ID A0A165WX68_DAUCS Unreviewed; 496 AA.
AC A0A165WX68;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZM97748.1};
GN ORFNames=DCAR_014890 {ECO:0000313|EMBL:KZM97748.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM97748.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZM97748.1, ECO:0000313|Proteomes:UP000077755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM97748.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZM97748.1}.
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DR EMBL; LNRQ01000004; KZM97748.1; -; Genomic_DNA.
DR RefSeq; XP_017245116.1; XM_017389627.1.
DR AlphaFoldDB; A0A165WX68; -.
DR EnsemblPlants; KZM97748; KZM97748; DCAR_014890.
DR GeneID; 108216790; -.
DR Gramene; KZM97748; KZM97748; DCAR_014890.
DR KEGG; dcr:108216790; -.
DR OMA; MLGHTTI; -.
DR OrthoDB; 2957273at2759; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000077755; Chromosome 4.
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 Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation 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:SF38; DIACYLGLYCEROL O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR31650; O-ACYLTRANSFERASE (WSD1-LIKE) FAMILY PROTEIN; 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:UP000077755};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 209..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..275
FT /note="O-acyltransferase WSD1-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03007"
FT DOMAIN 347..490
FT /note="O-acyltransferase WSD1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06974"
SQ SEQUENCE 496 AA; 55915 MW; F0A17A3624EA6478 CRC64;
MDSVPSLRAL KHVKVGQEHQ KSRLLERGDE DGQPLSPVAR LFHEPGSNVY IVAIMGFRVK
LHPDVVKPVL THVFLKHPRF SSLQVEDKES GELKWIPTEV DLENHFIVSE LDPPLQAADK
FVEDYVSDLS KTNIPNTKPL WDIHLLNVKT SDAEAFLIYR IHHSIGDGMS LMALILAHSR
QVSDPSALPT LPAMNKESNF LKLRGFRSVV YVLWNTLIAI FMFVLTALFL KDTRTPLKGP
PGVELKPRRF VRRTIDLQDF KSVKNAMQCT INDVVLGVTQ AGLSRYLNRR YGDLQKYNGA
TDLEKKNYLP KNIRLRATFF FNLRASTKIN AVVPDAVEEG AKTAKFGNKI GYVILPFNIG
IQADPLDYIW QAKAVIDRKK ASLEPLFTYL FLKLVIKFFG VKTAGVFCHK IFFNTTLWFS
NVPGPQEEIA FDGHPVAFTA CSCYGQPNAL MIHVISYTDK ITFVLSVDED TIPDPHRLCD
DLEESLKLIK AAAVPS
//