UniProtKB - P60588 (PLPP1_PIG)
Protein
Phospholipid phosphatase 1
Gene
PLPP1
Organism
Sus scrofa (Pig)
Status
Functioni
Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P (Ref. 1, PubMed:8702556, PubMed:1334090). Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (By similarity). Through its extracellular phosphatase activity allows both the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes (By similarity). It is for instance essential for the extracellular hydrolysis of S1P and subsequent conversion into intracellular S1P (By similarity). Involved in the regulation of inflammation, platelets activation, cell proliferation and migration among other processes (By similarity). May also have an intracellular activity to regulate phospholipid-mediated signaling pathways (By similarity).By similarity3 Publications
Catalytic activityi
- EC:3.1.3.42 PublicationsThis reaction proceeds in the forward1 Publication direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-dihexadecanoyl-sn-glycerol + phosphateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + phosphate2 PublicationsThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-octadecenoyl)-glycerol + phosphateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- EC:3.1.3.106By similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + phosphateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + H+ + phosphateBy similarityEC:3.1.3.81By similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-octadecenoyl) ethanolamine + phosphateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphateBy similarityThis reaction proceeds in the forwardBy similarity direction.
Activity regulationi
Magnesium-independent phospholipid phosphatase (PubMed:1334090). Insensitive to N-ethylmaleimide (PubMed:1334090).1 Publication
pH dependencei
Optimum pH is 7-7.4 with 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate as substrate.1 Publication
: phospholipid metabolism Pathwayi
This protein is involved in the pathway phospholipid metabolism, which is part of Lipid metabolism.2 PublicationsView all proteins of this organism that are known to be involved in the pathway phospholipid metabolism and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 171 | Proton donorsBy similarity | 1 | |
Active sitei | 223 | NucleophileBy similarity | 1 | |
Sitei | 227 | Stabilizes the active site histidine for nucleophilic attackBy similarity | 1 |
GO - Molecular functioni
- ceramide-1-phosphate phosphatase activity Source: UniProtKB
- diacylglycerol diphosphate phosphatase activity Source: UniProtKB
- phosphatidate phosphatase activity Source: UniProtKB
- sphingosine-1-phosphate phosphatase activity Source: UniProtKB
GO - Biological processi
- ceramide metabolic process Source: UniProtKB
- phospholipid catabolic process Source: UniProtKB
- phospholipid dephosphorylation Source: UniProtKB
- signal transduction Source: UniProtKB
- sphingosine metabolic process Source: UniProtKB
Keywordsi
Molecular function | Hydrolase |
Biological process | Lipid metabolism |
Enzyme and pathway databases
UniPathwayi | UPA00085 |
Names & Taxonomyi
Protein namesi | Recommended name: Phospholipid phosphatase 1Curated (EC:3.1.3.-By similarity, EC:3.1.3.106By similarity, EC:3.1.3.42 Publications, EC:3.1.3.81By similarity)Alternative name(s): Lipid phosphate phosphohydrolase 1 PAP2-alpha Phosphatidate phosphohydrolase type 2a Phosphatidic acid phosphatase 2a Short name: PAP-2a Short name: PAP2a |
Gene namesi | |
Organismi | Sus scrofa (Pig) |
Taxonomic identifieri | 9823 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus |
Proteomesi |
|
Organism-specific databases
VGNCi | VGNC:91570, PLPP1 |
Subcellular locationi
Plasma membrane
- Cell membrane 1 Publication; Multi-pass membrane protein Sequence analysis
- Apical cell membrane By similarity; Multi-pass membrane protein Sequence analysis
Other locations
- Membrane raft By similarity; Multi-pass membrane protein Sequence analysis
- caveola By similarity; Multi-pass membrane protein Sequence analysis
Plasma Membrane
- apical plasma membrane Source: UniProtKB
- caveola Source: UniProtKB
- integral component of plasma membrane Source: UniProtKB
Other locations
- integral component of membrane Source: UniProtKB
- membrane raft Source: UniProtKB
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 6 | CytoplasmicBy similarity | 6 | |
Transmembranei | 7 – 27 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 28 – 53 | ExtracellularBy similarityAdd BLAST | 26 | |
Transmembranei | 54 – 74 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 75 – 94 | CytoplasmicBy similarityAdd BLAST | 20 | |
Transmembranei | 95 – 115 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 116 – 164 | ExtracellularBy similarityAdd BLAST | 49 | |
Transmembranei | 165 – 185 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 186 – 196 | CytoplasmicBy similarityAdd BLAST | 11 | |
Transmembranei | 197 – 216 | HelicalSequence analysisAdd BLAST | 20 | |
Topological domaini | 217 – 229 | ExtracellularBy similarityAdd BLAST | 13 | |
Transmembranei | 230 – 250 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 251 – 285 | CytoplasmicBy similarityAdd BLAST | 35 |
Keywords - Cellular componenti
Cell membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000220907 | 1 – 285 | Phospholipid phosphatase 1Add BLAST | 285 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 142 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Post-translational modificationi
N-glycosylated. N-linked sugars are of the complex type (PubMed:8702556). N-glycosylation is not required for the phosphatase activity (By similarity).By similarity1 Publication
Keywords - PTMi
GlycoproteinInteractioni
Subunit structurei
Forms functional homodimers and homooligomers that are not required for substrate recognition and catalytic activity (By similarity). Can also form heterooligomers with PLPP2 and PLPP3 (By similarity).
