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Protein

Phospholipid phosphatase 1

Gene

Plpp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), diacyl glycerol pyrophosphate (DGPP), ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > C-1-P > S-1-P.

Catalytic activityi

A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Chemistry

SwissLipidsiSLP:000000610.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid phosphatase 1Imported (EC:3.1.3.4)
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
Name:Plpp1Imported
Synonyms:Lpp1, Ppap2a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621832. Plpp1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence analysis
Transmembranei7 – 2721HelicalSequence analysisAdd
BLAST
Topological domaini28 – 5326ExtracellularSequence analysisAdd
BLAST
Transmembranei54 – 7421HelicalSequence analysisAdd
BLAST
Topological domaini75 – 8814CytoplasmicSequence analysisAdd
BLAST
Transmembranei89 – 10921HelicalSequence analysisAdd
BLAST
Topological domaini110 – 16455ExtracellularSequence analysisAdd
BLAST
Transmembranei165 – 18521HelicalSequence analysisAdd
BLAST
Topological domaini186 – 1949CytoplasmicSequence analysis
Transmembranei195 – 21521HelicalSequence analysisAdd
BLAST
Topological domaini216 – 22914ExtracellularSequence analysisAdd
BLAST
Transmembranei230 – 25021HelicalSequence analysisAdd
BLAST
Topological domaini251 – 28232CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282Phospholipid phosphatase 1PRO_0000220908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiO08564.
PRIDEiO08564.

PTM databases

iPTMnetiO08564.
PhosphoSiteiO08564.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000062843.

Structurei

3D structure databases

ProteinModelPortaliO08564.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3030. Eukaryota.
COG0671. LUCA.
HOGENOMiHOG000041307.
HOVERGENiHBG002048.
InParanoidiO08564.
PhylomeDBiO08564.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR028670. LPP1.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PANTHERiPTHR10165:SF26. PTHR10165:SF26. 1 hit.
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: O08564-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MFDKPRLPYV VLDVICVLLA GLPFIILTSR HTPFQRGVFC TDESIKYPYR
60 70 80 90 100
EDTIPYALLG GIVIPFCIIV MITGETLSVY FNVLHSNSFV SNHYIATIYK
110 120 130 140 150
AVGAFLFGAS ASQSLTDIAK YSIGRLRPHF LAVCNPDWSK INCSDGYIEN
160 170 180 190 200
FVCQGNEQKV REGRLSFYSG HSSFSMYCML FVALYLQARM KGDWARLLRP
210 220 230 240 250
MLQFGLVALS IYVGLSRVSD YKHHWSDVLI GLIQGAVVAI LVVLYVTDFF
260 270 280
KTTESNKERK EDSHTTLHET TNRQSYARNH EP
Length:282
Mass (Da):31,996
Last modified:July 1, 1997 - v1
Checksum:iA4ED3DEB33FD7943
GO
Isoform 2 (identifier: O08564-2) [UniParc]FASTAAdd to basket

Also known as: LPP1a

The sequence of this isoform differs from the canonical sequence as follows:
     21-70: GLPFIILTSR...GIVIPFCIIV → SMPMAVVNLG...LVGLGIPIFS

Show »
Length:283
Mass (Da):31,922
Checksum:i3D2B45015891C873
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei21 – 7050GLPFI…FCIIV → SMPMAVVNLGQIYPFQRGFF CSDNSVKYPYHDSTVTTSVL VLVGLGIPIFS in isoform 2. 1 PublicationVSP_009653Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90556 mRNA. Translation: AAB50246.1.
AF503609 mRNA. Translation: AAM28631.1.
UniGeneiRn.61687.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90556 mRNA. Translation: AAB50246.1.
AF503609 mRNA. Translation: AAM28631.1.
UniGeneiRn.61687.

3D structure databases

ProteinModelPortaliO08564.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000062843.

Chemistry

SwissLipidsiSLP:000000610.

PTM databases

iPTMnetiO08564.
PhosphoSiteiO08564.

Proteomic databases

PaxDbiO08564.
PRIDEiO08564.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi621832. Plpp1.

Phylogenomic databases

eggNOGiKOG3030. Eukaryota.
COG0671. LUCA.
HOGENOMiHOG000041307.
HOVERGENiHBG002048.
InParanoidiO08564.
PhylomeDBiO08564.

Miscellaneous databases

PROiO08564.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR028670. LPP1.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PANTHERiPTHR10165:SF26. PTHR10165:SF26. 1 hit.
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid and sphingolipid phosphate esters."
    Jasinska R., Zhang Q.-X., Pilquil C., Singh I., Xu J., Dewald J., Dillon D.A., Berthiaume L.G., Carman G.M., Waggoner D.W., Brindley D.N.
    Biochem. J. 340:677-686(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    Tissue: Liver.
  2. "Molecular cloning and expression of pulmonary lipid phosphate phosphohydrolases."
    Nanjundan M., Possmayer F.
    Am. J. Physiol. 281:L1484-L1493(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Strain: Sprague-Dawley.
    Tissue: Lung.
  3. "Phosphatidate phosphohydrolase catalyzes the hydrolysis of ceramide 1-phosphate, lysophosphatidate, and sphingosine 1-phosphate."
    Waggoner D.W., Gomez-Munoz A., Dewald J., Brindley D.N.
    J. Biol. Chem. 271:16506-16509(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiPLPP1_RAT
AccessioniPrimary (citable) accession number: O08564
Secondary accession number(s): Q8K594
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: July 1, 1997
Last modified: June 8, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.