PDCT1_ARATH
ID PDCT1_ARATH Reviewed; 301 AA.
AC Q9LVZ7; Q94JW1;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Phosphatidylcholine:diacylglycerol cholinephosphotransferase 1 {ECO:0000305};
DE Short=AtPDCT1 {ECO:0000305};
DE EC=2.7.8.- {ECO:0000269|PubMed:19833868};
DE AltName: Full=Protein REDUCED OLEATE DESATURATION 1 {ECO:0000303|PubMed:19833868};
GN Name=ROD1 {ECO:0000303|PubMed:19833868};
GN OrderedLocusNames=At3g15820 {ECO:0000312|Araport:AT3G15820};
GN ORFNames=MSJ11.22 {ECO:0000312|EMBL:BAB02313.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=19833868; DOI=10.1073/pnas.0908848106;
RA Lu C., Xin Z., Ren Z., Miquel M., Browse J.;
RT "An enzyme regulating triacylglycerol composition is encoded by the ROD1
RT gene of Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:18837-18842(2009).
RN [6]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=22371508; DOI=10.1104/pp.111.192153;
RA Hu Z., Ren Z., Lu C.;
RT "The phosphatidylcholine diacylglycerol cholinephosphotransferase is
RT required for efficient hydroxy fatty acid accumulation in transgenic
RT Arabidopsis.";
RL Plant Physiol. 158:1944-1954(2012).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22932756; DOI=10.1104/pp.112.204438;
RA Bates P.D., Fatihi A., Snapp A.R., Carlsson A.S., Browse J., Lu C.;
RT "Acyl editing and headgroup exchange are the major mechanisms that direct
RT polyunsaturated fatty acid flux into triacylglycerols.";
RL Plant Physiol. 160:1530-1539(2012).
CC -!- FUNCTION: Functions as phosphatidylcholine:diacylglycerol
CC cholinephosphotransferase that catalyzes the transfer of the
CC phosphocholine headgroup from phosphatidylcholine (PC) to
CC diacylglycerol, a major reaction for the transfer of 18:1 into
CC phosphatidylcholine for desaturation and also for the reverse transfer
CC of 18:2 and 18:3 into the triacylglycerols synthesis pathway.
CC {ECO:0000269|PubMed:19833868, ECO:0000269|PubMed:22371508,
CC ECO:0000269|PubMed:22932756}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + 1,2-ditetradecanoyl-sn-
CC glycero-3-phosphocholine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1,2-ditetradecanoyl-sn-glycerol;
CC Xref=Rhea:RHEA:56412, ChEBI:CHEBI:45240, ChEBI:CHEBI:52333,
CC ChEBI:CHEBI:74669, ChEBI:CHEBI:80651;
CC Evidence={ECO:0000269|PubMed:19833868};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56413;
CC Evidence={ECO:0000269|PubMed:19833868};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=4.5 nmol/min/mg enzyme with phosphatidylcholine as substrate (at
CC 23 degrees Celsius) {ECO:0000269|PubMed:19833868};
CC pH dependence:
CC Optimum pH is 6.5-7 at 23 degrees Celsius.
CC {ECO:0000269|PubMed:19833868};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Reduction of 18:2 and 18:3 triacylglycerols (TAG)
CC accumulation in seeds by 40 percent. {ECO:0000269|PubMed:19833868,
CC ECO:0000269|PubMed:22932756}.
CC -!- SIMILARITY: Belongs to the phosphatidylcholine:diacylglycerol
CC cholinephosphotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK49592.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB017071; BAB02313.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75730.1; -; Genomic_DNA.
DR EMBL; AF372876; AAK49592.1; ALT_INIT; mRNA.
DR EMBL; BT004552; AAO42798.1; -; mRNA.
DR EMBL; AY086160; AAM63365.1; -; mRNA.
DR RefSeq; NP_566527.1; NM_112452.3.
DR AlphaFoldDB; Q9LVZ7; -.
DR BioGRID; 6159; 4.
DR IntAct; Q9LVZ7; 4.
DR STRING; 3702.AT3G15820.1; -.
DR SwissLipids; SLP:000001901; -.
DR iPTMnet; Q9LVZ7; -.
DR PaxDb; Q9LVZ7; -.
DR PRIDE; Q9LVZ7; -.
DR ProteomicsDB; 236719; -.
DR EnsemblPlants; AT3G15820.1; AT3G15820.1; AT3G15820.
DR GeneID; 820825; -.
DR Gramene; AT3G15820.1; AT3G15820.1; AT3G15820.
DR KEGG; ath:AT3G15820; -.
DR Araport; AT3G15820; -.
DR TAIR; locus:2093257; AT3G15820.
DR eggNOG; ENOG502QRYQ; Eukaryota.
DR HOGENOM; CLU_079484_0_0_1; -.
DR InParanoid; Q9LVZ7; -.
DR OMA; VAAMMMF; -.
DR OrthoDB; 895973at2759; -.
DR PhylomeDB; Q9LVZ7; -.
DR BioCyc; ARA:AT3G15820-MON; -.
DR BioCyc; MetaCyc:AT3G15820-MON; -.
DR PRO; PR:Q9LVZ7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LVZ7; baseline and differential.
DR Genevisible; Q9LVZ7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; IDA:TAIR.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IMP:TAIR.
PE 1: Evidence at protein level;
KW Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..301
FT /note="Phosphatidylcholine:diacylglycerol
FT cholinephosphotransferase 1"
FT /id="PRO_0000425110"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 216
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /evidence="ECO:0000250"
FT ACT_SITE 260
FT /evidence="ECO:0000250"
FT CONFLICT 1
FT /note="M -> I (in Ref. 3; AAK49592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 32977 MW; 4423EA943357E0DF CRC64;
MSAAAAETDV SLRRRSNSLN GNHTNGVAID GTLDNNNRRV GDTNTHMDIS AKKTDNGYAN
GVGGGGWRSK ASFTTWTARD IVYVVRYHWI PCMFAAGLLF FMGVEYTLQM IPARSEPFDL
GFVVTRSLNR VLASSPDLNT VLAALNTVFV GMQTTYIVWT WLVEGRARAT IAALFMFTCR
GILGYSTQLP LPQDFLGSGV DFPVGNVSFF LFFSGHVAGS MIASLDMRRM QRLRLAMVFD
ILNVLQSIRL LGTRGHYTID LAVGVGAGIL FDSLAGKYEE MMSKRHLGTG FSLISKDSLV
N
