PLPP3_MOUSE
ID PLPP3_MOUSE Reviewed; 312 AA.
AC Q99JY8; Q3TVM4; Q3TXR7; Q8BTB7;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Phospholipid phosphatase 3 {ECO:0000305};
DE EC=3.1.3.- {ECO:0000269|PubMed:12925589, ECO:0000269|PubMed:21319224};
DE EC=3.1.3.4 {ECO:0000269|PubMed:12925589};
DE AltName: Full=Lipid phosphate phosphohydrolase 3;
DE AltName: Full=PAP2-beta;
DE AltName: Full=Phosphatidate phosphohydrolase type 2b;
DE AltName: Full=Phosphatidic acid phosphatase 2b;
DE Short=PAP-2b;
DE Short=PAP2b;
GN Name=Plpp3 {ECO:0000312|MGI:MGI:1915166}; Synonyms=Lpp3, Ppap2b;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP PROTEIN SEQUENCE OF 283-293, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12925589; DOI=10.1242/dev.00635;
RA Escalante-Alcalde D., Hernandez L., Le Stunff H., Maeda R., Lee H.-S.,
RA Cheng G. Jr., Sciorra V.A., Daar I., Spiegel S., Morris A.J., Stewart C.L.;
RT "The lipid phosphatase LPP3 regulates extra-embryonic vasculogenesis and
RT axis patterning.";
RL Development 130:4623-4637(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, TOPOLOGY, AND MOTIF.
RX PubMed=16099422; DOI=10.1016/j.bbrc.2005.07.157;
RA Humtsoe J.O., Bowling R.A. Jr., Feng S., Wary K.K.;
RT "Murine lipid phosphate phosphohydrolase-3 acts as a cell-associated
RT integrin ligand.";
RL Biochem. Biophys. Res. Commun. 335:906-919(2005).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=17610274; DOI=10.1002/dvg.20314;
RA Escalante-Alcalde D., Sanchez-Sanchez R., Stewart C.L.;
RT "Generation of a conditional Ppap2b/Lpp3 null allele.";
RL Genesis 45:465-469(2007).
RN [7]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=19123136; DOI=10.1387/ijdb.082745de;
RA Escalante-Alcalde D., Morales S.L., Stewart C.L.;
RT "Generation of a reporter-null allele of Ppap2b/Lpp3and its expression
RT during embryogenesis.";
RL Int. J. Dev. Biol. 53:139-147(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21319224; DOI=10.1002/glia.21126;
RA Lopez-Juarez A., Morales-Lazaro S., Sanchez-Sanchez R., Sunkara M.,
RA Lomeli H., Velasco I., Morris A.J., Escalante-Alcalde D.;
RT "Expression of LPP3 in Bergmann glia is required for proper cerebellar
RT sphingosine-1-phosphate metabolism/signaling and development.";
RL Glia 59:577-589(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27125875; DOI=10.1093/cvr/cvw090;
RA Chatterjee I., Baruah J., Lurie E.E., Wary K.K.;
RT "Endothelial lipid phosphate phosphatase-3 deficiency that disrupts the
RT endothelial barrier function is a modifier of cardiovascular development.";
RL Cardiovasc. Res. 111:105-118(2016).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=29889835; DOI=10.1371/journal.pone.0198063;
RA Federico L., Yang L., Brandon J., Panchatcharam M., Ren H., Mueller P.,
RA Sunkara M., Escalante-Alcalde D., Morris A.J., Smyth S.S.;
RT "Lipid phosphate phosphatase 3 regulates adipocyte sphingolipid synthesis,
RT but not developmental adipogenesis or diet-induced obesity in mice.";
RL PLoS ONE 13:E0198063-E0198063(2018).
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. Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-
CC octadecenoyl)-ethanolamine phosphate, a potential physiological
CC compound. Has both an extracellular and an intracellular phosphatase
CC activity, allowing the hydrolysis and the cellular uptake of these
CC bioactive lipid mediators from the milieu, regulating signal
CC transduction in different cellular processes. Through the
CC dephosphorylation of extracellular sphingosine-1-phosphate and the
CC regulation of its extra- and intracellular availability, plays a role
CC in vascular homeostasis, regulating endothelial cell migration,
CC adhesion, survival, proliferation and the production of pro-
CC inflammatory cytokines (By similarity). By maintaining the appropriate
CC levels of this lipid in the cerebellum, also ensure its proper
CC development and function (PubMed:21319224). Through its intracellular
CC lipid phosphatase activity may act in early compartments of the
CC secretory pathway, regulating the formation of Golgi to endoplasmic
CC reticulum retrograde transport carriers (By similarity).
CC {ECO:0000250|UniProtKB:O14495, ECO:0000269|PubMed:21319224}.
CC -!- FUNCTION: Independently of this phosphatase activity may also function
CC in the Wnt signaling pathway and the stabilization of beta-
CC catenin/CTNNB1, thereby regulating cell proliferation, migration and
CC differentiation in angiogenesis or yet in tumor growth
CC (PubMed:12925589, PubMed:27125875). Also plays a role in integrin-
CC mediated cell-cell adhesion in angiogenesis (PubMed:16099422).
