DGAT2_XENTR
ID DGAT2_XENTR Reviewed; 361 AA.
AC Q6P342;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 {ECO:0000250|UniProtKB:Q96PD7};
DE Short=ARAT {ECO:0000250|UniProtKB:Q96PD7};
DE Short=Retinol O-fatty-acyltransferase {ECO:0000250|UniProtKB:Q96PD7};
DE EC=2.3.1.76 {ECO:0000250|UniProtKB:Q96PD7};
DE AltName: Full=Diglyceride acyltransferase 2;
GN Name=dgat2; ORFNames=TEgg014n15.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) 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. Probably plays a central
CC role in cytosolic lipid accumulation (By similarity).
CC {ECO:0000250|UniProtKB:Q96PD7}.
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 -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
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}.
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; CR855594; CAJ81957.1; -; mRNA.
DR EMBL; BC064191; AAH64191.1; -; mRNA.
DR RefSeq; NP_989372.1; NM_204041.2.
DR AlphaFoldDB; Q6P342; -.
DR PaxDb; Q6P342; -.
DR DNASU; 395003; -.
DR GeneID; 395003; -.
DR KEGG; xtr:395003; -.
DR CTD; 84649; -.
DR Xenbase; XB-GENE-1017054; dgat2.
DR eggNOG; KOG0831; Eukaryota.
DR HOGENOM; CLU_023995_0_0_1; -.
DR InParanoid; Q6P342; -.
DR OMA; NDPKHAG; -.
DR OrthoDB; 1347007at2759; -.
DR PhylomeDB; Q6P342; -.
DR TreeFam; TF314707; -.
DR Reactome; R-XTR-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-XTR-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000025317; Expressed in egg cell and 17 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum 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:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IBA:GO_Central.
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:0006640; P:monoacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISS:UniProtKB.
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_0000249050"
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"
SQ SEQUENCE 361 AA; 40492 MW; AA7D809B1F9554A8 CRC64;
MKTIIAAYSG VLRGTGSSLL SAVHDLPNIP WLSKSSVVRH LQIISVLQWV LSFLILGVAC
TAVLVYIFCT DLWLIAALYL TWMVLDWNTP YKGGRRSSWV RNWAVWRYFR DYFPIKLVKT
HNLLPSRNYI FGYHPHGIMC LGAFCNFGTE ATGVSKKFPG IKCHLATLAG NFRMPVLREY
LMSGGICPVA RDTIDYILSK NGTGNAVVIA VGGAAESLNC RPGKNTVTLK QRKGFVKVAL
QHGADLVPVY SFGENEAYKQ VVFEEGSWGR WIQKKFQKYV GFAPCLFHGC SFFSSNSWGL
VPYANPITTV VGEPITVPKI EQPTQKDVEL YHAMYVTSLQ RLFDKYKTKL GLHDSEMLEI
V
