ID A0A0D3DRK0_BRAOL Unreviewed; 547 AA.
AC A0A0D3DRK0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:Bo8g077590.1};
GN Name=106307573 {ECO:0000313|EnsemblPlants:Bo8g077590.1};
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:Bo8g077590.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo8g077590.1, 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:Bo8g077590.1}
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 RefSeq; XP_013600014.1; XM_013744560.1.
DR AlphaFoldDB; A0A0D3DRK0; -.
DR STRING; 109376.A0A0D3DRK0; -.
DR EnsemblPlants; Bo8g077590.1; Bo8g077590.1; Bo8g077590.
DR GeneID; 106307573; -.
DR Gramene; Bo8g077590.1; Bo8g077590.1; Bo8g077590.
DR KEGG; boe:106307573; -.
DR eggNOG; ENOG502QTZ2; Eukaryota.
DR HOGENOM; CLU_027831_0_0_1; -.
DR OMA; MESIRWR; -.
DR OrthoDB; 2957273at2759; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000032141; Chromosome C8.
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 PANTHER; PTHR31650; O-ACYLTRANSFERASE (WSD1-LIKE) FAMILY PROTEIN; 1.
DR PANTHER; PTHR31650:SF70; WAX ESTER SYNTHASE_DIACYLGLYCEROL ACYLTRANSFERASE 6; 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 241..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..321
FT /note="O-acyltransferase WSD1-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03007"
FT DOMAIN 392..536
FT /note="O-acyltransferase WSD1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06974"
SQ SEQUENCE 547 AA; 62044 MW; AF16B1F6F8283D65 CRC64;
MEIKVEPKAM EIKVEPKAME IKVEPKTMEI KLEQEAMEIK IHRDIPEATV KKTKEEEQPL
SPAARVFHAP AFNCYVITVI GVKKKIEPDV VIEGLKQTLI RHPRFSSKMV NKTNKNKQTQ
RWVRTNVVTN NHVIVPDIQT QHIENANADK FLDSYVSDLT LVPLDTSKPL WELHLLDLKT
SDAENVAVLK FHHSLGDGMS LMALVLACMR KTSNLNELPT LPYQNRTSSG SSRLTGGSWR
GFRFLWLFMV LWSTIMLVLN TICDALRFIA TAMFLKDTKT PIKGDYRLSM PTRMSLVHLT
VSLDDIKLIK TNMKMTVNDV VIGVTQAGLS KYLERRYGEK KNVVGDDQKS KKNSNEMPKR
IRLRSALLVN LRPTTGIQDL ADMMDKGSKC RWGNMIGYIV FPFSIGLRKD PLEHLGTAKK
IIDRKKNSLE AALTFIVGKL MIKAFGVKVT ANLLNRMLSN TTMSFSNLIG PIEEISFFGH
PITYMAPSVY GHPHALTMHF QSYMNKMTIS LTVDPTVISN PHQLLDDWEE SLRNIKTAVQ
ERSSTHQ
//
