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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

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

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

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

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

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
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_989578.1. NM_204247.1.
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_989578.1. NM_204247.1.
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.

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: February 4, 2015
This is version 93 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.