PDAT1_ARATH
ID PDAT1_ARATH Reviewed; 671 AA.
AC Q9FNA9; Q6YC80;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Phospholipid:diacylglycerol acyltransferase 1;
DE Short=AtPDAT;
DE EC=2.3.1.158 {ECO:0000250|UniProtKB:O94680};
GN Name=PDAT1; Synonyms=PDAT; OrderedLocusNames=At5g13640;
GN ORFNames=MSH12.10, T6I14.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15355352; DOI=10.1111/j.1432-1033.2004.04317.x;
RA Noiriel A., Benveniste P., Banas A., Stymne S., Bouvier-Nave P.;
RT "Expression in yeast of a novel phospholipase A1 cDNA from Arabidopsis
RT thaliana.";
RL Eur. J. Biochem. 271:3752-3764(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15247387; DOI=10.1104/pp.104.044354;
RA Stahl U., Carlsson A.S., Lenman M., Dahlqvist A., Huang B., Banas W.,
RA Banas A., Stymne S.;
RT "Cloning and functional characterization of a phospholipid:diacylglycerol
RT acyltransferase from Arabidopsis.";
RL Plant Physiol. 135:1324-1335(2004).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=15907694; DOI=10.1016/j.plaphy.2005.01.013;
RA Mhaske V., Beldjilali K., Ohlrogge J., Pollard M.;
RT "Isolation and characterization of an Arabidopsis thaliana knockout line
RT for phospholipid: diacylglycerol transacylase gene (At5g13640).";
RL Plant Physiol. Biochem. 43:413-417(2005).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20040537; DOI=10.1105/tpc.109.071795;
RA Zhang M., Fan J., Taylor D.C., Ohlrogge J.B.;
RT "DGAT1 and PDAT1 acyltransferases have overlapping functions in Arabidopsis
RT triacylglycerol biosynthesis and are essential for normal pollen and seed
RT development.";
RL Plant Cell 21:3885-3901(2009).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20101470; DOI=10.1007/s11745-010-3385-4;
RA Li R., Yu K., Hildebrand D.F.;
RT "DGAT1, DGAT2 and PDAT expression in seeds and other tissues of epoxy and
RT hydroxy fatty acid accumulating plants.";
RL Lipids 45:145-157(2010).
CC -!- FUNCTION: Triacylglycerol formation by an acyl-CoA independent pathway.
CC The enzyme preferentially transfers acyl groups from the sn-2 position
CC of a phospholipid to diacylglycerol, thus forming an sn-1-
CC lysophospholipid. Involved in epoxy and hydroxy fatty acid accumulation
CC in seeds. Has complementary functions with DAG1 that are essential for
CC triacylglycerol synthesis and normal development of both seeds and
CC pollen. {ECO:0000269|PubMed:15247387, ECO:0000269|PubMed:20040537,
CC ECO:0000269|PubMed:20101470}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + a glycerophospholipid = a
CC monoacylglycerophospholipid + a triacyl-sn-glycerol;
CC Xref=Rhea:RHEA:14057, ChEBI:CHEBI:17815, ChEBI:CHEBI:64615,
CC ChEBI:CHEBI:136912, ChEBI:CHEBI:136913; EC=2.3.1.158;
CC Evidence={ECO:0000250|UniProtKB:O94680};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in young developing
CC seeds. {ECO:0000269|PubMed:15247387, ECO:0000269|PubMed:20040537,
CC ECO:0000269|PubMed:20101470}.
CC -!- DEVELOPMENTAL STAGE: Peak of expression in seeds 9 days after
CC flowering. {ECO:0000269|PubMed:20101470}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. No changes in the fatty
CC acid content and composition of seeds. Dgat1 and pdat1 double mutants
CC produce sterile deformed pollen. {ECO:0000269|PubMed:15907694,
CC ECO:0000269|PubMed:20040537}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO17787.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO17787.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY160110; AAO17787.1; ALT_SEQ; mRNA.