By similarityFamily & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 120 – 128 | Phosphatase sequence motif IBy similarity | 9 | |
Regioni | 168 – 171 | Phosphatase sequence motif IIBy similarity | 4 | |
Regioni | 216 – 227 | Phosphatase sequence motif IIIBy similarityAdd BLAST | 12 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 5 – 7 | PDZ-binding; involved in localization to the apical cell membraneBy similarity | 3 |
Sequence similaritiesi
Belongs to the PA-phosphatase related phosphoesterase family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG3030, Eukaryota |
GeneTreei | ENSGT00940000156730 |
OrthoDBi | 1354951at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR028670, LPP1 IPR036938, P_Acid_Pase_2/haloperoxi_sf IPR000326, P_Acid_Pase_2/haloperoxidase IPR043216, PLPP |
PANTHERi | PTHR10165, PTHR10165, 1 hit PTHR10165:SF26, PTHR10165:SF26, 1 hit |
Pfami | View protein in Pfam PF01569, PAP2, 1 hit |
SMARTi | View protein in SMART SM00014, acidPPc, 1 hit |
SUPFAMi | SSF48317, SSF48317, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
P60588-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MFDKTRLPYV ALDVLCVLLA GLPFAILTSR HTPFQRGLFC NDESIKYPYK
60 70 80 90 100
EDTIPYPLLG GIIIPFSIIV MIVGETLSVY FNLLHSNSFI RNNYIATIYK
110 120 130 140 150
AIGTFLFGAA ASQSLTDIAK YSIGRLRPHF LDVCDPDWSK INCSDGYIEN
160 170 180 190 200
YICRGNAQKV KEGRLSFYSG HSSFSMYCML FVALYLQARM KGDWARLLRP
210 220 230 240 250
TLQFGLVAVS IYVGLSRVSD YKHHWSDVLT GLIQGALVAI VVAVYVSDFF
260 270 280
KERNSPFKER KEEDSHTTLH ETPTTGNHYR NSHQP
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF1SLL5 | F1SLL5_PIG | Lipid phosphate phosphohydrolase 1 | PLPP1 | 290 | Annotation score: | ||
A0A286ZXH9 | A0A286ZXH9_PIG | Lipid phosphate phosphohydrolase 1 | PLPP1 | 286 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AEMK02000102 Genomic DNA No translation available. |
RefSeqi | XP_003133999.3, XM_003133951.5 |
Genome annotation databases
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AEMK02000102 Genomic DNA No translation available. |
RefSeqi | XP_003133999.3, XM_003133951.5 |
3D structure databases
SMRi | P60588 |
ModBasei | Search... |
Genome annotation databases
Organism-specific databases
CTDi | 8611 |
VGNCi | VGNC:91570, PLPP1 |
Phylogenomic databases
eggNOGi | KOG3030, Eukaryota |
GeneTreei | ENSGT00940000156730 |
OrthoDBi | 1354951at2759 |
Enzyme and pathway databases
UniPathwayi | UPA00085 |
Family and domain databases
InterProi | View protein in InterPro IPR028670, LPP1 IPR036938, P_Acid_Pase_2/haloperoxi_sf IPR000326, P_Acid_Pase_2/haloperoxidase IPR043216, PLPP |
PANTHERi | PTHR10165, PTHR10165, 1 hit PTHR10165:SF26, PTHR10165:SF26, 1 hit |
Pfami | View protein in Pfam PF01569, PAP2, 1 hit |
SMARTi | View protein in SMART SM00014, acidPPc, 1 hit |
SUPFAMi | SSF48317, SSF48317, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PLPP1_PIG | |
Accessioni | P60588Primary (citable) accession number: P60588 Secondary accession number(s): A0A286ZIK9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 15, 2004 |
Last sequence update: | February 26, 2020 | |
Last modified: | February 10, 2021 | |
This is version 53 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families