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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

Gene

Enpp1

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

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.4 Publications
A nucleoside triphosphate + H2O = a nucleotide + diphosphate.4 Publications

Cofactori

Zn2+2 PublicationsNote: Binds 2 Zn2+ 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)DescriptionActionsGraphical viewLength
    Metal bindingi200Zinc 1; catalytic1 Publication1
    Active sitei238AMP-threonine intermediate1 Publication1
    Metal bindingi238Zinc 1; catalytic1 Publication1
    Binding sitei259Substrate1
    Binding sitei277Substrate1
    Binding sitei322Substrate1
    Metal bindingi358Zinc 2; catalytic1 Publication1
    Metal bindingi362Zinc 2; via tele nitrogen; catalytic1 Publication1
    Metal bindingi405Zinc 1; catalytic1 Publication1
    Metal bindingi406Zinc 1; via tele nitrogen; catalytic1 Publication1
    Metal bindingi517Zinc 2; via tele nitrogen; catalytic1 Publication1
    Metal bindingi781Calcium1 Publication1
    Metal bindingi783Calcium1 Publication1
    Metal bindingi785Calcium1 Publication1
    Metal bindingi787Calcium; via carbonyl oxygen1 Publication1
    Metal bindingi789Calcium1 Publication1
    Sitei896Essential for catalytic activityBy similarity1

    GO - Molecular functioni

    • ATP binding Source: MGI
    • calcium ion binding Source: UniProtKB
    • insulin receptor binding Source: MGI
    • NADH pyrophosphatase activity Source: UniProtKB-EC
    • nucleic acid binding Source: InterPro
    • nucleoside-triphosphate diphosphatase activity Source: MGI
    • nucleotide diphosphatase activity Source: UniProtKB
    • phosphodiesterase I activity Source: UniProtKB
    • polysaccharide binding Source: InterPro
    • protein homodimerization activity Source: MGI
    • scavenger receptor activity Source: InterPro
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Biomineralization

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.1.4.1. 3474.
    3.6.1.9. 3474.

    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:3.1.4.14 Publications)
    Nucleotide pyrophosphatase (EC:3.6.1.94 Publications)
    Short name:
    NPPase
    Alternative name(s):
    Nucleotide diphosphataseCurated
    Gene namesi
    Name:Enpp1
    Synonyms:Npps, Pc1, Pdnp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Unplaced

    Organism-specific databases

    MGIiMGI:97370. Enpp1.

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini1 – 58CytoplasmicSequence analysisAdd BLAST58
    Transmembranei59 – 79Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
    Topological domaini80 – 906ExtracellularSequence analysisAdd BLAST827

    GO - Cellular componenti

    • basolateral plasma membrane Source: UniProtKB-SubCell
    • cell surface Source: BHF-UCL
    • extracellular space Source: BHF-UCL
    • integral component of membrane Source: UniProtKB
    • integral component of plasma membrane Source: UniProtKB
    • lysosomal membrane Source: MGI
    • plasma membrane Source: MGI
    Complete GO annotation...

    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.

