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P06802

- ENPP1_MOUSE

UniProt

P06802 - ENPP1_MOUSE

Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

Gene

Enpp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 4 (19 Sep 2002)
      Previous versions | rss
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    Functioni

    Appears to modulate insulin sensitivity By similarity. By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling.By similarity2 Publications

    Catalytic activityi

    Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
    A dinucleotide + H2O = 2 mononucleotides.

    Cofactori

    Binds 2 zinc ions per subunit.2 Publications

    Enzyme regulationi

    At low concentrations of ATP, a phosphorylated intermediate is formed which inhibits further hydrolysis.

    Kineticsi

    1. KM=46 µM for ATP1 Publication
    2. KM=4.3 mM for UTP1 Publication
    3. KM=4.2 mM for GTP1 Publication
    4. KM=1.2 mM for CTP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei84 – 852Cleavage
    Metal bindingi200 – 2001Zinc 1; catalytic1 Publication
    Active sitei238 – 2381AMP-threonine intermediate1 Publication
    Metal bindingi238 – 2381Zinc 1; catalytic1 Publication
    Binding sitei259 – 2591Substrate
    Binding sitei277 – 2771Substrate
    Binding sitei322 – 3221Substrate
    Metal bindingi358 – 3581Zinc 2; catalytic1 Publication
    Metal bindingi362 – 3621Zinc 2; via tele nitrogen; catalytic1 Publication
    Metal bindingi405 – 4051Zinc 1; catalytic1 Publication
    Metal bindingi406 – 4061Zinc 1; via tele nitrogen; catalytic1 Publication
    Metal bindingi517 – 5171Zinc 2; via tele nitrogen; catalytic1 Publication
    Metal bindingi781 – 7811Calcium1 Publication
    Metal bindingi783 – 7831Calcium1 Publication
    Metal bindingi785 – 7851Calcium1 Publication
    Metal bindingi787 – 7871Calcium; via carbonyl oxygen1 Publication
    Metal bindingi789 – 7891Calcium1 Publication
    Sitei896 – 8961Essential for catalytic activityBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. NADH pyrophosphatase activity Source: UniProtKB-EC
    3. nucleic acid binding Source: InterPro
    4. nucleotide diphosphatase activity Source: UniProtKB
    5. phosphodiesterase I activity Source: UniProtKB
    6. polysaccharide binding Source: InterPro
    7. scavenger receptor activity Source: InterPro
    8. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: UniProtKB
    2. biomineral tissue development Source: UniProtKB-KW
    3. bone remodeling Source: MGI
    4. immune response Source: InterPro
    5. negative regulation of fat cell differentiation Source: BHF-UCL
    6. negative regulation of ossification Source: MGI
    7. nucleic acid phosphodiester bond hydrolysis Source: GOC

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Biomineralization

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_216155. Vitamin B2 (riboflavin) metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
    Short name:
    E-NPP 1
    Alternative name(s):
    Lymphocyte antigen 41
    Short name:
    Ly-41
    Phosphodiesterase I/nucleotide pyrophosphatase 1
    Plasma-cell membrane glycoprotein PC-1
    Including the following 2 domains:
    Alkaline phosphodiesterase I (EC:3.1.4.1)
    Nucleotide pyrophosphatase (EC:3.6.1.9)
    Short name:
    NPPase
    Gene namesi
    Name:Enpp1
    Synonyms:Npps, Pc1, Pdnp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:97370. Enpp1.

    Subcellular locationi

    Cell membrane; Single-pass type II membrane protein. Basolateral cell membrane; Single-pass type II membrane protein. Secreted
    Note: Targeted to the basolateral membrane in polarized epithelial cells and in hepatocytes, and to matrix vesicles in osteoblasts. In bile duct cells and cancer cells, located to the apical cytoplasmic side By similarity. The proteolytically processed form is secreted.By similarity

