PLPP2_RAT
ID PLPP2_RAT Reviewed; 276 AA.
AC Q8K593;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Phospholipid phosphatase 2 {ECO:0000305};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:O43688};
DE EC=3.1.3.4 {ECO:0000250|UniProtKB:O43688};
DE AltName: Full=Lipid phosphate phosphohydrolase 2;
DE AltName: Full=PAP2-gamma;
DE Short=PAP2-G;
DE AltName: Full=Phosphatidate phosphohydrolase type 2c;
DE AltName: Full=Phosphatidic acid phosphatase 2c;
DE Short=PAP-2c;
DE Short=PAP2c;
GN Name=Plpp2 {ECO:0000312|RGD:628893}; Synonyms=Lpp2, Ppap2c;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RA Zhao L., Nanjundan M., Possmayer F.;
RT "Expression of lipid phosphate phosphohydrolase isoforms in rat lung
RT development.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=11704545; DOI=10.1152/ajplung.2001.281.6.l1484;
RA Nanjundan M., Possmayer F.;
RT "Molecular cloning and expression of pulmonary lipid phosphate
RT phosphohydrolases.";
RL Am. J. Physiol. 281:L1484-L1493(2001).
RN [4]
RP FUNCTION.
RX PubMed=16467304; DOI=10.1074/jbc.m511710200;
RA Morris K.E., Schang L.M., Brindley D.N.;
RT "Lipid phosphate phosphatase-2 activity regulates S-phase entry of the cell
RT cycle in Rat2 fibroblasts.";
RL J. Biol. Chem. 281:9297-9306(2006).
CC -!- FUNCTION: Magnesium-independent phospholipid phosphatase that catalyzes
CC the dephosphorylation of a variety of glycerolipid and sphingolipid
CC phosphate esters including phosphatidate/PA, lysophosphatidate/LPA,
CC sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P. Has no
CC apparent extracellular phosphatase activity and therefore most probably
CC acts intracellularly. Also acts on N-oleoyl ethanolamine phosphate/N-
CC (9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological
CC compound. Through dephosphorylation of these bioactive lipid mediators
CC produces new bioactive compounds and may regulate signal transduction
CC in different cellular processes (By similarity). Indirectly regulates,
CC for instance, cell cycle G1/S phase transition through its phospholipid
CC phosphatase activity (PubMed:16467304). {ECO:0000250|UniProtKB:O43688,
CC ECO:0000269|PubMed:16467304}.
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:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC Evidence={ECO:0000250|UniProtKB:O43688};
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:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237;
CC Evidence={ECO:0000250|UniProtKB:O43688};
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:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC Evidence={ECO:0000250|UniProtKB:O43688};
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:0000250|UniProtKB:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737;
CC Evidence={ECO:0000250|UniProtKB:O43688};
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:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885;
CC Evidence={ECO:0000250|UniProtKB:O43688};
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:0000250|UniProtKB:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
CC Evidence={ECO:0000250|UniProtKB:O43688};
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:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744;
CC Evidence={ECO:0000250|UniProtKB:O43688};
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:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041;
CC Evidence={ECO:0000250|UniProtKB:O43688};
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:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC -!- ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase.
CC Insensitive to N-ethylmaleimide. {ECO:0000250|UniProtKB:O43688}.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000250|UniProtKB:O43688}.
CC -!- SUBUNIT: Forms functional homodimers and homooligomers. Can also form
CC heterooligomers with PLPP1 and PLPP3. {ECO:0000250|UniProtKB:O43688}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O43688}; Multi-
CC pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:O43688}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:O43688};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:O43688}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain.
CC {ECO:0000269|PubMed:11704545}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O43688}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; AF503611; AAM28632.1; -; mRNA.
DR EMBL; BC062088; AAH62088.1; -; mRNA.
DR RefSeq; NP_640345.1; NM_139252.1.
DR AlphaFoldDB; Q8K593; -.
DR STRING; 10116.ENSRNOP00000000193; -.
DR GlyGen; Q8K593; 2 sites.
DR PaxDb; Q8K593; -.
DR Ensembl; ENSRNOT00000000193; ENSRNOP00000000193; ENSRNOG00000000177.
DR GeneID; 246115; -.
DR KEGG; rno:246115; -.
DR UCSC; RGD:628893; rat.
DR CTD; 8612; -.
DR RGD; 628893; Plpp2.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000155885; -.
DR HOGENOM; CLU_021458_3_1_1; -.
DR InParanoid; Q8K593; -.
DR OMA; MDVVCVL; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q8K593; -.
DR TreeFam; TF316040; -.
DR Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00085; -.
DR PRO; PR:Q8K593; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000000177; Expressed in jejunum and 18 other tissues.
DR Genevisible; Q8K593; RN.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum 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:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0106235; F:ceramide-1-phosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB.
DR GO; GO:0046839; P:phospholipid dephosphorylation; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:UniProtKB.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0006670; P:sphingosine metabolic process; ISS:UniProtKB.
DR InterPro; IPR028674; LPP2.
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:SF25; PTHR10165:SF25; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Endoplasmic reticulum; Endosome; Glycoprotein; Hydrolase;
KW Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..276
FT /note="Phospholipid phosphatase 2"
FT /id="PRO_0000220911"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..51
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..161
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..225
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 117..125
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 164..167
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 212..223
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 252..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="Proton donors"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT ACT_SITE 219
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT SITE 223
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 276 AA; 31101 MW; 41A0E1243458E24C CRC64;
MERRWVFVLL DVLCVLVASL PFIILTLVNA PYKRGFYCGD DSIRYPYRPD TITHGLMAGV
IITATVVLVS SGEAYLVYTD RLYSRSDFNN YVAAIYKVLG TFLFGAAVSQ SLTDLAKYMI
GRLRPSFLAV CDPDWSRVNC SGYVQVEVCR GSPANVTEAR LSFYSGHSSF GMYCMLFLAL
YVQARLCWKW ARLLRPTVQF FLVAFAIYVG YTRVSDNKHH WSDVLVGLLQ GALVACLTVC
YVSDFFKSRP PQSCQENEES ERKPSLSLTL TLGDRP
