ID LPAT1_ARATH Reviewed; 356 AA.
AC Q8GXU8; Q9M0A2;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic {ECO:0000305};
DE EC=2.3.1.51 {ECO:0000269|PubMed:14976237};
DE EC=2.3.1.n4 {ECO:0000269|PubMed:15169931};
DE AltName: Full=Lysophosphatidyl acyltransferase 1 {ECO:0000303|PubMed:14976237};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1995 {ECO:0000305};
DE Flags: Precursor;
GN Name=LPAT1 {ECO:0000305};
GN Synonyms=ATS2 {ECO:0000303|PubMed:15169931}, EMB1995 {ECO:0000305},
GN LPAAT1 {ECO:0000303|PubMed:14976237};
GN OrderedLocusNames=At4g30580 {ECO:0000312|Araport:AT4G30580};
GN ORFNames=F17I23.80 {ECO:0000312|EMBL:CAB79776.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 2).
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] (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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15169931; DOI=10.1093/pcp/pch064;
RA Yu B., Wakao S., Fan J., Benning C.;
RT "Loss of plastidic lysophosphatidic acid acyltransferase causes embryo-
RT lethality in Arabidopsis.";
RL Plant Cell Physiol. 45:503-510(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14976237; DOI=10.1104/pp.103.035832;
RA Kim H.U., Huang A.H.C.;
RT "Plastid lysophosphatidyl acyltransferase is essential for embryo
RT development in Arabidopsis.";
RL Plant Physiol. 134:1206-1216(2004).
RN [7]
RP MUTAGENESIS OF ALA-290.
RX PubMed=20488893; DOI=10.1104/pp.110.157982;
RA Kim H.U., Vijayan P., Carlsson A.S., Barkan L., Browse J.;
RT "A mutation in the LPAT1 gene suppresses the sensitivity of fab1 plants to
RT low temperature.";
RL Plant Physiol. 153:1135-1143(2010).
RN [8]
RP MUTAGENESIS OF PRO-230.
RX PubMed=26224803; DOI=10.1104/pp.15.00931;
RA Gao J., Wallis J.G., Browse J.;
RT "Mutations in the prokaryotic pathway rescue the fatty acid biosynthesis1
RT mutant in the cold.";
RL Plant Physiol. 169:442-452(2015).
CC -!- FUNCTION: Plastidial enzyme of the prokaryotic glycerol-3-phosphate
CC pathway that converts lysophosphatidic acid (LPA) into phosphatidic
CC acid by incorporating an acyl moiety at position sn-2
CC (PubMed:15169931). Utilizes palmitoyl-ACP (16:0-ACP) to produce
CC phosphatidic acid containing a saturated group at position sn-2, which
CC is characteristic of lipids synthesized by the prokaryotic pathway
CC (PubMed:15169931). In vitro, can use 16:0-CoA as acyl donor
CC (PubMed:14976237). Essential for embryo development during the
CC transition from the globular to the heart stage when chloroplasts begin
CC to form (PubMed:15169931, PubMed:14976237).
CC {ECO:0000269|PubMed:14976237, ECO:0000269|PubMed:15169931}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + a fatty acyl-[ACP] = a 1,2-
CC diacyl-sn-glycero-3-phosphate + holo-[ACP]; Xref=Rhea:RHEA:42296,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:57970,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:64479, ChEBI:CHEBI:138651;
CC EC=2.3.1.n4; Evidence={ECO:0000269|PubMed:15169931};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42297;
CC Evidence={ECO:0000305};
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:14976237};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:15169931}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GXU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GXU8-2; Sequence=VSP_013594;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC leaves. Expressed at lower level in silique walls compared to leaves.
CC {ECO:0000269|PubMed:14976237, ECO:0000269|PubMed:15169931}.
CC -!- DEVELOPMENTAL STAGE: Expression transiently increases in siliques 4
CC hours after flowering. {ECO:0000269|PubMed:15169931}.
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-phosphate. {ECO:0000250|UniProtKB:Q9D517}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality due to embryo development
CC arrest at globular stage. {ECO:0000269|PubMed:14976237,
CC ECO:0000269|PubMed:15169931}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; AL161577; CAB79776.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85783.1; -; Genomic_DNA.
DR EMBL; AY136460; AAM97125.1; -; mRNA.
DR EMBL; BT006253; AAP13361.1; -; mRNA.
DR EMBL; AK118028; BAC42660.1; -; mRNA.
DR PIR; G85357; G85357.
DR RefSeq; NP_194787.2; NM_119204.4. [Q8GXU8-1]
DR AlphaFoldDB; Q8GXU8; -.
DR SMR; Q8GXU8; -.
DR BioGRID; 14468; 1.
DR STRING; 3702.Q8GXU8; -.
DR PaxDb; 3702-AT4G30580-1; -.
DR ProteomicsDB; 238444; -. [Q8GXU8-1]
DR EnsemblPlants; AT4G30580.1; AT4G30580.1; AT4G30580. [Q8GXU8-1]
DR GeneID; 829181; -.
DR Gramene; AT4G30580.1; AT4G30580.1; AT4G30580. [Q8GXU8-1]
DR KEGG; ath:AT4G30580; -.
DR Araport; AT4G30580; -.
DR TAIR; AT4G30580; ATS2.
DR eggNOG; KOG2848; Eukaryota.
DR HOGENOM; CLU_027938_1_0_1; -.
DR InParanoid; Q8GXU8; -.
DR OMA; YAITAFN; -.
DR OrthoDB; 52351at2759; -.
DR PhylomeDB; Q8GXU8; -.
DR BioCyc; MetaCyc:AT4G30580-MONOMER; -.
DR BRENDA; 2.3.1.51; 399.
DR UniPathway; UPA00557; UER00613.
DR PRO; PR:Q8GXU8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GXU8; baseline and differential.
DR Genevisible; Q8GXU8; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IMP:TAIR.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR00530; AGP_acyltrn; 1.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Chloroplast; Developmental protein;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Plastid; Reference proteome; Transferase;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..356
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
FT LPAT1, chloroplastic"
FT /id="PRO_0000024701"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 202..207
FT /note="HXXXXD motif"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_013594"
FT MUTAGEN 230
FT /note="P->L: In lpat1-4; suppression of the sensitivity of
FT fab1 mutant plants to low temperature."
FT /evidence="ECO:0000269|PubMed:26224803"
FT MUTAGEN 290
FT /note="A->T: In lpat1-3; suppression of the sensitivity of
FT fab1 mutant plants to low temperature."
FT /evidence="ECO:0000269|PubMed:20488893"
SQ SEQUENCE 356 AA; 39395 MW; 27A9EB5EBE028940 CRC64;
MDVASARSIS SHPSYYGKPI CSSQSSLIRI SRDKVCCFGR ISNGMTSFTT SLHAVPSEKF
MGETRRTGIQ WSNRSLRHDP YRFLDKKSPR SSQLARDITV RADLSGAATP DSSFPEPEIK
LSSRLRGIFF CVVAGISATF LIVLMIIGHP FVLLFDPYRR KFHHFIAKLW ASISIYPFYK
INIEGLENLP SSDTPAVYVS NHQSFLDIYT LLSLGKSFKF ISKTGIFVIP IIGWAMSMMG
VVPLKRMDPR SQVDCLKRCM ELLKKGASVF FFPEGTRSKD GRLGSFKKGA FTVAAKTGVA
VVPITLMGTG KIMPTGSEGI LNHGNVRVII HKPIHGSKAD VLCNEARSKI AESMDL
//
