PLPP1_MOUSE
ID PLPP1_MOUSE Reviewed; 283 AA.
AC Q61469; Q61690; Q6GT30; Q8BPB8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Phospholipid phosphatase 1 {ECO:0000305};
DE EC=3.1.3.- {ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:10620492, ECO:0000269|PubMed:10818444, ECO:0000269|PubMed:17379599};
DE EC=3.1.3.106 {ECO:0000269|PubMed:15461590, ECO:0000269|PubMed:19215222};
DE EC=3.1.3.4 {ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:19215222, ECO:0000269|PubMed:8702556};
DE EC=3.1.3.81 {ECO:0000269|PubMed:10359651};
DE AltName: Full=35 kDa PAP;
DE Short=mPAP;
DE AltName: Full=Hydrogen peroxide-inducible protein 53;
DE Short=Hic53;
DE AltName: Full=Lipid phosphate phosphohydrolase 1;
DE AltName: Full=PAP2-alpha;
DE AltName: Full=Phosphatidate phosphohydrolase type 2a;
DE AltName: Full=Phosphatidic acid phosphatase 2a;
DE Short=PAP-2a;
DE Short=PAP2a;
GN Name=Plpp1 {ECO:0000312|MGI:MGI:108412}; Synonyms=Hpic53, Lpp1, Ppap2a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RC TISSUE=Calvaria;
RX PubMed=7556647; DOI=10.1016/0014-5793(95)00957-b;
RA Egawa K., Yoshiwara M., Shibanuma M., Nose K.;
RT "Isolation of a novel ras-recision gene that is induced by hydrogen
RT peroxide from a mouse osteoblastic cell line, MC3T3-E1.";
RL FEBS Lett. 372:74-77(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, AND GLYCOSYLATION.
RC TISSUE=Kidney;
RX PubMed=8702556; DOI=10.1074/jbc.271.31.18931;
RA Kai M., Wada I., Imai S., Sakane F., Kanoh H.;
RT "Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase
RT (type 2) bound to plasma membranes.";
RL J. Biol. Chem. 271:18931-18938(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N;
RA Yokoyama K., Tigyi G.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY, SUBCELLULAR
RP LOCATION, AND TOPOLOGY.
RC TISSUE=Liver;
RX PubMed=10359651; DOI=10.1042/bj3400677;
RA Jasinska R., Zhang Q.-X., Pilquil C., Singh I., Xu J., Dewald J.,
RA Dillon D.A., Berthiaume L.G., Carman G.M., Waggoner D.W., Brindley D.N.;
RT "Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid and
RT sphingolipid phosphate esters.";
RL Biochem. J. 340:677-686(1999).
RN [7]
RP SUBUNIT.
RX PubMed=14725715; DOI=10.1186/1471-2091-5-2;
RA Burnett C., Makridou P., Hewlett L., Howard K.;
RT "Lipid phosphate phosphatases dimerise, but this interaction is not
RT required for in vivo activity.";
RL BMC Biochem. 5:2-2(2004).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND PATHWAY.
RX PubMed=10818444; DOI=10.1111/j.1749-6632.2000.tb06540.x;
RA Xu J., Zhang Q.X., Pilquil C., Berthiaume L.G., Waggoner D.W.,
RA Brindley D.N.;
RT "Lipid phosphate phosphatase-1 in the regulation of lysophosphatidate
RT signaling.";
RL Ann. N. Y. Acad. Sci. 905:81-90(2000).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, GLYCOSYLATION AT ASN-142, AND
RP MUTAGENESIS OF THR-5; LEU-106; THR-116; LYS-120; THR-122; ARG-127; PRO-128;
RP ASN-142; TYR-168; SER-169; GLY-170; HIS-171; ARG-217; TYR-221; HIS-223;
RP ILE-233 AND ASN-276.
RX PubMed=10620492; DOI=10.1042/bj3450181;
RA Zhang Q.X., Pilquil C.S., Dewald J., Berthiaume L.G., Brindley D.N.;
RT "Identification of structurally important domains of lipid phosphate
RT phosphatase-1: implications for its sites of action.";
RL Biochem. J. 345:181-184(2000).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=11535125; DOI=10.1042/0264-6021:3580637;
RA Nanjundan M., Possmayer F.;
RT "Pulmonary lipid phosphate phosphohydrolase in plasma membrane signalling
RT platforms.";
RL Biochem. J. 358:637-646(2001).
RN [11]
RP OVEREXPRESSION.
RX PubMed=14687668; DOI=10.1016/j.cellsig.2003.08.012;
RA Yue J., Yokoyama K., Balazs L., Baker D.L., Smalley D., Pilquil C.,
RA Brindley D.N., Tigyi G.;
RT "Mice with transgenic overexpression of lipid phosphate phosphatase-1
RT display multiple organotypic deficits without alteration in circulating
RT lysophosphatidate level.";
RL Cell. Signal. 16:385-399(2004).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF ARG-217.
