LPP2_ARATH
ID LPP2_ARATH Reviewed; 290 AA.
AC Q9XI60;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Lipid phosphate phosphatase 2;
DE Short=AtLPP2;
DE EC=3.1.3.-;
DE AltName: Full=Phosphatidic acid phosphatase 2;
DE Short=AtPAP2;
DE AltName: Full=Prenyl diphosphate phosphatase;
GN Name=LPP2; Synonyms=PAP2; OrderedLocusNames=At1g15080; ORFNames=F9L1.2;
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 [MRNA], FUNCTION, ACTIVITY REGULATION, INDUCTION, AND
RP TISSUE SPECIFICITY.
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Tokuhiro K., Muramoto N., Yamada Y., Asami O., Hirai M., Obata S., Ohto C.,
RA Muramatsu M.;
RT "Prenyl alcohol production by overexpression of prenyl diphosphate
RT phosphatase in Yeast Saccharomyces cerevisiae.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Katagiri T., Shinozaki K.;
RT "A cDNA sequence encoding a phosphatidic acid phosphatase in Arabidopsis
RT thaliana.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15960620; DOI=10.1111/j.1365-313x.2005.02431.x;
RA Katagiri T., Ishiyama K., Kato T., Tabata S., Kobayashi M., Shinozaki K.;
RT "An important role of phosphatidic acid in ABA signaling during germination
RT in Arabidopsis thaliana.";
RL Plant J. 43:107-117(2005).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=21277215; DOI=10.1016/j.plaphy.2011.01.010;
RA Paradis S., Villasuso A.L., Aguayo S.S., Maldiney R., Habricot Y.,
RA Zalejski C., Machado E., Sotta B., Miginiac E., Jeannette E.;
RT "Arabidopsis thaliana lipid phosphate phosphatase 2 is involved in abscisic
RT acid signalling in leaves.";
RL Plant Physiol. Biochem. 49:357-362(2011).
CC -!- FUNCTION: May play a general 'housekeeping role' in lipid metabolism.
CC Exhibits both diacylglycerol pyrophosphate (DGPP) phosphatase and
CC phosphatidate (PA) phosphatase activities with no preference for either
CC substrate. May play a role downstream of the ABA signaling pathway
CC during seed germination and in stomatal movement in leaves.
CC {ECO:0000269|PubMed:11278556, ECO:0000269|PubMed:15960620,
CC ECO:0000269|PubMed:21277215}.
CC -!- ACTIVITY REGULATION: PA phosphatase activity not inhibited by N-
CC ethylmaleimide. {ECO:0000269|PubMed:11278556}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, buds, flowers
CC and siliques. {ECO:0000269|PubMed:11278556,
CC ECO:0000269|PubMed:15960620}.
CC -!- INDUCTION: Constitutively expressed. Not induced by stress, mastoparan
CC or hypersensitive response elicitor harpin. Down-regulated by ABA.
CC {ECO:0000269|PubMed:11278556, ECO:0000269|PubMed:21277215}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show hypersensitivity to ABA and
CC significant PA accumulation during seed germination.
CC {ECO:0000269|PubMed:15960620}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; AB053950; BAC41335.1; -; mRNA.
DR EMBL; AB061407; BAB47574.1; -; mRNA.
DR EMBL; AC007591; AAD39637.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29263.1; -; Genomic_DNA.
DR EMBL; BT003912; AAO41959.1; -; mRNA.
DR EMBL; BT004969; AAO50502.1; -; mRNA.
DR EMBL; AY087673; AAM65210.1; -; mRNA.
DR PIR; E86284; E86284.
DR RefSeq; NP_172961.1; NM_101377.5.
DR AlphaFoldDB; Q9XI60; -.
DR BioGRID; 23312; 7.
DR IntAct; Q9XI60; 6.
DR STRING; 3702.AT1G15080.1; -.
DR PaxDb; Q9XI60; -.
DR PRIDE; Q9XI60; -.
DR ProteomicsDB; 238519; -.
DR EnsemblPlants; AT1G15080.1; AT1G15080.1; AT1G15080.
DR GeneID; 838072; -.
DR Gramene; AT1G15080.1; AT1G15080.1; AT1G15080.
DR KEGG; ath:AT1G15080; -.
DR Araport; AT1G15080; -.
DR TAIR; locus:2037758; AT1G15080.
DR eggNOG; KOG3030; Eukaryota.
DR HOGENOM; CLU_021458_5_1_1; -.
DR InParanoid; Q9XI60; -.
DR OMA; WFSYRRY; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q9XI60; -.
DR BioCyc; ARA:MON-AT1G15080; -.
DR BioCyc; MetaCyc:MON-AT1G15080; -.
DR PRO; PR:Q9XI60; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XI60; baseline and differential.
DR Genevisible; Q9XI60; AT.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:TAIR.
DR GO; GO:0003993; F:acid phosphatase activity; ISS:TAIR.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:TAIR.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
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 Glycoprotein; Hydrolase; Membrane; Reference proteome; Stress response;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..290
FT /note="Lipid phosphate phosphatase 2"
FT /id="PRO_0000220916"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 290 AA; 32702 MW; BF14A9A0C23B4429 CRC64;
MPEIHLGAHT IRSHGVTVAR FHMHDWLILL LLIVIEIVLN VIEPFHRFVG EDMLTDLRYP
LQDNTIPFWA VPLIAVVLPF AVICVYYFIR NDVYDLHHAI LGLLFSVLIT GVITDAIKDA
VGRPRPDFFW RCFPDGIGIF HNVTKNVLCT GAKDVVKEGH KSFPSGHTSW SFAGLGFLSL
YLSGKIRVFD QRGHVAKLCI VILPLLVAAL VGVSRVDDYW HHWQDVFGGA IIGLTVATFC
YLQFFPPPYD PDGWGPHAYF QMLADSRNDV QDSAGMNHLS VRQTELESVR
