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Q99JY8

- LPP3_MOUSE

UniProt

Q99JY8 - LPP3_MOUSE

Protein

Lipid phosphate phosphohydrolase 3

Gene

Ppap2b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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

    1. integrin binding Source: MGI
    2. lipid phosphatase activity Source: MGI
    3. phosphatidate phosphatase activity Source: UniProtKB-EC
    4. sphingosine-1-phosphate phosphatase activity Source: MGI

    GO - Biological processi

    1. Bergmann glial cell differentiation Source: MGI
    2. blood vessel development Source: MGI
    3. canonical Wnt signaling pathway Source: BHF-UCL
    4. canonical Wnt signaling pathway involved in positive regulation of cell-cell adhesion Source: Ensembl
    5. canonical Wnt signaling pathway involved in positive regulation of endothelial cell migration Source: Ensembl
    6. canonical Wnt signaling pathway involved in positive regulation of wound healing Source: Ensembl
    7. cell adhesion Source: MGI
    8. dephosphorylation Source: GOC
    9. gastrulation with mouth forming second Source: MGI
    10. homotypic cell-cell adhesion Source: Ensembl
    11. negative regulation of protein phosphorylation Source: BHF-UCL
    12. phospholipid metabolic process Source: MGI
    13. positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
    14. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    15. protein stabilization Source: BHF-UCL
    16. regulation of sphingolipid mediated signaling pathway Source: MGI
    17. regulation of Wnt signaling pathway Source: MGI
    18. single organismal cell-cell adhesion Source: MGI

    Keywords - Molecular functioni

    Developmental protein, Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_198151. 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: Chromosome 4

    Organism-specific databases

    MGIiMGI:1915166. Ppap2b.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: MGI

    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.1 Publication

    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

    PaxDbiQ99JY8.
    PRIDEiQ99JY8.

    PTM databases

    PhosphoSiteiQ99JY8.

    Expressioni

    Gene expression databases

    BgeeiQ99JY8.
    CleanExiMM_PPAP2B.
    GenevestigatoriQ99JY8.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ99JY8.
    SMRiQ99JY8. Positions 142-271.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3333CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini55 – 8531LumenalSequence AnalysisAdd
    BLAST
    Topological domaini107 – 12317CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini145 – 19450LumenalSequence AnalysisAdd
    BLAST
    Topological domaini216 – 22611CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini248 – 25811LumenalSequence AnalysisAdd
    BLAST
    Topological domaini280 – 31233CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei34 – 5421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei86 – 10621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei124 – 14421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei195 – 21521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei227 – 24721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei259 – 27921HelicalSequence AnalysisAdd
    BLAST

    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

    MQSYKYDKAI VPESKNGGSP ALNNNPRKGG SKRVLLICLD LFCLFMAALP    50
    FLIIETSTIK PYRRGFYCND ESIKYPLKVS ETINDAVLCA VGIVIAILAI 100
    ITGEFYRIYY LKEKSRSTTQ NPYVAALYKQ VGCFLFGCAI SQSFTDIAKV 150
    SIGRLRPHFL SVCDPDFSQI NCSEGYIQNY RCRGEDSKVQ EARKSFFSGH 200
    ASFSMFTMLY LVLYLQARFT WRGARLLRPL LQFTLLMMAF YTGLSRVSDY 250
    KHHPSDVLAG FAQGALVACC IVFFVSDLFK TKTSLSLPAP AIRREILSPV 300
    DIIDRNNHHN MV 312
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK159136 mRNA. Translation: BAE34848.1 .
    AK160056 mRNA. Translation: BAE35594.1 .
    BC005558 mRNA. Translation: AAH05558.1 .
    CCDSi CCDS18417.1.
    RefSeqi NP_542122.1. NM_080555.2.
    UniGenei Mm.348326.

    3D structure databases

    ProteinModelPortali Q99JY8.
    SMRi Q99JY8. Positions 142-271.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q99JY8. 5 interactions.
    MINTi MINT-4612030.
    STRINGi 10090.ENSMUSP00000065719.

    PTM databases

    PhosphoSitei Q99JY8.

    Proteomic databases

    PaxDbi Q99JY8.
    PRIDEi Q99JY8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000064139 ; ENSMUSP00000065719 ; ENSMUSG00000028517 .
    GeneIDi 67916.
    KEGGi mmu:67916.
    UCSCi uc008tye.1. mouse.

    Organism-specific databases

    CTDi 8613.
    MGIi MGI:1915166. Ppap2b.

    Phylogenomic databases

    eggNOGi COG0671.
    GeneTreei ENSGT00620000087654.
    HOGENOMi HOG000041307.
    HOVERGENi HBG002048.
    InParanoidi Q99JY8.
    KOi K01080.
    OMAi NNNCKDH.
    OrthoDBi EOG7C5M9Q.
    PhylomeDBi Q99JY8.
    TreeFami TF316040.

    Enzyme and pathway databases

    Reactomei REACT_198151. Sphingolipid de novo biosynthesis.

    Miscellaneous databases

    ChiTaRSi PPAP2B. mouse.
    NextBioi 325938.
    PROi Q99JY8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99JY8.
    CleanExi MM_PPAP2B.
    Genevestigatori Q99JY8.

    Family and domain databases

    Gene3Di 1.20.144.10. 1 hit.
    InterProi IPR028675. LPP3.
    IPR000326. P_Acid_Pase_2/haloperoxidase.
    [Graphical view ]
    PANTHERi PTHR10165:SF79. PTHR10165:SF79. 1 hit.
    Pfami PF01569. PAP2. 1 hit.
    [Graphical view ]
    SMARTi SM00014. acidPPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48317. SSF48317. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 103 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