DGAT1_HUMAN
ID DGAT1_HUMAN Reviewed; 488 AA.
AC O75907; B2RWQ2; D3DWL6; Q96BB8;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Diacylglycerol O-acyltransferase 1 {ECO:0000305};
DE EC=2.3.1.20 {ECO:0000269|PubMed:16214399, ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611};
DE AltName: Full=ACAT-related gene product 1;
DE AltName: Full=Acyl-CoA retinol O-fatty-acyltransferase {ECO:0000303|PubMed:16214399};
DE Short=ARAT {ECO:0000303|PubMed:16214399};
DE Short=Retinol O-fatty-acyltransferase {ECO:0000303|PubMed:16214399};
DE EC=2.3.1.76 {ECO:0000269|PubMed:16214399};
DE AltName: Full=Diglyceride acyltransferase;
GN Name=DGAT1 {ECO:0000303|PubMed:16214399, ECO:0000312|HGNC:HGNC:2843};
GN Synonyms=AGRP1 {ECO:0000303|PubMed:9756920}, DGAT;
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], AND FUNCTION.
RX PubMed=9756920; DOI=10.1074/jbc.273.41.26765;
RA Oelkers P., Behari A., Cromley D., Billheimer J.T., Sturley S.L.;
RT "Characterization of two human genes encoding acyl coenzyme A:cholesterol
RT acyltransferase-related enzymes.";
RL J. Biol. Chem. 273:26765-26771(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yamasaki Y., Watanabe T.K., Tanigami A.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
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, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP FUNCTION.
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 FUNCTION, AND 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 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).
RN [8]
RP INVOLVEMENT IN DIAR7.
RX PubMed=23114594; DOI=10.1172/jci64873;
RA Haas J.T., Winter H.S., Lim E., Kirby A., Blumenstiel B., DeFelice M.,
RA Gabriel S., Jalas C., Branski D., Grueter C.A., Toporovski M.S.,
RA Walther T.C., Daly M.J., Farese R.V. Jr.;
RT "DGAT1 mutation is linked to a congenital diarrheal disorder.";
RL J. Clin. Invest. 122:4680-4684(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-18, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10] {ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS)IN COMPLEX WITH
RP (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, AND
RP MUTAGENESIS OF GLN-375; ASN-378; VAL-381; HIS-382; CYS-385; ILE-386;
RP TYR-390; LYS-391; ARG-404; VAL-407; SER-411; HIS-415; MET-434; GLN-437;
RP GLN-465 AND VAL-469.
RX PubMed=32433611; DOI=10.1038/s41586-020-2289-6;
RA Sui X., Wang K., Gluchowski N.L., Elliott S.D., Liao M., Walther T.C.,
RA Farese R.V. Jr.;
RT "Structure and catalytic mechanism of a human triacylglycerol-synthesis
RT enzyme.";
RL Nature 581:323-328(2020).
RN [11] {ECO:0007744|PDB:6VP0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH
RP (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404;
RP SER-411; HIS-415 AND GLU-416.
RX PubMed=32433610; DOI=10.1038/s41586-020-2280-2;
RA Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V.,
RA Laganowsky A., Yan N., Zhou M.;
RT "Structure and mechanism of human diacylglycerol O-acyltransferase 1.";
RL Nature 581:329-332(2020).
RN [12]
RP VARIANT DIAR7 458-TRP--ALA-488 DEL.
RX PubMed=30237576; DOI=10.1038/s41436-018-0138-x;
RA Maddirevula S., Alzahrani F., Al-Owain M., Al Muhaizea M.A., Kayyali H.R.,
RA AlHashem A., Rahbeeni Z., Al-Otaibi M., Alzaidan H.I., Balobaid A.,
RA El Khashab H.Y., Bubshait D.K., Faden M., Yamani S.A., Dabbagh O.,
RA Al-Mureikhi M., Jasser A.A., Alsaif H.S., Alluhaydan I., Seidahmed M.Z.,
RA Alabbasi B.H., Almogarri I., Kurdi W., Akleh H., Qari A., Al Tala S.M.,
RA Alhomaidi S., Kentab A.Y., Salih M.A., Chedrawi A., Alameer S., Tabarki B.,
RA Shamseldin H.E., Patel N., Ibrahim N., Abdulwahab F., Samira M., Goljan E.,
RA Abouelhoda M., Meyer B.F., Hashem M., Shaheen R., AlShahwan S.,
RA Alfadhel M., Ben-Omran T., Al-Qattan M.M., Monies D., Alkuraya F.S.;
RT "Autozygome and high throughput confirmation of disease genes candidacy.";
RL Genet. Med. 21:736-742(2019).
