ID F6I6D6_VITVI Unreviewed; 510 AA.
AC F6I6D6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCB62532.1};
GN OrderedLocusNames=VIT_15s0046g00590 {ECO:0000313|EMBL:CCB62532.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB62532.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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: Belongs to the long-chain O-acyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009587}.
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 EMBL; FN596755; CCB62532.1; -; Genomic_DNA.
DR RefSeq; XP_010661940.1; XM_010663638.2.
DR AlphaFoldDB; F6I6D6; -.
DR STRING; 29760.F6I6D6; -.
DR PaxDb; 29760-VIT_15s0046g00590-t01; -.
DR GeneID; 100852926; -.
DR KEGG; vvi:100852926; -.
DR eggNOG; ENOG502QTZ2; Eukaryota.
DR HOGENOM; CLU_027831_0_0_1; -.
DR InParanoid; F6I6D6; -.
DR OrthoDB; 2957273at2759; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000009183; Chromosome 15.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR InterPro; IPR045034; O-acyltransferase_WSD1-like.
DR InterPro; IPR009721; O-acyltransferase_WSD1_C.
DR InterPro; IPR004255; O-acyltransferase_WSD1_N.
DR PANTHER; PTHR31650:SF1; DIACYGLYCEROL O-ACYLTRANSFERASE TGS4-RELATED; 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 Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 78..290
FT /note="O-acyltransferase WSD1-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03007"
FT DOMAIN 357..500
FT /note="O-acyltransferase WSD1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06974"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 57625 MW; BFFCBC8F446F9BC2 CRC64;
MEPVGDLDSR QQALKPIQTK RSAAREVEGD GKKPEDIKEE EEGEALSPVG RIFHETCFNV
YVIAIAGFKI RINVDVVKAN LEHTLLKHPR FSSLQVKDVK KDGGMKWVPT KVDLDKHIII
PSLHHTISSP DKMVEDYISN LSKTYIDYSK PLWELHILNI KTSDAESVAV FRIHHSLGDG
MSLMSLVLAC SRQISNPKAL PTLPVKKTSN PDPVKSGRIW WTIRLVWNTI IDVLMFLATT
LFLKDTMTPL SNGWKKGGGH VPRRFVYRTV SLDDIKLIKN GMKTTINDVV MGVSLAGLSR
YLNRRYGETK EDKGATQKKN NLPKNIRLRA TLMMNIRPSP GLHALAEMME KGSKAKWGNW
IGSMLLPFVI ALYDDPLDYV RQTKATIDRK KHSHEAIFTC FIIKTVLKLF GAKVAAFLYH
RVMNHTTMCF SNVVGPMEEI GFYGHPMAFL APSVYGQPQG LMIHFQSYIN KMTFILSVDE
EIIPDPNQLC DDLEESLKFI KDAVIARDLV
//