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi28A → G: No effect on basolateral sorting in epithelial cells. 1 Publication1
    Mutagenesisi30S → A or D: Little change in baolateral sorting in epithelial cells. 1 Publication1
    Mutagenesisi31L → 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 Publications1
    Mutagenesisi32L → 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 Publications1
    Mutagenesisi42L → A: No change in increased NPP activity in oestoblastic matrix vesicles. 1 Publication1
    Mutagenesisi57Y → G: No change in increased NPP activity in oestoblastic matrix vesicles. 1 Publication1
    Mutagenesisi200D → N: Decreases phosphodiesterase activity by 95%. Abolishes formation of nucleotidylated intermediate. 1 Publication1
    Mutagenesisi237K → A: Decreases phosphodiesterase activity by 40%. Decreased formation of nucleotidylated intermediate. 1 Publication1
    Mutagenesisi238T → A: Abolishes all phosphodiesterase activity. Abolishes formation of nucleotidylated intermediate. 1 Publication1
    Mutagenesisi238T → S: Decreases phosphodiesterase activity by 95%. Accumulates nucleotidylated intermediate. 1 Publication1
    Mutagenesisi239F → A: Decreases phosphodiesterase activity by 50%. Decreased formation of nucleotidylated intermediate. 2 Publications1
    Mutagenesisi242H → L: Strongly decreased phosphodiesterase activity. 1 Publication1
    Mutagenesisi304 – 323Missing : Nearly abolishes activity with nucleotide phosphates. Confers very low activity with lysophospholipids. 1 PublicationAdd BLAST20
    Mutagenesisi308D → A: Decreased phosphodiesterase activity. 1 Publication1
    Mutagenesisi322Y → A: Strongly decreased phosphodiesterase activity. 1 Publication1
    Mutagenesisi358D → Q: Decreases phosphodiesterase activity by 90%. Accumulates nucleotidylated intermediate. 1 Publication1
    Mutagenesisi362H → Q: Decreases phosphodiesterase activity by 95%. 65% activity can be restored by addition of Zn(2+) ions. Accumulates nucleotidylated intermediate. 1 Publication1
    Mutagenesisi405D → N: Abolishes all phosphodiesterase activity. 10% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. 1 Publication1
    Mutagenesisi406H → Q: Abolishes all phosphodiesterase activity. 15% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. 1 Publication1
    Mutagenesisi517H → Q: Abolishes all phosphodiesterase activity. 60% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001885651 – 906Ectonucleotide pyrophosphatase/phosphodiesterase family member 1Add BLAST906

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei25PhosphoserineBy similarity1
    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
    Glycosylationi161N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi177 ↔ 223
    Disulfide bondi185 ↔ 397
    Modified residuei238PhosphothreonineBy similarity1
    Glycosylationi267N-linked (GlcNAc...)2 Publications1
    Glycosylationi323N-linked (GlcNAc...)3 Publications1
    Disulfide bondi413 ↔ 512
    Glycosylationi459N-linked (GlcNAc...)1 Publication1
    Disulfide bondi462 ↔ 849
    Glycosylationi567N-linked (GlcNAc...)2 Publications1
    Disulfide bondi596 ↔ 653
    Disulfide bondi607 ↔ 707
    Disulfide bondi609 ↔ 692
    Glycosylationi624N-linked (GlcNAc...)2 Publications1
    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.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei84 – 85Cleavage2

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP06802.
    PaxDbiP06802.
    PRIDEiP06802.

    PTM databases

    iPTMnetiP06802.
    PhosphoSitePlusiP06802.
    SwissPalmiP06802.

    Expressioni

    Tissue specificityi

    Selectively expressed on the surface of antibody-secreting cells.

    Gene expression databases

    BgeeiENSMUSG00000037370.

    Interactioni

    Subunit structurei

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

    GO - Molecular functioni

    Protein-protein interaction databases

    DIPiDIP-59981N.
    STRINGi10090.ENSMUSP00000101159.

