S., Stone S.J., Zhou P., Yen C.-L.E., Tow B., Lardizabal K.D., Voelker T., Farese R.V. Jr. J. Biol. Chem. 276:38870-38876(2001) [PubMed: 11481335] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Liver.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., 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 S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., 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 K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., 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 S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Liver.
[4]	"Concerted elevation of acyl-coenzyme A:diacylglycerol acyltransferase (DGAT) activity through independent stimulation of mRNA expression of DGAT1 and DGAT2 by carbohydrate and insulin." Meegalla R.L., Billheimer J.T., Cheng D. Biochem. Biophys. Res. Commun. 298:317-323(2002) [PubMed: 12413942] [Abstract] Cited for: INDUCTION.
[5]	"A novel diacylglycerol acyltransferase (DGAT2) is decreased in human psoriatic skin and increased in diabetic mice." Wakimoto K., Chiba H., Michibata H., Seishima M., Kawasaki S., Okubo K., Mitsui H., Torii H., Imai Y. Biochem. Biophys. Res. Commun. 310:296-302(2003) [PubMed: 14521909] [Abstract] Cited for: INDUCTION.
[6]	"Lipopenia and skin barrier abnormalities in DGAT2-deficient mice." Stone S.J., Myers H.M., Watkins S.M., Brown B.E., Feingold K.R., Elias P.M., Farese R.V. Jr. J. Biol. Chem. 279:11767-11776(2004) [PubMed: 14668353] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[7]	"Niacin noncompetitively inhibits DGAT2 but not DGAT1 activity in HepG2 cells." Ganji S.H., Tavintharan S., Zhu D., Xing Y., Kamanna V.S., Kashyap M.L. J. Lipid Res. 45:1835-1845(2004) [PubMed: 15258194] [Abstract] Cited for: ENZYME REGULATION.
[8]	"Antisense oligonucleotide reduction of DGAT2 expression improves hepatic steatosis and hyperlipidemia in obese mice." Yu X.X., Murray S.F., Pandey S.K., Booten S.L., Bao D., Song X.Z., Kelly S., Chen S., McKay R., Monia B.P., Bhanot S. Hepatology 42:362-371(2005) [PubMed: 16001399] [Abstract] Cited for: INDUCTION.
[9]	"Increased very low density lipoprotein secretion and gonadal fat mass in mice overexpressing liver DGAT1." Yamazaki T., Sasaki E., Kakinuma C., Yano T., Miura S., Ezaki O. J. Biol. Chem. 280:21506-21514(2005) [PubMed: 15797871] [Abstract] Cited for: FUNCTION.
[10]	"Membrane topology and identification of key functional amino acid residues of murine acyl-CoA:diacylglycerol acyltransferase-2." Stone S.J., Levin M.C., Farese R.V. Jr. J. Biol. Chem. 281:40273-40282(2006) [PubMed: 17035227] [Abstract] Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF384160 mRNA. Translation: AAK84175.1. AK002443 mRNA. Translation: BAB22105.1. BC043447 mRNA. Translation: AAH43447.1.
IPI	IPI00121397.
RefSeq	NP_080660.1. NM_026384.3.
UniGene	Mm.180189.
3D structure databases
ProteinModelPortal	Q9DCV3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9DCV3.
Proteomic databases
PRIDE	Q9DCV3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000033001; ENSMUSP00000033001; ENSMUSG00000030747.
GeneID	67800.
KEGG	mmu:67800.
UCSC	uc009ile.1. mouse.
Organism-specific databases
CTD	84649.
MGI	MGI:1915050. Dgat2.
Phylogenomic databases
eggNOG	roNOG04766.
GeneTree	ENSGT00550000074276.
HOGENOM	HBG561030.
HOVERGEN	HBG065791.
InParanoid	Q9DCV3.
OMA	LYHAMYV.
OrthoDB	EOG4R502S.
PhylomeDB	Q9DCV3.
Enzyme and pathway databases
BRENDA	2.3.1.20. 3474.
Gene expression databases
ArrayExpress	Q9DCV3.
Bgee	Q9DCV3.
CleanEx	MM_DGAT2.
Genevestigator	Q9DCV3.
GermOnline	ENSMUSG00000030747. Mus musculus.
Family and domain databases
InterPro	IPR007130. DAGAT. [Graphical view]
KO	K11160.
PANTHER	PTHR12317. DAGAT. 1 hit.
Pfam	PF03982. DAGAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	325591.
SOURCE	Search...

Entry information

Entry name

DGAT2_MOUSE

Accession

Primary (citable) accession number: Q9DCV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	June 1, 2001
Last modified:	November 16, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program