LPCT2_ARATH
ID LPCT2_ARATH Reviewed; 539 AA.
AC Q8S8S2; O64646; Q8GY20;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Lysophospholipid acyltransferase LPEAT2 {ECO:0000303|PubMed:19445718};
DE EC=2.3.1.23 {ECO:0000269|PubMed:19445718, ECO:0000269|PubMed:28408542};
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 2 {ECO:0000303|PubMed:19445718};
DE Short=AtLPEAT2 {ECO:0000303|PubMed:19445718};
GN Name=LPEAT2 {ECO:0000303|PubMed:19445718};
GN OrderedLocusNames=At2g45670 {ECO:0000312|Araport:AT2G45670};
GN ORFNames=F17K2.20;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP ALTERNATIVE SPLICING.
RX PubMed=16098107; DOI=10.1111/j.1365-313x.2005.02473.x;
RA Hori K., Watanabe Y.;
RT "UPF3 suppresses aberrant spliced mRNA in Arabidopsis.";
RL Plant J. 43:530-540(2005).
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 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 [8]
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 lower activity on
CC lysophosphatidylcholine (LPC) and lysophosphatidylserine (LPS)
CC (PubMed:19445718). Exhibits acylation activity on both LPE and LPC
CC (PubMed:28408542). Has a preference for 18:1-LPE over 16:0-LPE as
CC acceptor (PubMed:19445718). Palmitoyl-CoA (16:0-CoA) is a better acyl
CC donor than oleoyl-CoA (18:1-CoA) (PubMed:19445718, PubMed:28408542).
CC Among several different acyl-CoA species the best acyl donor is
CC eicosanoyl-CoA (20:0-CoA) (PubMed:28408542). Activity is calcium-
CC independent (PubMed:19445718). Its activity is essential for
CC maintaining adequate levels of phosphatidylethanolamine (PE), LPE and
CC LPC in the cells, which is crucial for plant growth regulation
CC (PubMed:28408542). {ECO:0000269|PubMed:19445718,
CC 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-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 9.0. {ECO:0000269|PubMed:19445718};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:33809440}; Single-pass membrane protein
CC {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:33809440};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8S8S2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8S8S2-2; Sequence=VSP_046521, VSP_046522;
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 -!- MISCELLANEOUS: The ratio of isoform 2/isoform 1 mRNA is increased about
CC 15-fold in the nonsense mRNA reducing factor mutant upf3-1.
CC {ECO:0000305|PubMed:16098107}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; AC003680; AAC06169.1; -; Genomic_DNA.
DR EMBL; AC003680; AAM14898.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10584.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10585.1; -; Genomic_DNA.
DR EMBL; AK117916; BAC42554.1; -; mRNA.
DR EMBL; AK175608; BAD43371.1; -; mRNA.
DR EMBL; AK175656; BAD43419.1; -; mRNA.
DR EMBL; AK175838; BAD43601.1; -; mRNA.
DR EMBL; AK176251; BAD44014.1; -; mRNA.
DR EMBL; AK176419; BAD44182.1; -; mRNA.
DR EMBL; AK176460; BAD44223.1; -; mRNA.
DR PIR; T00880; T00880.
DR RefSeq; NP_566051.1; NM_130129.5. [Q8S8S2-1]
DR RefSeq; NP_566052.1; NM_130130.4. [Q8S8S2-2]
DR AlphaFoldDB; Q8S8S2; -.
DR SMR; Q8S8S2; -.
DR BioGRID; 4511; 10.
DR IntAct; Q8S8S2; 10.
DR STRING; 3702.AT2G45670.1; -.
DR PaxDb; Q8S8S2; -.
DR PRIDE; Q8S8S2; -.
DR ProteomicsDB; 238482; -. [Q8S8S2-1]
DR EnsemblPlants; AT2G45670.1; AT2G45670.1; AT2G45670. [Q8S8S2-1]
DR EnsemblPlants; AT2G45670.2; AT2G45670.2; AT2G45670. [Q8S8S2-2]
DR GeneID; 819175; -.
DR Gramene; AT2G45670.1; AT2G45670.1; AT2G45670. [Q8S8S2-1]
DR Gramene; AT2G45670.2; AT2G45670.2; AT2G45670. [Q8S8S2-2]
DR KEGG; ath:AT2G45670; -.
DR Araport; AT2G45670; -.
DR TAIR; locus:2043639; AT2G45670.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG2898; Eukaryota.
DR HOGENOM; CLU_025017_3_1_1; -.
DR InParanoid; Q8S8S2; -.
DR OMA; VQQTRMG; -.
DR PhylomeDB; Q8S8S2; -.
DR BioCyc; ARA:AT2G45670-MON; -.
DR BRENDA; 2.3.1.121; 399.
DR UniPathway; UPA00085; -.
DR PRO; PR:Q8S8S2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S8S2; baseline and differential.
DR Genevisible; Q8S8S2; AT.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
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:0005509; F:calcium ion binding; IEA:InterPro.
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; cd00051; EFh; 2.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Calcium; Endosome; Golgi apparatus;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..539
FT /note="Lysophospholipid acyltransferase LPEAT2"
FT /id="PRO_0000422379"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 426..455
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 457..492
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 493..528
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 178..183
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 481
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 506
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 508
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 510
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 512
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 517
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 236..281
FT /note="RKASCDRFPRLLLFPEGTTTNGKVLISFQLGAFIPGYPIQPVVVRY -> GC
FT KYREKLPAIDFLVCCYSPKEPRLMGKFLFPSNSVLSSLVTLFNL (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_046521"
FT VAR_SEQ 282..539
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_046522"
FT CONFLICT 233
FT /note="E -> G (in Ref. 3; BAC42554 and 4; BAD43371/
FT BAD43419/BAD43601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 61022 MW; 235A3D368725C5E8 CRC64;
MADPDLSSPL IHHQSSDQPE VVISIADDDD DESGLNLLPA VVDPRVSRGF EFDHLNPYGF
LSESEPPVLG PTTVDPFRNN TPGVSGLYEA IKLVICLPIA LIRLVLFAAS LAVGYLATKL
ALAGWKDKEN PMPLWRCRIM WITRICTRCI LFSFGYQWIR RKGKPARREI APIVVSNHVS
YIEPIFYFYE LSPTIVASES HDSLPFVGTI IRAMQVIYVN RFSQTSRKNA VHEIKRKASC
DRFPRLLLFP EGTTTNGKVL ISFQLGAFIP GYPIQPVVVR YPHVHFDQSW GNISLLTLMF
RMFTQFHNFM EVEYLPVIYP SEKQKQNAVR LSQKTSHAIA TSLNVVQTSH SFADLMLLNK
ATELKLENPS NYMVEMARVE SLFHVSSLEA TRFLDTFVSM IPDSSGRVRL HDFLRGLKLK
PCPLSKRIFE FIDVEKVGSI TFKQFLFASG HVLTQPLFKQ TCELAFSHCD ADGDGYITIQ
ELGEALKNTI PNLNKDEIRG MYHLLDDDQD QRISQNDLLS CLRRNPLLIA IFAPDLAPT