    GO - Cellular componenti

    1. basolateral plasma membrane Source: UniProtKB-SubCell
    2. cell surface Source: BHF-UCL
    3. extracellular space Source: BHF-UCL
    4. integral component of membrane Source: UniProtKB
    5. integral component of plasma membrane Source: UniProtKB
    6. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Defects in Enpp1 are the cause of the tiptoe walking (ttw) phenotype. Ttw mice exhibit ossification of the spinal ligaments.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi28 – 281A → G: No effect on basolateral sorting in epithelial cells. 1 Publication
    Mutagenesisi30 – 301S → A or D: Little change in baolateral sorting in epithelial cells. 1 Publication
    Mutagenesisi31 – 311L → A: 60% of ENPP1 redirected to apical surface in epithelial cells. 75% of ENPP1 redirected to apical surface in epithelial cells; abrogation of increased NPP activity in oestoblastic matrix vesicles; when associated with A-32. 2 Publications
    Mutagenesisi32 – 321L → A: 70% of ENPP1 redirected to apical surface in epithelial cells; abrogation of increased NPP activity in oestoblastic matrix vesicles. 75% of ENPP1 redirected to apical surface in epithelial cells; abrogation of increased NPP activity in oestoblastic matrix vesicles; when associated with A-31. 2 Publications
    Mutagenesisi42 – 421L → A: No change in increased NPP activity in oestoblastic matrix vesicles. 1 Publication
    Mutagenesisi57 – 571Y → G: No change in increased NPP activity in oestoblastic matrix vesicles. 1 Publication
    Mutagenesisi200 – 2001D → N: Decreases phosphodiesterase activity by 95%. Abolishes formation of nucleotidylated intermediate. 1 Publication
    Mutagenesisi237 – 2371K → A: Decreases phosphodiesterase activity by 40%. Decreased formation of nucleotidylated intermediate. 1 Publication
    Mutagenesisi238 – 2381T → A: Abolishes all phosphodiesterase activity. Abolishes formation of nucleotidylated intermediate. 1 Publication
    Mutagenesisi238 – 2381T → S: Decreases phosphodiesterase activity by 95%. Accumulates nucleotidylated intermediate. 1 Publication
    Mutagenesisi239 – 2391F → A: Decreases phosphodiesterase activity by 50%. Decreased formation of nucleotidylated intermediate. 2 Publications
    Mutagenesisi242 – 2421H → L: Strongly decreased phosphodiesterase activity. 1 Publication
    Mutagenesisi304 – 32320Missing: Nearly abolishes activity with nucleotide phosphates. Confers very low activity with lysophospholipids. Add
    BLAST
    Mutagenesisi308 – 3081D → A: Decreased phosphodiesterase activity. 1 Publication
    Mutagenesisi322 – 3221Y → A: Strongly decreased phosphodiesterase activity. 1 Publication
    Mutagenesisi358 – 3581D → Q: Decreases phosphodiesterase activity by 90%. Accumulates nucleotidylated intermediate. 1 Publication
    Mutagenesisi362 – 3621H → Q: Decreases phosphodiesterase activity by 95%. 65% activity can be restored by addition of Zn(2+) ions. Accumulates nucleotidylated intermediate. 1 Publication
    Mutagenesisi405 – 4051D → N: Abolishes all phosphodiesterase activity. 10% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. 1 Publication
    Mutagenesisi406 – 4061H → Q: Abolishes all phosphodiesterase activity. 15% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. 1 Publication
    Mutagenesisi517 – 5171H → Q: Abolishes all phosphodiesterase activity. 60% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. 1 Publication

    Keywords - Diseasei

    Disease mutation

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 906906Ectonucleotide pyrophosphatase/phosphodiesterase family member 1PRO_0000188565Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi90 ↔ 104PROSITE-ProRule annotation
    Disulfide bondi94 ↔ 122PROSITE-ProRule annotation
    Disulfide bondi102 ↔ 115PROSITE-ProRule annotation
    Disulfide bondi108 ↔ 114PROSITE-ProRule annotation
    Disulfide bondi131 ↔ 148PROSITE-ProRule annotation
    Disulfide bondi136 ↔ 166PROSITE-ProRule annotation
    Disulfide bondi146 ↔ 159PROSITE-ProRule annotation
    Disulfide bondi152 ↔ 158PROSITE-ProRule annotation
    Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi177 ↔ 223
    Disulfide bondi185 ↔ 397
    Glycosylationi267 – 2671N-linked (GlcNAc...)2 Publications
    Glycosylationi323 – 3231N-linked (GlcNAc...)3 Publications
    Disulfide bondi413 ↔ 512
    Glycosylationi459 – 4591N-linked (GlcNAc...)1 Publication
    Disulfide bondi462 ↔ 849
    Glycosylationi567 – 5671N-linked (GlcNAc...)2 Publications
    Disulfide bondi596 ↔ 653
    Disulfide bondi607 ↔ 707
    Disulfide bondi609 ↔ 692
    Glycosylationi624 – 6241N-linked (GlcNAc...)2 Publications
    Disulfide bondi819 ↔ 829

    Post-translational modificationi

    The N-terminal is blocked.
    N-glycosylated.5 Publications
    A secreted form is produced through cleavage at Lys-85 by intracellular processing.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP06802.
    PaxDbiP06802.
    PRIDEiP06802.

