LPP3_ARATH
ID LPP3_ARATH Reviewed; 364 AA.
AC Q8LFD1; A8MR10; Q9M882;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Putative lipid phosphate phosphatase 3, chloroplastic;
DE Short=AtLPP3;
DE EC=3.1.3.-;
DE AltName: Full=Phosphatidate phosphohydrolase 3;
DE AltName: Full=Phosphatidic acid phosphatase 3;
DE Flags: Precursor;
GN Name=LPP3; OrderedLocusNames=At3g02600; ORFNames=F16B3.23;
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.
RX PubMed=11278556; DOI=10.1074/jbc.m009726200;
RA Pierrugues O., Brutesco C., Oshiro J., Gouy M., Deveaux Y., Carman G.M.,
RA Thuriaux P., Kazmaier M.;
RT "Lipid phosphate phosphatases in Arabidopsis. Regulation of the AtLPP1 gene
RT in response to stress.";
RL J. Biol. Chem. 276:20300-20308(2001).
RN [2]
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 [3]
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 [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.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LFD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LFD1-2; Sequence=VSP_053602;
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF32467.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC021640; AAF32467.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73834.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73835.1; -; Genomic_DNA.
DR EMBL; AY084915; AAM61477.1; -; mRNA.
DR RefSeq; NP_001078095.1; NM_001084626.2. [Q8LFD1-2]
DR RefSeq; NP_001078096.1; NM_001084627.1.
DR RefSeq; NP_001078097.1; NM_001084628.2.
DR RefSeq; NP_001078098.1; NM_001084629.2.
DR RefSeq; NP_001319453.1; NM_001337421.1.
DR RefSeq; NP_001327797.1; NM_001337423.1.
DR RefSeq; NP_001327798.1; NM_001337424.1.
DR RefSeq; NP_001327799.1; NM_001337425.1.
DR RefSeq; NP_001327800.1; NM_001337422.1.
DR RefSeq; NP_001327801.1; NM_001337419.1.
DR RefSeq; NP_001327802.1; NM_001337420.1.
DR RefSeq; NP_566177.1; NM_111128.2. [Q8LFD1-1]
DR AlphaFoldDB; Q8LFD1; -.
DR STRING; 3702.AT3G02600.1; -.
DR iPTMnet; Q8LFD1; -.
DR SwissPalm; Q8LFD1; -.
DR PaxDb; Q8LFD1; -.
DR PRIDE; Q8LFD1; -.
DR ProteomicsDB; 238423; -. [Q8LFD1-1]
DR EnsemblPlants; AT3G02600.1; AT3G02600.1; AT3G02600. [Q8LFD1-1]
DR EnsemblPlants; AT3G02600.2; AT3G02600.2; AT3G02600. [Q8LFD1-2]
DR GeneID; 821299; -.
DR Gramene; AT3G02600.1; AT3G02600.1; AT3G02600. [Q8LFD1-1]
DR Gramene; AT3G02600.2; AT3G02600.2; AT3G02600. [Q8LFD1-2]
DR KEGG; ath:AT3G02600; -.
DR Araport; AT3G02600; -.
DR TAIR; locus:2076919; AT3G02600.
DR eggNOG; KOG3030; Eukaryota.
DR InParanoid; Q8LFD1; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q8LFD1; -.
DR PRO; PR:Q8LFD1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LFD1; baseline and differential.
DR Genevisible; Q8LFD1; AT.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; ISS:TAIR.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:TAIR.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; PTHR10165; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chloroplast; Hydrolase; Membrane; Plastid;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..364
FT /note="Putative lipid phosphate phosphatase 3,
FT chloroplastic"
FT /id="PRO_0000025414"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 18..48
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053602"
SQ SEQUENCE 364 AA; 40775 MW; 905F149C235E4A18 CRC64;
MARFSFPCFP NFGGFNQAVT NRGPEISETA DNWVSPSDIP LIEPNSKEHR MREAQLGGHT
LRSHGMTVAR THMHDWIILV LLVILECVLL IIHPFYRFVG KDMMTDLSYP LKSNTVPIWS
VPVYAMLLPL VIFIFIYFRR RDVYDLHHAV LGLLYSVLVT AVLTDAIKNA VGRPRPDFFW
RCFPDGKALY DSLGDVICHG DKSVIREGHK SFPSGHTSWS FSGLGFLSLY LSGKIQAFDG
KGHVAKLCIV ILPLLFAALV GISRVDDYWH HWQDVFAGGL LGLAISTICY LQFFPPPYHT
EGWGPYAYFQ VLEAARVQGA ANGAVQQPPP QVNNGEEEDG GFMGLHLVDN PTMRREEDVE
TGRG