CC -!- FUNCTION: Catalyzes the terminal and only committed step in
CC triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as
CC substrates (PubMed:16214399, PubMed:18768481, PubMed:28420705,
CC PubMed:9756920, PubMed:32433611, PubMed:32433610). Highly expressed in
CC epithelial cells of the small intestine and its activity is essential
CC for the absorption of dietary fats (PubMed:18768481). In liver, plays a
CC role in esterifying exogenous fatty acids to glycerol, and is required
CC to synthesize fat for storage (PubMed:16214399). Also present in female
CC mammary glands, where it produces fat in the milk (By similarity). May
CC be involved in VLDL (very low density lipoprotein) assembly
CC (PubMed:18768481). 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 (PubMed:16214399). 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) (PubMed:28420705).
CC {ECO:0000250|UniProtKB:Q8MK44, ECO:0000250|UniProtKB:Q9Z2A7,
CC ECO:0000269|PubMed:16214399, ECO:0000269|PubMed:18768481,
CC ECO:0000269|PubMed:28420705, ECO:0000269|PubMed:32433610,
CC ECO:0000269|PubMed:32433611, ECO:0000269|PubMed:9756920}.
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:16214399, ECO:0000269|PubMed:32433610,
CC ECO:0000269|PubMed:32433611};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869;
CC Evidence={ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611};
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:0000269|PubMed:16214399};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489;
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:18768481};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912;
CC Evidence={ECO:0000305|PubMed:18768481};
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:18768481,
CC ECO:0000269|PubMed:32433610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC Evidence={ECO:0000269|PubMed:32433610, ECO:0000305|PubMed:18768481};
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 -!- 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:0000269|PubMed:28420705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916;
CC Evidence={ECO:0000305|PubMed:28420705};
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:0000269|PubMed:28420705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38380;
CC Evidence={ECO:0000305|PubMed:28420705};
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 -!- ACTIVITY REGULATION: XP620 is a selective DGAT1 inhibitor.
CC {ECO:0000269|PubMed:16214399}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25.9 uM for retinol {ECO:0000269|PubMed:16214399};
CC KM=13.9 uM for palmitoyl coenzyme A {ECO:0000269|PubMed:16214399};
CC KM=14.6 uM for (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:32433610};
CC KM=8.6 uM for octadecanoyl-CoA {ECO:0000269|PubMed:32433610};
CC KM=6.4 uM for hexadecanoyl-coA {ECO:0000269|PubMed:32433610};
CC KM=6.2 uM for (9Z)-hexadecenoyl-CoA {ECO:0000269|PubMed:32433610};
CC KM=597.1 uM for 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as
CC homodimer) {ECO:0000269|PubMed:32433610};
CC KM=497.5 uM for 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as
CC homotetramer) {ECO:0000269|PubMed:32433610};
CC Vmax=956.6 pmol/min/ug enzyme with (9Z)-octadecenoyl-CoA as substrate
CC {ECO:0000269|PubMed:32433610};
CC Vmax=839.4 pmol/min/ug enzyme with octadecanoyl-CoA as substrate
CC {ECO:0000269|PubMed:32433610};
CC Vmax=767.8 pmol/min/ug enzyme with hexadecanoyl-coA as substrate
CC {ECO:0000269|PubMed:32433610};
CC Vmax=838.6 pmol/min/ug enzyme with (9Z)-hexadecenoyl-CoA as substrate
CC {ECO:0000269|PubMed:32433610};
CC Vmax=3310 pmol/min/ug enzyme with 1,2-di-(9Z-octadecenoyl)-sn-
CC glycerol (with DGAT1 as homodimer) as substrate
CC {ECO:0000269|PubMed:32433610};
CC Vmax=3628 pmol/min/ug enzyme with 1,2-di-(9Z-octadecenoyl)-sn-
CC glycerol (with DGAT1 as homotetramer) as substrate
CC {ECO:0000269|PubMed:32433610};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC -!- SUBUNIT: Homodimer or homotetramer; both forms have similar enzymatic
CC activities. {ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611}.
