ID   PLPP4_MOUSE             Reviewed;         271 AA.
AC   Q0VBU9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 110.
DE   RecName: Full=Phospholipid phosphatase 4 {ECO:0000250|UniProtKB:Q5VZY2};
DE            EC=3.1.3.4 {ECO:0000250|UniProtKB:Q5VZY2};
DE            EC=3.6.1.75 {ECO:0000250|UniProtKB:Q5VZY2};
GN   Name=Plpp4 {ECO:0000312|MGI:MGI:2685936};
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   TISSUE=Brain;
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).
CC   -!- FUNCTION: Magnesium-independent phospholipid phosphatase with broad
CC       substrate specificity. Preferentially catalyzes the conversion of
CC       diacylglycerol pyrophosphate into phosphatidate but can also act on
CC       phosphatidate and lysophosphatidate. Phospholipid phosphatases are
CC       involved in both the synthesis of lipids and the degradation or
CC       generation of lipid-signaling molecules like diacylglycerol.
CC       {ECO:0000250|UniProtKB:Q5VZY2}.
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=3.6.1.75;
CC         Evidence={ECO:0000250|UniProtKB:Q5VZY2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450;
CC         Evidence={ECO:0000250|UniProtKB:Q5VZY2};
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:0000250|UniProtKB:Q5VZY2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC         Evidence={ECO:0000250|UniProtKB:Q5VZY2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dioctanoyl-sn-glycero-3-diphosphate + H2O = 1,2-
CC         dioctanoyl-sn-glycero-3-phosphate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:42856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:78229, ChEBI:CHEBI:82765;
CC         Evidence={ECO:0000250|UniProtKB:Q5VZY2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42857;
CC         Evidence={ECO:0000250|UniProtKB:Q5VZY2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dioctanoyl-sn-glycero-3-phosphate + H2O = 1,2-dioctanoyl-
CC         sn-glycerol + phosphate; Xref=Rhea:RHEA:42860, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:76979, ChEBI:CHEBI:78229;
CC         Evidence={ECO:0000250|UniProtKB:Q5VZY2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42861;
CC         Evidence={ECO:0000250|UniProtKB:Q5VZY2};
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:0000250|UniProtKB:Q5VZY2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC         Evidence={ECO:0000250|UniProtKB:Q5VZY2};
CC   -!- ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase.
CC       Inhibited by N-ethylmaleimide. {ECO:0000250|UniProtKB:Q5VZY2}.
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000250|UniProtKB:Q5VZY2}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q5VZY2}; Multi-
CC       pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000305}.
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DR   EMBL; BC120497; AAI20498.1; -; mRNA.
DR   CCDS; CCDS40154.1; -.
DR   RefSeq; NP_001074432.1; NM_001080963.1.
DR   AlphaFoldDB; Q0VBU9; -.
DR   STRING; 10090.ENSMUSP00000091557; -.
DR   iPTMnet; Q0VBU9; -.
DR   PhosphoSitePlus; Q0VBU9; -.
DR   PaxDb; 10090-ENSMUSP00000091557; -.
DR   ProteomicsDB; 289451; -.
DR   Antibodypedia; 46311; 93 antibodies from 19 providers.
DR   DNASU; 381925; -.
DR   Ensembl; ENSMUST00000094018.6; ENSMUSP00000091557.5; ENSMUSG00000070366.6.
DR   GeneID; 381925; -.
DR   KEGG; mmu:381925; -.
DR   UCSC; uc009jzl.1; mouse.
DR   AGR; MGI:2685936; -.
DR   CTD; 196051; -.
DR   MGI; MGI:2685936; Plpp4.
DR   VEuPathDB; HostDB:ENSMUSG00000070366; -.
DR   eggNOG; KOG3030; Eukaryota.
DR   GeneTree; ENSGT00940000158288; -.
DR   HOGENOM; CLU_021458_5_4_1; -.
DR   InParanoid; Q0VBU9; -.
DR   OMA; WFSYRRY; -.
DR   OrthoDB; 25293at2759; -.
DR   PhylomeDB; Q0VBU9; -.
DR   TreeFam; TF323722; -.
DR   Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
DR   UniPathway; UPA00085; -.
DR   BioGRID-ORCS; 381925; 1 hit in 46 CRISPR screens.
DR   ChiTaRS; Plpp4; mouse.
DR   PRO; PR:Q0VBU9; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q0VBU9; Protein.
DR   Bgee; ENSMUSG00000070366; Expressed in olfactory bulb and 37 other cell types or tissues.
DR   ExpressionAtlas; Q0VBU9; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; ISO:MGI.
DR   GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR   GO; GO:0046839; P:phospholipid dephosphorylation; ISO:MGI.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0090279; P:regulation of calcium ion import; ISS:UniProtKB.
DR   CDD; cd03390; PAP2_containing_1_like; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
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; LIPID PHOSPHATE PHOSPHATASE; 1.
DR   PANTHER; PTHR10165:SF90; PHOSPHOLIPID PHOSPHATASE 4; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..271
FT                   /note="Phospholipid phosphatase 4"
FT                   /id="PRO_0000286944"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          102..110
FT                   /note="Phosphatase sequence motif I"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VZY2"
FT   REGION          143..146
FT                   /note="Phosphatase sequence motif II"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VZY2"
FT   REGION          195..205
FT                   /note="Phosphatase sequence motif III"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VZY2"
FT   REGION          249..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        146
FT                   /note="Proton donors"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   ACT_SITE        202
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
FT   SITE            206
FT                   /note="Stabilizes the active site histidine for
FT                   nucleophilic attack"
FT                   /evidence="ECO:0000250|UniProtKB:O34349"
SQ   SEQUENCE   271 AA;  30444 MW;  944F8A1561DDA97B CRC64;
     MRELAIEIGV RALLFGVFVF TEFLDPFQRV IQPEEIWLYK NPLVQSDNIP TRLMFAISFL
     TPLAVICVVK IIRRTDKTEI KEAFLAVSLA LALNGVCTNT IKLIVGRPRP DFFYRCFPDG
     VMNSEMRCTG DPDLVSEGRK SFPSIHSSFA FSGLGFTTFY LAGKLHCFTE SGRGKSWRLC
     AAILPLYCAM MIALSRMCDY KHHWQDSFVG GVIGLIFAYI CYRQHYPPLA NTACHKPYVS
     LRVPTSLKKE ERPTADSAPS LPLEGITEGP V
//