    PTM databases

    PhosphoSiteiP06802.

    Expressioni

    Tissue specificityi

    Selectively expressed on the surface of antibody-secreting cells.

    Gene expression databases

    ArrayExpressiP06802.
    BgeeiP06802.
    GenevestigatoriP06802.

    Interactioni

    Subunit structurei

    Homodimer. The secreted form is monomeric. Interacts with INSR By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-59981N.

    Structurei

    Secondary structure

    1
    906
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni94 – 963
    Beta strandi100 – 1034
    Helixi108 – 1114
    Helixi118 – 1225
    Helixi124 – 1263
    Turni133 – 1375
    Beta strandi145 – 1473
    Helixi152 – 1554
    Helixi162 – 1676
    Turni172 – 1743
    Beta strandi194 – 1996
    Helixi204 – 2096
    Helixi211 – 2133
    Helixi215 – 2228
    Beta strandi224 – 2285
    Helixi238 – 24710
    Helixi251 – 2544
    Beta strandi259 – 2635
    Turni264 – 2674
    Beta strandi268 – 2703
    Beta strandi272 – 2743
    Helixi275 – 2784
    Turni280 – 2823
    Helixi288 – 2914
    Beta strandi299 – 3035
    Turni305 – 3084
    Beta strandi311 – 3133
    Beta strandi317 – 3193
    Helixi328 – 33912
    Turni343 – 3453
    Beta strandi348 – 3547
    Helixi358 – 3647
    Beta strandi366 – 3683
    Helixi369 – 39123
    Beta strandi399 – 4035
    Beta strandi413 – 4186
    Helixi420 – 4234
    Beta strandi428 – 4325
    Beta strandi434 – 4363
    Beta strandi438 – 4436
    Turni444 – 4463
    Turni448 – 4503
    Helixi453 – 4608
    Beta strandi468 – 4736
    Helixi474 – 4763
    Helixi479 – 4813
    Beta strandi487 – 4893
    Beta strandi491 – 4966
    Beta strandi501 – 5055
    Turni506 – 5083
    Beta strandi512 – 5165
    Helixi524 – 5263
    Beta strandi530 – 5345
    Beta strandi539 – 5435
    Helixi548 – 5503
    Helixi551 – 5599
    Turni570 – 5734
    Helixi574 – 5763
    Beta strandi577 – 5793
    Beta strandi591 – 5944
    Beta strandi611 – 6133
    Helixi617 – 6248
    Helixi631 – 6377
    Beta strandi651 – 6566
    Beta strandi658 – 6658
    Turni666 – 6694
    Beta strandi670 – 6789
    Helixi703 – 7053
    Helixi707 – 7093
    Beta strandi712 – 72211
    Turni728 – 7314
    Helixi736 – 7383
    Helixi740 – 7423
    Beta strandi743 – 7475
    Helixi748 – 75912
    Helixi761 – 7688
    Beta strandi772 – 7798
    Beta strandi785 – 7873
    Helixi791 – 7966
    Beta strandi799 – 8013
    Beta strandi804 – 8063
    Beta strandi810 – 82112
    Helixi826 – 8283
    Beta strandi830 – 84011
    Turni846 – 8494
    Helixi855 – 86511
    Helixi870 – 8778
    Helixi889 – 8968

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4B56X-ray3.00A/B87-906[»]
    4GTWX-ray2.70A/B92-906[»]
    4GTXX-ray3.20A/B92-906[»]
    4GTYX-ray3.19A/B92-906[»]
    4GTZX-ray3.19A/B92-906[»]
    ProteinModelPortaliP06802.
    SMRiP06802. Positions 88-903.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5858CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini80 – 906827ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei59 – 7921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini86 – 12641SMB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini127 – 17145SMB 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni173 – 573401PhosphodiesteraseAdd
    BLAST
    Regioni579 – 62850LinkerAdd
    BLAST
    Regioni635 – 906272NucleaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi27 – 348Di-leucine motif

    Domaini

    The di-leucine motif is required for basolateral targeting in polarized epithelial cells, and for targeting to matrix vesicles derived from mineralizing cells.