CC -!- INTERACTION:
CC O75907; O75907: DGAT1; NbExp=4; IntAct=EBI-3906527, EBI-3906527;
CC O75907; PRO_0000045602 [Q99IB8]; Xeno; NbExp=2; IntAct=EBI-3906527, EBI-6927873;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Z2A7}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:32433610, ECO:0000269|PubMed:32433611}.
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:0000305|PubMed:32433610, ECO:0000305|PubMed:32433611}.
CC -!- DOMAIN: The MBOAT fold forms a reaction chamber in the endoplasmic
CC reticulum membrane that encloses the active sites (PubMed:32433611,
CC PubMed:32433610). The reaction chamber has a tunnel to the cytosolic
CC side and its entrance recognizes the hydrophilic CoA motif of an acyl-
CC CoA molecule (PubMed:32433610). The chamber has separate entrances for
CC each of the two substrates, acyl-CoA and 1,2-diacyl-sn-glycerol
CC (PubMed:32433610). {ECO:0000269|PubMed:32433610,
CC ECO:0000269|PubMed:32433611}.
CC -!- DISEASE: Diarrhea 7, protein-losing enteropathy type (DIAR7)
CC [MIM:615863]: A life-threatening disease characterized by severe,
CC intractable, watery diarrhea. {ECO:0000269|PubMed:23114594,
CC ECO:0000269|PubMed:30237576}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR EMBL; AF059202; AAC63997.1; -; mRNA.
DR EMBL; AB057815; BAC66170.1; -; mRNA.
DR EMBL; CH471162; EAW82127.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82129.1; -; Genomic_DNA.
DR EMBL; BC015762; AAH15762.1; -; mRNA.
DR EMBL; BC023565; AAH23565.1; -; mRNA.
DR EMBL; BC150649; AAI50650.1; -; mRNA.
DR CCDS; CCDS6420.1; -.
DR RefSeq; NP_036211.2; NM_012079.5.
DR PDB; 6VP0; EM; 3.10 A; C/E=1-488.
DR PDB; 6VYI; EM; 3.00 A; A/B=1-488.
DR PDB; 6VZ1; EM; 3.20 A; A/B=1-488.
DR PDBsum; 6VP0; -.
DR PDBsum; 6VYI; -.
DR PDBsum; 6VZ1; -.
DR AlphaFoldDB; O75907; -.
DR SMR; O75907; -.
DR BioGRID; 114241; 40.
DR IntAct; O75907; 13.
DR MINT; O75907; -.
DR STRING; 9606.ENSP00000482264; -.
DR BindingDB; O75907; -.
DR ChEMBL; CHEMBL6009; -.
DR DrugCentral; O75907; -.
DR GuidetoPHARMACOLOGY; 2821; -.
DR SwissLipids; SLP:000000308; -.
DR TCDB; 2.A.50.4.1; the glycerol uptake (gup) or membrane-bound acyl transferase (mboat) family.
DR iPTMnet; O75907; -.
DR PhosphoSitePlus; O75907; -.
DR BioMuta; DGAT1; -.
DR EPD; O75907; -.
DR jPOST; O75907; -.
DR MassIVE; O75907; -.
DR MaxQB; O75907; -.
DR PaxDb; O75907; -.
DR PeptideAtlas; O75907; -.
DR PRIDE; O75907; -.
DR ProteomicsDB; 50257; -.
DR Antibodypedia; 28443; 324 antibodies from 31 providers.
DR DNASU; 8694; -.
DR Ensembl; ENST00000528718.6; ENSP00000482264.1; ENSG00000185000.12.
DR Ensembl; ENST00000644790.2; ENSP00000495489.1; ENSG00000285482.2.
DR GeneID; 8694; -.
DR KEGG; hsa:8694; -.
DR MANE-Select; ENST00000528718.6; ENSP00000482264.1; NM_012079.6; NP_036211.2.
DR UCSC; uc003zbv.5; human.
DR CTD; 8694; -.
DR DisGeNET; 8694; -.
DR GeneCards; DGAT1; -.
DR HGNC; HGNC:2843; DGAT1.
DR HPA; ENSG00000185000; Tissue enhanced (intestine).
DR MalaCards; DGAT1; -.
DR MIM; 604900; gene.
DR MIM; 615863; phenotype.
DR neXtProt; NX_O75907; -.
DR OpenTargets; ENSG00000185000; -.
