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Q924C3

- ENPP1_RAT

UniProt

Q924C3 - ENPP1_RAT

Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

Gene

Enpp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (19 Sep 2002)
      Previous versions | rss
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    Functioni

    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. Appears to modulate insulin sensitivity By similarity.By similarity

    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.By similarity

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei84 – 852CleavageBy similarity
    Metal bindingi200 – 2001Zinc 1; catalyticBy similarity
    Active sitei238 – 2381AMP-threonine intermediateBy similarity
    Metal bindingi238 – 2381Zinc 1; catalyticBy similarity
    Binding sitei259 – 2591SubstrateBy similarity
    Binding sitei277 – 2771SubstrateBy similarity
    Binding sitei322 – 3221SubstrateBy similarity
    Metal bindingi358 – 3581Zinc 2; catalyticBy similarity
    Metal bindingi362 – 3621Zinc 2; via tele nitrogen; catalyticBy similarity
    Metal bindingi405 – 4051Zinc 1; catalyticBy similarity
    Metal bindingi406 – 4061Zinc 1; via tele nitrogen; catalyticBy similarity
    Metal bindingi517 – 5171Zinc 2; via tele nitrogen; catalyticBy similarity
    Metal bindingi781 – 7811CalciumBy similarity
    Metal bindingi783 – 7831CalciumBy similarity
    Metal bindingi785 – 7851CalciumBy similarity
    Metal bindingi787 – 7871Calcium; via carbonyl oxygenBy similarity
    Metal bindingi789 – 7891CalciumBy similarity
    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. immune response Source: InterPro
    4. 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

    SABIO-RKQ924C3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
    Short name:
    E-NPP 1
    Alternative name(s):
    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi628825. Enpp1.

    Subcellular locationi

    Cell membrane By similarity; Single-pass type II membrane protein By similarity. Basolateral cell membrane By similarity; Single-pass type II membrane protein By similarity. Secreted By similarity
    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. The proteolytically processed form is secreted By similarity.By similarity

    GO - Cellular componenti

    1. basolateral plasma membrane Source: UniProtKB-SubCell
    2. extracellular region Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB
    4. integral component of plasma membrane Source: UniProtKB
    5. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 906906Ectonucleotide pyrophosphatase/phosphodiesterase family member 1PRO_0000188566Add
    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 ↔ 223PROSITE-ProRule annotation
    Disulfide bondi185 ↔ 397PROSITE-ProRule annotation
    Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi413 ↔ 512PROSITE-ProRule annotation
    Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi462 ↔ 849PROSITE-ProRule annotation
    Glycosylationi567 – 5671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi596 ↔ 653PROSITE-ProRule annotation
    Disulfide bondi607 ↔ 707PROSITE-ProRule annotation
    Disulfide bondi609 ↔ 692PROSITE-ProRule annotation
    Glycosylationi624 – 6241N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi819 ↔ 829PROSITE-ProRule annotation

    Post-translational modificationi

    A secreted form is produced through cleavage at Lys-85 by intracellular processing.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ924C3.
    PRIDEiQ924C3.

    PTM databases

    PhosphoSiteiQ924C3.

    Expressioni

    Gene expression databases

    GenevestigatoriQ924C3.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    MINTiMINT-4997931.

    Structurei

    3D structure databases

    ProteinModelPortaliQ924C3.
    SMRiQ924C3. Positions 129-171.
    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 – 17044SMB 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni173 – 573401PhosphodiesteraseAdd
    BLAST
    Regioni579 – 62850LinkerBy similarityAdd
    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 epithelial cells, and for targeting to matrix vesicles derived from mineralizing cells.By similarity

    Sequence similaritiesi

    Contains 2 SMB (somatomedin-B) domains.Curated

    Keywords - Domaini

    Repeat, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1524.
    HOGENOMiHOG000037439.
    HOVERGENiHBG051484.
    InParanoidiQ924C3.
    KOiK01513.
    PhylomeDBiQ924C3.