CC {ECO:0000269|PubMed:12925589, ECO:0000269|PubMed:16099422,
CC ECO:0000269|PubMed:27125875}.
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:12925589};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC Evidence={ECO:0000269|PubMed:12925589};
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:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237;
CC Evidence={ECO:0000250|UniProtKB:O14495};
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:0000250|UniProtKB:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC Evidence={ECO:0000250|UniProtKB:O14495};
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:12925589};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737;
CC Evidence={ECO:0000269|PubMed:12925589};
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:0000250|UniProtKB:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885;
CC Evidence={ECO:0000250|UniProtKB:O14495};
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:21319224};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
CC Evidence={ECO:0000269|PubMed:21319224};
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:0000250|UniProtKB:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744;
CC Evidence={ECO:0000250|UniProtKB:O14495};
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:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041;
CC Evidence={ECO:0000250|UniProtKB:O14495};
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:O14495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161;
CC Evidence={ECO:0000250|UniProtKB:O14495};
CC -!- ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase.
CC Insensitive to N-ethylmaleimide. {ECO:0000250|UniProtKB:O14495}.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:12925589, ECO:0000269|PubMed:21319224}.
CC -!- SUBUNIT: Forms functional homodimers and homooligomers that are not
CC required for substrate recognition and catalytic activity. Can also
CC form heterooligomers with other PLPP2 and PLPP3. Interacts with CTNND1;
CC negatively regulates the PLPP3-mediated stabilization of beta-
CC catenin/CTNNB1. {ECO:0000250|UniProtKB:O14495}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16099422,
CC ECO:0000269|PubMed:21319224}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P97544}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:O14495}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P97544}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O14495}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P97544}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000250|UniProtKB:O14495};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:O14495}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P97544}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000250|UniProtKB:O14495}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P97544}. Membrane raft
CC {ECO:0000250|UniProtKB:O14495}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P97544}. Note=Cycles between the endoplasmic
CC reticulum and the Golgi. {ECO:0000250|UniProtKB:O14495}.
CC -!- TISSUE SPECIFICITY: Detected in lung, cerebellum and heart atrium.
CC {ECO:0000269|PubMed:12925589, ECO:0000269|PubMed:21319224}.
CC -!- DEVELOPMENTAL STAGE: Display a characteristic dynamic and changing
CC pattern of expression throughout the life cycle of the mouse
CC (PubMed:12925589). Expression during early stages of development is
CC specific of structures where multiple inductive interactions occur such
CC as the limb buds, mammary gland primordia, heart cushions and valves
CC among others (PubMed:19123136). Detected in a few cells of the extra-
CC embryonic ectoderm of 6.5 dpc embryos. By 7.5 dpc, starts to be
CC strongly expressed in the anterior visceral endoderm, as well as in the
CC extra-embryonic membranes. By 8.0 dpc, expression extends to a highly
CC localized region around the node and appears at the tip of the
CC allantois. At 8.5 dpc, predominantly expressed in the allantois, the
CC developing gut, the pericardio-peritoneal canal and somites. In 9.5 dpc
CC embryos, persists in the umbilical cord, and is also found in the
CC chorionic region. In later mid-gestation embryos, present at high
CC levels in the apical ectodermal ridge and mesenchyme of the limb buds,
CC in the peripheral nervous system, cranial nerves, and mammary gland
CC primordia (PubMed:12925589). {ECO:0000269|PubMed:12925589,
CC ECO:0000269|PubMed:19123136}.
CC -!- DOMAIN: The integrin-binding motif mediates the binding to integrin
CC alpha-5/beta-1 (ITGA5:ITGB1) and integrin alpha-V/beta-3 (ITGAV:ITGB3)
CC and is required for the function in integrin-mediated cell-cell
CC adhesion. {ECO:0000269|PubMed:16099422}.
CC -!- DOMAIN: The dityrosine basolateral targeting motif mediates
CC localization to the basolateral membrane in polarized cells.
CC {ECO:0000250|UniProtKB:O14495}.
CC -!- PTM: N-glycosylated. Contains high-mannose oligosaccharides.
CC {ECO:0000250|UniProtKB:O14495}.
CC -!- DISRUPTION PHENOTYPE: The homozygous knockout of Plpp3 is embryonic
CC lethal (PubMed:12925589, PubMed:17610274, PubMed:19123136). It is
CC characterized by a delay in development, absence of chorioallantoic
CC fusion at the 6 somite stage, allantois compaction, impaired remodeling
CC of the primary capillary plexus of the yolk sac and gastrulation
CC defects with low penetrance. Persistence of open neural tube is also
CC frequently observed (PubMed:12925589, PubMed:19123136). Conditional
CC knockout of Plpp3 in the cerebellum is associated with defects in
CC postnatal cerebellum development, modifications in the cytoarchitecture
CC and arrangement of Bergmann glia with a mild non-progressive motor
CC coordination defect (PubMed:21319224). Conditional knockout of Plpp3 in
CC endothelial cells is associated with vascular leakage and hemorrhage
CC that likely result in insufficient cardiovascular development and the
CC observed embryonic lethality (PubMed:27125875). Conditional knockout of
CC Plpp3 in adipocytes does not affect the development of the adipose
CC tissue. However, mutant homozygous mice display lower accumulation of
CC ceramide and sphingomyelin on high fat or Western diets compared to
CC control animals (PubMed:29889835). {ECO:0000269|PubMed:12925589,
CC ECO:0000269|PubMed:17610274, ECO:0000269|PubMed:19123136,
CC ECO:0000269|PubMed:21319224, ECO:0000269|PubMed:27125875,
CC ECO:0000269|PubMed:29889835}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; AK159136; BAE34848.1; -; mRNA.
