DGAT2_BOVIN
ID DGAT2_BOVIN Reviewed; 361 AA.
AC Q70VZ8; A5D9B3; Q6B852; Q6PP93; Q6PP94; Q6PP95; Q6PP96;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Diacylglycerol O-acyltransferase 2 {ECO:0000305};
DE EC=2.3.1.20 {ECO:0000250|UniProtKB:Q96PD7};
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:Q96PD7};
DE AltName: Full=Diglyceride acyltransferase 2;
GN Name=DGAT2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=14970677; DOI=10.1159/000075723;
RA Winter A., van Eckeveld M., Bininda-Emonds O.R.P., Habermann F.A.,
RA Fries R.;
RT "Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus)
RT and other mammals.";
RL Cytogenet. Genome Res. 102:42-47(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-111; 156-205 AND 231-352, AND
RP NUCLEOTIDE SEQUENCE [MRNA] OF 93-361.
RA Xu X.R., Xu S.Z., Li J.Y.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential acyltransferase that catalyzes the terminal and
CC only committed step in triacylglycerol synthesis by using
CC diacylglycerol and fatty acyl CoA as substrates. Required for synthesis
CC and storage of intracellular triglycerides (By similarity). Probably
CC plays a central role in cytosolic lipid accumulation. In liver, is
CC primarily responsible for incorporating endogenously synthesized fatty
CC acids into triglycerides (By similarity). Functions also as an acyl-CoA
CC retinol acyltransferase (ARAT) (By similarity). Also able to use 1-
CC monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of
CC monoalkyl-monoacylglycerol (MAMAG) (By similarity).
CC {ECO:0000250|UniProtKB:Q96PD7, ECO:0000250|UniProtKB:Q9DCV3}.
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:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
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:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
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:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
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:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
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:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
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:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
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:Q96PD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916;
CC Evidence={ECO:0000250|UniProtKB:Q96PD7};
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:Q9DCV3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38164;
CC Evidence={ECO:0000250|UniProtKB:Q9DCV3};
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:Q9DCV3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38436;
CC Evidence={ECO:0000250|UniProtKB:Q9DCV3};
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:Q9DCV3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38440;
CC Evidence={ECO:0000250|UniProtKB:Q9DCV3};
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:Q9DCV3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072;
CC Evidence={ECO:0000250|UniProtKB:Q9DCV3};
CC -!- ACTIVITY REGULATION: Inhibited by niacin. {ECO:0000250}.
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC -!- SUBUNIT: Forms multimeric complexes consisting of several DGAT2
CC subunits (By similarity). Interacts with SLC27A1 and this interaction
CC is enhanced in the presence of ZFYVE1 (By similarity).
CC {ECO:0000250|UniProtKB:Q96PD7, ECO:0000250|UniProtKB:Q9DCV3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q96PD7}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AJ519787; CAD58592.1; -; mRNA.
DR EMBL; AJ534368; CAD58968.1; -; Genomic_DNA.
DR EMBL; AJ534369; CAD58968.1; JOINED; Genomic_DNA.
DR EMBL; AJ534370; CAD58968.1; JOINED; Genomic_DNA.
DR EMBL; AJ534371; CAD58968.1; JOINED; Genomic_DNA.
DR EMBL; AJ534372; CAD58968.1; JOINED; Genomic_DNA.
DR EMBL; BT030532; ABQ12972.1; -; mRNA.
DR EMBL; AY589091; AAT02657.1; -; Genomic_DNA.
DR EMBL; AY589092; AAT02658.1; -; Genomic_DNA.
DR EMBL; AY589093; AAT02659.1; -; Genomic_DNA.
DR EMBL; AY589094; AAT02660.1; -; Genomic_DNA.
DR EMBL; AY675174; AAT78344.1; -; mRNA.
DR RefSeq; NP_991362.2; NM_205793.2.
DR AlphaFoldDB; Q70VZ8; -.
DR STRING; 9913.ENSBTAP00000001536; -.
DR PaxDb; Q70VZ8; -.
DR GeneID; 404129; -.
DR KEGG; bta:404129; -.
DR CTD; 84649; -.
DR eggNOG; KOG0831; Eukaryota.
DR HOGENOM; CLU_023995_0_0_1; -.
DR InParanoid; Q70VZ8; -.
DR OrthoDB; 1347007at2759; -.
DR TreeFam; TF314707; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:AgBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:AgBase.
DR GO; GO:0016021; C:integral component of membrane; ISS:AgBase.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:AgBase.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:AgBase.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; ISS:AgBase.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:AgBase.
DR GO; GO:0050252; F:retinol O-fatty-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0071400; P:cellular response to oleic acid; ISS:AgBase.
DR GO; GO:0035356; P:cellular triglyceride homeostasis; ISS:AgBase.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:AgBase.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046339; P:diacylglycerol metabolic process; ISS:AgBase.
DR GO; GO:0060613; P:fat pad development; ISS:AgBase.
DR GO; GO:0055089; P:fatty acid homeostasis; ISS:AgBase.
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:0019915; P:lipid storage; ISS:AgBase.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; ISS:AgBase.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; ISS:AgBase.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; ISS:AgBase.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISS:AgBase.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Endoplasmic reticulum; Glycerol metabolism;
KW Lipid biosynthesis; Lipid droplet; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..361
FT /note="Diacylglycerol O-acyltransferase 2"
FT /id="PRO_0000249044"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..65
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 35
FT /note="A -> S (in Ref. 2; ABQ12972)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="L -> P (in Ref. 3; AAT02660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 40896 MW; C84BA6DF0242675A CRC64;
MKTLIAAYSG VLRGTGSSIL SALQDLFSVT WLNRAKVEKQ LQVISVLQWV LSFLVLGVAC
SVILMYTFCT DCWLIAVLYF TWLVFDWNTP KKGGRRSQWV RNWAVWRYFR DYFPIQLVKT
HNLLTSRNYI FGYHPHGIMG LGAFCNFSTE ATEVSKKFPG IRPYLATLAG NFRMPVLREY
LMSGGICPVN RDTIDYLLSK NGSGNAIIIV VGGAAESLSS MPGKNAVTLR NRKGFVKLAL
RHGADLVPTY SFGENEVYKQ VIFEEGSWGR WVQKKFQKYI GFAPCIFHGR GLFSSDTWGL
VPYSKPITTV VGEPITIPRL ERPTQQDIDL YHAMYVQALV KLFDQHKTKF GLPETEVLEV
N
