MOGT2_MOUSE
ID MOGT2_MOUSE Reviewed; 334 AA.
AC Q80W94;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=2-acylglycerol O-acyltransferase 2 {ECO:0000305};
DE EC=2.3.1.22 {ECO:0000269|PubMed:12730219};
DE AltName: Full=Acyl-CoA:monoacylglycerol acyltransferase 2;
DE Short=MGAT2;
DE AltName: Full=Diacylglycerol acyltransferase 2-like protein 5;
DE AltName: Full=Monoacylglycerol O-acyltransferase 1-like;
DE AltName: Full=Monoacylglycerol O-acyltransferase 2;
GN Name=Mogat2 {ECO:0000312|MGI:MGI:2663253}; Synonyms=Dgat2l5, Mgat1l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Intestine;
RX PubMed=12621063; DOI=10.1074/jbc.m301633200;
RA Yen C.-L.E., Farese R.V. Jr.;
RT "MGAT2, a monoacylglycerol acyltransferase expressed in the small
RT intestine.";
RL J. Biol. Chem. 278:18532-18537(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12576479; DOI=10.1074/jbc.m300139200;
RA Cao J., Lockwood J., Burn P., Shi Y.;
RT "Cloning and functional characterization of a mouse intestinal acyl-
RT CoA:monoacylglycerol acyltransferase, MGAT2.";
RL J. Biol. Chem. 278:13860-13866(2003).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC
RP ACTIVITY.
RX PubMed=12730219; DOI=10.1074/jbc.m302835200;
RA Cao J., Burn P., Shi Y.;
RT "Properties of the mouse intestinal acyl-CoA:monoacylglycerol
RT acyltransferase, MGAT2.";
RL J. Biol. Chem. 278:25657-25663(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14966132; DOI=10.1074/jbc.m313272200;
RA Cao J., Hawkins E., Brozinick J., Liu X., Zhang H., Burn P., Shi Y.;
RT "A predominant role of acyl-CoA:monoacylglycerol acyltransferase-2 in
RT dietary fat absorption implicated by tissue distribution, subcellular
RT localization, and up-regulation by high fat diet.";
RL J. Biol. Chem. 279:18878-18886(2004).
CC -!- FUNCTION: Catalyzes the formation of diacylglycerol from 2-
CC monoacylglycerol and fatty acyl-CoA. Has a preference toward
CC monoacylglycerols containing unsaturated fatty acids in an order of
CC C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of
CC dietary fat in the small intestine by catalyzing the resynthesis of
CC triacylglycerol in enterocytes. May play a role in diet-induced
CC obesity. Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl
CC acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (By
CC similarity). {ECO:0000250|UniProtKB:Q3SYC2,
CC ECO:0000269|PubMed:12576479, ECO:0000269|PubMed:12730219,
CC ECO:0000269|PubMed:14966132}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acylglycerol + an acyl-CoA = a 1,2-diacyl-sn-glycerol +
CC CoA; Xref=Rhea:RHEA:32947, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; EC=2.3.1.22;
CC Evidence={ECO:0000269|PubMed:12730219};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32948;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-
CC (9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:37911,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-
CC (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:37915,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + butanoyl-CoA = 1-butyryl-2-
CC (9Z)-octadecenoyl-sn-glycerol + CoA; Xref=Rhea:RHEA:38051,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:73990,
CC ChEBI:CHEBI:75443; Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38052;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + octanoyl-CoA = 1-octanoyl-2-
CC (9Z)-octadecenoyl-sn-glycerol + CoA; Xref=Rhea:RHEA:38059,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:73990,
CC ChEBI:CHEBI:75462; Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38060;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + dodecanoyl-CoA = 1-dodecanoyl-
CC 2-(9Z)-octadecenoyl-sn-glycerol + CoA; Xref=Rhea:RHEA:38063,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:73990,
CC ChEBI:CHEBI:75463; Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38064;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + tetradecanoyl-CoA = 1-
CC tetradecanoyl-2-(9Z)-octadecenoyl-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38067, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:73990, ChEBI:CHEBI:75465;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38068;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38071, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:73990, ChEBI:CHEBI:75466;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + octadecanoyl-CoA = 1-
CC octadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38075, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:73990, ChEBI:CHEBI:75468;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38076;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + eicosanoyl-CoA = 1-eicosanoyl-
CC 2-(9Z)-octadecenoyl-sn-glycerol + CoA; Xref=Rhea:RHEA:38079,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:73990,
CC ChEBI:CHEBI:75470; Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38080;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2-(9Z-octadecenoyl)-glycerol =