RX PubMed=15461590; DOI=10.1042/bj20041160;
RA Zhao Y., Usatyuk P.V., Cummings R., Saatian B., He D., Watkins T.,
RA Morris A., Spannhake E.W., Brindley D.N., Natarajan V.;
RT "Lipid phosphate phosphatase-1 regulates lysophosphatidic acid-induced
RT calcium release, NF-kappaB activation and interleukin-8 secretion in human
RT bronchial epithelial cells.";
RL Biochem. J. 385:493-502(2005).
RN [13]
RP FUNCTION.
RX PubMed=17057224; DOI=10.1074/jbc.m601670200;
RA Pilquil C., Dewald J., Cherney A., Gorshkova I., Tigyi G., English D.,
RA Natarajan V., Brindley D.N.;
RT "Lipid phosphate phosphatase-1 regulates lysophosphatidate-induced
RT fibroblast migration by controlling phospholipase D2-dependent
RT phosphatidate generation.";
RL J. Biol. Chem. 281:38418-38429(2006).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=17379599; DOI=10.1074/jbc.m701279200;
RA Zhao Y., Kalari S.K., Usatyuk P.V., Gorshkova I., He D., Watkins T.,
RA Brindley D.N., Sun C., Bittman R., Garcia J.G., Berdyshev E.V.,
RA Natarajan V.;
RT "Intracellular generation of sphingosine 1-phosphate in human lung
RT endothelial cells: role of lipid phosphate phosphatase-1 and sphingosine
RT kinase 1.";
RL J. Biol. Chem. 282:14165-14177(2007).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19215222; DOI=10.1042/bj20081888;
RA Tomsig J.L., Snyder A.H., Berdyshev E.V., Skobeleva A., Mataya C.,
RA Natarajan V., Brindley D.N., Lynch K.R.;
RT "Lipid phosphate phosphohydrolase type 1 (LPP1) degrades extracellular
RT lysophosphatidic acid in vivo.";
RL Biochem. J. 419:611-618(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Magnesium-independent phospholipid phosphatase of the plasma
CC membrane that catalyzes the dephosphorylation of a variety of
CC glycerolipid and sphingolipid phosphate esters including
CC phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol
CC pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-
CC phosphate/C1P (PubMed:8702556, PubMed:10359651, PubMed:10818444,
CC PubMed:10620492, PubMed:15461590, PubMed:19215222). Also acts on N-
CC oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine
CC phosphate, a potential physiological compound (By similarity). Through
CC its extracellular phosphatase activity allows both the hydrolysis and
CC the cellular uptake of these bioactive lipid mediators from the milieu,
CC regulating signal transduction in different cellular processes
CC (PubMed:17379599). It is for instance essential for the extracellular
CC hydrolysis of S1P and subsequent conversion into intracellular S1P
CC (PubMed:17379599). Involved in the regulation of inflammation,
CC platelets activation, cell proliferation and migration among other
CC processes (PubMed:15461590, PubMed:17057224). May also have an
CC intracellular activity to regulate phospholipid-mediated signaling
CC pathways (PubMed:17057224). {ECO:0000250|UniProtKB:O14494,
CC ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:10620492,
CC ECO:0000269|PubMed:10818444, ECO:0000269|PubMed:15461590,
CC ECO:0000269|PubMed:17057224, ECO:0000269|PubMed:17379599,
CC ECO:0000269|PubMed:19215222, ECO:0000269|PubMed:8702556}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC Evidence={ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:19215222,
CC ECO:0000269|PubMed:8702556};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC Evidence={ECO:0000305|PubMed:10359651};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-
CC dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859,
CC ChEBI:CHEBI:82929; Evidence={ECO:0000250|UniProtKB:O14494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237;
CC Evidence={ECO:0000250|UniProtKB:O14494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-
CC di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333,
CC ChEBI:CHEBI:74546; Evidence={ECO:0000269|PubMed:19215222,
CC ECO:0000269|PubMed:8702556};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC Evidence={ECO:0000269|PubMed:19215222};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol +
CC phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589;
CC Evidence={ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:10620492,
CC ECO:0000269|PubMed:10818444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737;
CC Evidence={ECO:0000269|PubMed:10359651};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-
CC octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937,
CC ChEBI:CHEBI:84973; Evidence={ECO:0000269|PubMed:10818444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885;
CC Evidence={ECO:0000305|PubMed:10818444};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol +
CC phosphate; Xref=Rhea:RHEA:33155, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683;
CC EC=3.1.3.106; Evidence={ECO:0000269|PubMed:15461590,
CC ECO:0000269|PubMed:19215222};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33156;
CC Evidence={ECO:0000305|PubMed:19215222};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:75757; Evidence={ECO:0000269|PubMed:15461590,
CC ECO:0000269|PubMed:19215222};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC Evidence={ECO:0000269|PubMed:19215222};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.1.3.81;
CC Evidence={ECO:0000269|PubMed:10359651};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450;
CC Evidence={ECO:0000305|PubMed:10359651};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine;
CC Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:60119;
CC Evidence={ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:17379599};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
CC Evidence={ECO:0000305|PubMed:10359651};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-
CC enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674;
CC Evidence={ECO:0000269|PubMed:10359651};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744;
CC Evidence={ECO:0000305|PubMed:10359651};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-
CC octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815,
CC ChEBI:CHEBI:85376; Evidence={ECO:0000250|UniProtKB:O14494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041;
CC Evidence={ECO:0000250|UniProtKB:O14494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-
CC octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466,
CC ChEBI:CHEBI:145465; Evidence={ECO:0000250|UniProtKB:O14494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161;
CC Evidence={ECO:0000250|UniProtKB:O14494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate;
CC Xref=Rhea:RHEA:41255, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64839, ChEBI:CHEBI:75466;
CC Evidence={ECO:0000250|UniProtKB:O08564};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41256;
CC Evidence={ECO:0000250|UniProtKB:O08564};
CC -!- ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase.
