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O14495

- LPP3_HUMAN

UniProt

O14495 - LPP3_HUMAN

Protein

Lipid phosphate phosphohydrolase 3

Gene

PPAP2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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). The relative catalytic efficiency is LPA = PA > C-1-P > S-1-P. May be involved in cell adhesion and in cell-cell interactions.

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by sphingosine, zinc ions and propanolol. Not inhibited by N-ethylmaleimide treatment.

    GO - Molecular functioni

    1. lipid phosphatase activity Source: Ensembl
    2. phosphatidate phosphatase activity Source: UniProtKB-EC
    3. phosphoprotein phosphatase activity Source: ProtInc
    4. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.
    SignaLinkiO14495.

    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
    Vascular endothelial growth factor and type I collagen-inducible protein
    Short name:
    VCIP
    Gene namesi
    Name:PPAP2B
    Synonyms:LPP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9229. PPAP2B.

    Subcellular locationi

    GO - Cellular componenti

    1. adherens junction Source: BHF-UCL
    2. extracellular vesicular exosome Source: UniProt
    3. Golgi apparatus Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW
    5. membrane Source: ProtInc
    6. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33553.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 311311Lipid phosphate phosphohydrolase 3PRO_0000220912Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Phosphoserine2 Publications
    Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence Analysis
    Modified residuei297 – 2971Phosphoserine1 Publication

    Post-translational modificationi

    N-glycosylated. Contains high-mannose oligosaccharides.

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiO14495.
    PaxDbiO14495.
    PRIDEiO14495.

    PTM databases

    PhosphoSiteiO14495.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Highly expressed in heart and placenta.

    Inductioni

    By EGF, VEGF, FGF2 and phorbol myristate acetate (PMA).1 Publication

    Gene expression databases

    BgeeiO14495.
    CleanExiHS_PPAP2B.
    GenevestigatoriO14495.

    Organism-specific databases

    HPAiHPA028892.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTNND1O607169EBI-766232,EBI-701927

    Protein-protein interaction databases

    BioGridi114171. 3 interactions.
    IntActiO14495. 4 interactions.
    MINTiMINT-4648964.
    STRINGi9606.ENSP00000294390.

    Structurei

    3D structure databases

    ProteinModelPortaliO14495.
    SMRiO14495. Positions 140-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3333CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini55 – 8531LumenalSequence AnalysisAdd
    BLAST
    Topological domaini107 – 12216CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini144 – 19350LumenalSequence AnalysisAdd
    BLAST
    Topological domaini215 – 22713CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini249 – 2579LumenalSequence Analysis
    Topological domaini279 – 31133CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei34 – 5421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei86 – 10621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei123 – 14321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei194 – 21421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei228 – 24821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei258 – 27821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0671.
    HOGENOMiHOG000041307.
    HOVERGENiHBG002048.
    InParanoidiO14495.
    KOiK01080.
    OMAiNNNCKDH.
    OrthoDBiEOG7C5M9Q.
    PhylomeDBiO14495.
    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.

    O14495-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQNYKYDKAI VPESKNGGSP ALNNNPRRSG SKRVLLICLD LFCLFMAGLP    50
    FLIIETSTIK PYHRGFYCND ESIKYPLKTG ETINDAVLCA VGIVIAILAI 100
    ITGEFYRIYY LKKSRSTIQN PYVAALYKQV GCFLFGCAIS QSFTDIAKVS 150
    IGRLRPHFLS VCNPDFSQIN CSEGYIQNYR CRGDDSKVQE ARKSFFSGHA 200
    SFSMYTMLYL VLYLQARFTW RGARLLRPLL QFTLIMMAFY TGLSRVSDHK 250
    HHPSDVLAGF AQGALVACCI VFFVSDLFKT KTTLSLPAPA IRKEILSPVD 300
    IIDRNNHHNM M 311
    Length:311
    Mass (Da):35,116
    Last modified:January 1, 1998 - v1
    Checksum:iCB3F60189044DA31
    GO

    Sequence cautioni

    The sequence AAB50222.1 differs from that shown. Reason: Frameshift at position 225.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321K → M in AAV38396. 1 PublicationCurated
    Sequence conflicti282 – 2821T → M in AAH09196. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000889 mRNA. Translation: BAA22594.1.
    AF017786 mRNA. Translation: AAC63433.1.
    AF480883 mRNA. Translation: AAO84481.1.
    AF043329 mRNA. Translation: AAD02271.1.
    U79294 mRNA. Translation: AAB50222.1. Frameshift.
    AK312439 mRNA. Translation: BAG35348.1.
    BT019589 mRNA. Translation: AAV38396.1.
    CH471059 Genomic DNA. Translation: EAX06651.1.
    CH471059 Genomic DNA. Translation: EAX06652.1.
    CH471059 Genomic DNA. Translation: EAX06653.1.
    BC009196 mRNA. Translation: AAH09196.1.
    CCDSiCCDS604.1.
    RefSeqiNP_003704.3. NM_003713.4.
    UniGeneiHs.405156.
    Hs.619002.