DR EMBL; AK160056; BAE35594.1; -; mRNA.
DR EMBL; BC005558; AAH05558.1; -; mRNA.
DR CCDS; CCDS18417.1; -.
DR RefSeq; NP_542122.1; NM_080555.2.
DR AlphaFoldDB; Q99JY8; -.
DR BioGRID; 212532; 6.
DR CORUM; Q99JY8; -.
DR IntAct; Q99JY8; 6.
DR MINT; Q99JY8; -.
DR STRING; 10090.ENSMUSP00000065719; -.
DR GlyConnect; 2585; 1 N-Linked glycan (1 site).
DR GlyGen; Q99JY8; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q99JY8; -.
DR PhosphoSitePlus; Q99JY8; -.
DR SwissPalm; Q99JY8; -.
DR jPOST; Q99JY8; -.
DR MaxQB; Q99JY8; -.
DR PaxDb; Q99JY8; -.
DR PeptideAtlas; Q99JY8; -.
DR PRIDE; Q99JY8; -.
DR ProteomicsDB; 289772; -.
DR DNASU; 67916; -.
DR Ensembl; ENSMUST00000064139; ENSMUSP00000065719; ENSMUSG00000028517.
DR GeneID; 67916; -.
DR KEGG; mmu:67916; -.
DR UCSC; uc008tye.1; mouse.
DR CTD; 8613; -.
DR MGI; MGI:1915166; Plpp3.
DR VEuPathDB; HostDB:ENSMUSG00000028517; -.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000156450; -.
DR HOGENOM; CLU_021458_3_0_1; -.
DR InParanoid; Q99JY8; -.
DR OMA; FTMLYLV; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q99JY8; -.
DR TreeFam; TF316040; -.
DR BRENDA; 3.1.3.4; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 67916; 1 hit in 42 CRISPR screens.
DR ChiTaRS; Plpp3; mouse.
DR PRO; PR:Q99JY8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q99JY8; protein.
DR Bgee; ENSMUSG00000028517; Expressed in vestibular membrane of cochlear duct and 289 other tissues.
DR Genevisible; Q99JY8; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0106235; F:ceramide-1-phosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IDA:MGI.
DR GO; GO:0042577; F:lipid phosphatase activity; IMP:MGI.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IMP:MGI.
DR GO; GO:0060020; P:Bergmann glial cell differentiation; IMP:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:MGI.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0046839; P:phospholipid dephosphorylation; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IMP:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR GO; GO:1902068; P:regulation of sphingolipid mediated signaling pathway; IMP:MGI.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; IDA:MGI.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0006670; P:sphingosine metabolic process; ISS:UniProtKB.
DR GO; GO:0042060; P:wound healing; ISO:MGI.
DR InterPro; IPR028675; LPP3.
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:SF79; PTHR10165:SF79; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..312
FT /note="Phospholipid phosphatase 3"
FT /id="PRO_0000220913"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16099422"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..85
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16099422"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16099422"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..194
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16099422"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16099422"
FT TRANSMEM 227..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..258
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16099422"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16099422"
FT REGION 149..157
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 197..200
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 245..256
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 276..312
FT /note="Mediates interaction with CTNND1"
FT /evidence="ECO:0000250|UniProtKB:O14495"
FT MOTIF 109..110
FT /note="Dityrosine basolateral targeting motif"
FT /evidence="ECO:0000250|UniProtKB:O14495"
FT MOTIF 183..185
FT /note="Integrin-binding motif"
FT /evidence="ECO:0000269|PubMed:16099422"
FT ACT_SITE 200
FT /note="Proton donors"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT ACT_SITE 252
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT SITE 256
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14495"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 187
FT /note="S -> C (in Ref. 1; BAE34848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 35216 MW; D782986E04B57D7D CRC64;
MQSYKYDKAI VPESKNGGSP ALNNNPRKGG SKRVLLICLD LFCLFMAALP FLIIETSTIK
PYRRGFYCND ESIKYPLKVS ETINDAVLCA VGIVIAILAI ITGEFYRIYY LKEKSRSTTQ
NPYVAALYKQ VGCFLFGCAI SQSFTDIAKV SIGRLRPHFL SVCDPDFSQI NCSEGYIQNY
RCRGEDSKVQ EARKSFFSGH ASFSMFTMLY LVLYLQARFT WRGARLLRPL LQFTLLMMAF
YTGLSRVSDY KHHPSDVLAG FAQGALVACC IVFFVSDLFK TKTSLSLPAP AIRREILSPV
DIIDRNNHHN MV
