MOGT1_MOUSE
ID MOGT1_MOUSE Reviewed; 335 AA.
AC Q91ZV4; E9QLA2; Q9DCL0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=2-acylglycerol O-acyltransferase 1 {ECO:0000305};
DE EC=2.3.1.22 {ECO:0000269|PubMed:12077311};
DE AltName: Full=Acyl-CoA:monoacylglycerol acyltransferase 1;
DE Short=MGAT1;
DE AltName: Full=Diacylglycerol acyltransferase 2-like protein 1;
DE AltName: Full=Monoacylglycerol O-acyltransferase 1;
GN Name=Mogat1 {ECO:0000312|MGI:MGI:1915643}; Synonyms=Dgat2l1;
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].
RC TISSUE=Liver;
RX PubMed=11481335; DOI=10.1074/jbc.m106219200;
RA Cases S., Stone S.J., Zhou P., Yen C.-L.E., Tow B., Lardizabal K.D.,
RA Voelker T., Farese R.V. Jr.;
RT "Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and
RT related family members.";
RL J. Biol. Chem. 276:38870-38876(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12077311; DOI=10.1073/pnas.132274899;
RA Yen C.-L.E., Stone S.J., Cases S., Zhou P., Farese R.V. Jr.;
RT "Identification of a gene encoding MGAT1, a monoacylglycerol
RT acyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8512-8517(2002).
RN [6]
RP FUNCTION, TISSUE 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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the formation of diacylglycerol from 2-
CC monoacylglycerol and fatty acyl-CoA. Probably not involved in
CC absorption of dietary fat in the small intestine.
CC {ECO:0000269|PubMed:12077311, ECO:0000269|PubMed:12621063}.
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:12077311};
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 -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:12077311}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:12077311}.
CC -!- TISSUE SPECIFICITY: Expressed at high level in kidney and stomach.
CC Expressed at lower level in brown and white adipose tissue, uterus and
CC liver. Not detected in small intestine. {ECO:0000269|PubMed:12077311}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF384162; AAK84177.1; -; mRNA.
DR EMBL; AK002693; BAB22288.1; -; mRNA.
DR EMBL; AC158559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106135; AAI06136.1; -; mRNA.
DR CCDS; CCDS15085.1; -.
DR RefSeq; NP_080989.2; NM_026713.3.
DR RefSeq; XP_017177770.1; XM_017322281.1.
DR AlphaFoldDB; Q91ZV4; -.
DR STRING; 10090.ENSMUSP00000109152; -.
DR SwissLipids; SLP:000000300; -.
DR GlyGen; Q91ZV4; 1 site.
DR iPTMnet; Q91ZV4; -.
DR PhosphoSitePlus; Q91ZV4; -.
DR jPOST; Q91ZV4; -.
DR MaxQB; Q91ZV4; -.
DR PaxDb; Q91ZV4; -.
DR PRIDE; Q91ZV4; -.
DR ProteomicsDB; 295579; -.
DR Antibodypedia; 34362; 112 antibodies from 21 providers.
DR DNASU; 68393; -.
DR Ensembl; ENSMUST00000012331; ENSMUSP00000012331; ENSMUSG00000012187.
DR Ensembl; ENSMUST00000113524; ENSMUSP00000109152; ENSMUSG00000012187.
DR GeneID; 68393; -.
DR KEGG; mmu:68393; -.
DR UCSC; uc007bqk.1; mouse.
DR CTD; 116255; -.
DR MGI; MGI:1915643; Mogat1.
DR VEuPathDB; HostDB:ENSMUSG00000012187; -.
DR eggNOG; KOG0831; Eukaryota.
DR GeneTree; ENSGT01030000234582; -.
DR HOGENOM; CLU_023995_0_1_1; -.
DR InParanoid; Q91ZV4; -.
DR OMA; ISMAAFI; -.
DR OrthoDB; 1347007at2759; -.
DR PhylomeDB; Q91ZV4; -.
DR TreeFam; TF314707; -.
DR BRENDA; 2.3.1.22; 3474.
DR Reactome; R-MMU-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00282; -.
DR BioGRID-ORCS; 68393; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Mogat1; mouse.
DR PRO; PR:Q91ZV4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91ZV4; protein.
DR Bgee; ENSMUSG00000012187; Expressed in epithelium of stomach and 81 other tissues.
DR ExpressionAtlas; Q91ZV4; baseline and differential.
DR Genevisible; Q91ZV4; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; IDA:MGI.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase 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:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Glycerol metabolism; Glycoprotein;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..335
FT /note="2-acylglycerol O-acyltransferase 1"
FT /id="PRO_0000249059"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 85..86
FT /note="KE -> FL (in Ref. 2; BAB22288)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="T -> I (in Ref. 1; AAK84177 and 4; AAI06136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 38791 MW; A2691D9E6451AD30 CRC64;
MMVEFAPLNT PLARCLQTAA VLQWVLSFLL LVQVCIGIMV MLVLYNYWFL YIPYLVWFYY
DWRTPEQGGR RWNWVQSWPV WKYFKEYFPI CLVKTQDLDP GHNYIFGFHP HGIFVPGAFG
NFCTKYSDFK KLFPGFTSYL HVAKIWFCFP LFREYLMSNG PVSVSKESLS HVLSKDGGGN
VSIIVLGGAK EALEAHPGTF TLCIRQRKGF VKMALTHGAS LVPVFSFGEN DLYKQINNPK
GSWLRTIQDA MYDSMGVALP LIYARGIFQH YFGIMPYRKL IYTVVGRPIP VQQTLNPTSE
QIEELHQTYL EELKKLFNEH KGKYGIPEHE TLVFK
