MOGT3_HUMAN
ID MOGT3_HUMAN Reviewed; 341 AA.
AC Q86VF5; Q496A6; Q496A7; Q496A8; Q9UDW7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=2-acylglycerol O-acyltransferase 3 {ECO:0000305};
DE EC=2.3.1.20 {ECO:0000269|PubMed:27184406};
DE EC=2.3.1.22 {ECO:0000269|PubMed:27184406};
DE AltName: Full=Acyl-CoA:monoacylglycerol acyltransferase 3 {ECO:0000303|PubMed:27184406};
DE Short=MGAT3 {ECO:0000303|PubMed:27184406};
DE AltName: Full=Diacylglycerol O-acyltransferase candidate 7;
DE Short=hDC7;
DE AltName: Full=Diacylglycerol acyltransferase 2-like protein 7;
DE AltName: Full=Monoacylglycerol O-acyltransferase 3;
GN Name=MOGAT3 {ECO:0000312|HGNC:HGNC:23249}; Synonyms=DC7, DGAT2L7;
GN ORFNames=UNQ9383/PRO34208;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12618427; DOI=10.1074/jbc.c300042200;
RA Cheng D., Nelson T.C., Chen J., Walker S.G., Wardwell-Swanson J.,
RA Meegalla R., Taub R., Billheimer J.T., Ramaker M., Feder J.N.;
RT "Identification of acyl coenzyme A:monoacylglycerol acyltransferase 3, an
RT intestinal specific enzyme implicated in dietary fat absorption.";
RL J. Biol. Chem. 278:13611-13614(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP CATALYTIC ACTIVITY.
RX PubMed=16214399; DOI=10.1016/j.bbalip.2005.09.003;
RA Orland M.D., Anwar K., Cromley D., Chu C.H., Chen L., Billheimer J.T.,
RA Hussain M.M., Cheng D.;
RT "Acyl coenzyme A dependent retinol esterification by acyl coenzyme A:
RT diacylglycerol acyltransferase 1.";
RL Biochim. Biophys. Acta 1737:76-82(2005).
RN [6]
RP CATALYTIC ACTIVITY.
RX PubMed=18768481; DOI=10.1074/jbc.m800494200;
RA Cheng D., Iqbal J., Devenny J., Chu C.H., Chen L., Dong J., Seethala R.,
RA Keim W.J., Azzara A.V., Lawrence R.M., Pelleymounter M.A., Hussain M.M.;
RT "Acylation of acylglycerols by acyl coenzyme A:diacylglycerol
RT acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the intestinal
RT fat absorption.";
RL J. Biol. Chem. 283:29802-29811(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-265,
RP AND UBIQUITINATION.
RX PubMed=27184406; DOI=10.1016/j.bbrc.2016.05.071;
RA Brandt C., McFie P.J., Stone S.J.;
RT "Biochemical characterization of human acyl coenzyme A: 2-monoacylglycerol
RT acyltransferase-3 (MGAT3).";
RL Biochem. Biophys. Res. Commun. 475:264-270(2016).
RN [8]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=28420705; DOI=10.1194/jlr.m073445;
RA Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.;
RT "Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid
RT acyltransferases.";
RL J. Lipid Res. 58:1091-1099(2017).
