DAT1C_SOYBN
ID DAT1C_SOYBN Reviewed; 517 AA.
AC K7LC65; Q6DNG7;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Diacylglycerol O-acyltransferase 1C {ECO:0000305};
DE Short=GmDGAT1C {ECO:0000305};
DE EC=2.3.1.20 {ECO:0000305};
GN Name=DGAT1C {ECO:0000305};
GN OrderedLocusNames=Glyma09g07520 {ECO:0000312|EMBL:KRH37423.1};
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 112-517.
RA Zhang F., Yang M., Xu Y.;
RT "Cloning and functional analysis of soybean diacylglycerol O-
RT acyltransferase gene by RNAi.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in triacylglycerol (TAG) synthesis. Catalyzes the
CC acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using
CC acyl-CoA. {ECO:0000250|UniProtKB:Q5GKZ7}.
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:0000305};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5GKZ7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000305}.
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DR EMBL; CM000842; KRH37423.1; -; Genomic_DNA.
DR EMBL; AY652765; AAT73629.1; -; mRNA.
DR AlphaFoldDB; K7LC65; -.
DR SMR; K7LC65; -.
DR STRING; 3847.GLYMA09G07520.2; -.
DR PRIDE; K7LC65; -.
DR EnsemblPlants; KRH37423; KRH37423; GLYMA_09G065300.
DR Gramene; KRH37423; KRH37423; GLYMA_09G065300.
DR eggNOG; KOG0380; Eukaryota.
DR HOGENOM; CLU_018190_0_1_1; -.
DR InParanoid; K7LC65; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000008827; Chromosome 9.
DR GO; GO:0009941; C:chloroplast envelope; IBA:GO_Central.
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:0004144; F:diacylglycerol O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..517
FT /note="Diacylglycerol O-acyltransferase 1C"
FT /id="PRO_0000438907"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 388..394
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT COMPBIAS 53..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 443
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT CONFLICT 138
FT /note="R -> Q (in Ref. 2; AAT73629)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="L -> S (in Ref. 2; AAT73629)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="Q -> R (in Ref. 2; AAT73629)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="F -> S (in Ref. 2; AAT73629)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 59287 MW; 5E134531D6BBE337 CRC64;
MAISDVPAAA GTTATTTSDS DLRQPSLRRR SSAGVLFDAA RDSGSDNSLT GKITDDDNIK
DHKPNNHAAS DDNVGAAAND AGQEHRQPVA DFKYAYRPSV PAHRRIKESP LSSDNIFRQS
HAGLFNLCIV VLVAVNSRLI IENLMKYGWL IKYGFWFSSK SLRDWPLFMC CLSLAIFPLA
AFVVERLAQQ KCISEPVVVL LHLIISTVEL CYPVLVILRC DSAFVSGVTL MLLTCIVWLK
LVSYAHTNYD MRALTVSNEK GETLPNTLIM EYPYTVTFRS LAYFMVAPTL CYQTSYPRTP
SVRKGWVFRQ LVKLIIFTGV MGFIIEQYMN PIVQNSTHPL KGNLLYAIER ILKLSVPNVY
VWLCMFYCFF HLWLNILAEL VRFGDREFYK DWWNAKTVEE YWRMWNMPVH KWMVRHIYFP
CLRRGIPKGA ASLIAFLVSA VFHELCIAVP CHMFKLWAFI GIMFQVPLVL ITNYLQNKYR
NSMVGNMIFW FIFCILGQPM SVLLYYHDLM NRKGEVD
