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P97687

- ENTP1_RAT

UniProt

P97687 - ENTP1_RAT

Protein

Ectonucleoside triphosphate diphosphohydrolase 1

Gene

Entpd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.1 Publication

    Catalytic activityi

    A nucleoside 5'-triphosphate + 2 H2O = a nucleoside 5'-phosphate + 2 phosphate.1 Publication

    Cofactori

    Ca2+ or Mg2+.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei174 – 1741Proton acceptorBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. hydrolase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Calcium, Magnesium, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ectonucleoside triphosphate diphosphohydrolase 1 (EC:3.6.1.5)
    Short name:
    NTPDase 1
    Alternative name(s):
    Ecto-ATP diphosphohydrolase 1
    Short name:
    Ecto-ATPDase 1
    Short name:
    Ecto-ATPase 1
    Ecto-apyrase
    Lymphoid cell activation antigen
    CD_antigen: CD39
    Gene namesi
    Name:Entpd1
    Synonyms:Cd39
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi69265. Entpd1.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 511511Ectonucleoside triphosphate diphosphohydrolase 1PRO_0000209904Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi84 ↔ 1081 Publication
    Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi254 ↔ 3001 Publication
    Disulfide bondi281 ↔ 3241 Publication
    Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi337 ↔ 3421 Publication
    Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi391 ↔ 4141 Publication
    Glycosylationi429 – 4291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiP97687.

    PTM databases

    PhosphoSiteiP97687.

    Expressioni

    Tissue specificityi

    Expressed in primary neurons and astrocytes, kidney, liver, muscle, thymus, lung and spleen.1 Publication

    Gene expression databases

    GenevestigatoriP97687.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.By similarity

    Structurei

    Secondary structure

    1
    511
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi47 – 559
    Beta strandi60 – 689
    Beta strandi79 – 857
    Beta strandi87 – 893
    Helixi91 – 944
    Helixi98 – 1003
    Helixi101 – 11515
    Helixi118 – 1214
    Beta strandi125 – 1306
    Helixi132 – 1409
    Helixi142 – 15716
    Beta strandi159 – 16810
    Helixi171 – 18515
    Turni186 – 1894
    Beta strandi209 – 2135
    Beta strandi215 – 2228
    Beta strandi229 – 2313
    Helixi232 – 2343
    Beta strandi235 – 2406
    Beta strandi243 – 25311
    Helixi257 – 26812
    Beta strandi273 – 2797
    Beta strandi287 – 2915
    Helixi292 – 2954
    Helixi299 – 3046
    Beta strandi311 – 3177
    Helixi321 – 3299
    Beta strandi338 – 3447
    Beta strandi356 – 3605
    Helixi361 – 37212
    Helixi380 – 39112
    Helixi395 – 4017
    Helixi407 – 4104
    Helixi413 – 42513
    Helixi432 – 4376
    Beta strandi438 – 4403
    Beta strandi442 – 4443
    Beta strandi447 – 4515
    Helixi452 – 4598

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZX0X-ray2.50A/B/C/D38-477[»]
    3ZX2X-ray1.81A/B/C/D38-477[»]
    3ZX3X-ray1.70A/B/C/D38-477[»]
    ProteinModelPortaliP97687.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini38 – 478441ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini500 – 51112CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei17 – 3721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei479 – 49921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni46 – 171126N-terminal lobeAdd
    BLAST
    Regioni205 – 441237C-terminal lobeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the GDA1/CD39 NTPase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG018982.
    KOiK01510.
    PhylomeDBiP97687.

