ID   PDAT2_ARATH             Reviewed;         665 AA.
AC   Q9FYC7;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Putative phospholipid:diacylglycerol acyltransferase 2;
DE            Short=AtPDAT2;
DE            EC=2.3.1.158 {ECO:0000250|UniProtKB:O94680};
GN   Name=PDAT2; OrderedLocusNames=At3g44830; ORFNames=F28D10.20;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
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   [3]
RP   GENE FAMILY, AND NOMENCLATURE.
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   [4]
RP   GENE FAMILY.
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).
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AL391254; CAC03533.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77959.1; -; Genomic_DNA.
DR   PIR; T51780; T51780.
DR   RefSeq; NP_190069.1; NM_114352.2.
DR   AlphaFoldDB; Q9FYC7; -.
DR   STRING; 3702.AT3G44830.1; -.
DR   ESTHER; arath-PDAT2; PC-sterol_acyltransferase.
DR   PaxDb; Q9FYC7; -.
DR   PRIDE; Q9FYC7; -.
DR   ProteomicsDB; 236288; -.
DR   EnsemblPlants; AT3G44830.1; AT3G44830.1; AT3G44830.
DR   GeneID; 823617; -.
DR   Gramene; AT3G44830.1; AT3G44830.1; AT3G44830.
DR   KEGG; ath:AT3G44830; -.
DR   Araport; AT3G44830; -.
DR   TAIR; locus:2082147; AT3G44830.
DR   eggNOG; KOG2369; Eukaryota.
DR   HOGENOM; CLU_016065_1_0_1; -.
DR   InParanoid; Q9FYC7; -.
DR   OMA; WLIGYLC; -.
DR   OrthoDB; 828056at2759; -.
DR   PhylomeDB; Q9FYC7; -.
DR   BioCyc; ARA:AT3G44830-MON; -.
DR   BRENDA; 2.3.1.158; 399.
DR   PRO; PR:Q9FYC7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9FYC7; baseline and differential.
DR   Genevisible; Q9FYC7; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0046027; F:phospholipid:diacylglycerol acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR   Pfam; PF02450; LCAT; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Glycerol metabolism; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..665
FT                   /note="Putative phospholipid:diacylglycerol acyltransferase
FT                   2"
FT                   /id="PRO_0000398612"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        237
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        567
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        620
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   665 AA;  73653 MW;  3F63789FC1AEB8AF CRC64;
     MSPLLRFRKL SSFSEDTINP KPKQSATVEK PKRRRSGRCS CVDSCCWLIG YLCTAWWLLL
     FLYHSVPVPA MLQAPESPGT RLSRDGVKAF HPVILVPGIV TGGLELWEGR PCAEGLFRKR
     LWGASFSEIL RRPLCWLEHL SLDSETGLDP SGIRVRAVPG LVAADYFAPC YFAWAVLIEN
     LAKIGYEGKN LHMASYDWRL SFHNTEVRDQ SLSRLKSKIE LMYATNGFKK VVVVPHSMGA
     IYFLHFLKWV ETPLPDGGGG GGPGWCAKHI KSVVNIGPAF LGVPKAVSNL LSAEGKDIAY
     ARSLAPGLLD SELLKLQTLE HLMRMSHSWD SIVSLLPKGG EAIWGDLDSH AEEGLNCIYS
     KRKSSQLSLS NLHKQNYSLK PVSRVKEPAK YGRIVSFGKR ASELPSSQLS TLNVKELSRV
     DGNSNDSTSC GEFWSEYNEM SRESIVKVAE NTAYTATTVL DLLRFIAPKM MRRAEAHFSH
     GIADDLDDPK YGHYKYWSNP LETKLPEAPE MEMYCLYGVG IPTERSYIYK LATSSGKCKS
     SIPFRIDGSL DGDDVCLKGG TRFADGDESV PVISAGFMCA KGWRGKTRFN PSGMDTFLRE
     YKHKPPGSLL ESRGTESGAH VDIMGNVGLI EDVLRIAAGA SGQEIGGDRI YSDVMRMSER
     ISIKL