ID DGAT1_DICDI Reviewed; 617 AA. AC Q55BH9; DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 2. DT 03-MAY-2023, entry version 99. DE RecName: Full=Diacylglycerol O-acyltransferase 1 {ECO:0000305}; DE EC=2.3.1.20 {ECO:0000250|UniProtKB:O75907}; DE AltName: Full=Acyl-CoA retinol O-fatty-acyltransferase; DE Short=ARAT; DE Short=Retinol O-fatty-acyltransferase; DE EC=2.3.1.76 {ECO:0000250|UniProtKB:O75907}; GN Name=dgat1; ORFNames=DDB_G0271342; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=12097910; DOI=10.1038/nature00847; RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., RA Noegel A.A.; RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum."; RL Nature 418:79-85(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). CC -!- FUNCTION: Catalyzes the terminal and only committed step in CC triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as CC substrates. {ECO:0000250|UniProtKB:O75907}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol CC + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; CC Evidence={ECO:0000250|UniProtKB:O75907}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869; CC Evidence={ECO:0000250|UniProtKB:O75907}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester + CC CoA; Xref=Rhea:RHEA:11488, ChEBI:CHEBI:17336, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:58342, ChEBI:CHEBI:63410; EC=2.3.1.76; CC Evidence={ECO:0000250|UniProtKB:O75907}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489; CC Evidence={ECO:0000250|UniProtKB:O75907}; 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:O75907}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912; CC Evidence={ECO:0000250|UniProtKB:O75907}; 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:O75907}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220; CC Evidence={ECO:0000250|UniProtKB:O75907}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl CC hexadecanoate + CoA; Xref=Rhea:RHEA:38175, ChEBI:CHEBI:17336, CC ChEBI:CHEBI:17616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; CC Evidence={ECO:0000250|UniProtKB:O75907, CC ECO:0000250|UniProtKB:Q9Z2A7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176; CC Evidence={ECO:0000250|UniProtKB:O75907, CC ECO:0000250|UniProtKB:Q9Z2A7}; 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:O75907}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341; CC Evidence={ECO:0000250|UniProtKB:O75907}; 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:O75907}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55345; CC Evidence={ECO:0000250|UniProtKB:O75907}; 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:O75907}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916; CC Evidence={ECO:0000250|UniProtKB:O75907}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H(+) CC = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O; Xref=Rhea:RHEA:38379, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:52323, ChEBI:CHEBI:53753; CC Evidence={ECO:0000250|UniProtKB:O75907}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38380; CC Evidence={ECO:0000250|UniProtKB:O75907}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-2-(5Z,8Z,11Z,14Z- CC eicosatetraenoyl)-sn-glycerol = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)- CC eicosatetraenoyl-3-(9Z)-octadecenoyl-sn-glycerol + CoA; CC Xref=Rhea:RHEA:38307, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, CC ChEBI:CHEBI:75728, ChEBI:CHEBI:75729; CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38308; CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexadecane-1,2-diol + 2 hexadecanoyl-CoA = 1,2-O,O- CC dihexadecanoyl-1,2-hexadecanediol + 2 CoA; Xref=Rhea:RHEA:38211, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75586, CC ChEBI:CHEBI:75608; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38212; CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; 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:Q9Z2A7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38172; CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; 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:Q9Z2A7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072; CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2- CC di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoA; CC Xref=Rhea:RHEA:38163, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57379, ChEBI:CHEBI:75583; CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38164; CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl CC hexadecanoate; Xref=Rhea:RHEA:38167, ChEBI:CHEBI:16125, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75584; CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38168; CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=13-cis-retinol + hexadecanoyl-CoA = 13-cis-retinyl CC hexadecanoate + CoA; Xref=Rhea:RHEA:55296, ChEBI:CHEBI:45479, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:138722; CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55297; CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-octadecenoyl-CoA + 1,3-di-(9Z-octadecenoyl)-glycerol = CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38435, CC ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, CC ChEBI:CHEBI:75735; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38436; CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-octadecenoyl-CoA + 2,3-di-(9Z)-octadecenoyl-sn-glycerol = CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38439, CC ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, CC ChEBI:CHEBI:75824; Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38440; CC Evidence={ECO:0000250|UniProtKB:Q9Z2A7}; CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q9Z2A7}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:O75907}. CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family. CC Sterol o-acyltransferase subfamily. {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; AAFI02000006; EAL71801.2; -; Genomic_DNA. DR RefSeq; XP_645633.2; XM_640541.2. DR AlphaFoldDB; Q55BH9; -. DR SMR; Q55BH9; -. DR STRING; 44689.DDB0304727; -. DR PaxDb; Q55BH9; -. DR EnsemblProtists; EAL71801; EAL71801; DDB_G0271342. DR GeneID; 8617825; -. DR KEGG; ddi:DDB_G0271342; -. DR dictyBase; DDB_G0271342; dgat1. DR eggNOG; KOG0380; Eukaryota. DR HOGENOM; CLU_018190_0_0_1; -. DR InParanoid; Q55BH9; -. DR OMA; WAFMGIM; -. DR PhylomeDB; Q55BH9; -. DR Reactome; R-DDI-1482883; Acyl chain remodeling of DAG and TAG. DR Reactome; R-DDI-6798695; Neutrophil degranulation. DR Reactome; R-DDI-75109; Triglyceride biosynthesis. DR UniPathway; UPA00230; -. DR PRO; PR:Q55BH9; -. DR Proteomes; UP000002195; Chromosome 2. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:dictyBase. DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:dictyBase. DR GO; GO:0050252; F:retinol O-fatty-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008611; P:ether lipid biosynthetic process; IDA:dictyBase. DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW. DR GO; GO:0140042; P:lipid droplet formation; IMP:dictyBase. DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; ISS:UniProtKB. DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:dictyBase. DR InterPro; IPR004299; MBOAT_fam. DR InterPro; IPR014371; Oat_ACAT_DAG_ARE. DR PANTHER; PTHR10408:SF7; DIACYLGLYCEROL O-ACYLTRANSFERASE 1; 1. DR PANTHER; PTHR10408; STEROL O-ACYLTRANSFERASE; 1. DR Pfam; PF03062; MBOAT; 1. DR PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1. PE 3: Inferred from homology; KW Acyltransferase; Endoplasmic reticulum; Glycerol metabolism; KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..617 FT /note="Diacylglycerol O-acyltransferase 1" FT /id="PRO_0000377488" FT TRANSMEM 217..237 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 254..274 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 306..326 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 399..419 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 449..469 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 520..540 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 545..565 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 570..590 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 95..186 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 477..483 FT /note="FYXDWWN motif" FT /evidence="ECO:0000250|UniProtKB:O75907" FT COMPBIAS 1..38 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 95..146 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 161..186 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 532 FT /evidence="ECO:0000250|UniProtKB:O75907" SQ SEQUENCE 617 AA; 71946 MW; DCD8FD193A3023D7 CRC64; MEPIPPSNGN KNNSMDKQPQ QPQQPQQQQQ QQQQQRRDQR NSKLNELNET ERVRNRFISH EFHKLDRTKS RIDAPKISFS DSESESDSEF FLAKRNTNNN NQNNTSPTFS SANGKQSNLT QRKINTQIQS KQPTNNNVQP LTDDEGTINH SNHHHHHHNQ NNNGNNNNNN NNNNNNNKIS TPPKQEEKMT MNGLFTLRPS ILSSESNGSS YRGFLNLLLI LLITASFRLV ILNHLLYGIR INLDLYKISE YHRWPGVMIS LMINLFIIAA YLIEKAAAKQ LLPDRICYLL RIINCAAVII VPSGSIIAFS PNPASGIIVM ILICTFSMKI ISYAYENSKQ RKLNPDNKKF VIDPTNTSIY PNNLSLRSTY WFMLVPTLVY QLSYPRSPKI RKGYLLRRIV EALSLSLLIL WMVNQYMLPL VQNSIEPLEK IDIVLIVERI MKLSLPNLYV WLLGFYVFFH LYLNIVAEIT RFGDREFYRD WWNSTGLDYF WRTWNMPVHH WMVVLIYTPM RRRGFSKNMG YFMCFFVSAI FHELVISIPF HSLKLWGFFG IMSQMVLIAL TKNLMNGRNL GNVIFWISIV LGQPLVVLLY YRNFVLENPE WYRNVEPPTS PPVMPFY //