LPPE1_ARATH
ID LPPE1_ARATH Reviewed; 279 AA.
AC F4J220; Q9SVK7;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Lipid phosphate phosphatase epsilon 1, chloroplastic;
DE Short=AtLPPE1;
DE EC=3.1.3.-;
DE AltName: Full=Phosphatidic acid phosphatase epsilon 1;
DE AltName: Full=Plastidic phosphatidic acid phosphatase epsilon 1;
DE Flags: Precursor;
GN Name=LPPE1; OrderedLocusNames=At3g50920; ORFNames=F18B3.200;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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 FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17652095; DOI=10.1074/jbc.m704385200;
RA Nakamura Y., Tsuchiya M., Ohta H.;
RT "Plastidic phosphatidic acid phosphatases identified in a distinct
RT subfamily of lipid phosphate phosphatases with prokaryotic origin.";
RL J. Biol. Chem. 282:29013-29021(2007).
CC -!- FUNCTION: Exhibits phosphatidate phosphatase (PAP) activity in vitro.
CC May play a secondary role as PAP in plastids.
CC {ECO:0000269|PubMed:17652095}.
CC -!- ACTIVITY REGULATION: Inhibited by Mg(2+).
CC {ECO:0000269|PubMed:17652095}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:17652095};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000305|PubMed:17652095}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:17652095}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4J220-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4J220-2; Sequence=VSP_053603;
CC -!- TISSUE SPECIFICITY: Expressed in root tips, root branch points,
CC cotyledons and leaves. {ECO:0000269|PubMed:17652095}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:17652095}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; AL049862; CAB42921.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78725.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78726.1; -; Genomic_DNA.
DR EMBL; BT010900; AAR24678.1; -; mRNA.
DR EMBL; AK176736; BAD44499.1; -; mRNA.
DR PIR; T08413; T08413.
DR RefSeq; NP_001030835.1; NM_001035758.3. [F4J220-2]
DR RefSeq; NP_190661.2; NM_114952.4. [F4J220-1]
DR AlphaFoldDB; F4J220; -.
DR SMR; F4J220; -.
DR BioGRID; 9574; 8.
DR IntAct; F4J220; 8.
DR STRING; 3702.AT3G50920.1; -.
DR iPTMnet; F4J220; -.
DR PaxDb; F4J220; -.
DR PRIDE; F4J220; -.
DR ProteomicsDB; 238794; -. [F4J220-1]
DR EnsemblPlants; AT3G50920.1; AT3G50920.1; AT3G50920. [F4J220-1]
DR EnsemblPlants; AT3G50920.2; AT3G50920.2; AT3G50920. [F4J220-2]
DR GeneID; 824256; -.
DR Gramene; AT3G50920.1; AT3G50920.1; AT3G50920. [F4J220-1]
DR Gramene; AT3G50920.2; AT3G50920.2; AT3G50920. [F4J220-2]
DR KEGG; ath:AT3G50920; -.
DR Araport; AT3G50920; -.
DR TAIR; locus:2077987; AT3G50920.
DR eggNOG; KOG3146; Eukaryota.
DR InParanoid; F4J220; -.
DR OMA; WLGINEI; -.
DR OrthoDB; 1312138at2759; -.
DR PhylomeDB; F4J220; -.
DR PRO; PR:F4J220; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J220; baseline and differential.
DR Genevisible; F4J220; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0047874; F:dolichyldiphosphatase activity; IBA:GO_Central.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:TAIR.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; IDA:TAIR.
DR GO; GO:0008610; P:lipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR CDD; cd03382; PAP2_dolichyldiphosphatase; 1.
DR InterPro; IPR039667; Dolichyldiphosphatase_PAP2.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Hydrolase; Membrane; Plastid;
KW Plastid inner membrane; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..88
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 89..279
FT /note="Lipid phosphate phosphatase epsilon 1,
FT chloroplastic"
FT /id="PRO_0000425227"
FT TRANSMEM 126..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT /id="VSP_053603"
SQ SEQUENCE 279 AA; 30595 MW; 25569B3300D396D1 CRC64;
MAASSSLLLL LHCPTCNFYF DSSSYLKRSR LSSYSSIISR GSPLFVSSFG SMTVKRFSSR
VGSRSNDGNE QFGALEQESF INNSSEIRKD LVTGGGIEAI VNRLSKWVVS VLFGSIILLR
HDGAALWAVI GSISNSALSV VLKRILNQER PTTTLRSDPG MPSSHAQSIS FISVFAVLSV
MEWLGTNGVS LFLSGLILAL GSYFIRLRVS QKLHTSSQVV VGAIVGSLFC ILWYTMWNSL
LREAFEASLL VQISVFLFAA TFALAFAAYV VLNWFKDER
