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Protein

Phospholipid phosphatase 1

Gene

Plpp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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

  • ceramide metabolic process Source: MGI
  • diacylglycerol biosynthetic process Source: MGI
  • protein dephosphorylation Source: MGI
  • signal transduction Source: MGI
  • sphingosine metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.1.3.81. 3474.
ReactomeiR-MMU-1660661. Sphingolipid de novo biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid phosphatase 1By similarity (EC:3.1.3.4)
Alternative name(s):
35 kDa PAP
Short name:
mPAP
Hydrogen peroxide-inducible protein 53
Short name:
Hic53
Lipid phosphate phosphohydrolase 1
PAP2-alpha
Phosphatidate phosphohydrolase type 2a
Phosphatidic acid phosphatase 2a
Short name:
PAP-2a
Short name:
PAP2a
Gene namesi
Name:Plpp1By similarity
Synonyms:Hpic53, Lpp1, Ppap2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:108412. 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 – 19914CytoplasmicSequence analysisAdd
BLAST
Transmembranei200 – 22021HelicalSequence analysisAdd
BLAST
Topological domaini221 – 2299ExtracellularSequence analysis
Transmembranei230 – 25021HelicalSequence analysisAdd
BLAST
Topological domaini251 – 28333CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: Ensembl
  • integral component of plasma membrane Source: MGI
  • membrane Source: UniProtKB
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 283283Phospholipid phosphatase 1PRO_0000220906Add
BLAST

Amino acid modifications

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

Post-translational modificationi

N-glycosylated. Contains high-mannose oligosaccharide.

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ61469.
PRIDEiQ61469.

PTM databases

iPTMnetiQ61469.
PhosphoSiteiQ61469.

Expressioni

Tissue specificityi

Highly expressed in kidney and lung. Almost undetectable in brain, heart, bone, muscle or spleen.

Inductioni

Moderately, by hydrogen peroxide, calcium ionophore and dexamethasone.1 Publication

Gene expression databases

BgeeiQ61469.
CleanExiMM_PPAP2A.
GenevisibleiQ61469. MM.

Interactioni

Subunit structurei

Homodimer. This complex seems not to be involved in substrate recognition, it may confer only structural or functional stability.1 Publication

Protein-protein interaction databases

IntActiQ61469. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ61469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00620000087654.
HOGENOMiHOG000041307.
HOVERGENiHBG002048.
InParanoidiQ61469.
KOiK01080.
OMAiDWAQVNC.
OrthoDBiEOG7C5M9Q.
PhylomeDBiQ61469.
TreeFamiTF316040.

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

Isoform 1 (identifier: Q61469-1) [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
MFDKTRLPYV ALDVICVLLA GLPFAILTSR HTPFQRGIFC NDDSIKYPYK
60 70 80 90 100
EDTIPYALLG GIVIPFCIIV MSIGESLSVY FNVLHSNSFV GNPYIATIYK
110 120 130 140 150
AVGAFLFGVS ASQSLTDIAK YTIGSLRPHF LAICNPDWSK INCSDGYIED
160 170 180 190 200
YICQGNEEKV KEGRLSFYSG HSSFSMYCML FVALYLQARM KGDWARLLRP
210 220 230 240 250
MLQFGLIAFS IYVGLSRVSD YKHHWSDVTV GLIQGAAMAI LVALYVSDFF
260 270 280
KDTHSYKERK EEDPHTTLHE TASSRNYSTN HEP
Length:283
Mass (Da):31,892
Last modified:November 1, 1996 - v1
Checksum:i669690568E549CC6
GO
Isoform 2 (identifier: Q61469-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     21-70: GLPFAILTSR...GIVIPFCIIV → AMPMTILKLG...ILGLGLPIFS

Show »
Length:284
Mass (Da):31,996
Checksum:i72588D6301E3DD29
GO

Sequence cautioni

The sequence AAA85353.1 differs from that shown. Reason: Frameshift at several positions. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei21 – 7050GLPFA…FCIIV → AMPMTILKLGKVYPFQRGFF CTDNSVKYPYHDSTIPSRIL AILGLGLPIFS in isoform 2. 3 PublicationsVSP_009652Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L43371 mRNA. Translation: AAA85353.1. Sequence problems.
D84376 mRNA. Translation: BAA12335.1.
AY247795 mRNA. Translation: AAP04434.1.
AY247796 mRNA. Translation: AAP04435.1.
AK077275 mRNA. Translation: BAC36724.1.
BC061161 mRNA. Translation: AAH61161.1.
CCDSiCCDS26776.1. [Q61469-2]
CCDS26777.1. [Q61469-1]
PIRiS66668.
RefSeqiNP_032273.1. NM_008247.3. [Q61469-2]
NP_032929.1. NM_008903.2. [Q61469-1]
UniGeneiMm.291029.
Mm.317186.

