LPP1_ARATH
ID LPP1_ARATH Reviewed; 327 AA.
AC Q9ZU49; Q3EC91; Q8H0G3; Q8LDP8; Q945N3; Q94LY6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Lipid phosphate phosphatase 1;
DE Short=AtLPP1;
DE EC=3.1.3.-;
DE AltName: Full=Phosphatidic acid phosphatase 1;
DE Short=AtPAP1;
DE AltName: Full=Prenyl diphosphate phosphatase;
GN Name=LPP1; Synonyms=PAP1; OrderedLocusNames=At2g01180; ORFNames=F10A8.6;
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Katagiri T., Shinozaki K.;
RT "One of the biological functions of the gene encoding phosphatidic acid
RT phosphatase (PAP) correlates cell elongation in Arabidopsis thaliana.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-327.
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.
CC -!- FUNCTION: Plays a general role in cellular responses to stress, may be
CC by attenuating the signal produced by phospholipases. Exhibits both
CC diacylglycerol pyrophosphate (DGPP) phosphatase and phosphatidate (PA)
CC phosphatase activities. Substrate preference is diacylglycerol
CC pyrophosphate > phosphatidate. {ECO:0000269|PubMed:11278556}.
CC -!- ACTIVITY REGULATION: PA phosphatase activity inhibited by N-
CC ethylmaleimide with an IC(50) value of 10 mM.
CC {ECO:0000269|PubMed:11278556}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZU49-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZU49-2; Sequence=VSP_053601;
CC -!- TISSUE SPECIFICITY: Strongly expressed in leaves, moderately in roots,
CC weakly in floral hamps and flower buds, and not detected in adult
CC flowers and seedpods. {ECO:0000269|PubMed:11278556}.
CC -!- INDUCTION: Rapid increase in response to severe radiation stress (gamma
CC rays or UV-B). Returns to basal level 45 min after the radiation
CC injury. Also induced by mastoparan and by the hypersensitive response
CC elicitor harpin. In this later case, induction is also observed in the
CC leaves adjacent to those that were infiltrated with harpin.
CC {ECO:0000269|PubMed:11278556}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX819931; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AB004318; BAB47575.1; -; mRNA.
DR EMBL; AC006200; AAD14518.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC05411.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05412.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61748.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61749.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61752.1; -; Genomic_DNA.
DR EMBL; AF412050; AAL06503.1; -; mRNA.
DR EMBL; AY143886; AAN28825.1; -; mRNA.
DR EMBL; AY085869; AAM63082.1; -; mRNA.
DR EMBL; BX819931; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB053949; BAC41334.1; -; mRNA.
DR PIR; E84421; E84421.
DR RefSeq; NP_001318171.1; NM_001335038.1. [Q9ZU49-1]
DR RefSeq; NP_001323949.1; NM_001335041.1. [Q9ZU49-2]
DR RefSeq; NP_001323950.1; NM_001335040.1. [Q9ZU49-1]
DR RefSeq; NP_565255.1; NM_126179.5. [Q9ZU49-1]
DR RefSeq; NP_973389.1; NM_201660.2. [Q9ZU49-2]
DR AlphaFoldDB; Q9ZU49; -.
DR BioGRID; 50; 4.
DR IntAct; Q9ZU49; 1.
DR STRING; 3702.AT2G01180.1; -.
DR iPTMnet; Q9ZU49; -.
DR PaxDb; Q9ZU49; -.
DR PRIDE; Q9ZU49; -.
DR ProteomicsDB; 238589; -. [Q9ZU49-1]
DR EnsemblPlants; AT2G01180.1; AT2G01180.1; AT2G01180. [Q9ZU49-1]
DR EnsemblPlants; AT2G01180.2; AT2G01180.2; AT2G01180. [Q9ZU49-2]
DR EnsemblPlants; AT2G01180.4; AT2G01180.4; AT2G01180. [Q9ZU49-1]
DR EnsemblPlants; AT2G01180.5; AT2G01180.5; AT2G01180. [Q9ZU49-2]
DR EnsemblPlants; AT2G01180.8; AT2G01180.8; AT2G01180. [Q9ZU49-1]
DR GeneID; 814646; -.
DR Gramene; AT2G01180.1; AT2G01180.1; AT2G01180. [Q9ZU49-1]
DR Gramene; AT2G01180.2; AT2G01180.2; AT2G01180. [Q9ZU49-2]
DR Gramene; AT2G01180.4; AT2G01180.4; AT2G01180. [Q9ZU49-1]
DR Gramene; AT2G01180.5; AT2G01180.5; AT2G01180. [Q9ZU49-2]
DR Gramene; AT2G01180.8; AT2G01180.8; AT2G01180. [Q9ZU49-1]
DR KEGG; ath:AT2G01180; -.
DR Araport; AT2G01180; -.
DR TAIR; locus:2038826; AT2G01180.
DR eggNOG; KOG3030; Eukaryota.
DR InParanoid; Q9ZU49; -.
DR PhylomeDB; Q9ZU49; -.
DR BioCyc; ARA:MON-AT2G01180; -.
DR BioCyc; MetaCyc:MON-AT2G01180; -.
DR PRO; PR:Q9ZU49; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZU49; baseline and differential.
DR Genevisible; Q9ZU49; AT.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:TAIR.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0010224; P:response to UV-B; IEP: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; Hydrolase; Hypersensitive response; Membrane;
KW Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..327
FT /note="Lipid phosphate phosphatase 1"
FT /id="PRO_0000220915"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..25
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_053601"
FT CONFLICT 103
FT /note="L -> V (in Ref. 6; AAM63082)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="V -> A (in Ref. 5; AAL06503/AAN28825)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="H -> Q (in Ref. 6; AAM63082)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="A -> G (in Ref. 6; AAM63082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 36683 MW; BAF6F345817BA245 CRC64;
MTIGSFFSSL LFWRNSQDQE AQRGRMQEID LSVHTIKSHG GRVASKHKHD WIILVILIAI
EIGLNLISPF YRYVGKDMMT DLKYPFKDNT VPIWSVPVYA VLLPIIVFVC FYLKRTCVYD
LHHSILGLLF AVLITGVITD SIKVATGRPR PNFYWRCFPD GKELYDALGG VVCHGKAAEV
KEGHKSFPSG HTSWSFAGLT FLSLYLSGKI KAFNNEGHVA KLCLVIFPLL AACLVGISRV
DDYWHHWQDV FAGALIGTLV AAFCYRQFYP NPYHEEGWGP YAYFKAAQER GVPVTSSQNG
DALRAMSLQM DSTSLENMES GTSTAPR
