DGAT1_CORAE
ID DGAT1_CORAE Reviewed; 539 AA.
AC A0A161IUT7;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Diacylglycerol O-acyltransferase 1 {ECO:0000305};
DE Short=CaDGAT1 {ECO:0000303|PubMed:27208257};
DE EC=2.3.1.20 {ECO:0000269|PubMed:27208257};
GN Name=DGAT1 {ECO:0000303|PubMed:27208257};
OS Corylus americana (American hazelnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Betulaceae; Corylus.
OX NCBI_TaxID=78632;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27208257; DOI=10.1104/pp.16.00315;
RA Roesler K., Shen B., Bermudez E., Li C., Hunt J., Damude H.G., Ripp K.G.,
RA Everard J.D., Booth J.R., Castaneda L., Feng L., Meyer K.;
RT "An improved variant of soybean type 1 diacylglycerol acyltransferase
RT increases the oil content and decreases the soluble carbohydrate content of
RT soybeans.";
RL Plant Physiol. 171:878-893(2016).
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. Has a marked
CC preference for oleoyl-CoA as substrate. {ECO:0000269|PubMed:27208257}.
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; KU744408; ANC50790.1; -; mRNA.
DR AlphaFoldDB; A0A161IUT7; -.
DR SMR; A0A161IUT7; -.
DR BRENDA; 2.3.1.20; 17273.
DR UniPathway; UPA00282; -.
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; IDA:UniProtKB.
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; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..539
FT /note="Diacylglycerol O-acyltransferase 1"
FT /id="PRO_0000438908"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 410..416
FT /note="FYXDWWN motif"
FT /evidence="ECO:0000250|UniProtKB:O75907"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 465
FT /evidence="ECO:0000250|UniProtKB:O75907"
SQ SEQUENCE 539 AA; 61695 MW; FB0EF885100E5DEF CRC64;
MAISDMPEST GTTATTATMP HGGSDLRRRH NATETTEVSD SNSKTTDPDS GNSVRESVRV
RDSSTDESLA RKSCEDDGSR SEVVIESANP VTNGNDGGEK IANGEDRRTD FAAVKLAYRP
SVPAHRRIKE SPLSSDAIFR QSHAGLFNLC IVVLVAVNSR LIIENLMKYG WLIKTGFWFS
SRSLRDWPLL MCCLTLPIFP AAAFVVEKLV QWKYISEPVV LLLHFIITTA ALLYPVFVIL
RCDSVVLSGV TLMLFACIVW LKLVSYTHTN YDMRALAKSI DKGDVLPNSL NTDYPYSVSF
KSLAYFMVAP TLCYQTSYPR TACIRKSWVV RQLVKLIIFT GVMGFIIEQY INPIVKNSQH
PLKGNLLYAI ERVLKLSVPN LYVWLCMFYC FFHLWLNILA ELLRFGDREF YKDWWNAKTV
EEYWRLWNMP VHKWMVRHIY FPCLRNGIPK GVAILIAFFV SAIFHELCIA VPCHIFKLWA
FIGIMCQVPL VLITNYLQNK FRNSMVGNMI FWFFFCILGQ PMCVLLYYHD LMNRKGKTE
