LPPG_ARATH
ID LPPG_ARATH Reviewed; 226 AA.
AC Q6NLA5; Q9LYX7;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Lipid phosphate phosphatase gamma;
DE Short=AtLPPG;
DE EC=3.1.3.-;
DE AltName: Full=Phosphatidic acid phosphatase gamma;
DE AltName: Full=Plastidic phosphatidic acid phosphatase gamma;
GN Name=LPPG; OrderedLocusNames=At5g03080; ORFNames=F15A17.110;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) 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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Exhibits phosphatidate phosphatase (PAP) activity in vitro.
CC May play a primary 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 6.0-8.0. {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 -!- TISSUE SPECIFICITY: Expressed in root tips, root branch points,
CC vascular tissue of cotyledons and leaves, pistil, anthers and
CC filaments. {ECO:0000269|PubMed:17652095}.
CC -!- DISRUPTION PHENOTYPE: Lethal effect when homozygous, due to defect in
CC pollen germination and pollen tube growth.
CC {ECO:0000269|PubMed:17652095}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB86075.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163002; CAB86075.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90554.1; -; Genomic_DNA.
DR EMBL; BT010758; AAR23728.1; -; mRNA.
DR EMBL; BT012429; AAS92345.1; -; mRNA.
DR EMBL; AK228952; BAF00841.1; -; mRNA.
DR PIR; T48329; T48329.
DR RefSeq; NP_195928.1; NM_120386.4.
DR AlphaFoldDB; Q6NLA5; -.
DR SMR; Q6NLA5; -.
DR STRING; 3702.AT5G03080.1; -.
DR iPTMnet; Q6NLA5; -.
DR PaxDb; Q6NLA5; -.
DR PRIDE; Q6NLA5; -.
DR ProteomicsDB; 238387; -.
DR EnsemblPlants; AT5G03080.1; AT5G03080.1; AT5G03080.
DR GeneID; 831801; -.
DR Gramene; AT5G03080.1; AT5G03080.1; AT5G03080.
DR KEGG; ath:AT5G03080; -.
DR Araport; AT5G03080; -.
DR TAIR; locus:2143433; AT5G03080.
DR eggNOG; KOG3146; Eukaryota.
DR HOGENOM; CLU_074922_1_2_1; -.
DR InParanoid; Q6NLA5; -.
DR OMA; VYATLIW; -.
DR OrthoDB; 1312138at2759; -.
DR PhylomeDB; Q6NLA5; -.
DR BRENDA; 3.1.3.4; 399.
DR PRO; PR:Q6NLA5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6NLA5; baseline and differential.
DR Genevisible; Q6NLA5; 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:0048868; P:pollen tube development; IMP:TAIR.
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 Acetylation; Chloroplast; Hydrolase; Membrane; Plastid;
KW Plastid inner membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..226
FT /note="Lipid phosphate phosphatase gamma"
FT /id="PRO_0000425229"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 226 AA; 25754 MW; 6C0535638F9CBB2B CRC64;
MDLIPQQLKA VTLTHVRYRP GDQLGHFLAW ISLVPVFISL GGFVSHFLFR RELQGIFFGI
GLVISQFINE FIKTSVEQAR PETCTLLEAC DSHGWPSSHS QFMFFFATYF SLMGCKGIGF
WFGLRSRWIM NLLHWSLAVV TMYSRVYLGY HTVAQVFAGA ALGGIVGASW FWVVNSVLYP
FFPVIEESVL GRWLYVKDTS HIPDVLKFEY DNARAARKDM DSAKSD
