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Database: UniProt
Entry: A0A165WX68_DAUCS
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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
//
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