Genome annotation databases

EnsembliENSMUST00000016144; ENSMUSP00000016144; ENSMUSG00000021759. [Q61469-2]
ENSMUST00000070951; ENSMUSP00000064423; ENSMUSG00000021759. [Q61469-1]
GeneIDi19012.
KEGGimmu:19012.
UCSCiuc007rwq.2. mouse. [Q61469-1]
uc007rwr.2. mouse. [Q61469-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L43371 mRNA. Translation: AAA85353.1. Sequence problems.
D84376 mRNA. Translation: BAA12335.1.
AY247795 mRNA. Translation: AAP04434.1.
AY247796 mRNA. Translation: AAP04435.1.
AK077275 mRNA. Translation: BAC36724.1.
BC061161 mRNA. Translation: AAH61161.1.
CCDSiCCDS26776.1. [Q61469-2]
CCDS26777.1. [Q61469-1]
PIRiS66668.
RefSeqiNP_032273.1. NM_008247.3. [Q61469-2]
NP_032929.1. NM_008903.2. [Q61469-1]
UniGeneiMm.291029.
Mm.317186.

3D structure databases

ProteinModelPortaliQ61469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61469. 1 interaction.

PTM databases

iPTMnetiQ61469.
PhosphoSiteiQ61469.

Proteomic databases

MaxQBiQ61469.
PRIDEiQ61469.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000016144; ENSMUSP00000016144; ENSMUSG00000021759. [Q61469-2]
ENSMUST00000070951; ENSMUSP00000064423; ENSMUSG00000021759. [Q61469-1]
GeneIDi19012.
KEGGimmu:19012.
UCSCiuc007rwq.2. mouse. [Q61469-1]
uc007rwr.2. mouse. [Q61469-2]

Organism-specific databases

CTDi8611.
MGIiMGI:108412. Plpp1.

Phylogenomic databases

GeneTreeiENSGT00620000087654.
HOGENOMiHOG000041307.
HOVERGENiHBG002048.
InParanoidiQ61469.
KOiK01080.
OMAiDWAQVNC.
OrthoDBiEOG7C5M9Q.
PhylomeDBiQ61469.
TreeFamiTF316040.

Enzyme and pathway databases

BRENDAi3.1.3.81. 3474.
ReactomeiR-MMU-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

ChiTaRSiPpap2a. mouse.
PROiQ61469.
SOURCEiSearch...

Gene expression databases

BgeeiQ61469.
CleanExiMM_PPAP2A.
GenevisibleiQ61469. MM.

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

« Hide 'large scale' publications
  1. "Isolation of a novel ras-recision gene that is induced by hydrogen peroxide from a mouse osteoblastic cell line, MC3T3-E1."
    Egawa K., Yoshiwara M., Shibanuma M., Nose K.
    FEBS Lett. 372:74-77(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
    Tissue: Calvaria.
  2. "Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes."
    Kai M., Wada I., Imai S., Sakane F., Kanoh H.
    J. Biol. Chem. 271:18931-18938(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  3. Yokoyama K., Tigyi G.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Strain: FVB/N.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Ovary and Uterus.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  6. "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: CHARACTERIZATION.
    Tissue: Liver.
  7. "Lipid phosphate phosphatases dimerise, but this interaction is not required for in vivo activity."
    Burnett C., Makridou P., Hewlett L., Howard K.
    BMC Biochem. 5:2-2(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "Mice with transgenic overexpression of lipid phosphate phosphatase-1 display multiple organotypic deficits without alteration in circulating lysophosphatidate level."
    Yue J., Yokoyama K., Balazs L., Baker D.L., Smalley D., Pilquil C., Brindley D.N., Tigyi G.
    Cell. Signal. 16:385-399(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: OVEREXPRESSION.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiPLPP1_MOUSE
AccessioniPrimary (citable) accession number: Q61469
Secondary accession number(s): Q61690, Q6GT30, Q8BPB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Overexpression elicited a number of phenotypic alteration without affecting several aspects of LPA signaling. Phenotypic abnormalities affect primarily three organs: the liver, the skin, and the reproductive organs. There is a reduction on body size, birth weight, abnormalities in fur growth, and a severely impaired spermatogenesis.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.