    Sequence similaritiesi

    Contains 2 SMB (somatomedin-B) domains.Curated

    Keywords - Domaini

    Repeat, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1524.
    GeneTreeiENSGT00660000095322.
    HOGENOMiHOG000034646.
    HOVERGENiHBG051484.
    InParanoidiP06802.
    KOiK01513.
    PhylomeDBiP06802.

    Family and domain databases

    Gene3Di3.40.570.10. 1 hit.
    3.40.720.10. 1 hit.
    InterProiIPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR001604. DNA/RNA_non-sp_Endonuclease.
    IPR024873. E-NPP.
    IPR020821. Extracellular_endonuc_su_A.
    IPR002591. Phosphodiest/P_Trfase.
    IPR020436. Somatomedin_B_chordata.
    IPR001212. Somatomedin_B_dom.
    [Graphical view]
    PANTHERiPTHR10151. PTHR10151. 1 hit.
    PfamiPF01223. Endonuclease_NS. 1 hit.
    PF01663. Phosphodiest. 1 hit.
    PF01033. Somatomedin_B. 2 hits.
    [Graphical view]
    PRINTSiPR00022. SOMATOMEDINB.
    SMARTiSM00892. Endonuclease_NS. 1 hit.
    SM00477. NUC. 1 hit.
    SM00201. SO. 2 hits.
    [Graphical view]
    SUPFAMiSSF53649. SSF53649. 1 hit.
    PROSITEiPS00524. SMB_1. 2 hits.
    PS50958. SMB_2. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: P06802-1) [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

    MERDGDQAGH GPRHGSAGNG RELESPAAAS LLAPMDLGEE PLEKAERARP    50
    AKDPNTYKVL SLVLSVCVLT TILGCIFGLK PSCAKEVKSC KGRCFERTFS 100
    NCRCDAACVS LGNCCLDFQE TCVEPTHIWT CNKFRCGEKR LSRFVCSCAD 150
    DCKTHNDCCI NYSSVCQDKK SWVEETCESI DTPECPAEFE SPPTLLFSLD 200
    GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPMYPTKTFP NHYSIVTGLY 250
    PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVKSG 300
    TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSHERPHFY 350
    TLYLEEPDSS GHSHGPVSSE VIKALQKVDR LVGMLMDGLK DLGLDKCLNL 400
    ILISDHGMEQ GSCKKYVYLN KYLGDVNNVK VVYGPAARLR PTDVPETYYS 450
    FNYEALAKNL SCREPNQHFR PYLKPFLPKR LHFAKSDRIE PLTFYLDPQW 500
    QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG AEVDSFENIE 550
    VYNLMCDLLG LIPAPNNGSH GSLNHLLKKP IYNPSHPKEE GFLSQCPIKS 600
    TSNDLGCTCD PWIVPIKDFE KQLNLTTEDV DDIYHMTVPY GRPRILLKQH 650
    HVCLLQQQQF LTGYSLDLLM PLWASYTFLR NDQFSRDDFS NCLYQDLRIP 700
    LSPVHKCSYY KSNSKLSYGF LTPPRLNRVS NHIYSEALLT SNIVPMYQSF 750
    QVIWHYLHDT LLQRYAHERN GINVVSGPVF DFDYDGRYDS LEILKQNSRV 800
    IRSQEILIPT HFFIVLTSCK QLSETPLECS ALESSAYILP HRPDNIESCT 850
    HGKRESSWVE ELLTLHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP 900
    IFSQED 906
    Length:906
    Mass (Da):103,176
    Last modified:September 19, 2002 - v4
    Checksum:i068D45B0ED0F224D
    GO
    Isoform 1 (identifier: P06802-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         630-630: Missing.

    Show »
    Length:905
    Mass (Da):103,076
    Checksum:iFB6EEEA0FF659421
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti651 – 6511H → R in allele ENPP1b. 1 Publication
    Natural varianti680 – 6801R → S in allele ENPP1b. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei630 – 6301Missing in isoform 1. 2 PublicationsVSP_006748

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02700 mRNA. Translation: AAA39893.2.
    AF339910 mRNA. Translation: AAK84174.1.
    AK088857 mRNA. Translation: BAC40616.1.
    L04516 Unassigned DNA. No translation available.
    M12552 mRNA. Translation: AAA39892.1.
    CCDSiCCDS35870.1. [P06802-2]
    PIRiA27410.
    RefSeqiXP_006512660.1. XM_006512597.1.
    UniGeneiMm.27254.
    Mm.478860.