    Structurei

    Secondary structure

    1906
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni94 – 96Combined sources3
    Beta strandi100 – 103Combined sources4
    Helixi108 – 111Combined sources4
    Helixi118 – 122Combined sources5
    Helixi124 – 126Combined sources3
    Turni133 – 137Combined sources5
    Beta strandi145 – 147Combined sources3
    Helixi152 – 155Combined sources4
    Helixi162 – 167Combined sources6
    Turni172 – 174Combined sources3
    Beta strandi194 – 199Combined sources6
    Helixi204 – 209Combined sources6
    Helixi211 – 213Combined sources3
    Helixi215 – 222Combined sources8
    Beta strandi224 – 228Combined sources5
    Helixi238 – 247Combined sources10
    Helixi251 – 254Combined sources4
    Beta strandi259 – 263Combined sources5
    Turni264 – 267Combined sources4
    Beta strandi268 – 270Combined sources3
    Beta strandi272 – 274Combined sources3
    Helixi275 – 278Combined sources4
    Turni280 – 282Combined sources3
    Helixi288 – 294Combined sources7
    Beta strandi299 – 303Combined sources5
    Beta strandi307 – 309Combined sources3
    Beta strandi311 – 313Combined sources3
    Beta strandi317 – 319Combined sources3
    Helixi328 – 338Combined sources11
    Turni343 – 345Combined sources3
    Beta strandi348 – 354Combined sources7
    Helixi358 – 364Combined sources7
    Beta strandi366 – 368Combined sources3
    Helixi369 – 391Combined sources23
    Beta strandi399 – 403Combined sources5
    Beta strandi413 – 418Combined sources6
    Helixi420 – 423Combined sources4
    Beta strandi428 – 432Combined sources5
    Beta strandi434 – 436Combined sources3
    Beta strandi438 – 443Combined sources6
    Turni444 – 446Combined sources3
    Turni448 – 450Combined sources3
    Helixi453 – 460Combined sources8
    Beta strandi468 – 473Combined sources6
    Helixi474 – 476Combined sources3
    Helixi479 – 481Combined sources3
    Beta strandi487 – 489Combined sources3
    Beta strandi491 – 496Combined sources6
    Beta strandi501 – 505Combined sources5
    Turni506 – 508Combined sources3
    Beta strandi512 – 516Combined sources5
    Helixi524 – 526Combined sources3
    Beta strandi530 – 534Combined sources5
    Beta strandi539 – 543Combined sources5
    Helixi548 – 550Combined sources3
    Helixi551 – 559Combined sources9
    Turni570 – 573Combined sources4
    Helixi574 – 576Combined sources3
    Beta strandi577 – 579Combined sources3
    Beta strandi591 – 594Combined sources4
    Beta strandi611 – 613Combined sources3
    Helixi617 – 624Combined sources8
    Helixi631 – 637Combined sources7
    Beta strandi651 – 656Combined sources6
    Beta strandi658 – 665Combined sources8
    Turni666 – 669Combined sources4
    Beta strandi670 – 678Combined sources9
    Helixi703 – 705Combined sources3
    Helixi707 – 709Combined sources3
    Beta strandi712 – 722Combined sources11
    Turni728 – 731Combined sources4
    Helixi736 – 738Combined sources3
    Helixi740 – 742Combined sources3
    Beta strandi743 – 747Combined sources5
    Helixi748 – 759Combined sources12
    Helixi761 – 768Combined sources8
    Beta strandi772 – 779Combined sources8
    Beta strandi785 – 787Combined sources3
    Helixi791 – 796Combined sources6
    Beta strandi799 – 801Combined sources3
    Beta strandi804 – 806Combined sources3
    Beta strandi810 – 821Combined sources12
    Helixi826 – 828Combined sources3
    Beta strandi830 – 840Combined sources11
    Turni846 – 849Combined sources4
    Turni851 – 853Combined sources3
    Helixi855 – 865Combined sources11
    Helixi870 – 877Combined sources8
    Helixi889 – 896Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini86 – 126SMB 1PROSITE-ProRule annotationAdd BLAST41
    Domaini127 – 171SMB 2PROSITE-ProRule annotationAdd BLAST45

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni173 – 573PhosphodiesteraseAdd BLAST401
    Regioni579 – 628LinkerAdd BLAST50
    Regioni635 – 906NucleaseAdd BLAST272

