PLPP4_MOUSE
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 03-AUG-2022, entry version 104.
DE RecName: Full=Phospholipid phosphatase 4 {ECO:0000250|UniProtKB:Q5VZY2};
DE EC=3.1.3.4 {ECO:0000250|UniProtKB:Q5VZY2};
DE EC=3.1.3.81 {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=3.1.3.81;
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; Q0VBU9; -.
DR PRIDE; Q0VBU9; -.
DR ProteomicsDB; 289451; -.
DR Antibodypedia; 46311; 82 antibodies from 19 providers.
DR DNASU; 381925; -.
DR Ensembl; ENSMUST00000094018; ENSMUSP00000091557; ENSMUSG00000070366.
DR GeneID; 381925; -.
DR KEGG; mmu:381925; -.
DR UCSC; uc009jzl.1; mouse.
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; 1621899at2759; -.
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 41 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 35 other tissues.
DR ExpressionAtlas; Q0VBU9; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR InterPro; IPR028668; PLPP4/5.
DR PANTHER; PTHR10165; PTHR10165; 1.
DR PANTHER; PTHR10165:SF90; PTHR10165:SF90; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 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