CC 1-(9Z,12Z)-octadecadienoyl-2-(9Z)-octadecenoyl-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38083, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:73990, ChEBI:CHEBI:75471;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38084;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 2-(9Z-octadecenoyl)-
CC glycerol = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-octadecenoyl-sn-
CC glycerol + CoA; Xref=Rhea:RHEA:38087, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57368, ChEBI:CHEBI:73990, ChEBI:CHEBI:75472;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38088;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-dodecanoylglycerol = 1-dodecanoyl-2-
CC (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38115,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75539,
CC ChEBI:CHEBI:75579; Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38116;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-tetradecanoylglycerol = 1-
CC tetradecanoyl-2-(9Z-octadecenoyl)-glycerol + CoA;
CC Xref=Rhea:RHEA:38119, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75562, ChEBI:CHEBI:75582;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38120;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoylglycerol = 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)glycerol + CoA; Xref=Rhea:RHEA:38123,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:69081,
CC ChEBI:CHEBI:75585; Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38124;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoylglycerol = 1-
CC octadecanoyl-2-(9Z)-octadecenoylglycerol + CoA; Xref=Rhea:RHEA:38127,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75555,
CC ChEBI:CHEBI:75590; Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38128;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z-octadecadienoyl)-glycerol =
CC 1-(9Z,12Z-octadecadienoyl)-2-(9Z-octadecenoyl)-glycerol + CoA;
CC Xref=Rhea:RHEA:38131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75568, ChEBI:CHEBI:75614;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38132;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z,15Z-octadecatrienoyl)-
CC glycerol = 1-(9Z,12Z,15Z-octadecatrienoyl)-2-(9Z-octadecenoyl)-
CC glycerol + CoA; Xref=Rhea:RHEA:38135, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:75609, ChEBI:CHEBI:75610;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38136;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-
CC glycerol = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-(9Z-octadecenoyl)-
CC glycerol + CoA; Xref=Rhea:RHEA:38139, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:75611, ChEBI:CHEBI:75612;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38140;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecane-1,2-diol + hexadecanoyl-CoA = 2-hydroxyhexadecyl
CC hexadecanoate + CoA; Xref=Rhea:RHEA:38171, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:75586, ChEBI:CHEBI:75587;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38172;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-decanoylglycerol = 1-decanoyl-2-(9Z-
CC octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:75547,
CC ChEBI:CHEBI:85787; Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38020;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-
CC (9Z-octadecenyl)-mono-(9Z-octadecenoyl)-glycerol + CoA;
CC Xref=Rhea:RHEA:55340, ChEBI:CHEBI:34116, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:138734;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol =
CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-mono-(9Z-
CC octadecenoyl)-glycerol = 1-O-(9Z-octadecenyl)-2,3-di-(9Z-
CC octadecenoyl)glycerol + CoA; Xref=Rhea:RHEA:55344, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:138734, ChEBI:CHEBI:138735;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55345;
CC Evidence={ECO:0000250|UniProtKB:Q3SYC2};
CC -!- ACTIVITY REGULATION: Inhibited by oleic acid and sphingosine, while it
CC is stimulated by phosphatidylcholine, phosphatidylserine and
CC phosphatidic acid. {ECO:0000269|PubMed:12730219}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:12730219};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14966132}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14966132}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q3SYC2}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in small intestine. Detected in
CC the small intestine in a proximal-to-distal gradient that correlated
CC with fat absorption pattern. Present not only in the villi, but also in
CC the crypt regions of the small intestine, which suggests that
CC expression occurs prior to the maturation of enterocytes. Not
CC detectable in other sections of the digestive tract, including stomach,
CC cecum, colon and rectum, or other tissues such as kidney, liver and
CC adipocytes (at protein level). Also detected in kidney, adipose and
CC stomach. Expressed at very low level in liver, skeletal muscle and
CC spleen. Not expressed in brain, heart, lung, skin, testis and thymus.
