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Protein

Lipid phosphate phosphohydrolase 3

Gene

Ppap2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

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

GO - Molecular functioni

  • integrin binding Source: MGI
  • lipid phosphatase activity Source: MGI
  • phosphatidate phosphatase activity Source: UniProtKB-EC
  • sphingosine-1-phosphate phosphatase activity Source: MGI

GO - Biological processi

  • Bergmann glial cell differentiation Source: MGI
  • blood vessel development Source: MGI
  • canonical Wnt signaling pathway Source: BHF-UCL
  • canonical Wnt signaling pathway involved in positive regulation of cell-cell adhesion Source: MGI
  • canonical Wnt signaling pathway involved in positive regulation of endothelial cell migration Source: MGI
  • canonical Wnt signaling pathway involved in positive regulation of wound healing Source: MGI
  • cell adhesion Source: MGI
  • dephosphorylation Source: GOC
  • gastrulation with mouth forming second Source: MGI
  • homotypic cell-cell adhesion Source: MGI
  • negative regulation of protein phosphorylation Source: BHF-UCL
  • phospholipid metabolic process Source: MGI
  • positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • protein stabilization Source: BHF-UCL
  • regulation of sphingolipid mediated signaling pathway Source: MGI
  • regulation of Wnt signaling pathway Source: MGI
  • single organismal cell-cell adhesion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_335233. Sphingolipid de novo biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ppap2b
Synonyms:Lpp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1915166. Ppap2b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3333CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei34 – 5421HelicalSequence AnalysisAdd
BLAST
Topological domaini55 – 8531LumenalSequence AnalysisAdd
BLAST
Transmembranei86 – 10621HelicalSequence AnalysisAdd
BLAST
Topological domaini107 – 12317CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei124 – 14421HelicalSequence AnalysisAdd
BLAST
Topological domaini145 – 19450LumenalSequence AnalysisAdd
BLAST
Transmembranei195 – 21521HelicalSequence AnalysisAdd
BLAST
Topological domaini216 – 22611CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei227 – 24721HelicalSequence AnalysisAdd
BLAST
Topological domaini248 – 25811LumenalSequence AnalysisAdd
BLAST
Transmembranei259 – 27921HelicalSequence AnalysisAdd
BLAST
Topological domaini280 – 31233CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 312312Lipid phosphate phosphohydrolase 3PRO_0000220913Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191PhosphoserineBy similarity
Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence Analysis
Modified residuei298 – 2981PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ99JY8.
PaxDbiQ99JY8.
PRIDEiQ99JY8.

PTM databases

PhosphoSiteiQ99JY8.

Expressioni

Gene expression databases

BgeeiQ99JY8.
CleanExiMM_PPAP2B.
GenevisibleiQ99JY8. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ99JY8. 5 interactions.
MINTiMINT-4612030.
STRINGi10090.ENSMUSP00000065719.

Structurei

3D structure databases

ProteinModelPortaliQ99JY8.
SMRiQ99JY8. Positions 142-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0671.
GeneTreeiENSGT00620000087654.
HOGENOMiHOG000041307.
HOVERGENiHBG002048.
InParanoidiQ99JY8.
KOiK01080.
OMAiNNNCKDH.
OrthoDBiEOG7C5M9Q.
PhylomeDBiQ99JY8.
TreeFamiTF316040.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR028675. LPP3.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PANTHERiPTHR10165:SF79. PTHR10165:SF79. 1 hit.
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.

Sequencei

Sequence statusi: Complete.

Q99JY8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSYKYDKAI VPESKNGGSP ALNNNPRKGG SKRVLLICLD LFCLFMAALP
60 70 80 90 100
FLIIETSTIK PYRRGFYCND ESIKYPLKVS ETINDAVLCA VGIVIAILAI
110 120 130 140 150
ITGEFYRIYY LKEKSRSTTQ NPYVAALYKQ VGCFLFGCAI SQSFTDIAKV
160 170 180 190 200
SIGRLRPHFL SVCDPDFSQI NCSEGYIQNY RCRGEDSKVQ EARKSFFSGH
210 220 230 240 250
ASFSMFTMLY LVLYLQARFT WRGARLLRPL LQFTLLMMAF YTGLSRVSDY
260 270 280 290 300
KHHPSDVLAG FAQGALVACC IVFFVSDLFK TKTSLSLPAP AIRREILSPV
310
DIIDRNNHHN MV
Length:312
Mass (Da):35,216
Last modified:June 1, 2001 - v1
Checksum:iD782986E04B57D7D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1871S → C in BAE34848 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK159136 mRNA. Translation: BAE34848.1.
AK160056 mRNA. Translation: BAE35594.1.
BC005558 mRNA. Translation: AAH05558.1.
CCDSiCCDS18417.1.
RefSeqiNP_542122.1. NM_080555.2.
UniGeneiMm.348326.

Genome annotation databases

EnsembliENSMUST00000064139; ENSMUSP00000065719; ENSMUSG00000028517.
GeneIDi67916.
KEGGimmu:67916.
UCSCiuc008tye.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK159136 mRNA. Translation: BAE34848.1.
AK160056 mRNA. Translation: BAE35594.1.
BC005558 mRNA. Translation: AAH05558.1.
CCDSiCCDS18417.1.
RefSeqiNP_542122.1. NM_080555.2.
UniGeneiMm.348326.

3D structure databases

ProteinModelPortaliQ99JY8.
SMRiQ99JY8. Positions 142-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99JY8. 5 interactions.
MINTiMINT-4612030.
STRINGi10090.ENSMUSP00000065719.

PTM databases

PhosphoSiteiQ99JY8.

Proteomic databases

MaxQBiQ99JY8.
PaxDbiQ99JY8.
PRIDEiQ99JY8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064139; ENSMUSP00000065719; ENSMUSG00000028517.
GeneIDi67916.
KEGGimmu:67916.
UCSCiuc008tye.1. mouse.

Organism-specific databases

CTDi8613.
MGIiMGI:1915166. Ppap2b.

Phylogenomic databases

eggNOGiCOG0671.
GeneTreeiENSGT00620000087654.
HOGENOMiHOG000041307.
HOVERGENiHBG002048.
InParanoidiQ99JY8.
KOiK01080.
OMAiNNNCKDH.
OrthoDBiEOG7C5M9Q.
PhylomeDBiQ99JY8.
TreeFamiTF316040.

Enzyme and pathway databases

ReactomeiREACT_335233. Sphingolipid de novo biosynthesis.

Miscellaneous databases

ChiTaRSiPpap2b. mouse.
NextBioi325938.
PROiQ99JY8.
SOURCEiSearch...

Gene expression databases

BgeeiQ99JY8.
CleanExiMM_PPAP2B.
GenevisibleiQ99JY8. MM.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR028675. LPP3.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PANTHERiPTHR10165:SF79. PTHR10165:SF79. 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. "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].
    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. Cited for: FUNCTION, DISEASE.

Entry informationi

Entry nameiLPP3_MOUSE
AccessioniPrimary (citable) accession number: Q99JY8
Secondary accession number(s): Q3TVM4, Q3TXR7, Q8BTB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: June 1, 2001
Last modified: July 22, 2015
This is version 112 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, Direct protein sequencing, 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

External Data

Dasty 3

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 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.