LPCT1_ARATH
ID LPCT1_ARATH Reviewed; 398 AA.
AC Q8L7R3; Q8LG31; Q9SAG5;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Lysophospholipid acyltransferase LPEAT1 {ECO:0000303|PubMed:19445718};
DE EC=2.3.1.23 {ECO:0000269|PubMed:19445718, ECO:0000269|PubMed:28408542};
DE EC=2.3.1.51 {ECO:0000269|PubMed:19445718};
DE EC=2.3.1.n6 {ECO:0000269|PubMed:19445718};
DE EC=2.3.1.n7 {ECO:0000269|PubMed:19445718, ECO:0000269|PubMed:28408542};
DE AltName: Full=Lysophosphatidylethanolamine acyltransferase 1 {ECO:0000303|PubMed:19445718};
DE Short=AtLPEAT1 {ECO:0000303|PubMed:19445718};
GN Name=LPEAT1 {ECO:0000303|PubMed:19445718};
GN OrderedLocusNames=At1g80950 {ECO:0000312|Araport:AT1G80950};
GN ORFNames=F23A5.31 {ECO:0000312|EMBL:AAF14683.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=19445718; DOI=10.1186/1471-2229-9-60;
RA Staalberg K., Staahl U., Stymne S., Ohlrogge J.;
RT "Characterization of two Arabidopsis thaliana acyltransferases with
RT preference for lysophosphatidylethanolamine.";
RL BMC Plant Biol. 9:60-60(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=22923678; DOI=10.1104/pp.112.204263;
RA Nikolovski N., Rubtsov D., Segura M.P., Miles G.P., Stevens T.J.,
RA Dunkley T.P., Munro S., Lilley K.S., Dupree P.;
RT "Putative glycosyltransferases and other plant Golgi apparatus proteins are
RT revealed by LOPIT proteomics.";
RL Plant Physiol. 160:1037-1051(2012).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28408542; DOI=10.1104/pp.17.00391;
RA Jasieniecka-Gazarkiewicz K., Lager I., Carlsson A.S., Gutbrod K.,
RA Peisker H., Doermann P., Stymne S., Banas A.;
RT "Acyl-CoA:lysophosphatidylethanolamine acyltransferase activity regulates
RT growth of Arabidopsis.";
RL Plant Physiol. 174:986-998(2017).
RN [11]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=33809440; DOI=10.3390/ijms22063006;
RA Jasieniecka-Gazarkiewicz K., Demski K., Gidda S.K., Klinska S.,
RA Niedojadlo J., Lager I., Carlsson A.S., Minina E.A., Mullen R.T.,
RA Bozhkov P.V., Stymne S., Banas A.;
RT "Subcellular localization of acyl-CoA: lysophosphatidylethanolamine
RT acyltransferases (LPEATs) and the effects of knocking-out and
RT overexpression of their genes on autophagy markers level and life span of
RT A. thaliana.";
RL Int. J. Mol. Sci. 22:0-0(2021).
CC -!- FUNCTION: Possesses acyl-CoA-dependent lysophospholipid acyltransferase
CC activity with a subset of lysophospholipids as substrates
CC (PubMed:19445718, PubMed:28408542). Exhibits strong acylation activity
CC on lysophosphatidylethanolamine (LPE) and lysophosphatidate (LPA), and
CC lower activity on lysophosphatidylcholine (LPC) and
CC lysophosphatidylserine (LPS) (PubMed:19445718). Exhibits acylation
CC activity on both LPE and LPC (PubMed:28408542). Has a preference for
CC 18:1-LPE over 16:0-LPE as acceptor (PubMed:19445718). Palmitoyl-CoA
CC (16:0-CoA) is a better acyl donor than oleoyl-CoA (18:1-CoA)
CC (PubMed:19445718, PubMed:28408542). Among several different acyl-CoA
CC species the best acyl donor is palmitoyl-CoA (16:0-CoA)
CC (PubMed:28408542). Activity is calcium-independent (PubMed:19445718).
CC Its activity is essential for maintaining adequate levels of
CC phosphatidylethanolamine (PE), LPE and LPC in the cells, which is
CC crucial for plant growth regulation (PubMed:28408542).
