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O93295

- ENTP8_CHICK

UniProt

O93295 - ENTP8_CHICK

Protein

Ectonucleoside triphosphate diphosphohydrolase 8

Gene

ENTPD8

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    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+ or Mg2+. Has lower efficiency with Mg2+ By similarity.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

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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

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

    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    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...

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 2821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei464 – 48623HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GDA1/CD39 NTPase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5371.
    HOGENOMiHOG000059572.
    HOVERGENiHBG018982.
    InParanoidiQ90X66.
    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

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    MEYKGKVVAG LLTATCVFSI IALILSAVDV KDVFLPPGTK YGLVFDAGST    50
    HTALYVYQWP ADKENGTGIV SQVESCTVNG SGISSYADDP AGAGASLKPC 100
    LDKAMAVIPV EQQWQTPTYL GATAGMRLLR EQNSTKAEQV FAEVSKAIRE 150
    FPVDFRGAQI LTGNEEGSFG WITVNYLLET LIKFSFAGKW EHPQNTEVLG 200
    ALDLGGASTQ ITFQPGVTIE DKNTSVLFRL YGTNYSLYTH SYLCYGQIQA 250
    SKRLMAALHQ DGSYVQNISH PCYPKGYRRI ITIAEIYDSP CVPTPSMLSP 300
    AQILTVTGTG NPAACPTAIL KLFNLTCGAN RTCGFDGVYQ PPVRGQFFAF 350
    AGFYYTFSFL NLTGQQSLSH VNATVWDFCN KNWSELVETF PQNKEHLHTY 400
    CVVGLYILTL LVDGYKFDEH TWSNIHFSQK AGNADIGWTL GFMLNLTNMI 450
    PTEALEHVKG HEPSLWAGAI SFIVLAIVAG LVAILLQCFW KSK 493
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF041355 mRNA. Translation: AAC26491.1.
    AF426405 mRNA. Translation: AAL25086.1.
    RefSeqiNP_989578.1. NM_204247.1.
    UniGeneiGga.49226.

    Genome annotation databases

    GeneIDi374095.
    KEGGigga:374095.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF041355 mRNA. Translation: AAC26491.1 .
    AF426405 mRNA. Translation: AAL25086.1 .
    RefSeqi NP_989578.1. NM_204247.1.
    UniGenei Gga.49226.

    3D structure databases

    ProteinModelPortali O93295.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9031.ENSGALP00000014500.

    Proteomic databases

    PaxDbi O93295.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 374095.
    KEGGi gga:374095.

    Organism-specific databases

    CTDi 377841.

    Phylogenomic databases

    eggNOGi COG5371.
    HOGENOMi HOG000059572.
    HOVERGENi HBG018982.
    InParanoidi Q90X66.
    KOi K01510.
    PhylomeDBi O93295.

    Miscellaneous databases

    NextBioi 20813614.
    PROi O93295.

    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. "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: October 1, 2014
    This is version 89 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