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi27 – 34Di-leucine motif8

    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

    eggNOGiKOG2645. Eukaryota.
    COG1524. LUCA.
    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.
    IPR029890. ENPP1.
    IPR020821. Extracellular_endonuc_su_A.
    IPR002591. Phosphodiest/P_Trfase.
    IPR020436. Somatomedin_B_chordata.
    IPR001212. Somatomedin_B_dom.
    [Graphical view]
    PANTHERiPTHR10151. PTHR10151. 1 hit.
    PTHR10151:SF77. PTHR10151:SF77. 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.
    SSF90188. SSF90188. 2 hits.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MERDGDQAGH GPRHGSAGNG RELESPAAAS LLAPMDLGEE PLEKAERARP
    60 70 80 90 100
    AKDPNTYKVL SLVLSVCVLT TILGCIFGLK PSCAKEVKSC KGRCFERTFS
    110 120 130 140 150
    NCRCDAACVS LGNCCLDFQE TCVEPTHIWT CNKFRCGEKR LSRFVCSCAD
    160 170 180 190 200
    DCKTHNDCCI NYSSVCQDKK SWVEETCESI DTPECPAEFE SPPTLLFSLD
    210 220 230 240 250
    GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPMYPTKTFP NHYSIVTGLY
    260 270 280 290 300
    PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVKSG
    310 320 330 340 350
    TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSHERPHFY
    360 370 380 390 400
    TLYLEEPDSS GHSHGPVSSE VIKALQKVDR LVGMLMDGLK DLGLDKCLNL
    410 420 430 440 450
    ILISDHGMEQ GSCKKYVYLN KYLGDVNNVK VVYGPAARLR PTDVPETYYS
    460 470 480 490 500
    FNYEALAKNL SCREPNQHFR PYLKPFLPKR LHFAKSDRIE PLTFYLDPQW
    510 520 530 540 550
    QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG AEVDSFENIE
    560 570 580 590 600
    VYNLMCDLLG LIPAPNNGSH GSLNHLLKKP IYNPSHPKEE GFLSQCPIKS
    610 620 630 640 650
    TSNDLGCTCD PWIVPIKDFE KQLNLTTEDV DDIYHMTVPY GRPRILLKQH
    660 670 680 690 700
    HVCLLQQQQF LTGYSLDLLM PLWASYTFLR NDQFSRDDFS NCLYQDLRIP
    710 720 730 740 750
    LSPVHKCSYY KSNSKLSYGF LTPPRLNRVS NHIYSEALLT SNIVPMYQSF
    760 770 780 790 800
    QVIWHYLHDT LLQRYAHERN GINVVSGPVF DFDYDGRYDS LEILKQNSRV
    810 820 830 840 850
    IRSQEILIPT HFFIVLTSCK QLSETPLECS ALESSAYILP HRPDNIESCT
    860 870 880 890 900
    HGKRESSWVE ELLTLHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP

    IFSQED
    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)DescriptionActionsGraphical viewLength
    Natural varianti651H → R in allele ENPP1b. 1 Publication1
    Natural varianti680R → S in allele ENPP1b. 1 Publication1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_006748630Missing in isoform 1. 2 Publications1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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]
    CCDS78802.1. [P06802-1]
    PIRiA27410.
    RefSeqiNP_001295256.1. NM_001308327.1.
    UniGeneiMm.27254.
    Mm.478860.

    Genome annotation databases

    GeneIDi18605.
    KEGGimmu:18605.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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]
    CCDS78802.1. [P06802-1]
    PIRiA27410.
    RefSeqiNP_001295256.1. NM_001308327.1.
    UniGeneiMm.27254.
    Mm.478860.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-59981N.
    STRINGi10090.ENSMUSP00000101159.

    PTM databases

    iPTMnetiP06802.
    PhosphoSitePlusiP06802.
    SwissPalmiP06802.

    Proteomic databases

    MaxQBiP06802.
    PaxDbiP06802.
    PRIDEiP06802.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi18605.
    KEGGimmu:18605.

    Organism-specific databases

    CTDi5167.
    MGIiMGI:97370. Enpp1.

    Phylogenomic databases

    eggNOGiKOG2645. Eukaryota.
    COG1524. LUCA.
    HOGENOMiHOG000034646.
    HOVERGENiHBG051484.
    InParanoidiP06802.
    KOiK01513.
    PhylomeDBiP06802.

    Enzyme and pathway databases

    BRENDAi3.1.4.1. 3474.
    3.6.1.9. 3474.

    Miscellaneous databases

    PROiP06802.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSMUSG00000037370.

    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.
    IPR029890. ENPP1.
    IPR020821. Extracellular_endonuc_su_A.
    IPR002591. Phosphodiest/P_Trfase.
    IPR020436. Somatomedin_B_chordata.
    IPR001212. Somatomedin_B_dom.
    [Graphical view]
    PANTHERiPTHR10151. PTHR10151. 1 hit.
    PTHR10151:SF77. PTHR10151:SF77. 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.
    SSF90188. SSF90188. 2 hits.
    PROSITEiPS00524. SMB_1. 2 hits.
    PS50958. SMB_2. 2 hits.
    [Graphical view]
    ProtoNetiSearch...

    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: November 30, 2016
    This is version 171 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

    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 one 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.