DR Orphanet; 329242; Congenital chronic diarrhea with protein-losing enteropathy.
DR PharmGKB; PA27303; -.
DR VEuPathDB; HostDB:ENSG00000185000; -.
DR eggNOG; KOG0380; Eukaryota.
DR GeneTree; ENSGT00950000183081; -.
DR HOGENOM; CLU_018190_0_0_1; -.
DR InParanoid; O75907; -.
DR OMA; HAIIVWL; -.
DR OrthoDB; 1275897at2759; -.
DR PhylomeDB; O75907; -.
DR TreeFam; TF314921; -.
DR BRENDA; 2.3.1.20; 2681.
DR PathwayCommons; O75907; -.
DR Reactome; R-HSA-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-75109; Triglyceride biosynthesis.
DR SABIO-RK; O75907; -.
DR SignaLink; O75907; -.
DR SIGNOR; O75907; -.
DR UniPathway; UPA00230; -.
DR BioGRID-ORCS; 8694; 15 hits in 1074 CRISPR screens.
DR ChiTaRS; DGAT1; human.
DR GenomeRNAi; 8694; -.
DR Pharos; O75907; Tclin.
DR PRO; PR:O75907; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O75907; protein.
DR Bgee; ENSG00000185000; Expressed in duodenum and 92 other tissues.
DR ExpressionAtlas; O75907; baseline and differential.
DR Genevisible; O75907; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; IEA:Ensembl.
DR GO; GO:0016746; F:acyltransferase activity; TAS:ProtInc.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IDA:UniProtKB.
DR GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR GO; GO:0019915; P:lipid storage; ISS:BHF-UCL.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; ISS:BHF-UCL.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006641; P:triglyceride metabolic process; TAS:ProtInc.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:BHF-UCL.
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 3D-structure; Acyltransferase; Disease variant; Endoplasmic reticulum;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..488
FT /note="Diacylglycerol O-acyltransferase 1"
FT /id="PRO_0000207654"
FT TOPO_DOM 1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT TRANSMEM 84..118
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0,
FT ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1"
FT TOPO_DOM 119..130
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT TRANSMEM 131..156
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0,
FT ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1"
FT TOPO_DOM 157..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT TRANSMEM 162..184
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0,
FT ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1"
FT TOPO_DOM 185..191
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT TRANSMEM 192..223
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0,
FT ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1"
FT TOPO_DOM 224..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT TRANSMEM 274..308
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0,
FT ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1"
FT TOPO_DOM 309..315
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT TRANSMEM 316..353
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0,
FT ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1"
FT TOPO_DOM 354..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT TRANSMEM 400..420
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0,
FT ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1"
FT TOPO_DOM 421..428
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT TRANSMEM 429..447
FT /note="Helical; Name=8"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0,
FT ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1"
FT TOPO_DOM 448..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT TRANSMEM 450..481
FT /note="Helical; Name=9"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0,
FT ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1"
FT TOPO_DOM 482..488
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT REGION 1..91
FT /note="Involved in homomerization"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2A7"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000305|PubMed:32433610"
FT REGION 119..130
FT /note="Extracellular loop 1 (EL1)"
FT /evidence="ECO:0000269|PubMed:32433610"
FT REGION 131..488
FT /note="MBOAT fold"
FT /evidence="ECO:0000269|PubMed:32433610"
FT REGION 224..276
FT /note="Intracellular loop 1 (IL1)"
FT /evidence="ECO:0000269|PubMed:32433610"
FT REGION 354..399
FT /note="Intracellular loop 2 (IL2)"
FT /evidence="ECO:0000269|PubMed:32433610"
FT REGION 380..394
FT /note="Amphipathic helix (AH)"
FT /evidence="ECO:0000269|PubMed:32433610"
FT MOTIF 360..366
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000303|PubMed:32433610"
FT ACT_SITE 415
FT /evidence="ECO:0000269|PubMed:32433610"
FT BINDING 374..382
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0,
FT ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1"
FT BINDING 390
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611, ECO:0007744|PDB:6VP0,
FT ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1"
FT BINDING 404
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0007744|PDB:6VP0"
FT BINDING 477