CC Insensitive to N-ethylmaleimide. {ECO:0000250|UniProtKB:O14494}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=67 uM for 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC {ECO:0000269|PubMed:10818444};
CC Vmax=1.25 nmol/min/mg enzyme with 1,2-di-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphate as substrate {ECO:0000269|PubMed:10818444};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:10620492,
CC ECO:0000269|PubMed:10818444, ECO:0000269|PubMed:15461590,
CC ECO:0000269|PubMed:17379599, ECO:0000269|PubMed:19215222,
CC ECO:0000269|PubMed:8702556}.
CC -!- SUBUNIT: Forms functional homodimers and homooligomers that are not
CC required for substrate recognition and catalytic activity
CC (PubMed:14725715). Can also form heterooligomers with PLPP2 and PLPP3
CC (By similarity). {ECO:0000250|UniProtKB:O88956,
CC ECO:0000269|PubMed:14725715}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10359651,
CC ECO:0000269|PubMed:17379599, ECO:0000269|PubMed:19215222}; Multi-pass
CC membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein
CC {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O14494}; Multi-pass
CC membrane protein {ECO:0000255}. Membrane, caveola
CC {ECO:0000269|PubMed:11535125}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61469-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61469-2; Sequence=VSP_009652;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:19215222). Highly
CC expressed in kidney and lung. Almost undetectable in brain, heart,
CC bone, muscle or spleen. {ECO:0000269|PubMed:19215222}.
CC -!- INDUCTION: Moderately, by hydrogen peroxide, calcium ionophore and
CC dexamethasone. {ECO:0000269|PubMed:7556647}.
CC -!- PTM: N-glycosylated (PubMed:8702556, PubMed:10620492). N-linked sugars
CC are of the complex type (PubMed:8702556). N-glycosylation is not
CC required for the phosphatase activity (PubMed:10620492).
CC {ECO:0000269|PubMed:10620492, ECO:0000269|PubMed:8702556}.
CC -!- MISCELLANEOUS: Overexpression elicited a number of phenotypic
CC alteration without affecting several aspects of LPA signaling.
CC Phenotypic abnormalities affect primarily three organs: the liver, the
CC skin, and the reproductive organs. There is a reduction on body size,
CC birth weight, abnormalities in fur growth, and a severely impaired
CC spermatogenesis.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85353.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L43371; AAA85353.1; ALT_SEQ; mRNA.
DR EMBL; D84376; BAA12335.1; -; mRNA.
DR EMBL; AY247795; AAP04434.1; -; mRNA.
DR EMBL; AY247796; AAP04435.1; -; mRNA.
DR EMBL; AK077275; BAC36724.1; -; mRNA.
DR EMBL; BC061161; AAH61161.1; -; mRNA.
DR CCDS; CCDS26776.1; -. [Q61469-2]
DR CCDS; CCDS26777.1; -. [Q61469-1]
DR PIR; S66668; S66668.
DR RefSeq; NP_032273.1; NM_008247.3. [Q61469-2]
DR RefSeq; NP_032929.1; NM_008903.2. [Q61469-1]
DR AlphaFoldDB; Q61469; -.
DR BioGRID; 202316; 1.
DR IntAct; Q61469; 1.
DR SwissLipids; SLP:000001978; -.
DR GlyGen; Q61469; 1 site.
DR iPTMnet; Q61469; -.
DR PhosphoSitePlus; Q61469; -.
DR jPOST; Q61469; -.
DR MaxQB; Q61469; -.
