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Protein

Ectonucleoside triphosphate diphosphohydrolase 8

Gene

ENTPD8

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside ATPases catalyze the hydrolysis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides.2 Publications

Catalytic activityi

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

Cofactori

Ca2+By similarity, Mg2+By similarityNote: Ca(2+) or Mg(2+). Has lower efficiency with Mg2+.By similarity

Kineticsi

  1. KM=0.51 mM for ATP1 Publication
  2. KM=5.3 mM for ADP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei166 – 1661Proton acceptorBy similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.6.1.5. 1306.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ectonucleoside triphosphate diphosphohydrolase 8 (EC:3.6.1.5)
    Short name:
    E-NTPDase 8
    Short name:
    NTPDase 8
    Short name:
    NTPDase8
    Alternative name(s):
    Liver ecto-ATP diphosphohydrolase
    Gene namesi
    Name:ENTPD8
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539 Componenti: Unplaced

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 77CytoplasmicSequence Analysis
    Transmembranei8 – 2821HelicalSequence AnalysisAdd
    BLAST
    Topological domaini29 – 463435ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei464 – 48623HelicalSequence AnalysisAdd
    BLAST
    Topological domaini487 – 4937CytoplasmicSequence Analysis

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 493493Ectonucleoside triphosphate diphosphohydrolase 8PRO_0000209905Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi65 – 651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi76 ↔ 100By similarity
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi244 ↔ 291By similarity
    Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi327 ↔ 333By similarity
    Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi361 – 3611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi379 ↔ 401By similarity
    Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi445 – 4451N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO93295.

    Interactioni

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000014500.

    Structurei

    3D structure databases

    ProteinModelPortaliO93295.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GDA1/CD39 NTPase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5371.
    HOGENOMiHOG000059572.
    HOVERGENiHBG018982.
    InParanoidiO93295.
    KOiK01510.
    PhylomeDBiO93295.

    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.

    O93295-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEYKGKVVAG LLTATCVFSI IALILSAVDV KDVFLPPGTK YGLVFDAGST
    60 70 80 90 100
    HTALYVYQWP ADKENGTGIV SQVESCTVNG SGISSYADDP AGAGASLKPC
    110 120 130 140 150
    LDKAMAVIPV EQQWQTPTYL GATAGMRLLR EQNSTKAEQV FAEVSKAIRE
    160 170 180 190 200
    FPVDFRGAQI LTGNEEGSFG WITVNYLLET LIKFSFAGKW EHPQNTEVLG
    210 220 230 240 250
    ALDLGGASTQ ITFQPGVTIE DKNTSVLFRL YGTNYSLYTH SYLCYGQIQA
    260 270 280 290 300
    SKRLMAALHQ DGSYVQNISH PCYPKGYRRI ITIAEIYDSP CVPTPSMLSP
    310 320 330 340 350
    AQILTVTGTG NPAACPTAIL KLFNLTCGAN RTCGFDGVYQ PPVRGQFFAF
    360 370 380 390 400
    AGFYYTFSFL NLTGQQSLSH VNATVWDFCN KNWSELVETF PQNKEHLHTY
    410 420 430 440 450
    CVVGLYILTL LVDGYKFDEH TWSNIHFSQK AGNADIGWTL GFMLNLTNMI
    460 470 480 490
    PTEALEHVKG HEPSLWAGAI SFIVLAIVAG LVAILLQCFW KSK
    Length:493
    Mass (Da):54,035
    Last modified:November 1, 1998 - v1
    Checksum:iF14FF4C3AA2F3603
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161C → W AA sequence (PubMed:9295305).Curated
    Sequence conflicti21 – 211I → G AA sequence (PubMed:9632655).Curated
    Sequence conflicti278 – 2803RRI → QEN in AAL25086 (PubMed:11985621).Curated
    Sequence conflicti316 – 3161P → R in AAL25086 (PubMed:11985621).Curated
    Sequence conflicti325 – 3251L → F in AAL25086 (PubMed:11985621).Curated
    Sequence conflicti461 – 4622HE → QQ in AAL25086 (PubMed:11985621).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF041355 mRNA. Translation: AAC26491.1.
    AF426405 mRNA. Translation: AAL25086.1.
    RefSeqiNP_989578.2. NM_204247.2.
    UniGeneiGga.49226.

    Genome annotation databases

    GeneIDi374095.
    KEGGigga:374095.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF041355 mRNA. Translation: AAC26491.1.
    AF426405 mRNA. Translation: AAL25086.1.
    RefSeqiNP_989578.2. NM_204247.2.
    UniGeneiGga.49226.

    3D structure databases

    ProteinModelPortaliO93295.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000014500.

    Proteomic databases

    PaxDbiO93295.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi374095.
    KEGGigga:374095.

    Organism-specific databases

    CTDi377841.

    Phylogenomic databases

    eggNOGiCOG5371.
    HOGENOMiHOG000059572.
    HOVERGENiHBG018982.
    InParanoidiO93295.
    KOiK01510.
    PhylomeDBiO93295.

    Enzyme and pathway databases

    BRENDAi3.6.1.5. 1306.

    Miscellaneous databases

    NextBioi20813614.
    PROiO93295.

    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]
    ProtoNetiSearch...

    Publicationsi

    1. "Molecular cloning of the chicken oviduct ecto-ATP-diphosphohydrolase."
      Nagy A.K., Knowles A.F., Nagami G.T.
      J. Biol. Chem. 273:16043-16049(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-21 AND 150-156.
      Tissue: Oviduct.
    2. "Purification, characterization, cloning, and expression of the chicken liver ecto-ATP-diphosphohydrolase."
      Knowles A.F., Nagy A.K., Strobel R.S., Wu-Weis M.
      Eur. J. Biochem. 269:2373-2382(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
      Tissue: Liver.
    3. "Immunolocalization of the ecto-ATPase and ecto-apyrase in chicken gizzard and stomach. Purification and N-terminal sequence of the stomach ecto-apyrase."
      Lewis-Carl S., Kirley T.L.
      J. Biol. Chem. 272:23645-23652(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-17.
      Tissue: Stomach.
    4. "Either the carboxyl- or the amino-terminal region of the human ecto-ATPase (E-NTPDase 2) confers detergent and temperature sensitivity to the chicken ecto-ATP-diphosphohydrolase (E-NTPDase 8)."
      Mukasa T., Lee Y., Knowles A.F.
      Biochemistry 44:11160-11170(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiENTP8_CHICK
    AccessioniPrimary (citable) accession number: O93295
    Secondary accession number(s): Q90X66
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: November 1, 1998
    Last modified: April 1, 2015
    This is version 95 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.