MOGT2_HUMAN
ID MOGT2_HUMAN Reviewed; 334 AA.
AC Q3SYC2; A8K7I3; Q3SYC1; Q6ZQZ2; Q86UH6; Q9H630;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=2-acylglycerol O-acyltransferase 2 {ECO:0000305};
DE EC=2.3.1.22 {ECO:0000269|PubMed:12621063, ECO:0000269|PubMed:27184406};
DE AltName: Full=Acyl-CoA:monoacylglycerol acyltransferase 2;
DE Short=MGAT2;
DE Short=hMGAT2;
DE AltName: Full=Diacylglycerol O-acyltransferase candidate 5;
DE Short=hDC5;
DE AltName: Full=Diacylglycerol acyltransferase 2-like protein 5;
DE AltName: Full=Monoacylglycerol O-acyltransferase 2;
GN Name=MOGAT2 {ECO:0000312|HGNC:HGNC:23248}; Synonyms=DC5, DGAT2L5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 3),
RP FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND CATALYTIC ACTIVITY.
RC 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] (ISOFORMS 1 AND 2).
RC TISSUE=Small intestine, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP VAL-9.
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 [5]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=12824082; DOI=10.1152/ajpendo.00179.2003;
RA Lockwood J.F., Cao J., Burn P., Shi Y.;
RT "Human intestinal monoacylglycerol acyltransferase: differential features
RT in tissue expression and activity.";
RL Am. J. Physiol. 285:E927-E937(2003).
RN [6]
RP CATALYTIC ACTIVITY.
RX PubMed=16106050; DOI=10.1194/jlr.m500168-jlr200;
RA Yen C.-L.E., Brown C.H. IV, Monetti M., Farese R.V. Jr.;
RT "A human skin multifunctional O-acyltransferase that catalyzes the
RT synthesis of acylglycerols, waxes, and retinyl esters.";
RL J. Lipid Res. 46:2388-2397(2005).
RN [7]
RP CATALYTIC ACTIVITY.
RX PubMed=18768481; DOI=10.1074/jbc.m800494200;
RA Cheng D., Iqbal J., Devenny J., Chu C.H., Chen L., Dong J., Seethala R.,
RA Keim W.J., Azzara A.V., Lawrence R.M., Pelleymounter M.A., Hussain M.M.;
RT "Acylation of acylglycerols by acyl coenzyme A:diacylglycerol
RT acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the intestinal
RT fat absorption.";
RL J. Biol. Chem. 283:29802-29811(2008).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=27184406; DOI=10.1016/j.bbrc.2016.05.071;
RA Brandt C., McFie P.J., Stone S.J.;
RT "Biochemical characterization of human acyl coenzyme A: 2-monoacylglycerol
RT acyltransferase-3 (MGAT3).";
RL Biochem. Biophys. Res. Commun. 475:264-270(2016).
RN [9]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=28420705; DOI=10.1194/jlr.m073445;
RA Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.;
RT "Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid
RT acyltransferases.";
RL J. Lipid Res. 58:1091-1099(2017).
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)
CC (PubMed:28420705). {ECO:0000269|PubMed:12621063,
CC ECO:0000269|PubMed:27184406, ECO:0000269|PubMed:28420705}.
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:12621063, ECO:0000269|PubMed:27184406};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38052;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38060;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38064;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38068;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38076;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38080;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38084;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38088;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38116;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38120;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38124;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38128;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38132;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38136;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38140;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:16106050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38172;
CC Evidence={ECO:0000305|PubMed:16106050};
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:0000269|PubMed:12621063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38020;
CC Evidence={ECO:0000305|PubMed:12621063};
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:0000269|PubMed:28420705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341;
CC Evidence={ECO:0000305|PubMed:28420705};
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:0000269|PubMed:18768481};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC Evidence={ECO:0000305|PubMed:18768481};
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:0000269|PubMed:28420705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55345;
CC Evidence={ECO:0000305|PubMed:28420705};
CC -!- ACTIVITY REGULATION: Inhibited by oleic acid and sphingosine, while it
CC is stimulated by phosphatidylcholine, phosphatidylserine and
CC phosphatidic acid. {ECO:0000250|UniProtKB:Q80W94}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45 uM for sn-1-monooleoylglycerol {ECO:0000269|PubMed:12621063};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000269|PubMed:27184406}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12621063, ECO:0000269|PubMed:27184406}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12621063}. Cytoplasm, perinuclear
CC region {ECO:0000269|PubMed:27184406}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3SYC2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3SYC2-2; Sequence=VSP_020358;
CC Name=3; Synonyms=MGAT2V, Trunc;
CC IsoId=Q3SYC2-3; Sequence=VSP_020359, VSP_020360;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, small intestine, colon,
CC stomach and kidney. {ECO:0000269|PubMed:12621063,
CC ECO:0000269|PubMed:12824082}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY157608; AAO23672.1; -; mRNA.
DR EMBL; AK026297; BAB15436.1; -; mRNA.
DR EMBL; AK128620; BAC87534.1; -; mRNA.
DR EMBL; AK291998; BAF84687.1; -; mRNA.
DR EMBL; CH471076; EAW74983.1; -; Genomic_DNA.
DR EMBL; BC103876; AAI03877.1; -; mRNA.
DR EMBL; BC103877; AAI03878.1; -; mRNA.
DR EMBL; BC103878; AAI03879.1; -; mRNA.
DR CCDS; CCDS8240.1; -. [Q3SYC2-1]
DR RefSeq; NP_079374.2; NM_025098.3. [Q3SYC2-1]
DR AlphaFoldDB; Q3SYC2; -.
