DGAT1_CHLAE
ID DGAT1_CHLAE Reviewed; 491 AA.
AC Q9GMF1;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Diacylglycerol O-acyltransferase 1 {ECO:0000305};
DE EC=2.3.1.20 {ECO:0000250|UniProtKB:Q9Z2A7};
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:Q9Z2A7};
DE AltName: Full=Diglyceride acyltransferase;
GN Name=DGAT1; Synonyms=DGAT;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Joyce C.W., Davis M.A., Anderson R.A., Rudel L.L.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the terminal and only committed step in
CC triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as
CC substrates. Highly expressed in epithelial cells of the small intestine
CC and its activity is essential for the absorption of dietary fats. In
CC liver, plays a role in esterifying exogenous fatty acids to glycerol,
CC and is required to synthesize fat for storage (By similarity). Also
CC present in female mammary glands, where it produces fat in the milk (By
CC similarity). May be involved in VLDL (very low density lipoprotein)
CC assembly (By similarity). In contrast to DGAT2 it is not essential for
CC survival (By similarity). Functions as the major acyl-CoA retinol
CC acyltransferase (ARAT) in the skin, where it acts to maintain retinoid
CC homeostasis and prevent retinoid toxicity leading to skin and hair
CC disorders (By similarity). Exhibits additional acyltransferase
CC activities, includin acyl CoA:monoacylglycerol acyltransferase (MGAT),
CC wax monoester and wax diester synthases (By similarity). Also able to
CC use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis
CC of monoalkyl-monoacylglycerol (MAMAG) (By similarity).
CC {ECO:0000250|UniProtKB:O75907, ECO:0000250|UniProtKB:Q8MK44,
CC ECO:0000250|UniProtKB:Q9Z2A7}.
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 -!- SUBUNIT: Homodimer or homotetramer; both forms have similar enzymatic
CC activities. {ECO:0000250|UniProtKB:O75907}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Z2A7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Z2A7}.
CC -!- DOMAIN: The disordered N-terminal region is required for the
CC diacylglycerol O-acyltransferase activity and may regulate enzymatic
CC function via its interaction with the MBOAT fold.
CC {ECO:0000250|UniProtKB:O75907}.
CC -!- DOMAIN: The MBOAT fold forms a reaction chamber in the endoplasmic
CC reticulum membrane that encloses the active sites. The reaction chamber
CC has a tunnel to the cytosolic side and its entrance recognizes the
CC hydrophilic CoA motif of an acyl-CoA molecule. The chamber has separate
CC entrances for each of the two substrates, acyl-CoA and 1,2-diacyl-sn-
CC glycerol. {ECO:0000250|UniProtKB:O75907}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR EMBL; AF236018; AAF98557.1; -; mRNA.
DR AlphaFoldDB; Q9GMF1; -.
DR SMR; Q9GMF1; -.
DR UniPathway; UPA00230; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0050252; F:retinol O-fatty-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046339; P:diacylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR027251; Diacylglycerol_acylTrfase1.
DR InterPro; IPR004299; MBOAT_fam.
DR InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR PANTHER; PTHR10408; PTHR10408; 1.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
DR PIRSF; PIRSF500231; Oat_dag; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Phosphoprotein; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..491
FT /note="Diacylglycerol O-acyltransferase 1"
FT /id="PRO_0000207653"
FT TOPO_DOM 1..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 87..121
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 122..133
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 134..159
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 160..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 165..187
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 188..194
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 195..226
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 227..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 277..311
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 312..318
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 319..356
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 357..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 403..423
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 424..431
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 432..450
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 451..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 453..484
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 485..491
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..94
FT /note="Involved in homomerization"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2A7"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 122..133
FT /note="Extracellular loop 1 (EL1)"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 134..491
FT /note="MBOAT fold"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 227..279
FT /note="Intracellular loop 1 (IL1)"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 357..402
FT /note="Intracellular loop 2 (IL2)"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 383..397
FT /note="Amphipathic helix (AH)"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT MOTIF 363..369
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT ACT_SITE 418
FT /evidence="ECO:0000250|UniProtKB:Q9Z2A7"
FT BINDING 377..385
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT BINDING 393
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT BINDING 407
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT BINDING 480
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT SITE 419
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75907"
SQ SEQUENCE 491 AA; 55644 MW; BFD3683453D588DB CRC64;
MGDRGGAGGT RRRRTGSRPS SHGGGGPAAA EEEVRDAAAG PDMGAAGDAP APAPSKDADD
GVASGHWELR CHRLQDSLFS SDSGFNNYRG ILNWCVVMLI LSNARLFLEN LIKYGILVDP
IQVVSLFLKD PYSWPAPCLV IAANVFAVAA FQVEKRLAVG ALTEQAGLLL HVANLATILC
FPAAVVLLVE SITPVGSLLA LMVHTILFLK LFSYRDVNLW CRRARAKAAS AGKRASSAAA
PHTVSYPDNL TYRDLYYFLF APTLCYELNF PRSPRIRKRF LLRRILEMLF FTQLQVGLIQ
QWMVPTIQNS MKPFKDMDYS RIIERLLKLA VPNHLIWLIF FYWLFHSCLN AVAELMQFGD
REFYRDWWNS ESVTYFWQNW NIPVHKWCIR HFYKPMLRRG SSRWMARIGV FLASAFFHEY
LVSVPLRMFR LWAFTGMMAQ IPLAWFVGRF FQGNYGNAAV WLTLIIGQPI AVLMYVHDYY
VLNYEAPVAG A