    Genome annotation databases

    EnsembliENSMUST00000135846; ENSMUSP00000114273; ENSMUSG00000037370.
    GeneIDi18605.
    KEGGimmu:18605.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02700 mRNA. Translation: AAA39893.2 .
    AF339910 mRNA. Translation: AAK84174.1 .
    AK088857 mRNA. Translation: BAC40616.1 .
    L04516 Unassigned DNA. No translation available.
    M12552 mRNA. Translation: AAA39892.1 .
    CCDSi CCDS35870.1. [P06802-2 ]
    PIRi A27410.
    RefSeqi XP_006512660.1. XM_006512597.1.
    UniGenei Mm.27254.
    Mm.478860.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4B56 X-ray 3.00 A/B 87-906 [» ]
    4GTW X-ray 2.70 A/B 92-906 [» ]
    4GTX X-ray 3.20 A/B 92-906 [» ]
    4GTY X-ray 3.19 A/B 92-906 [» ]
    4GTZ X-ray 3.19 A/B 92-906 [» ]
    ProteinModelPortali P06802.
    SMRi P06802. Positions 88-903.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59981N.

    PTM databases

    PhosphoSitei P06802.

    Proteomic databases

    MaxQBi P06802.
    PaxDbi P06802.
    PRIDEi P06802.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000135846 ; ENSMUSP00000114273 ; ENSMUSG00000037370 .
    GeneIDi 18605.
    KEGGi mmu:18605.

    Organism-specific databases

    CTDi 5167.
    MGIi MGI:97370. Enpp1.

    Phylogenomic databases

    eggNOGi COG1524.
    GeneTreei ENSGT00660000095322.
    HOGENOMi HOG000034646.
    HOVERGENi HBG051484.
    InParanoidi P06802.
    KOi K01513.
    PhylomeDBi P06802.

    Enzyme and pathway databases

    Reactomei REACT_216155. Vitamin B2 (riboflavin) metabolism.

    Miscellaneous databases

    PROi P06802.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06802.
    Bgeei P06802.
    Genevestigatori P06802.

    Family and domain databases

    Gene3Di 3.40.570.10. 1 hit.
    3.40.720.10. 1 hit.
    InterProi IPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR001604. DNA/RNA_non-sp_Endonuclease.
    IPR024873. E-NPP.
    IPR020821. Extracellular_endonuc_su_A.
    IPR002591. Phosphodiest/P_Trfase.
    IPR020436. Somatomedin_B_chordata.
    IPR001212. Somatomedin_B_dom.
    [Graphical view ]
    PANTHERi PTHR10151. PTHR10151. 1 hit.
    Pfami PF01223. Endonuclease_NS. 1 hit.
    PF01663. Phosphodiest. 1 hit.
    PF01033. Somatomedin_B. 2 hits.
    [Graphical view ]
    PRINTSi PR00022. SOMATOMEDINB.
    SMARTi SM00892. Endonuclease_NS. 1 hit.
    SM00477. NUC. 1 hit.
    SM00201. SO. 2 hits.
    [Graphical view ]
    SUPFAMi SSF53649. SSF53649. 1 hit.
    PROSITEi PS00524. SMB_1. 2 hits.
    PS50958. SMB_2. 2 hits.
    [Graphical view ]
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    Publicationsi