DR BioGRID; 123154; 25.
DR IntAct; Q3SYC2; 1.
DR STRING; 9606.ENSP00000198801; -.
DR BindingDB; Q3SYC2; -.
DR ChEMBL; CHEMBL2439944; -.
DR SwissLipids; SLP:000000299; -.
DR iPTMnet; Q3SYC2; -.
DR PhosphoSitePlus; Q3SYC2; -.
DR BioMuta; MOGAT2; -.
DR DMDM; 114150036; -.
DR jPOST; Q3SYC2; -.
DR MassIVE; Q3SYC2; -.
DR PaxDb; Q3SYC2; -.
DR PeptideAtlas; Q3SYC2; -.
DR PRIDE; Q3SYC2; -.
DR ProteomicsDB; 61855; -. [Q3SYC2-1]
DR ProteomicsDB; 61856; -. [Q3SYC2-2]
DR ProteomicsDB; 61857; -. [Q3SYC2-3]
DR Antibodypedia; 31177; 155 antibodies from 28 providers.
DR DNASU; 80168; -.
DR Ensembl; ENST00000198801.10; ENSP00000198801.5; ENSG00000166391.15. [Q3SYC2-1]
DR Ensembl; ENST00000525093.5; ENSP00000436537.1; ENSG00000166391.15. [Q3SYC2-3]
DR Ensembl; ENST00000526712.1; ENSP00000436283.1; ENSG00000166391.15. [Q3SYC2-2]
DR GeneID; 80168; -.
DR KEGG; hsa:80168; -.
DR MANE-Select; ENST00000198801.10; ENSP00000198801.5; NM_025098.4; NP_079374.2.
DR UCSC; uc010rru.3; human. [Q3SYC2-1]
DR CTD; 80168; -.
DR DisGeNET; 80168; -.
DR GeneCards; MOGAT2; -.
DR HGNC; HGNC:23248; MOGAT2.
DR HPA; ENSG00000166391; Group enriched (intestine, liver).
DR MIM; 610270; gene.
DR neXtProt; NX_Q3SYC2; -.
DR OpenTargets; ENSG00000166391; -.
DR PharmGKB; PA134936582; -.
DR VEuPathDB; HostDB:ENSG00000166391; -.
DR eggNOG; KOG0831; Eukaryota.
DR GeneTree; ENSGT01030000234582; -.
DR HOGENOM; CLU_023995_0_1_1; -.
DR InParanoid; Q3SYC2; -.
DR OMA; PFYRDYI; -.
DR OrthoDB; 1347007at2759; -.
DR PhylomeDB; Q3SYC2; -.
DR TreeFam; TF314707; -.
DR BRENDA; 2.3.1.22; 2681.
DR PathwayCommons; Q3SYC2; -.
DR Reactome; R-HSA-75109; Triglyceride biosynthesis.
DR SABIO-RK; Q3SYC2; -.
DR SignaLink; Q3SYC2; -.
DR UniPathway; UPA00282; -.
DR BioGRID-ORCS; 80168; 4 hits in 1067 CRISPR screens.
DR ChiTaRS; MOGAT2; human.
DR GeneWiki; MOGAT2; -.
DR GenomeRNAi; 80168; -.
DR Pharos; Q3SYC2; Tchem.
DR PRO; PR:Q3SYC2; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q3SYC2; protein.
DR Bgee; ENSG00000166391; Expressed in ileal mucosa and 67 other tissues.
DR Genevisible; Q3SYC2; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; IBA:GO_Central.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0050892; P:intestinal absorption; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Cytoplasm; Endoplasmic reticulum;
KW Glycerol metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..334
FT /note="2-acylglycerol O-acyltransferase 2"
FT /id="PRO_0000249062"
FT TRANSMEM 23..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020358"
FT VAR_SEQ 218..284
FT /note="APLVPIFSFGENDLFDQIPNSSGSWLRYIQNRLQKIMGISLPLFHGRGVFQY
FT SFGLIPYRRPITTVV -> YQASGKSTLGSVGNWQGFYFGGKMAETNADSILVEIFSPF
FT TIKIIFWCLMPKYLEKFPQRRLSDLRN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020359"
FT VAR_SEQ 285..334
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020360"
FT VARIANT 9
FT /note="M -> V (in dbSNP:rs554202)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027390"
FT VARIANT 196
FT /note="P -> H (in dbSNP:rs34582952)"
FT /id="VAR_048857"
FT VARIANT 313
FT /note="C -> Y (in dbSNP:rs12281468)"
FT /id="VAR_027391"
FT CONFLICT 142
FT /note="L -> P (in Ref. 2; BAB15436)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="F -> L (in Ref. 2; BAC87534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 38196 MW; 57C4A964BAFA76BD CRC64;
MVEFAPLFMP WERRLQTLAV LQFVFSFLAL AEICTVGFIA LLFTRFWLLT VLYAAWWYLD
RDKPRQGGRH IQAIRCWTIW KYMKDYFPIS LVKTAELDPS RNYIAGFHPH GVLAVGAFAN
LCTESTGFSS IFPGIRPHLM MLTLWFRAPF FRDYIMSAGL VTSEKESAAH ILNRKGGGNL
LGIIVGGAQE ALDARPGSFT LLLRNRKGFV RLALTHGAPL VPIFSFGEND LFDQIPNSSG
SWLRYIQNRL QKIMGISLPL FHGRGVFQYS FGLIPYRRPI TTVVGKPIEV QKTLHPSEEE
VNQLHQRYIK ELCNLFEAHK LKFNIPADQH LEFC
