DAT1A_SOYBN
ID DAT1A_SOYBN Reviewed; 498 AA.
AC Q5GKZ7; A0A1B0V7W1; Q1MW31;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Diacylglycerol O-acyltransferase 1A {ECO:0000305};
DE Short=GmDGAT1A {ECO:0000303|PubMed:23322364};
DE EC=2.3.1.20 {ECO:0000269|PubMed:23322364};
GN Name=DGAT1A {ECO:0000303|PubMed:23322364};
GN Synonyms=DGAT {ECO:0000303|PubMed:16432735};
GN OrderedLocusNames=Glyma13g16560 {ECO:0000312|EMBL:KRH19213.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16432735; DOI=10.1007/s00122-006-0210-9;
RA Wang H.W., Zhang J.S., Gai J.Y., Chen S.Y.;
RT "Cloning and comparative analysis of the gene encoding diacylglycerol
RT acyltransferase from wild type and cultivated soybean.";
RL Theor. Appl. Genet. 112:1086-1097(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Jack;
RX PubMed=23322364; DOI=10.1007/s10142-012-0306-z;
RA Li R., Hatanaka T., Yu K., Wu Y., Fukushige H., Hildebrand D.;
RT "Soybean oil biosynthesis: role of diacylglycerol acyltransferases.";
RL Funct. Integr. Genomics 13:99-113(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Williams 82;
RX PubMed=27345221; DOI=10.1038/srep28541;
RA Chen B., Wang J., Zhang G., Liu J., Manan S., Hu H., Zhao J.;
RT "Two types of soybean diacylglycerol acyltransferases are differentially
RT involved in triacylglycerol biosynthesis and response to environmental
RT stresses and hormones.";
RL Sci. Rep. 6:28541-28541(2016).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
CC -!- FUNCTION: Major contributor to triacylglycerol (TAG) synthesis and oil
CC accumulation in developing seeds. Catalyzes the acylation of the sn-3
CC hydroxy group of sn-1,2-diacylglycerol using acyl-CoA (PubMed:23322364,
CC PubMed:27345221). Has a marked preference for oleoyl-CoA (18:1) and sn-
CC 1,2-dioleoylglycerol over vernoloyl-CoA and sn-1,2-divernoloylglycerol
CC (PubMed:23322364). Can use oleoyl-CoA, linoleoyl-CoA and linolenoyl-CoA
CC as substrates (PubMed:27345221). {ECO:0000269|PubMed:23322364,
CC ECO:0000269|PubMed:27345221}.
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:23322364};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27345221}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers and pods. Expressed at
CC low levels in roots, stems and leaves. {ECO:0000269|PubMed:23322364,
CC ECO:0000269|PubMed:27345221}.
CC -!- DEVELOPMENTAL STAGE: During seed development, expressed from 15 to 55
CC days after flowering (DAF), with a peak at 35 DAF.
CC {ECO:0000269|PubMed:23322364}.
CC -!- INDUCTION: Induced by heat shock, insect biting and abscisic acid
CC (ABA). Down-regulated by cold stress and treatment with jasmonate.
CC {ECO:0000269|PubMed:27345221}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR EMBL; AY496439; AAS78662.1; -; mRNA.
DR EMBL; AB257589; BAE93460.1; -; mRNA.
DR EMBL; KT878751; AMP18197.1; -; mRNA.
DR EMBL; CM000846; KRH19213.1; -; Genomic_DNA.
DR RefSeq; NP_001237289.1; NM_001250360.1.
DR AlphaFoldDB; Q5GKZ7; -.
DR SMR; Q5GKZ7; -.
DR STRING; 3847.GLYMA13G16560.2; -.
DR PRIDE; Q5GKZ7; -.
DR EnsemblPlants; KRH19213; KRH19213; GLYMA_13G106100.
DR GeneID; 548005; -.
DR Gramene; KRH19213; KRH19213; GLYMA_13G106100.
DR KEGG; gmx:548005; -.
DR eggNOG; KOG0380; Eukaryota.
DR OMA; HAIIVWL; -.
DR BRENDA; 2.3.1.20; 2483.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000008827; Chromosome 13.
DR GO; GO:0009941; C:chloroplast envelope; IBA:GO_Central.
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:0004144; F:diacylglycerol O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA: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; Glycerol metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..498
FT /note="Diacylglycerol O-acyltransferase 1A"
FT /id="PRO_0000438905"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 369..375
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT COMPBIAS 50..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 424
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT CONFLICT 15
FT /note="N -> S (in Ref. 3; AMP18197)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="V -> A (in Ref. 3; AMP18197)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="D -> G (in Ref. 2; BAE93460)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="Q -> H (in Ref. 2; BAE93460)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 57322 MW; 2878B966393E3EA7 CRC64;
MAISDEPETV ATALNHSSLR RRPTAAGLFN SPETTTDSSG DDLAKDSGSD DSISSDAANS
QPQQKQDTDF SVLKFAYRPS VPAHRKVKES PLSSDTIFRQ SHAGLFNLCI VVLVAVNSRL
IIENLMKYGW LIKSGFWFSS KSLRDWPLFM CCLSLVVFPF AAFIVEKLAQ QKCIPEPVVV
VLHIIITSAS LFYPVLVILR CDSAFLSGVT LMLFACVVWL KLVSYAHTNY DMRALTKSVE
KGEALPDTLN MDYPYNVSFK SLAYFLVAPT LCYQPSYPRT PYIRKGWLFR QLVKLIIFTG
VMGFIIEQYI NPIVQNSQHP LKGNLLYAIE RVLKLSVPNL YVWLCMFYCF FHLWLNILAE
LLRFGDREFY QDWWNAKTVE DYWRMWNMPV HKWMIRHLYF PCLRHGIPKA VALLIAFLVS
ALFHELCIAV PCHIFKLWAF GGIMFQVPLV FITNYLQNKF RNSMVGNMIF WFIFSILGQP
MCVLLYYHDL MNRKGKLD
