DGAT1_BOVIN
ID DGAT1_BOVIN Reviewed; 489 AA.
AC Q8MK44; Q148M3; Q8SQB0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Diacylglycerol O-acyltransferase 1 {ECO:0000305};
DE EC=2.3.1.20 {ECO:0000269|PubMed:18704537};
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};
DE AltName: Full=Diglyceride acyltransferase;
GN Name=DGAT1;
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], POLYMORPHISM, AND VARIANT ALA-232.
RX PubMed=11827942; DOI=10.1101/gr.224202;
RA Grisart B., Coppieters W., Farnir F., Karim L., Ford C., Berzi P.,
RA Cambisano N., Mni M., Reid S., Simon P., Spelman R., Georges M., Snell R.;
RT "Positional candidate cloning of a QTL in dairy cattle: identification of a
RT missense mutation in the bovine DGAT1 gene with major effect on milk yield
RT and composition.";
RL Genome Res. 12:222-231(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, AND VARIANT ALA-232.
RX PubMed=12077321; DOI=10.1073/pnas.142293799;
RA Winter A., Kramer W., Werner F.A.O., Kollers S., Kata S., Durstewitz G.,
RA Buitkamp J., Womack J.E., Thaller G., Fries R.;
RT "Association of a lysine-232/alanine polymorphism in a bovine gene encoding
RT acyl-CoA:diacylglycerol acyltransferase (DGAT1) with variation at a
RT quantitative trait locus for milk fat content.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9300-9305(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, POLYMORPHISM, AND VARIANT ALA-232.
RX PubMed=18704537; DOI=10.1007/s11745-008-3216-z;
RA Soerensen B.M., Chris Kazala E., Murdoch G.K., Keating A.F.,
RA Cruz-Hernandez C., Wegner J., Kennelly J.J., Okine E.K., Weselake R.J.;
RT "Effect of CLA and other C18 unsaturated fatty acids on DGAT in bovine milk
RT fat biosynthetic systems.";
RL Lipids 43:903-912(2008).
RN [5]
RP FUNCTION, POLYMORPHISM, AND VARIANT ALA-232.
RX PubMed=15342525; DOI=10.1534/genetics.103.022749;
RA Kuehn C., Thaller G., Winter A., Bininda-Emonds O.R., Kaupe B., Erhardt G.,
RA Bennewitz J., Schwerin M., Fries R.;
RT "Evidence for multiple alleles at the DGAT1 locus better explains a
RT quantitative trait locus with major effect on milk fat content in cattle.";
RL Genetics 167:1873-1881(2004).
CC -!- FUNCTION: Catalyzes the terminal and only committed step in
CC triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as
CC substrates (PubMed:18704537). Highly expressed in epithelial cells of
CC the small intestine and its activity is essential for the absorption of
CC dietary fats. In liver, plays a role in esterifying exogenous fatty
CC acids to glycerol, and is required to synthesize fat for storage (By
CC similarity). Also present in female mammary glands, where it produces
CC fat in the milk (PubMed:18704537, PubMed:15342525). May be involved in
CC VLDL (very low density lipoprotein) assembly (By similarity). In
CC contrast to DGAT2 it is not essential for survival (By similarity).
CC Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the
CC skin, where it acts to maintain retinoid homeostasis and prevent
CC retinoid toxicity leading to skin and hair disorders (By similarity).
CC Exhibits additional acyltransferase activities, includin acyl
CC CoA:monoacylglycerol acyltransferase (MGAT), wax monoester and wax
CC diester synthases (By similarity). Also able to use 1-monoalkylglycerol
CC (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-
CC monoacylglycerol (MAMAG) (By similarity).
CC {ECO:0000250|UniProtKB:O75907, ECO:0000250|UniProtKB:Q9Z2A7,
CC ECO:0000269|PubMed:15342525, ECO:0000269|PubMed:18704537}.