DR PeptideAtlas; Q61469; -.
DR PRIDE; Q61469; -.
DR ProteomicsDB; 289770; -. [Q61469-1]
DR ProteomicsDB; 289771; -. [Q61469-2]
DR Antibodypedia; 11159; 182 antibodies from 27 providers.
DR DNASU; 19012; -.
DR Ensembl; ENSMUST00000016144; ENSMUSP00000016144; ENSMUSG00000021759. [Q61469-2]
DR Ensembl; ENSMUST00000070951; ENSMUSP00000064423; ENSMUSG00000021759. [Q61469-1]
DR GeneID; 19012; -.
DR KEGG; mmu:19012; -.
DR UCSC; uc007rwq.2; mouse. [Q61469-1]
DR UCSC; uc007rwr.2; mouse. [Q61469-2]
DR CTD; 8611; -.
DR MGI; MGI:108412; Plpp1.
DR VEuPathDB; HostDB:ENSMUSG00000021759; -.
DR GeneTree; ENSGT00940000156730; -.
DR HOGENOM; CLU_021458_3_1_1; -.
DR InParanoid; Q61469; -.
DR OMA; AVCQPVM; -.
DR OrthoDB; 1354951at2759; -.
DR PhylomeDB; Q61469; -.
DR TreeFam; TF316040; -.
DR BRENDA; 3.1.3.81; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 19012; 2 hits in 44 CRISPR screens.
DR ChiTaRS; Plpp1; mouse.
DR PRO; PR:Q61469; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q61469; protein.
DR Bgee; ENSMUSG00000021759; Expressed in seminal vesicle and 275 other tissues.
DR Genevisible; Q61469; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0106235; F:ceramide-1-phosphate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0042577; F:lipid phosphatase activity; IDA:UniProtKB.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0006672; P:ceramide metabolic process; IDA:UniProtKB.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; TAS:MGI.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR GO; GO:0006670; P:sphingosine metabolic process; IDA:UniProtKB.
DR InterPro; IPR028670; LPP1.
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 PANTHER; PTHR10165:SF26; PTHR10165:SF26; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Hydrolase;
KW Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..283
FT /note="Phospholipid phosphatase 1"
FT /id="PRO_0000220906"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10359651"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..53
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:10359651"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10359651"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..164
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:10359651"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10359651"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..229
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:10359651"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10359651"
FT REGION 120..128
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 168..171
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 216..227
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 260..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 5..7
FT /note="PDZ-binding; involved in localization to the apical
FT cell membrane"
FT /evidence="ECO:0000250|UniProtKB:O14494"
FT ACT_SITE 171
FT /note="Proton donors"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT ACT_SITE 223
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT SITE 227
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10620492"
FT VAR_SEQ 21..70
FT /note="GLPFAILTSRHTPFQRGIFCNDDSIKYPYKEDTIPYALLGGIVIPFCIIV
FT -> AMPMTILKLGKVYPFQRGFFCTDNSVKYPYHDSTIPSRILAILGLGLPIFS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT /id="VSP_009652"
FT MUTAGEN 5
FT /note="T->P: Decreased lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 106
FT /note="L->S: Decreased lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 116
FT /note="T->I: No significant effect on lipid phosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 120
FT /note="K->R: Loss of lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 122
FT /note="T->S: No effect on lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 127
FT /note="R->K: Loss of lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 128
FT /note="P->I: Loss of lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 142
FT /note="N->Q: Loss of N-glycosylation. No significant effect
FT on lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 168
FT /note="Y->F: Decreased lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 169
FT /note="S->T: Loss of lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 170
FT /note="G->A: Decreased lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 171
FT /note="H->L: Loss of lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 217
FT /note="R->K: Loss of lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492,
FT ECO:0000269|PubMed:15461590"
FT MUTAGEN 221
FT /note="Y->W: Decreased lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 223
FT /note="H->L: Loss of lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 233
FT /note="I->T: No significant effect on lipid phosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:10620492"
FT MUTAGEN 276
FT /note="N->Q: No effect on lipid phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10620492"
SQ SEQUENCE 283 AA; 31892 MW; 669690568E549CC6 CRC64;
MFDKTRLPYV ALDVICVLLA GLPFAILTSR HTPFQRGIFC NDDSIKYPYK EDTIPYALLG
GIVIPFCIIV MSIGESLSVY FNVLHSNSFV GNPYIATIYK AVGAFLFGVS ASQSLTDIAK
YTIGSLRPHF LAICNPDWSK INCSDGYIED YICQGNEEKV KEGRLSFYSG HSSFSMYCML
FVALYLQARM KGDWARLLRP MLQFGLIAFS IYVGLSRVSD YKHHWSDVTV GLIQGAAMAI
LVALYVSDFF KDTHSYKERK EEDPHTTLHE TASSRNYSTN HEP