CC {ECO:0000269|PubMed:19445718, ECO:0000269|PubMed:28408542}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7;
CC Evidence={ECO:0000269|PubMed:19445718, ECO:0000269|PubMed:28408542};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000269|PubMed:19445718, ECO:0000269|PubMed:28408542};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000269|PubMed:19445718};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000269|PubMed:19445718};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000269|PubMed:19445718, ECO:0000269|PubMed:28408542};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000269|PubMed:19445718, ECO:0000269|PubMed:28408542};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:33191,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64379; EC=2.3.1.n6;
CC Evidence={ECO:0000269|PubMed:19445718};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33192;
CC Evidence={ECO:0000269|PubMed:19445718};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-9.0. {ECO:0000269|PubMed:19445718};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:33809440, ECO:0000305|PubMed:22923678}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphocholine. {ECO:0000250|UniProtKB:Q3TFD2}.
CC -!- DISRUPTION PHENOTYPE: Delayed senescence (PubMed:33809440). The double
CC mutants lpeat1 and lpeat2 exhibit impaired growth, small leaves, short
CC roots, reduced seed setting, reduced lipid content per fresh weight in
CC roots and seeds, and large increases in lysophosphatidylethanolamine
CC (LPE) and lysophosphatidylcholine (LPC) contents in leaves.
CC {ECO:0000269|PubMed:28408542, ECO:0000269|PubMed:33809440}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF14683.1; Type=Erroneous gene model prediction; 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; AC011713; AAF14683.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36471.1; -; Genomic_DNA.
DR EMBL; AY128312; AAM91515.1; -; mRNA.
DR EMBL; BT003346; AAO29964.1; -; mRNA.
DR EMBL; AY084489; AAM61059.1; -; mRNA.
DR PIR; E96842; E96842.
DR RefSeq; NP_565249.1; NM_106743.3.
DR AlphaFoldDB; Q8L7R3; -.
DR STRING; 3702.AT1G80950.1; -.
DR iPTMnet; Q8L7R3; -.
DR PaxDb; Q8L7R3; -.
DR PRIDE; Q8L7R3; -.
DR ProteomicsDB; 238774; -.
DR EnsemblPlants; AT1G80950.1; AT1G80950.1; AT1G80950.
DR GeneID; 844435; -.
DR Gramene; AT1G80950.1; AT1G80950.1; AT1G80950.
DR KEGG; ath:AT1G80950; -.
DR Araport; AT1G80950; -.
DR TAIR; locus:2025807; AT1G80950.
DR eggNOG; KOG4666; Eukaryota.
DR HOGENOM; CLU_042218_0_0_1; -.
DR InParanoid; Q8L7R3; -.
DR OrthoDB; 1266853at2759; -.
DR PhylomeDB; Q8L7R3; -.
DR BioCyc; ARA:AT1G80950-MON; -.
DR UniPathway; UPA00085; -.
DR PRO; PR:Q8L7R3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L7R3; baseline and differential.
DR Genevisible; Q8L7R3; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0047159; F:1-alkenylglycerophosphocholine O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0071618; F:lysophosphatidylethanolamine acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0050200; F:plasmalogen synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:TAIR.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..398
FT /note="Lysophospholipid acyltransferase LPEAT1"
FT /id="PRO_0000422378"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 194..199
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT CONFLICT 327
FT /note="V -> F (in Ref. 4; AAM61059)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 44713 MW; 38D88BBEFF822771 CRC64;
MESELKDLNS NSNPPSSKED RPLLKSESDL AAAIEELDKK FAPYARTDLY GTMGLGPFPM
TENIKLAVAL VTLVPLRFLL SMSILLLYYL ICRVFTLFSA PYRGPEEEED EGGVVFQEDY
AHMEGWKRTV IVRSGRFLSR VLLFVFGFYW IHESCPDRDS DMDSNPKTTS TEINQKGEAA
TEEPERPGAI VSNHVSYLDI LYHMSASFPS FVAKRSVGKL PLVGLISKCL GCVYVQREAK
SPDFKGVSGT VNERVREAHS NKSAPTIMLF PEGTTTNGDY LLTFKTGAFL AGTPVLPVIL
KYPYERFSVA WDTISGARHI LFLLCQVVNH LEVIRLPVYY PSQEEKDDPK LYASNVRKLM
ATEGNLILSE LGLSDKRIYH ATLNGNLSQT RDFHQKEE