    1. "Plasma cell membrane glycoprotein PC-1. Primary structure deduced from cDNA clones."
      van Driel I.R., Goding J.W.
      J. Biol. Chem. 262:4882-4887(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT.
      Strain: BALB/c.
    2. Goding J.W.
      Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 24; 46-47; 642 AND 693.
    3. "Identification of nucleotide pyrophosphatase/alkaline phosphodiesterase I activity associated with the mouse plasma cell differentiation antigen PC-1."
      Rebbe N.F., Tong B.D., Finley E.M., Hickman S.
      Proc. Natl. Acad. Sci. U.S.A. 88:5192-5196(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
      Strain: BALB/c.
      Tissue: Plasmacytoma.
    4. "Structural basis of allotypes of ecto-nucleotide pyrophosphatase/phosphodiesterase (plasma cell membrane glycoprotein PC-1) in the mouse and rat, and analysis of allele-specific xenogeneic antibodies."
      Banakh I., Sali A., Dubljevic V., Grobben B., Slegers H., Goding J.W.
      Eur. J. Immunogenet. 29:307-313(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS ARG-651 AND SER-680, ALTERNATIVE SPLICING.
    5. "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 1).
      Strain: NOD.
      Tissue: Thymus.
    6. "Identification and characterization of a soluble form of the plasma cell membrane glycoprotein PC-1 (5'-nucleotide phosphodiesterase)."
      Belli S.I., van Driel I.R., Goding J.W.
      Eur. J. Biochem. 217:421-428(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 168-188, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION.
    7. "Murine plasma cell membrane antigen PC-1: molecular cloning of cDNA and analysis of expression."
      van Driel I.R., Wilks A.F., Pietersz G.A., Goding J.W.
      Proc. Natl. Acad. Sci. U.S.A. 82:8619-8623(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 203-219.
    8. "The murine plasma cell antigen PC-1: purification and partial amino acid sequence."
      Stearne P.A., van Driel I.R., Grego B., Simpson R.J., Goding J.W.
      J. Immunol. 134:443-448(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 204-219; 332-351; 486-509; 716-725; 803-818 AND 855-867, SUBCELLULAR LOCATION.
    9. "Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location."
      Buckley M.F., Loveland K.A., McKinstry W.J., Garson O.M., Goding J.W.
      J. Biol. Chem. 265:17506-17511(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF POSSIBLE INITIATION SITE.
    10. "Mutation in Npps in a mouse model of ossification of the posterior longitudinal ligament of the spine."
      Okawa A., Nakamura I., Goto S., Moriya H., Nakamura Y., Ikegawa S.
      Nat. Genet. 19:271-273(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE, FUNCTION.
    11. "Structural and catalytic similarities between nucleotide pyrophosphatases/phosphodiesterases and alkaline phosphatases."
      Gijsbers R., Ceulemans H., Stalmans W., Bollen M.
      J. Biol. Chem. 276:1361-1368(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE, METAL-BINDING, MUTAGENESIS OF ASP-200; LYS-237; THR-238; PHE-239; ASP-358; HIS-362; ASP-405; HIS-406 AND HIS-517, CATALYTIC ACTIVITY.
    12. "Characterization of a di-leucine-based signal in the cytoplasmic tail of the nucleotide-pyrophosphatase NPP1 that mediates basolateral targeting but not endocytosis."
      Bello V., Goding J.W., Greengrass V., Sali A., Dubljevic V., Lenoir C., Trugnan G., Maurice M.
      Mol. Biol. Cell 12:3004-3015(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DI-LEUCINE MOTIF, MUTAGENESIS OF ALA-28; SER-30; LEU-31 AND LEU-32, SUBCELLULAR LOCATION.
    13. "Subcellular targeting and function of osteoblast nucleotide pyrophosphatase phosphodiesterase 1."
      Vaingankar S.M., Fitzpatrick T.A., Johnson K., Goding J.W., Maurice M., Terkeltaub R.
      Am. J. Physiol. 286:C1177-C1187(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DI-LEUCINE MOTIF, MUTAGENESIS OF LEU-31; LEU-32; LEU-42 AND TYR-57, SUBCELLULAR LOCATION.
    14. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
      Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
      Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-267; ASN-323 AND ASN-624.
      Tissue: Myoblast.
    15. "Crystal structure of Enpp1, an extracellular glycoprotein involved in bone mineralization and insulin signaling."
      Kato K., Nishimasu H., Okudaira S., Mihara E., Ishitani R., Takagi J., Aoki J., Nureki O.
      Proc. Natl. Acad. Sci. U.S.A. 109:16876-16881(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 92-906 IN COMPLEXES WITH AMP; CMP; GMP; TMP; CALCIUM AND ZINC, GLYCOSYLATION AT ASN-267; ASN-323 AND ASN-567, DISULFIDE BOND, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-239; HIS-242; 304-TRP--ASN-323; ASP-308 AND TYR-322, COFACTOR.
    16. "Structure of NPP1, an ectonucleotide pyrophosphatase/ phosphodiesterase involved in tissue calcification."
      Jansen S., Perrakis A., Ulens C., Winkler C., Andries M., Joosten R.P., Van Acker M., Luyten F.P., Moolenaar W.H., Bollen M.
      Structure 20:1948-1959(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 87-906 IN COMPLEX WITH CALCIUM; PHOSPHATE AND ZINC, DISULFIDE BONDS, METAL-BINDING SITES, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-323; ASN-459; ASN-567 AND ASN-624, COFACTOR.

    Entry informationi

    Entry nameiENPP1_MOUSE
    AccessioniPrimary (citable) accession number: P06802
    Secondary accession number(s): Q542E9, Q924C4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 146 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    It is uncertain whether Met-1 or Met-35 is the initiator.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

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