LPPD_ARATH
ID LPPD_ARATH Reviewed; 416 AA.
AC Q9M2G7;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Lipid phosphate phosphatase delta;
DE Short=AtLPPD;
DE EC=3.1.3.-;
DE AltName: Full=Phosphatidic acid phosphatase delta;
DE AltName: Full=Sphingoid phosphate phosphatase 1;
DE Short=AtSSP1;
DE AltName: Full=Sphingosine-1-phosphate phosphatase;
DE Short=AtSPPASE;
GN Name=LPPD; Synonyms=SPP1; OrderedLocusNames=At3g58490; ORFNames=F14P22.80;
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].
RA Nakagawa N., Imai H.;
RT "Arabidopsis thaliana AtSPP1 mRNA for sphingosine-1-phosphate
RT phosphatase.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21910031; DOI=10.1007/s10265-011-0451-9;
RA Nakagawa N., Kato M., Takahashi Y., Shimazaki K., Tamura K., Tokuji Y.,
RA Kihara A., Imai H.;
RT "Degradation of long-chain base 1-phosphate (LCBP) in Arabidopsis:
RT functional characterization of LCBP phosphatase involved in the dehydration
RT stress response.";
RL J. Plant Res. 125:439-449(2012).
CC -!- FUNCTION: Functions as sphingoid long-chain base phosphate (LCBP)
CC phosphatase. May play a role in the regulation of LCBP levels and be
CC involved in stomatal responses through LCBP-mediated ABA signaling.
CC {ECO:0000269|PubMed:21910031}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:21910031}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:21910031}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M2G7-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show increased sensitivity to ABA in
CC stomatal closure and decreased sensitivity to ABA-induced inhibition of
CC primary root growth. {ECO:0000269|PubMed:21910031}.
CC -!- SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB239190; BAE46997.1; -; mRNA.
DR EMBL; AL137082; CAB68187.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79788.1; -; Genomic_DNA.
DR PIR; T45669; T45669.
DR RefSeq; NP_191408.1; NM_115711.4. [Q9M2G7-1]
DR AlphaFoldDB; Q9M2G7; -.
DR SMR; Q9M2G7; -.
DR STRING; 3702.AT3G58490.1; -.
DR PaxDb; Q9M2G7; -.
DR PRIDE; Q9M2G7; -.
DR ProteomicsDB; 238424; -. [Q9M2G7-1]
DR EnsemblPlants; AT3G58490.1; AT3G58490.1; AT3G58490. [Q9M2G7-1]
DR GeneID; 825018; -.
DR Gramene; AT3G58490.1; AT3G58490.1; AT3G58490. [Q9M2G7-1]
DR KEGG; ath:AT3G58490; -.
DR Araport; AT3G58490; -.
DR TAIR; locus:2076441; AT3G58490.
DR eggNOG; KOG2822; Eukaryota.
DR HOGENOM; CLU_043042_0_0_1; -.
DR InParanoid; Q9M2G7; -.
DR PhylomeDB; Q9M2G7; -.
DR BioCyc; ARA:AT3G58490-MON; -.
DR PRO; PR:Q9M2G7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2G7; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008117; F:sphinganine-1-phosphate aldolase activity; IDA:TAIR.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0006665; P:sphingolipid metabolic process; IDA:TAIR.
DR GO; GO:0090332; P:stomatal closure; IMP:TAIR.
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 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Hydrolase; Lipid metabolism;
KW Membrane; Reference proteome; Sphingolipid metabolism; Stress response;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..416
FT /note="Lipid phosphate phosphatase delta"
FT /id="PRO_0000425224"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 119..127
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000305"
FT REGION 151..154
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000305"
FT REGION 198..209
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000305"
FT ACT_SITE 154
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT ACT_SITE 205
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
FT SITE 209
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:P0A924"
SQ SEQUENCE 416 AA; 46169 MW; 3DD3488FFF62831A CRC64;
MKKILERSME GSGTWQGLVL VGIVTWICAS SYLKFTHKFR SLLQPWVARQ VVGGVPLILR
IQKCQNGVLD AFFSGLSCVV SVPFYTAFLP LLFWSGHGRL ARQMTLLIAF CDYLGNCIKD
VVSAPRPSCP PVRRITATKD EEDNAMEYGL PSSHTLNTVC LSGYLLHYVL SSLEYESVSI
QYYGFALACL LVALIAFGRV YLGMHSVVDI VSGLAIGVLI LGLWLTVNEK LDDFITSKQN
VSSFWTALSF LLLFAYPTPE HPTPSYEYHT AFNGVTLGIV TGVQQTYSQF HHEAAPRIFS
PELPISSYLG RVMVGIPTIL LVKFCSKSLA KWTLPMVSNA LGIPIRSSMY IPKLKGYASG
KKTDEPKNSV GYLQKLCEFL SHDSFDIDTG IRFFQYAGLA WSVVDLVPSL FSYVNL