CC -!- FUNCTION: Catalyzes the formation of diacylglycerol from 2-
CC monoacylglycerol and fatty acyl-CoA. Also able to catalyze the terminal
CC step in triacylglycerol synthesis by using diacylglycerol and fatty
CC acyl-CoA as substrates. Has a preference toward palmitoyl-CoA and
CC oleoyl-CoA. May be involved in absorption of dietary fat in the small
CC intestine by catalyzing the resynthesis of triacylglycerol in
CC enterocytes. Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl
CC acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG)
CC (PubMed:28420705). {ECO:0000269|PubMed:12618427,
CC ECO:0000269|PubMed:27184406, ECO:0000269|PubMed:28420705}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acylglycerol + an acyl-CoA = a 1,2-diacyl-sn-glycerol +
CC CoA; Xref=Rhea:RHEA:32947, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; EC=2.3.1.22;
CC Evidence={ECO:0000269|PubMed:12618427, ECO:0000269|PubMed:27184406};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32948;
CC Evidence={ECO:0000305};
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:12618427, ECO:0000269|PubMed:27184406};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869;
CC Evidence={ECO:0000305};
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:0000269|PubMed:12618427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912;
CC Evidence={ECO:0000305|PubMed:12618427};
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:0000269|PubMed:12618427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072;
CC Evidence={ECO:0000305|PubMed:12618427};
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:0000269|PubMed:12618427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC Evidence={ECO:0000305|PubMed:12618427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-
CC CoA = 1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + CoA;
CC Xref=Rhea:RHEA:38299, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:75466, ChEBI:CHEBI:75688;
CC Evidence={ECO:0000269|PubMed:12618427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38300;
CC Evidence={ECO:0000305|PubMed:12618427};
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:0000269|PubMed:16214399};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176;
CC Evidence={ECO:0000305|PubMed:16214399};
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:0000269|PubMed:28420705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341;
CC Evidence={ECO:0000305|PubMed:28420705};
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:0000269|PubMed:28420705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55345;
CC Evidence={ECO:0000305|PubMed:28420705};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=9.3 nmol/min/mg enzyme with diacylglycerol as substrate
CC {ECO:0000269|PubMed:12618427};
CC Vmax=22.8 nmol/min/mg enzyme with 2-monoacylglycerol as substrate
CC {ECO:0000269|PubMed:12618427};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000269|PubMed:27184406}.
CC -!- INTERACTION:
CC Q86VF5-3; P07339: CTSD; NbExp=3; IntAct=EBI-25840143, EBI-2115097;
CC Q86VF5-3; G5E9A7: DMWD; NbExp=3; IntAct=EBI-25840143, EBI-10976677;
CC Q86VF5-3; P28799: GRN; NbExp=3; IntAct=EBI-25840143, EBI-747754;
CC Q86VF5-3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25840143, EBI-5235340;
CC Q86VF5-3; O76024: WFS1; NbExp=3; IntAct=EBI-25840143, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27184406}; Multi-pass membrane protein
CC {ECO:0000305}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:27184406}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86VF5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86VF5-2; Sequence=VSP_020361, VSP_020362;
CC Name=3;
CC IsoId=Q86VF5-3; Sequence=VSP_020363;
CC -!- TISSUE SPECIFICITY: Selectively expressed in the digestive system.
CC Highly expressed in the ileum, and at lower level in jejunum, duodenum,
CC colon, cecum and the rectum. Not expressed in the stomach and the
CC esophagus and trachea. Expressed at very low level in liver.
CC {ECO:0000269|PubMed:12618427}.
CC -!- PTM: Ubiquitinated. Ubiquitination leads to proteasomal degradation.
CC {ECO:0000269|PubMed:27184406}.
CC -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD45832.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY229854; AAO63579.1; -; mRNA.
DR EMBL; AY358200; AAQ88567.1; -; mRNA.
DR EMBL; AC004876; AAD45832.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC100953; AAI00954.1; -; mRNA.
DR EMBL; BC100954; AAI00955.1; -; mRNA.
DR EMBL; BC100955; AAI00956.1; -; mRNA.
DR CCDS; CCDS5714.1; -. [Q86VF5-1]
DR CCDS; CCDS75643.1; -. [Q86VF5-2]
DR RefSeq; NP_001274076.1; NM_001287147.1. [Q86VF5-2]
DR RefSeq; NP_835470.1; NM_178176.3. [Q86VF5-1]
DR RefSeq; XP_005250366.1; XM_005250309.3. [Q86VF5-3]
DR AlphaFoldDB; Q86VF5; -.
DR BioGRID; 131392; 23.
DR IntAct; Q86VF5; 5.
DR STRING; 9606.ENSP00000223114; -.
DR SwissLipids; SLP:000000307; -.
DR GlyGen; Q86VF5; 1 site.
DR BioMuta; MOGAT3; -.
DR DMDM; 74727570; -.
DR jPOST; Q86VF5; -.
DR MassIVE; Q86VF5; -.
DR PaxDb; Q86VF5; -.
DR PeptideAtlas; Q86VF5; -.
DR PRIDE; Q86VF5; -.
DR Antibodypedia; 2307; 104 antibodies from 24 providers.
DR DNASU; 346606; -.
DR Ensembl; ENST00000223114.9; ENSP00000223114.4; ENSG00000106384.12. [Q86VF5-1]
DR Ensembl; ENST00000379423.3; ENSP00000368734.3; ENSG00000106384.12. [Q86VF5-2]
DR Ensembl; ENST00000440203.6; ENSP00000403756.2; ENSG00000106384.12. [Q86VF5-3]
DR GeneID; 346606; -.