    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: Q924C3-1) [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

    MERDGEQAGQ GPRHGPAGNG RELESPAAAS LLAPMDLGEE PLEKAERART    50
    AKDPNTYKVL SLVLSVCVLT TILGCIFGLK PSCAKEVKSC KGRCFERTFS 100
    NCRCDAACVS LGNCCLDFQE TCVEPTHIWT CNKFRCGEKR LSRFVCSCAD 150
    DCKAHNDCCI NYSSVCQEKK SWVEEACETI DAPQCPAEFE SPPTLLFSLD 200
    GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPVYPTKTFP NHYSIVTGLY 250
    PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVRSG 300
    TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSYERPHFY 350
    TLYLEEPDSS GHSHGPVSSE VIKALQKVDH IVGMLMDGLK DLGLDKCLNL 400
    ILISDHGMEQ GSCKKYVYLN KYLGDVNNVK VVYGPAARLR PTEVPETYYS 450
    FNYEALAKNL SCRETNQHFR PYLKHFLPKR LHFAKNDRIE PLTFYLDPQW 500
    QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG AEVDSFENIE 550
    VYNLMCDLLG LIPAPNNESH GSLNHLLKKP IYTPSHPKEE SFLSQCPIKS 600
    VSSDLGCTCD PSIVPIMDFE KQFNLTTDAV EDVYSMTVPN GRPRNLQKQH 650
    RVCLLHQQQF LTGYSLDLLM PLWTSYTFLS NDQFSTDDFS NCLYQDLRIP 700
    LSPMHKCSYY KSTSKLSYGF LTPPRLNRVS RQIYSEALLT SNIVPMYQSF 750
    QVIWQYLHDT VLRRYAQERN GVNVVSGPVF DFDYDGRYDS SEILKQNTRV 800
    IRSQENLIPT HFFIVLTSCK QLSESPLKCT ALESSAFLLP HRPDNIESCT 850
    HGKQESAWVE ELLALHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP 900
    IFSQED 906
    Length:906
    Mass (Da):102,942
    Last modified:September 19, 2002 - v2
    Checksum:i71F56780B279A919
    GO
    Isoform 1 (identifier: Q924C3-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:905
    Mass (Da):102,843
    Checksum:i46EE88917B4BBCD3
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti440 – 4423RPT → NPP in strain: Wistar.
    Natural varianti457 – 4571A → T in strain: Lewis.
    Natural varianti555 – 5551M → I in strain: Lewis.
    Natural varianti568 – 5681E → G in strain: Wistar.
    Natural varianti583 – 5831T → I in strain: Lewis.
    Natural varianti592 – 5921F → V in strain: Lewis.
    Natural varianti624 – 6241N → K in strain: Lewis.
    Natural varianti640 – 6401N → H in strain: Lewis.
    Natural varianti774 – 7741V → I in strain: Lewis.
    Natural varianti806 – 8061N → I in strain: Lewis.
    Natural varianti850 – 8501T → I in strain: Lewis.
    Natural varianti898 – 8981H → Q in strain: Lewis.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei630 – 6301Missing in isoform 1. 1 PublicationVSP_006749

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF340185 mRNA. Translation: AAK69653.1.
    AF340186 mRNA. Translation: AAK69654.1.
    AF320054 mRNA. Translation: AAL26912.1.
    RefSeqiNP_445987.1. NM_053535.1. [Q924C3-1]
    UniGeneiRn.1199.

    Genome annotation databases

    GeneIDi85496.
    KEGGirno:85496.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF340185 mRNA. Translation: AAK69653.1 .
    AF340186 mRNA. Translation: AAK69654.1 .
    AF320054 mRNA. Translation: AAL26912.1 .
    RefSeqi NP_445987.1. NM_053535.1. [Q924C3-1 ]
    UniGenei Rn.1199.

    3D structure databases

    ProteinModelPortali Q924C3.
    SMRi Q924C3. Positions 129-171.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4997931.

    PTM databases

    PhosphoSitei Q924C3.

    Proteomic databases

    PaxDbi Q924C3.
    PRIDEi Q924C3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 85496.
    KEGGi rno:85496.

    Organism-specific databases

    CTDi 5167.
    RGDi 628825. Enpp1.

    Phylogenomic databases

    eggNOGi COG1524.
    HOGENOMi HOG000037439.
    HOVERGENi HBG051484.
    InParanoidi Q924C3.
    KOi K01513.
    PhylomeDBi Q924C3.

    Enzyme and pathway databases

    SABIO-RK Q924C3.

    Miscellaneous databases

    NextBioi 617598.
    PROi Q924C3.

    Gene expression databases

    Genevestigatori Q924C3.

    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 ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORMS 1 AND 2), VARIANTS.
      Strain: Lewis, Louvain and Wistar.
    2. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
      Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
      Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiENPP1_RAT
    AccessioniPrimary (citable) accession number: Q924C3
    Secondary accession number(s): Q91XQ3, Q920C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 102 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3