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:32433611,
FT ECO:0007744|PDB:6VYI, ECO:0007744|PDB:6VZ1"
FT SITE 416
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:32433610"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 458..488
FT /note="Missing (in DIAR7; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30237576"
FT /id="VAR_082141"
FT MUTAGEN 346
FT /note="L->W: Strongly reduced diacylglycerol O-
FT acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:32433610"
FT MUTAGEN 371
FT /note="T->A: Decreased diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433610"
FT MUTAGEN 375
FT /note="Q->A: Slightly decreased diacylglycerol O-
FT acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:32433611"
FT MUTAGEN 377
FT /note="W->F: Abolished diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433610"
FT MUTAGEN 378
FT /note="N->A,L: Abolished diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT MUTAGEN 381
FT /note="V->A: Does not affect diacylglycerol O-
FT acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:32433611"
FT MUTAGEN 381
FT /note="V->W: Decreased diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433611"
FT MUTAGEN 382
FT /note="H->A: Decreased diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT MUTAGEN 385
FT /note="C->W: Decreased diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433611"
FT MUTAGEN 386
FT /note="I->A: Slightly decreased diacylglycerol O-
FT acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:32433611"
FT MUTAGEN 390
FT /note="Y->A: Decreased diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT MUTAGEN 391
FT /note="K->A: Slightly decreased diacylglycerol O-
FT acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:32433611"
FT MUTAGEN 400
FT /note="K->L: Decreased diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433610"
FT MUTAGEN 404
FT /note="R->A: Does not affect diacylglycerol O-
FT acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:32433611"
FT MUTAGEN 404
FT /note="R->L: Decreased diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433610"
FT MUTAGEN 407
FT /note="V->F: Decreased diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433611"
FT MUTAGEN 411
FT /note="S->A,W: Abolished diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT MUTAGEN 411
FT /note="S->I: Decreased diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433611"
FT MUTAGEN 415
FT /note="H->A: Abolished diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433610,
FT ECO:0000269|PubMed:32433611"
FT MUTAGEN 416
FT /note="E->A: Abolished diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433610"
FT MUTAGEN 434
FT /note="M->A,I: Reduced diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433611"
FT MUTAGEN 437
FT /note="Q->A: Reduced diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433611"
FT MUTAGEN 465
FT /note="Q->A: Reduced diacylglycerol O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32433611"
FT MUTAGEN 469
FT /note="V->A: Slightly decreased diacylglycerol O-
FT acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:32433611"
FT CONFLICT 129
FT /note="Y -> H (in Ref. 1; AAC63997)"
FT /evidence="ECO:0000305"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 88..112
FT /evidence="ECO:0007829|PDB:6VYI"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6VZ1"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6VP0"
FT HELIX 132..154
FT /evidence="ECO:0007829|PDB:6VYI"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 161..184
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 191..225
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:6VZ1"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 275..299
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:6VYI"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 316..342
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 344..352
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:6VP0"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 379..388
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 391..395
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 400..419
FT /evidence="ECO:0007829|PDB:6VYI"
FT TURN 420..423
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 429..447
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 450..462
FT /evidence="ECO:0007829|PDB:6VYI"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:6VYI"
FT HELIX 466..478
FT /evidence="ECO:0007829|PDB:6VYI"
SQ SEQUENCE 488 AA; 55278 MW; 6574D5DBF15D6171 CRC64;
MGDRGSSRRR RTGSRPSSHG GGGPAAAEEE VRDAAAGPDV GAAGDAPAPA PNKDGDAGVG
SGHWELRCHR LQDSLFSSDS GFSNYRGILN WCVVMLILSN ARLFLENLIK YGILVDPIQV
VSLFLKDPYS WPAPCLVIAA NVFAVAAFQV EKRLAVGALT EQAGLLLHVA NLATILCFPA
AVVLLVESIT PVGSLLALMA HTILFLKLFS YRDVNSWCRR ARAKAASAGK KASSAAAPHT
VSYPDNLTYR DLYYFLFAPT LCYELNFPRS PRIRKRFLLR RILEMLFFTQ LQVGLIQQWM
VPTIQNSMKP FKDMDYSRII ERLLKLAVPN HLIWLIFFYW LFHSCLNAVA ELMQFGDREF
YRDWWNSESV TYFWQNWNIP VHKWCIRHFY KPMLRRGSSK WMARTGVFLA SAFFHEYLVS
VPLRMFRLWA FTGMMAQIPL AWFVGRFFQG NYGNAAVWLS LIIGQPIAVL MYVHDYYVLN
YEAPAAEA