DR KEGG; hsa:346606; -.
DR MANE-Select; ENST00000223114.9; ENSP00000223114.4; NM_178176.4; NP_835470.1.
DR UCSC; uc003uyc.5; human. [Q86VF5-1]
DR CTD; 346606; -.
DR DisGeNET; 346606; -.
DR GeneCards; MOGAT3; -.
DR HGNC; HGNC:23249; MOGAT3.
DR HPA; ENSG00000106384; Group enriched (intestine, liver).
DR MIM; 610184; gene.
DR neXtProt; NX_Q86VF5; -.
DR OpenTargets; ENSG00000106384; -.
DR PharmGKB; PA134959238; -.
DR VEuPathDB; HostDB:ENSG00000106384; -.
DR eggNOG; KOG0831; Eukaryota.
DR GeneTree; ENSGT01030000234582; -.
DR HOGENOM; CLU_023995_0_0_1; -.
DR InParanoid; Q86VF5; -.
DR OMA; NDPKHAG; -.
DR OrthoDB; 1347007at2759; -.
DR PhylomeDB; Q86VF5; -.
DR TreeFam; TF314707; -.
DR BRENDA; 2.3.1.22; 2681.
DR PathwayCommons; Q86VF5; -.
DR Reactome; R-HSA-75109; Triglyceride biosynthesis.
DR SignaLink; Q86VF5; -.
DR UniPathway; UPA00282; -.
DR BioGRID-ORCS; 346606; 10 hits in 1068 CRISPR screens.
DR GenomeRNAi; 346606; -.
DR Pharos; Q86VF5; Tbio.
DR PRO; PR:Q86VF5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q86VF5; protein.
DR Bgee; ENSG00000106384; Expressed in mucosa of transverse colon and 32 other tissues.
DR Genevisible; Q86VF5; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR007130; DAGAT.
DR Pfam; PF03982; DAGAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Cytoplasm; Endoplasmic reticulum;
KW Glycerol metabolism; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..341
FT /note="2-acylglycerol O-acyltransferase 3"
FT /id="PRO_0000249067"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 224..281
FT /note="ASLVPVYSFGENDIFRLKAFATGSWQHWCQLTFKKLMGFSPCIFWGRGLFSA
FT TSWGLL -> GPPHPRPPAPPPHRGGSQSLSRPLHDGPGAALRGAQGKLWGPRFHLPHL
FT HLGLAAAFR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020361"
FT VAR_SEQ 282..341
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020362"
FT VAR_SEQ 291..341
FT /note="VGRPIPVPQRLHPTEEEVNHYHALYMTALEQLFEEHKESCGVPASTCLTFI
FT -> GECPPPGGRPPAAAWASGIPRPPVSLSLQWAAPSPSPSASTPPRRKSITITPST
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020363"
FT MUTAGEN 265
FT /note="C->A: Reduces 60% 2-acylglycerol O-acyltransferase
FT activity. No effect on diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:27184406"
FT MUTAGEN 265
FT /note="C->Y: Catalitically inactive. No 2-acylglycerol O-
FT acyltransferase neither diacylglycerol O-acyltransferase
FT activities."
FT /evidence="ECO:0000269|PubMed:27184406"
FT CONFLICT 265
FT /note="C -> Y (in Ref. 4; AAI00954)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 38730 MW; 3F4981AE0D05B613 CRC64;
MGVATTLQPP TTSKTLQKQH LEAVGAYQYV LTFLFMGPFF SLLVFVLLFT SLWPFSVFYL
VWLYVDWDTP NQGGRRSEWI RNRAIWRQLR DYYPVKLVKT AELPPDRNYV LGAHPHGIMC
TGFLCNFSTE SNGFSQLFPG LRPWLAVLAG LFYLPVYRDY IMSFGLCPVS RQSLDFILSQ
PQLGQAVVIM VGGAHEALYS VPGEHCLTLQ KRKGFVRLAL RHGASLVPVY SFGENDIFRL
KAFATGSWQH WCQLTFKKLM GFSPCIFWGR GLFSATSWGL LPFAVPITTV VGRPIPVPQR
LHPTEEEVNH YHALYMTALE QLFEEHKESC GVPASTCLTF I