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:0000269|PubMed:18704537};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869;
CC Evidence={ECO:0000269|PubMed:18704537};
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176;
CC Evidence={ECO:0000250|UniProtKB:O75907};
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:O75907}.
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 -!- POLYMORPHISM: Lys-232 is associated with higher milk fat content.
CC {ECO:0000269|PubMed:11827942, ECO:0000269|PubMed:12077321,
CC ECO:0000269|PubMed:15342525, ECO:0000269|PubMed:18704537}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR EMBL; AY065621; AAL49962.1; -; Genomic_DNA.
DR EMBL; AJ318490; CAC86391.1; -; Genomic_DNA.
DR EMBL; BC118146; AAI18147.1; -; mRNA.
DR RefSeq; NP_777118.2; NM_174693.2.
DR AlphaFoldDB; Q8MK44; -.
DR SMR; Q8MK44; -.
DR STRING; 9913.ENSBTAP00000037256; -.
DR ChEMBL; CHEMBL4523395; -.
DR PaxDb; Q8MK44; -.
DR PRIDE; Q8MK44; -.
DR GeneID; 282609; -.
DR KEGG; bta:282609; -.
DR CTD; 8694; -.
DR eggNOG; KOG0380; Eukaryota.
DR InParanoid; Q8MK44; -.
DR OrthoDB; 1275897at2759; -.
DR BRENDA; 2.3.1.20; 908.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:AgBase.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..489
FT /note="Diacylglycerol O-acyltransferase 1"
FT /id="PRO_0000244770"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 81..115
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 116..127
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 128..153
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 154..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..181
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 182..188
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 189..220
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 221..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 275..309
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 310..316
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 317..354
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 355..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 401..421
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 422..429
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 430..448
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 449..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 451..482
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT TOPO_DOM 483..489
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..88
FT /note="Involved in homomerization"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2A7"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 116..127
FT /note="Extracellular loop 1 (EL1)"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 128..489
FT /note="MBOAT fold"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 225..277
FT /note="Intracellular loop 1 (IL1)"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 355..400
FT /note="Intracellular loop 2 (IL2)"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT REGION 381..395
FT /note="Amphipathic helix (AH)"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT MOTIF 361..367
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT COMPBIAS 35..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 416
FT /evidence="ECO:0000250|UniProtKB:Q9Z2A7"
FT BINDING 375..383
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT BINDING 391
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT BINDING 405
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT BINDING 478
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT SITE 417
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 VARIANT 232
FT /note="K -> A"
FT /evidence="ECO:0000269|PubMed:11827942,
FT ECO:0000269|PubMed:12077321, ECO:0000269|PubMed:15342525,
FT ECO:0000269|PubMed:18704537"
FT CONFLICT 425
FT /note="R -> G (in Ref. 2; CAC86391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 55602 MW; 4066D8C1B6743253 CRC64;
MGDRGGAGGS RRRRTGSRPS IQGGSGPAAA EEEVRDVGAG GDAPVRDTDK DGDVDVGSGH
WDLRCHRLQD SLFSSDSGFS NYRGILNWCV VMLILSNARL FLENLIKYGI LVDPIQVVSL
FLKDPYSWPA LCLVIVANIF AVAAFQVEKR LAVGALTEQA GLLLHGVNLA TILCFPAAVA
FLLESITPVG SVLALMVYTI LFLKLFSYRD VNLWCRERRA GAKAKAALAG KKANGGAAQR
TVSYPDNLTY RDLYYFLFAP TLCYELNFPR SPRIRKRFLL RRLLEMLFLT QLQVGLIQQW
MVPAIQNSMK PFKDMDYSRI VERLLKLAVP NHLIWLIFFY WLFHSCLNAV AELMQFGDRE
FYRDWWNSES ITYFWQNWNI PVHKWCIRHF YKPMLRRGSS KWAARTAVFL ASAFFHEYLV
SIPLRMFRLW AFTGMMAQIP LAWIVGRFFR GNYGNAAVWL SLIIGQPVAV LMYVHDYYVL
NREAPAAGT
