ID A0A0D3A9E2_BRAOL Unreviewed; 848 AA.
AC A0A0D3A9E2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:Bo1g078720.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo1g078720.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo1g078720.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo1g078720.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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:0000256|ARBA:ARBA00001039};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + a long chain fatty alcohol = a wax ester +
CC CoA; Xref=Rhea:RHEA:38443, ChEBI:CHEBI:10036, ChEBI:CHEBI:17135,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=2.3.1.75;
CC Evidence={ECO:0000256|ARBA:ARBA00029340};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004771}.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the long-chain O-
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00024360}.
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DR AlphaFoldDB; A0A0D3A9E2; -.
DR STRING; 109376.A0A0D3A9E2; -.
DR EnsemblPlants; Bo1g078720.1; Bo1g078720.1; Bo1g078720.
DR Gramene; Bo1g078720.1; Bo1g078720.1; Bo1g078720.
DR eggNOG; ENOG502QTZ2; Eukaryota.
DR HOGENOM; CLU_336286_0_0_1; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000032141; Chromosome C1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045034; O-acyltransferase_WSD1-like.
DR InterPro; IPR009721; O-acyltransferase_WSD1_C.
DR InterPro; IPR004255; O-acyltransferase_WSD1_N.
DR InterPro; IPR004252; Probable_transposase_24.
DR PANTHER; PTHR31650; O-ACYLTRANSFERASE (WSD1-LIKE) FAMILY PROTEIN; 1.
DR PANTHER; PTHR31650:SF69; WAX ESTER SYNTHASE_DIACYLGLYCEROL ACYLTRANSFERASE 4-RELATED; 1.
DR Pfam; PF03004; Transposase_24; 1.
DR Pfam; PF06974; WS_DGAT_C; 1.
DR Pfam; PF03007; WS_DGAT_cat; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 204..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..230
FT /note="O-acyltransferase WSD1-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03007"
FT DOMAIN 315..370
FT /note="O-acyltransferase WSD1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06974"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 848 AA; 95585 MW; 72BDC6D6712D167D CRC64;
MEIRTRRRRP HIPEIRVGKK EEEEEQPLSP AARLFHAPEF NCNIISVVGL KSKIKPAVII
EGIKQTLIRH PRFSCKMVES GNKRREQKWV QTKVVAEDHV VIPKIDMHNI GNANADAFLD
SYVSNLTTIP LDTSKPLWEV HILDLRTSDA ENVAILKIHH SVGDGMSLMS LVLACTRKTS
NPDELPSLPN QKSSLSGSRS YSRLLWLVMA LWSVVMLVLN TVCDALEFIA TAMFLKDTET
PIKGNFRLST SKRMCCVHRT KTVNDVILGV SQAGLSQYLK RRYGEQEEPM PKGIRLRAAL
LDLADIMAKG SKCTWGNWIG YIIFPFSISL CDDPLEHLRR AKFIIDRKKN SFEALLTFIV
GNFILKSFGV QDIPRKASDL FHRSIVQSNR SITFLRLSSI WSHDDQIRPR QRRGRGGTGS
QSRDSTHFQD SPSPHSSYHT SPSAAPAPAP LAPAAAPAPP PPGPPGVMSV ADLVQQPGRD
HLPYLTPYPH GHGQTWFNRS GNGISAWINR MMYSALDKGH PTFTHFPTEK QVLWFRQFAQ
EFNWNSDETL FIYHHFVHKV MDNYGKQIHE WKKKWEINKV PKSMNDTVWK ELCAHWDKEE
TKETSSTNST NRRSDRKGKG IYKHNLGAQS IATLGDRMAE ENDGEPVDDL ALMRRAYTNK
KTGQIDDGLV RDVVDLVQTQ VVDEVSQLQT EDDASTASTN LSRCRINEIV ESSVPKKKGR
LVGLGRRTRS VPPSSAPPPF VETEVLTAQL KDKDSLGIIR GNSSVGIFLS IDVYMSKTHR
SMNVRGNIPT KFSLGIFRGH FRQNNGPRNF LGNLFPRNSV GKFRGISDER RNSEELFPTT
CFVGMSSE
//