    Family and domain databases

    InterProiIPR000407. GDA1_CD39_NTPase.
    [Graphical view]
    PANTHERiPTHR11782. PTHR11782. 1 hit.
    PfamiPF01150. GDA1_CD39. 1 hit.
    [Graphical view]
    PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P97687-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEDIKDSKVK RFCSKNILII LGFSSVLAVI ALIAVGLTHN KPLPENVKYG    50
    IVLDAGSSHT NLYIYKWPAE KENDTGVVQL LEECQVKGPG ISKYAQKTDE 100
    IAAYLAECMK MSTERIPASK QHQTPVYLGA TAGMRLLRME SKQSADEVLA 150
    AVSRSLKSYP FDFQGAKIIT GQEEGAYGWI TINYLLGRFT QEQSWLNFIS 200
    DSQKQATFGA LDLGGSSTQV TFVPLNQTLE APETSLQFRL YGTDYTVYTH 250
    SFLCYGKDQA LWQKLAQDIQ VSSGGILKDP CFYPGYKKVV NVSELYGTPC 300
    TKRFEKKLPF NQFQVQGTGD YEQCHQSILK FFNNSHCPYS QCAFNGVFLP 350
    PLQGSFGAFS AFYFVMDFFK KMANDSVSSQ EKMTEITKNF CSKPWEEVKA 400
    SYPTVKEKYL SEYCFSGTYI LSLLLQGYNF TGTSWDQIHF MGKIKDSNAG 450
    WTLGYMLNLT NMIPAEQPLS PPLPHSTYIS LMVLFSLVLV AMVITGLFIF 500
    SKPSYFWKEA V 511
    Length:511
    Mass (Da):57,408
    Last modified:May 1, 1997 - v1
    Checksum:i4CC123D3E644C193
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti332 – 3321F → L(PubMed:10581401)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U81295 mRNA. Translation: AAC53195.1.
    Y15685 mRNA. Translation: CAA75730.1.
    RefSeqiNP_072109.1. NM_022587.1.
    UniGeneiRn.17491.

    Genome annotation databases

    GeneIDi64519.
    KEGGirno:64519.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U81295 mRNA. Translation: AAC53195.1 .
    Y15685 mRNA. Translation: CAA75730.1 .
    RefSeqi NP_072109.1. NM_022587.1.
    UniGenei Rn.17491.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ZX0 X-ray 2.50 A/B/C/D 38-477 [» ]
    3ZX2 X-ray 1.81 A/B/C/D 38-477 [» ]
    3ZX3 X-ray 1.70 A/B/C/D 38-477 [» ]
    ProteinModelPortali P97687.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P97687.
    ChEMBLi CHEMBL2767.

    PTM databases

    PhosphoSitei P97687.

    Proteomic databases

    PRIDEi P97687.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 64519.
    KEGGi rno:64519.

    Organism-specific databases

    CTDi 953.
    RGDi 69265. Entpd1.

    Phylogenomic databases

    HOVERGENi HBG018982.
    KOi K01510.
    PhylomeDBi P97687.

    Miscellaneous databases

    NextBioi 613322.
    PROi P97687.

    Gene expression databases

    Genevestigatori P97687.

    Family and domain databases

    InterProi IPR000407. GDA1_CD39_NTPase.
    [Graphical view ]
    PANTHERi PTHR11782. PTHR11782. 1 hit.
    Pfami PF01150. GDA1_CD39. 1 hit.
    [Graphical view ]
    PROSITEi PS01238. GDA1_CD39_NTPASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of brain ecto-apyrase: evidence for only one ecto-apyrase (CD39) gene."
      Wang T.-F., Rosenberg P.A., Guidotti G.
      Brain Res. Mol. Brain Res. 47:295-302(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, COFACTOR, GLYCOSYLATION, TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Hippocampus.
    2. "Evidence for alternative splicing of ecto-ATPase associated with termination of purinergic transmission."
      Vlajkovic S.M., Housley G.D., Greenwood D., Thorne P.R.
      Brain Res. Mol. Brain Res. 73:85-92(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Cochlea.
    3. "An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in rat brain."
      Kegel B., Braun N., Heine P., Maliszewski C.R., Zimmermann H.
      Neuropharmacology 36:1189-1200(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 432-511.
      Strain: Sprague-Dawley.
      Tissue: Brain.
    4. "Crystallographic evidence for a domain motion in rat nucleoside triphosphate diphosphohydrolase (NTPDase) 1."
      Zebisch M., Krauss M., Schafer P., Strater N.
      J. Mol. Biol. 415:288-306(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 38-477, DISULFIDE BONDS.

    Entry informationi

    Entry nameiENTP1_RAT
    AccessioniPrimary (citable) accession number: P97687
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3