ID D7LSF4_ARALL Unreviewed; 521 AA.
AC D7LSF4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Condensation domain-containing protein {ECO:0000313|EMBL:EFH53914.1};
GN ORFNames=ARALYDRAFT_485277 {ECO:0000313|EMBL:EFH53914.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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 EMBL; GL348717; EFH53914.1; -; Genomic_DNA.
DR RefSeq; XP_002877655.1; XM_002877609.1.
DR AlphaFoldDB; D7LSF4; -.
DR STRING; 81972.D7LSF4; -.
DR EnsemblPlants; fgenesh2_kg.5__1269__AT3G49190.1; fgenesh2_kg.5__1269__AT3G49190.1; fgenesh2_kg.5__1269__AT3G49190.1.
DR Gramene; fgenesh2_kg.5__1269__AT3G49190.1; fgenesh2_kg.5__1269__AT3G49190.1; fgenesh2_kg.5__1269__AT3G49190.1.
DR eggNOG; ENOG502QTZ2; Eukaryota.
DR HOGENOM; CLU_027831_0_0_1; -.
DR OrthoDB; 2957273at2759; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
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:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
DR GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
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:SF69; WAX ESTER SYNTHASE_DIACYLGLYCEROL ACYLTRANSFERASE 4-RELATED; 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|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 108..277
FT /note="O-acyltransferase WSD1-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03007"
FT DOMAIN 340..484
FT /note="O-acyltransferase WSD1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06974"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 59618 MW; 24729E6FBAE55968 CRC64;
MEIKTQRHIS ENEKEEEQPL SPAARLFHSP EFNCNIISVI GLKSKLDPCV IIRGFKETFI
RHPRFSSKLV TDENGQNQRW VRTNVVVEDH VIVPEIKLQN IENTDSFLED YVSDLMKIPL
DISRPLWELH LLDLKTSDAE NVAVLKIHHS VGDGMSIMSL VLACMRKTSN PDELPSLPYQ
YRSSSGSSLL TTGSRSDSRL LWLVKVLWTA VILGLNTICD TLEFIVTTLF VKDTETPIKG
DFRSTKSKRL RLVHRTVSLD DIKLIKNAMN MTVNDVVLGV TQASLSQYLE RRYGERETKR
KRKNLPKRIR LRSALLVNLR PTTGIQDIAD MMENGSKCRW GNWFGYIVFP FSIALRDDPL
EHLKRAQKII TRKKNSFGAM LTYIFCRIIV KFLGIQLAAT IINRMVSNTT MTFSNMVGPV
EQVSFYGHPI TYFASSGYGH PHALTINCQS YMNKMTITLI VDSTVISDPH RLCDDWQESL
RSIKAAVQKR GSLGLWDYLR LLSNRMAWLL YQMAGLLYKM L
//