DR EMBL; AB006704; BAB08690.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91921.1; -; Genomic_DNA.
DR EMBL; AY052715; AAK96619.1; -; mRNA.
DR RefSeq; NP_196868.1; NM_121367.3.
DR AlphaFoldDB; Q9FNA9; -.
DR STRING; 3702.AT5G13640.1; -.
DR ESTHER; arath-At5g13640; PC-sterol_acyltransferase.
DR iPTMnet; Q9FNA9; -.
DR PaxDb; Q9FNA9; -.
DR PRIDE; Q9FNA9; -.
DR ProteomicsDB; 236715; -.
DR EnsemblPlants; AT5G13640.1; AT5G13640.1; AT5G13640.
DR GeneID; 831208; -.
DR Gramene; AT5G13640.1; AT5G13640.1; AT5G13640.
DR KEGG; ath:AT5G13640; -.
DR Araport; AT5G13640; -.
DR TAIR; locus:2173244; AT5G13640.
DR eggNOG; KOG2369; Eukaryota.
DR HOGENOM; CLU_016065_1_0_1; -.
DR InParanoid; Q9FNA9; -.
DR OrthoDB; 828056at2759; -.
DR PhylomeDB; Q9FNA9; -.
DR BioCyc; ARA:AT5G13640-MON; -.
DR BioCyc; MetaCyc:AT5G13640-MON; -.
DR BRENDA; 2.3.1.158; 399.
DR BRENDA; 2.3.1.20; 399.
DR UniPathway; UPA00282; -.
DR PRO; PR:Q9FNA9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNA9; baseline and differential.
DR Genevisible; Q9FNA9; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0046027; F:phospholipid:diacylglycerol acyltransferase activity; IDA:TAIR.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IGI:TAIR.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR Pfam; PF02450; LCAT; 2.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Glycerol metabolism; Glycoprotein; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..671
FT /note="Phospholipid:diacylglycerol acyltransferase 1"
FT /id="PRO_0000398611"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..671
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 254
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255"
FT ACT_SITE 573
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 626
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 378
FT /note="Q -> H (in Ref. 2; AAO17787)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 671 AA; 74157 MW; ACDF2E7AFD5D1B55 CRC64;
MPLIHRKKPT EKPSTPPSEE VVHDEDSQKK PHESSKSHHK KSNGGGKWSC IDSCCWFIGC
VCVTWWFLLF LYNAMPASFP QYVTERITGP LPDPPGVKLK KEGLKAKHPV VFIPGIVTGG
LELWEGKQCA DGLFRKRLWG GTFGEVYKRP LCWVEHMSLD NETGLDPAGI RVRAVSGLVA
ADYFAPGYFV WAVLIANLAH IGYEEKNMYM AAYDWRLSFQ NTEVRDQTLS RMKSNIELMV
STNGGKKAVI VPHSMGVLYF LHFMKWVEAP APLGGGGGPD WCAKYIKAVM NIGGPFLGVP
KAVAGLFSAE AKDVAVARAI APGFLDTDIF RLQTLQHVMR MTRTWDSTMS MLPKGGDTIW
GGLDWSPEKG HTCCGKKQKN NETCGEAGEN GVSKKSPVNY GRMISFGKEV AEAAPSEINN
IDFRGAVKGQ SIPNHTCRDV WTEYHDMGIA GIKAIAEYKV YTAGEAIDLL HYVAPKMMAR
GAAHFSYGIA DDLDDTKYQD PKYWSNPLET KLPNAPEMEI YSLYGVGIPT ERAYVYKLNQ
SPDSCIPFQI FTSAHEEDED SCLKAGVYNV DGDETVPVLS AGYMCAKAWR GKTRFNPSGI
KTYIREYNHS PPANLLEGRG TQSGAHVDIM GNFALIEDIM RVAAGGNGSD IGHDQVHSGI
FEWSERIDLK L