    Genome annotation databases

    EnsembliENST00000371250; ENSP00000360296; ENSG00000162407.
    GeneIDi8613.
    KEGGihsa:8613.
    UCSCiuc001cyj.2. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000889 mRNA. Translation: BAA22594.1 .
    AF017786 mRNA. Translation: AAC63433.1 .
    AF480883 mRNA. Translation: AAO84481.1 .
    AF043329 mRNA. Translation: AAD02271.1 .
    U79294 mRNA. Translation: AAB50222.1 . Frameshift.
    AK312439 mRNA. Translation: BAG35348.1 .
    BT019589 mRNA. Translation: AAV38396.1 .
    CH471059 Genomic DNA. Translation: EAX06651.1 .
    CH471059 Genomic DNA. Translation: EAX06652.1 .
    CH471059 Genomic DNA. Translation: EAX06653.1 .
    BC009196 mRNA. Translation: AAH09196.1 .
    CCDSi CCDS604.1.
    RefSeqi NP_003704.3. NM_003713.4.
    UniGenei Hs.405156.
    Hs.619002.

    3D structure databases

    ProteinModelPortali O14495.
    SMRi O14495. Positions 140-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114171. 3 interactions.
    IntActi O14495. 4 interactions.
    MINTi MINT-4648964.
    STRINGi 9606.ENSP00000294390.

    PTM databases

    PhosphoSitei O14495.

    Proteomic databases

    MaxQBi O14495.
    PaxDbi O14495.
    PRIDEi O14495.

    Protocols and materials databases

    DNASUi 8613.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371250 ; ENSP00000360296 ; ENSG00000162407 .
    GeneIDi 8613.
    KEGGi hsa:8613.
    UCSCi uc001cyj.2. human.

    Organism-specific databases

    CTDi 8613.
    GeneCardsi GC01M056879.
    HGNCi HGNC:9229. PPAP2B.
    HPAi HPA028892.
    MIMi 607125. gene.
    neXtProti NX_O14495.
    PharmGKBi PA33553.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0671.
    HOGENOMi HOG000041307.
    HOVERGENi HBG002048.
    InParanoidi O14495.
    KOi K01080.
    OMAi NNNCKDH.
    OrthoDBi EOG7C5M9Q.
    PhylomeDBi O14495.
    TreeFami TF316040.

    Enzyme and pathway databases

    Reactomei REACT_115810. Sphingolipid de novo biosynthesis.
    SignaLinki O14495.

    Miscellaneous databases

    ChiTaRSi PPAP2B. human.
    GeneWikii PPAP2B.
    GenomeRNAii 8613.
    NextBioi 32277.
    PROi O14495.
    SOURCEi Search...

    Gene expression databases

    Bgeei O14495.
    CleanExi HS_PPAP2B.
    Genevestigatori O14495.

    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. "Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase."
      Kai M., Wada I., Imai S., Sakane F., Kanoh H.
      J. Biol. Chem. 272:24572-24578(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INDUCTION.
    2. "Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform."
      Roberts R., Sciorra V.A., Morris A.J.
      J. Biol. Chem. 273:22059-22067(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    3. "Regulation of cell-cell interactions by phosphatidic acid phosphatase 2b/VCIP."
      Humtsoe J.O., Feng S., Thakker G.D., Yang J., Hong J., Wary K.K.
      EMBO J. 22:1539-1554(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Molecular cloning of and expression of an isoform of human phosphatidic acid phosphatase cDNA."
      Leung D.W., Tompkins C.K.
      Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Large-scale concatenation cDNA sequencing."
      Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
      Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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].
      Tissue: Placenta.
    10. "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.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLPP3_HUMAN
    AccessioniPrimary (citable) accession number: O14495
    Secondary accession number(s): B2R651
    , D3DQ52, Q5U0F7, Q96GW0, Q99782
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2004
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3