CC {ECO:0000269|PubMed:12576479, ECO:0000269|PubMed:12621063,
CC ECO:0000269|PubMed:14966132}.
CC -!- INDUCTION: Up-regulated in mice fed a high fat diet, implicating a role
CC in diet-induced obesity (at protein level).
CC {ECO:0000269|PubMed:14966132}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY157609; AAO23673.1; -; mRNA.
DR EMBL; AK133854; BAE21888.1; -; mRNA.
DR EMBL; BC052831; AAH52831.1; -; mRNA.
DR CCDS; CCDS21478.1; -.
DR RefSeq; NP_803231.1; NM_177448.4.
DR AlphaFoldDB; Q80W94; -.
DR BioGRID; 231424; 1.
DR STRING; 10090.ENSMUSP00000064041; -.
DR BindingDB; Q80W94; -.
DR ChEMBL; CHEMBL3603729; -.
DR iPTMnet; Q80W94; -.
DR PhosphoSitePlus; Q80W94; -.
DR MaxQB; Q80W94; -.
DR PaxDb; Q80W94; -.
DR PeptideAtlas; Q80W94; -.
DR PRIDE; Q80W94; -.
DR ProteomicsDB; 295580; -.
DR Antibodypedia; 31177; 155 antibodies from 28 providers.
DR DNASU; 233549; -.
DR Ensembl; ENSMUST00000064231; ENSMUSP00000064041; ENSMUSG00000052396.
DR GeneID; 233549; -.
DR KEGG; mmu:233549; -.
DR UCSC; uc009ilf.2; mouse.
DR CTD; 80168; -.
DR MGI; MGI:2663253; Mogat2.
DR VEuPathDB; HostDB:ENSMUSG00000052396; -.
DR eggNOG; KOG0831; Eukaryota.
DR GeneTree; ENSGT01030000234582; -.
DR HOGENOM; CLU_023995_0_1_1; -.
DR InParanoid; Q80W94; -.
DR OMA; PFYRDYI; -.
DR OrthoDB; 1347007at2759; -.
DR PhylomeDB; Q80W94; -.
DR TreeFam; TF314707; -.
DR BRENDA; 2.3.1.22; 3474.
DR Reactome; R-MMU-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00282; -.
DR BioGRID-ORCS; 233549; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q80W94; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q80W94; protein.
DR Bgee; ENSMUSG00000052396; Expressed in epithelium of small intestine and 112 other tissues.
DR Genevisible; Q80W94; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; IDA:MGI.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:MGI.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; IDA:MGI.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0050892; P:intestinal absorption; IDA:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IDA:MGI.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046462; P:monoacylglycerol metabolic process; ISO:MGI.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:MGI.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Endoplasmic reticulum; Glycerol metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..334
FT /note="2-acylglycerol O-acyltransferase 2"
FT /id="PRO_0000249063"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 334 AA; 38591 MW; BFC7C84A22B607BD CRC64;
MVEFAPLLVP WERRLQTFAV LQWVFSFLAL AQLCIVIFVG LLFTRFWLFS VLYATWWYLD
WDKPRQGGRP IQFFRRLAIW KYMKDYFPVS LVKTAELDPS RNYIAGFHPH GVLAAGAFLN
LCTESTGFTS LFPGIRSYLM MLTVWFRAPF FRDYIMSGGL VSSEKVSADH ILSRKGGGNL
LAIIVGGAQE ALDARPGAYR LLLKNRKGFI RLALMHGAAL VPIFSFGENN LFNQVENTPG
TWLRWIQNRL QKIMGISLPL FHGRGVFQYS FGLMPFRQPI TTIVGKPIEV QMTPQPSREE
VDRLHQRYIK ELCKLFEEHK LKFNVPEDQH LEFC
