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Q99JY8 (LPP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipid phosphate phosphohydrolase 3

EC=3.1.3.4
Alternative name(s):
PAP2-beta
Phosphatidate phosphohydrolase type 2b
Phosphatidic acid phosphatase 2b
Short name=PAP-2b
Short name=PAP2b
Gene names
Name:Ppap2b
Synonyms:Lpp3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P) By similarity. Essential to the formation of the chorioallantoic placenta and extraembryonic vasculature. Also mediates gastrulation and axis formation, probably by regulating the Wnt signaling pathway. Ref.4

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Involvement in disease

Ppap2b deficient embryos fail to form a chorioallantoic placenta and yolk sac vasculature. A subset of embryos also show a shortening of the anterior-posterior axis and frequent duplication of axial structures. Loss of Ppap2b results in a marked increase in beta-catenin-mediated T-cell factor (TCF) transcription. Ref.4

Sequence similarities

Belongs to the PA-phosphatase related phosphoesterase family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Hydrolase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processBergmann glial cell differentiation

Inferred from mutant phenotype PubMed 21319224. Source: MGI

blood vessel development

Inferred from mutant phenotype Ref.4. Source: MGI

canonical Wnt signaling pathway

Inferred from direct assay PubMed 20123964. Source: BHF-UCL

canonical Wnt signaling pathway involved in positive regulation of cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway involved in positive regulation of endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway involved in positive regulation of wound healing

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from direct assay PubMed 16099422. Source: MGI

cell-cell adhesion

Inferred from direct assay PubMed 16099422. Source: MGI

dephosphorylation

Inferred from mutant phenotype Ref.4PubMed 21319224. Source: GOC

gastrulation with mouth forming second

Inferred from mutant phenotype Ref.4. Source: MGI

homotypic cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from direct assay PubMed 20123964. Source: BHF-UCL

phospholipid metabolic process

Inferred from mutant phenotype Ref.4. Source: MGI

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 16099422. Source: MGI

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 20123964. Source: BHF-UCL

protein stabilization

Inferred from direct assay PubMed 20123964. Source: BHF-UCL

regulation of Wnt signaling pathway

Inferred from direct assay Ref.4. Source: MGI

regulation of sphingolipid mediated signaling pathway

Inferred from mutant phenotype PubMed 21319224. Source: MGI

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 21319224. Source: MGI

   Molecular_functionintegrin binding

Inferred from direct assay PubMed 16099422. Source: MGI

lipid phosphatase activity

Inferred from mutant phenotype Ref.4. Source: MGI

phosphatidate phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

sphingosine-1-phosphate phosphatase activity

Inferred from mutant phenotype PubMed 21319224. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Lipid phosphate phosphohydrolase 3
PRO_0000220913

Regions

Topological domain1 – 3333Cytoplasmic Potential
Transmembrane34 – 5421Helical; Potential
Topological domain55 – 8531Lumenal Potential
Transmembrane86 – 10621Helical; Potential
Topological domain107 – 12317Cytoplasmic Potential
Transmembrane124 – 14421Helical; Potential
Topological domain145 – 19450Lumenal Potential
Transmembrane195 – 21521Helical; Potential
Topological domain216 – 22611Cytoplasmic Potential
Transmembrane227 – 24721Helical; Potential
Topological domain248 – 25811Lumenal Potential
Transmembrane259 – 27921Helical; Potential
Topological domain280 – 31233Cytoplasmic Potential

Amino acid modifications

Modified residue191Phosphoserine By similarity
Modified residue2981Phosphoserine By similarity
Glycosylation1711N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1871S → C in BAE34848. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99JY8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: D782986E04B57D7D

FASTA31235,216
        10         20         30         40         50         60 
MQSYKYDKAI VPESKNGGSP ALNNNPRKGG SKRVLLICLD LFCLFMAALP FLIIETSTIK 

        70         80         90        100        110        120 
PYRRGFYCND ESIKYPLKVS ETINDAVLCA VGIVIAILAI ITGEFYRIYY LKEKSRSTTQ 

       130        140        150        160        170        180 
NPYVAALYKQ VGCFLFGCAI SQSFTDIAKV SIGRLRPHFL SVCDPDFSQI NCSEGYIQNY 

       190        200        210        220        230        240 
RCRGEDSKVQ EARKSFFSGH ASFSMFTMLY LVLYLQARFT WRGARLLRPL LQFTLLMMAF 

       250        260        270        280        290        300 
YTGLSRVSDY KHHPSDVLAG FAQGALVACC IVFFVSDLFK TKTSLSLPAP AIRREILSPV 

       310 
DIIDRNNHHN MV 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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].
Strain: C57BL/6J.
[2]"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].
Strain: FVB/N.
Tissue: Mammary gland.
[3]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 283-293, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[4]"The lipid phosphatase LPP3 regulates extra-embryonic vasculogenesis and axis patterning."
Escalante-Alcalde D., Hernandez L., Le Stunff H., Maeda R., Lee H.-S., Cheng G. Jr., Sciorra V.A., Daar I., Spiegel S., Morris A.J., Stewart C.L.
Development 130:4623-4637(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISEASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK159136 mRNA. Translation: BAE34848.1.
AK160056 mRNA. Translation: BAE35594.1.
BC005558 mRNA. Translation: AAH05558.1.
RefSeqNP_542122.1. NM_080555.2.
UniGeneMm.348326.

3D structure databases

ProteinModelPortalQ99JY8.
SMRQ99JY8. Positions 142-271.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99JY8. 5 interactions.
MINTMINT-4612030.
STRING10090.ENSMUSP00000065719.

PTM databases

PhosphoSiteQ99JY8.

Proteomic databases

PaxDbQ99JY8.
PRIDEQ99JY8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000064139; ENSMUSP00000065719; ENSMUSG00000028517.
GeneID67916.
KEGGmmu:67916.
UCSCuc008tye.1. mouse.

Organism-specific databases

CTD8613.
MGIMGI:1915166. Ppap2b.

Phylogenomic databases

eggNOGCOG0671.
GeneTreeENSGT00620000087654.
HOGENOMHOG000041307.
HOVERGENHBG002048.
InParanoidQ99JY8.
KOK01080.
OMANNNCKDH.
OrthoDBEOG7C5M9Q.
PhylomeDBQ99JY8.
TreeFamTF316040.

Gene expression databases

BgeeQ99JY8.
CleanExMM_PPAP2B.
GenevestigatorQ99JY8.

Family and domain databases

Gene3D1.20.144.10. 1 hit.
InterProIPR028675. LPP3.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PANTHERPTHR10165:SF24. PTHR10165:SF24. 1 hit.
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMSSF48317. SSF48317. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPPAP2B. mouse.
NextBio325938.
PROQ99JY8.
SOURCESearch...

Entry information

Entry nameLPP3_MOUSE
AccessionPrimary (citable) accession number: Q99JY8
Secondary accession number(s): Q3TVM4, Q3TXR7, Q8BTB7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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