PLPP1_PIG
ID PLPP1_PIG Reviewed; 285 AA.
AC P60588; A0A286ZIK9;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 2.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Phospholipid phosphatase 1 {ECO:0000305};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:O14494};
DE EC=3.1.3.106 {ECO:0000250|UniProtKB:Q61469};
DE EC=3.1.3.4 {ECO:0000269|PubMed:1334090, ECO:0000269|PubMed:8702556};
DE EC=3.1.3.81 {ECO:0000250|UniProtKB:Q61469};
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:0000250|UniProtKB:O14494}; Synonyms=LPP1, PPAP2A;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc;
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
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 FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RC TISSUE=Thymus;
RX PubMed=1334090; DOI=10.1016/s0021-9258(19)74041-1;
RA Kanoh H., Imai S., Yamada K., Sakane F.;
RT "Purification and properties of phosphatidic acid phosphatase from porcine
RT thymus membranes.";
RL J. Biol. Chem. 267:25309-25314(1992).
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 (Ref.1, PubMed:8702556, PubMed:1334090). 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 (By
CC similarity). It is for instance essential for the extracellular
CC hydrolysis of S1P and subsequent conversion into intracellular S1P (By
CC similarity). Involved in the regulation of inflammation, platelets
CC activation, cell proliferation and migration among other processes (By
CC similarity). May also have an intracellular activity to regulate
CC phospholipid-mediated signaling pathways (By similarity).
CC {ECO:0000250|UniProtKB:O08564, ECO:0000250|UniProtKB:O14494,
CC ECO:0000269|PubMed:1334090, ECO:0000269|PubMed:8702556,
CC ECO:0000269|Ref.1}.
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:1334090, ECO:0000269|PubMed:8702556};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC Evidence={ECO:0000305|PubMed:8702556};
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:1334090,
CC ECO:0000269|PubMed:8702556};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC Evidence={ECO:0000305|PubMed:8702556};
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:O14494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737;
CC Evidence={ECO:0000250|UniProtKB:O14494};
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:O14494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885;
CC Evidence={ECO:0000250|UniProtKB:O14494};
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:0000250|UniProtKB:Q61469};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33156;
CC Evidence={ECO:0000250|UniProtKB:Q61469};
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:Q61469};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC Evidence={ECO:0000250|UniProtKB:Q61469};
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:Q61469};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450;
CC Evidence={ECO:0000250|UniProtKB:Q61469};
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:O14494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
CC Evidence={ECO:0000250|UniProtKB:O14494};
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:O14494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744;
CC Evidence={ECO:0000250|UniProtKB:O14494};
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 (PubMed:1334090). Insensitive to N-ethylmaleimide (PubMed:1334090).
CC {ECO:0000269|PubMed:1334090}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-7.4 with 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate as substrate. {ECO:0000269|PubMed:1334090};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:1334090, ECO:0000269|PubMed:8702556}.
CC -!- SUBUNIT: Forms functional homodimers and homooligomers that are not
CC required for substrate recognition and catalytic activity (By
CC similarity). Can also form heterooligomers with PLPP2 and PLPP3 (By
CC similarity). {ECO:0000250|UniProtKB:O88956,
CC ECO:0000250|UniProtKB:Q61469}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8702556};
CC Multi-pass 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:0000250|UniProtKB:Q61469}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: N-glycosylated. N-linked sugars are of the complex type
CC (PubMed:8702556). N-glycosylation is not required for the phosphatase
CC activity (By similarity). {ECO:0000250|UniProtKB:Q61469,
CC ECO:0000269|PubMed:8702556}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; AEMK02000102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003133999.3; XM_003133951.5.
DR AlphaFoldDB; P60588; -.
DR STRING; 9823.ENSSSCP00000017921; -.
DR Ensembl; ENSSSCT00000042472; ENSSSCP00000031391; ENSSSCG00000016912.
DR Ensembl; ENSSSCT00015023278; ENSSSCP00015009070; ENSSSCG00015017646.
DR Ensembl; ENSSSCT00025074606; ENSSSCP00025032325; ENSSSCG00025054555.
DR Ensembl; ENSSSCT00030099155; ENSSSCP00030045630; ENSSSCG00030070887.
DR Ensembl; ENSSSCT00035100779; ENSSSCP00035042829; ENSSSCG00035074260.
DR Ensembl; ENSSSCT00040054392; ENSSSCP00040022622; ENSSSCG00040040197.
DR Ensembl; ENSSSCT00045012611; ENSSSCP00045008646; ENSSSCG00045007483.
DR Ensembl; ENSSSCT00050082531; ENSSSCP00050035419; ENSSSCG00050060580.
DR Ensembl; ENSSSCT00055031058; ENSSSCP00055024725; ENSSSCG00055015648.
DR Ensembl; ENSSSCT00060055689; ENSSSCP00060023781; ENSSSCG00060041097.
DR Ensembl; ENSSSCT00065034385; ENSSSCP00065014261; ENSSSCG00065025681.
DR Ensembl; ENSSSCT00070003725; ENSSSCP00070003088; ENSSSCG00070001957.
DR GeneID; 100515451; -.
DR KEGG; ssc:100515451; -.
DR CTD; 8611; -.
DR VGNC; VGNC:91570; PLPP1.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000156730; -.
DR OrthoDB; 1354951at2759; -.
DR Reactome; R-SSC-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000008227; Chromosome 16.
DR Proteomes; UP000314985; Chromosome 16.
DR Bgee; ENSSSCG00000016912; Expressed in endocardial endothelium and 44 other tissues.
DR ExpressionAtlas; P60588; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0106235; F:ceramide-1-phosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IDA: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:0009395; P:phospholipid catabolic process; IDA:UniProtKB.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR GO; GO:0006670; P:sphingosine metabolic process; ISS: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 Cell membrane; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..285
FT /note="Phospholipid phosphatase 1"
FT /id="PRO_0000220907"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q61469"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..53
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q61469"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q61469"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..164
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q61469"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q61469"
FT TRANSMEM 197..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..229
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q61469"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q61469"
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 257..285
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 COMPBIAS 270..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000255"
SQ SEQUENCE 285 AA; 32321 MW; 702618FD8B4FAFCB CRC64;
MFDKTRLPYV ALDVLCVLLA GLPFAILTSR HTPFQRGLFC NDESIKYPYK EDTIPYPLLG
GIIIPFSIIV MIVGETLSVY FNLLHSNSFI RNNYIATIYK AIGTFLFGAA ASQSLTDIAK
YSIGRLRPHF LDVCDPDWSK INCSDGYIEN YICRGNAQKV KEGRLSFYSG HSSFSMYCML
FVALYLQARM KGDWARLLRP TLQFGLVAVS IYVGLSRVSD YKHHWSDVLT GLIQGALVAI
VVAVYVSDFF KERNSPFKER KEEDSHTTLH ETPTTGNHYR NSHQP
